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 30518

Title: Lim5 domain of PINCH1 protein

Deposition date: 2018-09-19 Original release date: 2018-10-26

Authors: Qin, J.; Vaynberg, J.

Citation: Qin, J.; Vaynberg, J.. "Lim5 domain of PINCH1 protein"  . ., .-..

Assembly members:
entity_1, polymer, 79 residues, 8994.751 Da.
entity_ZN, non-polymer, 65.409 Da.

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

Entity Sequences (FASTA):
entity_1: GSGDVCFHCNRVIEGDVVSA LNKAWCVNCFACSTCNTKLT LKNKFVEFDMKPVCKKCYEK FPLELKKRLKKLAETLGRK

Data sets:
Data typeCount
13C chemical shifts240
15N chemical shifts76
1H chemical shifts481

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 79 residues - 8994.751 Da.

1   GLYSERGLYASPVALCYSPHEHISCYSASN
2   ARGVALILEGLUGLYASPVALVALSERALA
3   LEUASNLYSALATRPCYSVALASNCYSPHE
4   ALACYSSERTHRCYSASNTHRLYSLEUTHR
5   LEULYSASNLYSPHEVALGLUPHEASPMET
6   LYSPROVALCYSLYSLYSCYSTYRGLULYS
7   PHEPROLEUGLULEULYSLYSARGLEULYS
8   LYSLEUALAGLUTHRLEUGLYARGLYS

Entity 2, entity_2, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Lim5-T, [U-15N], 0.5 mM; NaCl 20 mM

sample_2: 15N 13C Lim5-T, [U-13C; U-15N], 1.0 mM; NaCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

PIPP, Garrett - peak picking

xwinnmr, Bruker Biospin - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

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