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 25008

Title: Phosphotyrosine binding domain

Deposition date: 2014-06-11 Original release date: 2014-08-04

Authors: Mukherjee, Manjeet; Jing-Song, Fan; Sivaraman, Jayaraman

Citation: Mukherjee, Manjeet; Jing-Song, Fan; Sivaraman, Jayaraman. "Dimeric switch of Hakai-truncated monomers during substrate recognition: insights from solution studies and NMR Structure"  .

Assembly members:
entity_1, polymer, 89 residues, 10219.175 Da.
ZINC ION, non-polymer, 65.409 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6P-1

Entity Sequences (FASTA):
entity_1: VHFCDKCGLPIKVYGRMIPC KHVFCYDCAILHEKKGDKMC PGCSDPVQRIEQCTRGSLFM CSIVQGCKRTYLSQRDLQAH INHRHMRAG

Data sets:
Data typeCount
1H chemical shifts540
13C chemical shifts63
15N chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2ZINC ION_12
3ZINC ION_22
4ZINC ION_32

Entities:

Entity 1, entity_1 89 residues - 10219.175 Da.

1   VALHISPHECYSASPLYSCYSGLYLEUPRO
2   ILELYSVALTYRGLYARGMETILEPROCYS
3   LYSHISVALPHECYSTYRASPCYSALAILE
4   LEUHISGLULYSLYSGLYASPLYSMETCYS
5   PROGLYCYSSERASPPROVALGLNARGILE
6   GLUGLNCYSTHRARGGLYSERLEUPHEMET
7   CYSSERILEVALGLNGLYCYSLYSARGTHR
8   TYRLEUSERGLNARGASPLEUGLNALAHIS
9   ILEASNHISARGHISMETARGALAGLY

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; DTT 5 mM; D2O 5%; H2O 95%; potassium phosphate 50 mM

sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 0.05 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution, refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB15544 BAC33568 BAE00934 BAE01180 BAE38522
GB AAF89617 AAH19529 AAH27460 AAI30530 AAI30532
REF NP_001101488 NP_001179521 NP_001240776 NP_001240777 NP_001247656
SP Q4R7I8 Q75N03 Q9JIY2
TPG DAA30631
AlphaFold Q75N03 Q4R7I8 Q9JIY2

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