BMRB Entry 34161

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34161
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of the complex of TRPV5(655-725) with a Calmodulin E32Q/E68Q double mutant
Deposition date:
2017-07-09
Original release date:
2018-04-20
Authors:
Vuister, G.; Bokhovchuk, F.; Bate, N.; Kovalevskaya, N.; Goult, B.; Spronk, C.
Citation:

Citation: Bokhovchuk, F.; Bate, N.; Kovalevskaya, N.; Goult, B.; Spronk, C.; Vuister, G.. "The Structural Basis of Calcium Dependent Inactivation of the Transient Receptor Potential Vanilloid 5 Channel."  Biochemistry 57, 2623-2635 (2018).
PubMed: 29584409

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, 16937.652 Da.
entity_2, polymer, 73 residues, 7722.194 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMADQLTEEQIAEFKEAFSL FDKDGDGTITTKQLGTVMRS LGQNPTEAELQDMINEVDAD GNGTIDFPQFLTMMARKMKD TDSEEEIREAFRVFDKDGNG YISAAELRHVMTNLGEKLTD EEVDEMIREADIDGDGQVNY EEFVQMMTAK
entity_2: GADKEDDQEHPSEKQPSGAE SGTLARASLALPTSSLSRTA SQSSSHRGWEILRQNTLGHL NLGLNLSEGDGEE

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts181
1H chemical shifts1103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23

Entities:

Entity 1, entity_1 150 residues - 16937.652 Da.

1   SERMETALAASPGLNLEUTHRGLUGLUGLN
2   ILEALAGLUPHELYSGLUALAPHESERLEU
3   PHEASPLYSASPGLYASPGLYTHRILETHR
4   THRLYSGLNLEUGLYTHRVALMETARGSER
5   LEUGLYGLNASNPROTHRGLUALAGLULEU
6   GLNASPMETILEASNGLUVALASPALAASP
7   GLYASNGLYTHRILEASPPHEPROGLNPHE
8   LEUTHRMETMETALAARGLYSMETLYSASP
9   THRASPSERGLUGLUGLUILEARGGLUALA
10   PHEARGVALPHEASPLYSASPGLYASNGLY
11   TYRILESERALAALAGLULEUARGHISVAL
12   METTHRASNLEUGLYGLULYSLEUTHRASP
13   GLUGLUVALASPGLUMETILEARGGLUALA
14   ASPILEASPGLYASPGLYGLNVALASNTYR
15   GLUGLUPHEVALGLNMETMETTHRALALYS

Entity 2, entity_2 73 residues - 7722.194 Da.

1   GLYALAASPLYSGLUASPASPGLNGLUHIS
2   PROSERGLULYSGLNPROSERGLYALAGLU
3   SERGLYTHRLEUALAARGALASERLEUALA
4   LEUPROTHRSERSERLEUSERARGTHRALA
5   SERGLNSERSERSERHISARGGLYTRPGLU
6   ILELEUARGGLNASNTHRLEUGLYHISLEU
7   ASNLEUGLYLEUASNLEUSERGLUGLYASP
8   GLYGLUGLU

Entity 3, entity_3, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 220 ± 0.05 uM; hTRPV5(655-725) 220 ± 0.05 uM

sample_2: Calmodulin, [U-99% 15N], 380 ± 0.05 uM; hTRPV5(655-725), [U-99% 13C; U-99% 15N], 380 ± 0.05 uM

sample_conditions_1: ionic strength: 84 mM; pH: 7.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

Analysis v2.4, CCPN - chemical shift assignment, peak picking

AnalysisAssign v3.0, CCPN - chemical shift assignment

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA v15.6, Yasara Biosciences; Krieger et al. - refinement

NMRPipe v7.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

NMR spectrometers:

  • Bruker AVI 500 MHz
  • Bruker AVIII 600 MHz
  • Bruker AVII 800 MHz

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