BMRB Entry 34395

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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/BMR34395
MolProbity Validation Chart

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Title:
Solution structure and 1H, 13C and 15N chemical shift assignments for the complex of NECAP1 PHear domain with phosphorylated AP2 mu2 148-163
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.
entity_2, polymer, 15 residues, 1798.892 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSPNSMATELEYESVLCVKP DVSVYRIPPRASNRGYRASD WKLDQPDWTGRLRITSKGKT AYIKLEDKVSGELFAQAPVE QYPGIAVETVTDSSRYFVIR IQDGTGRSAFIGIGFTDRGD AFDFNVSLQDHFKWVKQE
entity_2: SQITSQVXGQIGWRR

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts140
1H chemical shifts1040

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

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

Entity 2, entity_2 15 residues - 1798.892 Da.

1   SERGLNILETHRSERGLNVALTPOGLYGLN
2   ILEGLYTRPARGARG

Samples:

sample_1: NECAP1 1-133, [U-98% 13C; U-98% 15N], 0.5 mM; AP2 mu2 148-163 0.5 mM; sodium acetate, [U-2H], 70 mM

sample_2: NECAP1, [U-98% 13C; U-98% 15N], 0.5 mM; AP2 mu2 148-163, [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-1H NOESY (reject 15N,13C coupled 1H in F1, accept 15N,13C coupled 1H in F2) tau(m) 150mssample_1isotropicsample_conditions_1
2D 1H-1H NOESY (reject 15N,13C coupled 1H in F1 and F2) tau(m) 150mssample_1isotropicsample_conditions_1
2D 1H-1H TOCSY (reject 15N,13C coupled 1H in F2)sample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic (constant time)sample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromatic (constant time)sample_2isotropicsample_conditions_1
2D 1H-1H NOESY (reject 15N,13C coupled 1H in F1, accept 13C coupled 1H in F2) tau(m) 150mssample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSY (1H,13C,1H)sample_2isotropicsample_conditions_1
3D HCCH-TOCSY (13C,13C,1H)sample_2isotropicsample_conditions_1
3D 1H-15N NOESY tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic tau(m) 150mssample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromatic tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromatic tau(m) 150mssample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic (reject 15N,13C coupled 1H in F1) tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic (reject 15N,13C coupled 1H in F1) tau(m) 150mssample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromatic (reject 15N,13C coupled 1H in F1) tau(m) 150mssample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromatic (reject 15N,13C coupled 1H in F1) tau(m) 150mssample_2isotropicsample_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