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 30388

Title: Solution NMR structure of cysteine-rich calcium bound domains of very low density lipoprotein receptor

Deposition date: 2017-12-21 Original release date: 2018-07-10

Authors: Banerjee, K.; Gruschus, J.; Tjandra, N.; Yakovlev, S.; Medved, L.

Citation: Banerjee, K.; Gruschus, J.; Tjandra, N.; Yakovlev, S.; Medved, L.. "Solution NMR structure of cysteine-rich calcium bound domains of very low density lipoprotein receptor"  To be Published ., .-..

Assembly members:
entity_1, polymer, 121 residues, 13175.093 Da.
entity_CA, non-polymer, 40.078 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: KTCAESDFVCNNGQCVPSRW KCDGDPDCEDGSDESPEQCH MRTCRIHEISCGAHSTQCIP VSWRCDGENDCDSGEDEENC GNITCSPDEFTCSSGRCISR NFVCNGQDDCSDGSDELDCA P

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts125
1H chemical shifts647

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22
4entity_2, 32

Entities:

Entity 1, entity_1 121 residues - 13175.093 Da.

1   LYSTHRCYSALAGLUSERASPPHEVALCYS
2   ASNASNGLYGLNCYSVALPROSERARGTRP
3   LYSCYSASPGLYASPPROASPCYSGLUASP
4   GLYSERASPGLUSERPROGLUGLNCYSHIS
5   METARGTHRCYSARGILEHISGLUILESER
6   CYSGLYALAHISSERTHRGLNCYSILEPRO
7   VALSERTRPARGCYSASPGLYGLUASNASP
8   CYSASPSERGLYGLUASPGLUGLUASNCYS
9   GLYASNILETHRCYSSERPROASPGLUPHE
10   THRCYSSERSERGLYARGCYSILESERARG
11   ASNPHEVALCYSASNGLYGLNASPASPCYS
12   SERASPGLYSERASPGLULEUASPCYSALA
13   PRO

Entity 2, entity_2, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: VLDLR, [U-99% 15N], 350 uM

sample_2: VLDLR, [U-99% 13C; U-99% 15N], 250 uM

sample_3: VLDLR, [U-99% 13C; U-99% 15N], 250 uM

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 760 mmHg; temperature: 306.5 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.2; pressure: 760 mmHg; temperature: 306.5 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis, CCPN - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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