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 10242

Title: Solution structures of the PDZ domain of human Interleukin-16

Deposition date: 2008-10-24 Original release date: 2009-11-03

Authors: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the PDZ domain of human Interleukin-16"  .

Assembly members:
PDZ domain, polymer, 119 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   Vector: P040614-09

Entity Sequences (FASTA):
PDZ domain: GSSGSSGATLKQLDGIHVTI LHKEEGAGLGFSLAGGADLE NKVITVHRVFPNGLASQEGT IQKGNEVLSINGKSLKGTTH HDALAILRQAREPRQAVIVT RKLTPEAMPDLNSSGPSSG

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts111
1H chemical shifts747

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ domain1

Entities:

Entity 1, PDZ domain 119 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALATHRLEU
2   LYSGLNLEUASPGLYILEHISVALTHRILE
3   LEUHISLYSGLUGLUGLYALAGLYLEUGLY
4   PHESERLEUALAGLYGLYALAASPLEUGLU
5   ASNLYSVALILETHRVALHISARGVALPHE
6   PROASNGLYLEUALASERGLNGLUGLYTHR
7   ILEGLNLYSGLYASNGLUVALLEUSERILE
8   ASNGLYLYSSERLEULYSGLYTHRTHRHIS
9   HISASPALALEUALAILELEUARGGLNALA
10   ARGGLUPROARGGLNALAVALILEVALTHR
11   ARGLYSLEUTHRPROGLUALAMETPROASP
12   LEUASNSERSERGLYPROSERSERGLY

Samples:

sample_1: PDZ domain, [U-13C; U-15N], 1 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 v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB
DBJ BAG54724
GB AAH50362 ACI00236

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