BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16285

Title: Solution structure of a PDZ protein

Deposition date: 2009-05-07 Original release date: 2012-08-06

Authors: Durney, Michael; Anklin, Clemens; Soni, Aditi; Birrane, Gabriel; Ladias, John

Citation: Durney, Michael. "Solution structure of a PDZ domain protein"  .

Assembly members:
TIP-1, polymer, 124 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: recombinant technology   Host organism: Escherichia coli   Vector: pHMTH

Entity Sequences (FASTA):
TIP-1: GSYIPGQPVTAVVQRVEIHK LRQGENLILGFSIGGGIDQD PSQNPFSEDKTDKGIYVTRV SEGGPAEIAGLQIGDKIMQV NGWDMTMVTHDQARKRLTKR SEEVVRLLVTRQSLQKAVQQ SMLS

Data sets:
Data typeCount
13C chemical shifts432
15N chemical shifts120
1H chemical shifts688

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TIP-11

Entities:

Entity 1, TIP-1 124 residues - Formula weight is not available

1   GLYSERTYRILEPROGLYGLNPROVALTHR
2   ALAVALVALGLNARGVALGLUILEHISLYS
3   LEUARGGLNGLYGLUASNLEUILELEUGLY
4   PHESERILEGLYGLYGLYILEASPGLNASP
5   PROSERGLNASNPROPHESERGLUASPLYS
6   THRASPLYSGLYILETYRVALTHRARGVAL
7   SERGLUGLYGLYPROALAGLUILEALAGLY
8   LEUGLNILEGLYASPLYSILEMETGLNVAL
9   ASNGLYTRPASPMETTHRMETVALTHRHIS
10   ASPGLNALAARGLYSARGLEUTHRLYSARG
11   SERGLUGLUVALVALARGLEULEUVALTHR
12   ARGGLNSERLEUGLNLYSALAVALGLNGLN
13   SERMETLEUSER

Samples:

sample_1: TIP-1, [U-100% 13C; U-100% 15N], 1-2 ± 0.25 mM; sodium phosphate 50 mM; NaCl 50 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker DMX 700 MHz
  • Bruker DMX 600 MHz

Related Database Links:

BMRB 17254 17255
PDB
DBJ BAB23703 BAE29879 BAE40411 BAE41827 BAE89417
GB AAB84248 AAF43104 AAG44368 AAH08166 AAH23980
REF NP_001029646 NP_001244463 NP_001272005 NP_055419 NP_083840
SP O14907 Q9DBG9
TPG DAA18859
AlphaFold O14907 Q9DBG9

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