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 10104

Title: The forkhead associated (FHA) domain like structure from mouse polynucleotide kinase 3'-phosphatase

Deposition date: 2007-02-13 Original release date: 2008-08-15

Authors: Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.

Citation: Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "The forkhead associated (FHA) domain like structure from mouse polynucleotide kinase 3'-phosphatase"  .

Assembly members:
polynucleotide kinase 3'-phosphatase, polymer, 119 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Vector: P030107-24

Entity Sequences (FASTA):
polynucleotide kinase 3'-phosphatase: GSSGSSGMSQLGSRGRLWLQ SPTGGPPPIFLPSDGQALVL GRGPLTQVTDRKCSRNQVEL IADPESRTVAVKQLGVNPST VGVQELKPGLSGSLSLGDVL YLVNGLYPLTLRWSGPSSG

Data sets:
Data typeCount
13C chemical shifts502
15N chemical shifts122
1H chemical shifts814

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1polynucleotide kinase 3'-phosphatase1

Entities:

Entity 1, polynucleotide kinase 3'-phosphatase 119 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETSERGLN
2   LEUGLYSERARGGLYARGLEUTRPLEUGLN
3   SERPROTHRGLYGLYPROPROPROILEPHE
4   LEUPROSERASPGLYGLNALALEUVALLEU
5   GLYARGGLYPROLEUTHRGLNVALTHRASP
6   ARGLYSCYSSERARGASNGLNVALGLULEU
7   ILEALAASPPROGLUSERARGTHRVALALA
8   VALLYSGLNLEUGLYVALASNPROSERTHR
9   VALGLYVALGLNGLULEULYSPROGLYLEU
10   SERGLYSERLEUSERLEUGLYASPVALLEU
11   TYRLEUVALASNGLYLEUTYRPROLEUTHR
12   LEUARGTRPSERGLYPROSERSERGLY

Samples:

sample_1: FHA domain, [U-13C; U-15N], 1.16 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker Biospin - collection

NMRPipe v20020425, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

Kujira v0.851, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAE43066
GB AAF36487 AAH57659 EDL22761 EDL22763
REF NP_001277693 NP_001277695 NP_067524 XP_006541101 XP_006541102
SP Q9JLV6
AlphaFold Q9JLV6

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