BMRB Entry 34394

Title:
Solution structure and 1H, 13C and 15N chemical shift assignments for NECAP1 PHear domain
Deposition date:
2019-04-18
Original release date:
2019-10-22
Authors:
Owen, D.; Neuhaus, D.; Yang, J.; Herrmann, T.
Citation:

Citation: Wrobel, A.; Kadlecova, Z.; Kamenicky, J.; Yang, J.; Herrmann, T.; Kelly, B.; McCoy, A.; Evans, P.; Martin, S.; Muller, S.; Sroubek, F.; Neuhaus, D.; Honing, S.; Owen, D.. "Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation."  Dev. Cell 50, 494-508 (2019).
PubMed: 31430451

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 15562.371 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

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts140
1H chemical shifts955

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 138 residues - 15562.371 Da.

1   GLYSERPROASNSERMETALATHRGLULEU
2   GLUTYRGLUSERVALLEUCYSVALLYSPRO
3   ASPVALSERVALTYRARGILEPROPROARG
4   ALASERASNARGGLYTYRARGALASERASP
5   TRPLYSLEUASPGLNPROASPTRPTHRGLY
6   ARGLEUARGILETHRSERLYSGLYLYSTHR
7   ALATYRILELYSLEUGLUASPLYSVALSER
8   GLYGLULEUPHEALAGLNALAPROVALGLU
9   GLNTYRPROGLYILEALAVALGLUTHRVAL
10   THRASPSERSERARGTYRPHEVALILEARG
11   ILEGLNASPGLYTHRGLYARGSERALAPHE
12   ILEGLYILEGLYPHETHRASPARGGLYASP
13   ALAPHEASPPHEASNVALSERLEUGLNASP
14   HISPHELYSTRPVALLYSGLNGLU

Samples:

sample_1: NECAP1 1-133, [U-98% 13C; U-98% 15N], 0.5 mM; sodium acetate, [U-2H], 70 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic (constant time)sample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromatic (constant time)sample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromatic tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-15N NOESY tau(m) 150mssample_1isotropicsample_conditions_1
3D HCCH-TOCSY (13C,13C,1H)sample_1isotropicsample_conditions_1
3D HCCH-COSY (1H,13C,1H)sample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment

Sparky v3.115, Goddard - chemical shift assignment

UNIO v2.8.1, Herrmann - structure calculation

Xplor-NIH v2.28, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Amber v11, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - structure calculation

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE 600 MHz
  • Bruker AVANCE III 800 MHz

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