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 10255

Title: Solution structure of the N-terminal PH domain of ARAP2 protein from human

Authors: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Li, H.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the N-terminal PH domain of ARAP2 protein from human"  . ., .-..

Assembly members:
PH domain, polymer, 115 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
PH domain: GSSGSSGKVKSGWLDKLSPQ GKRMFQKRWVKFDGLSISYY NNEKEMYSKGIIPLSAISTV RVQGDNKFEVVTTQRTFVFR VEKEEERNDWISILLNALKS QSLTSQSQASGPSSG

Data sets:
Data typeCount
13C chemical shifts465
15N chemical shifts101
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PH domain1

Entities:

Entity 1, PH domain 115 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLYSVALLYS
2   SERGLYTRPLEUASPLYSLEUSERPROGLN
3   GLYLYSARGMETPHEGLNLYSARGTRPVAL
4   LYSPHEASPGLYLEUSERILESERTYRTYR
5   ASNASNGLULYSGLUMETTYRSERLYSGLY
6   ILEILEPROLEUSERALAILESERTHRVAL
7   ARGVALGLNGLYASPASNLYSPHEGLUVAL
8   VALTHRTHRGLNARGTHRPHEVALPHEARG
9   VALGLULYSGLUGLUGLUARGASNASPTRP
10   ILESERILELEULEUASNALALEULYSSER
11   GLNSERLEUTHRSERGLNSERGLNALASER
12   GLYPROSERSERGLY

Samples:

sample_1: PH domain, [U-13C; U-15N], 0.62 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 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 v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA25506 BAG10357
GB AAI50259 AAI60097 AAL12170 EAW92870 EAW92872
REF NP_056045 XP_001090397 XP_001135477 XP_003832197 XP_003898614
SP Q8WZ64