BMRB Entry 10256

Title:
Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human
Deposition date:
2008-11-20
Original release date:
2009-11-20
Authors:
Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human"  .

Assembly members:

Assembly members:
PH domain, polymer, 107 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   Vector: P040921-07

Data sets:
Data typeCount
13C chemical shifts432
15N chemical shifts102
1H chemical shifts679

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 107 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUGLUTHR
2   SERSERTYRLEUASNVALLEUVALASNSER
3   GLNTRPLYSSERARGTRPCYSSERVALARG
4   ASPASNHISLEUHISPHETYRGLNASPARG
5   ASNARGSERLYSVALALAGLNGLNPROLEU
6   SERLEUVALGLYCYSGLUVALVALPROASP
7   PROSERPROASPHISLEUTYRSERPHEARG
8   ILELEUHISLYSGLYGLUGLULEUALALYS
9   LEUGLUALALYSSERSERGLUGLUMETGLY
10   HISTRPLEUGLYLEULEULEUSERGLUSER
11   GLYSERGLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 1.59 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: 298 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F - processing

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

Kujira v0.913, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB55135 BAF84401 BAG53870 BAH11936
GB AAH24314 AAH33212 AAQ05765 EAW49470 EAW49471
REF NP_001001936 NP_001248593 NP_001274753 NP_115939 XP_002821211
SP Q8N4X5
AlphaFold Q8N4X5

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