BMRB Entry 53480

Title:
Resonance assignment and dynamics of the S97L mutant Homer1 EVH1 domain
Deposition date:
2025-12-11
Original release date:
2026-06-06
Authors:
Fanni, F.; Batta, G.; Peterfia, B.; Gaspari, Z.
Citation:

Citation: Fanni, F.; Maruzs, B.; Kalman, Z.; Klumpler, T.; Batta, G.; Peterfia, B.; Gaspari, Z.. "Modulation of Homer1 EVH1 domain internal dynamics by putative autism-associated mutations"  FEBS Lett. ., .-. (2026).
PubMed: 42206738

Assembly members:

Assembly members:
entity_1, polymer, 121 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-15b

Data sets:
Data typeCount
13C chemical shifts404
15N chemical shifts103
1H chemical shifts462
T1 relaxation values85
T2 relaxation values84
heteronuclear NOE values79
order parameters81

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Homer protein homolog 1 S97L mutant1

Entities:

Entity 1, Homer protein homolog 1 S97L mutant 121 residues - Formula weight is not available

The sequence contains an expression tag (GSH) not part of the natural protein.

1   GLYSERHISMETGLYGLUGLNPROILEPHE
2   SERTHRARGALAHISVALPHEGLNILEASP
3   PROASNTHRLYSLYSASNTRPVALPROTHR
4   SERLYSHISALAVALTHRVALSERTYRPHE
5   TYRASPSERTHRARGASNVALTYRARGILE
6   ILESERLEUASPGLYSERLYSALAILEILE
7   ASNSERTHRILETHRPROASNMETTHRPHE
8   THRLYSTHRSERGLNLYSPHEGLYGLNTRP
9   ALAASPSERARGALAASNTHRVALTYRGLY
10   LEUGLYPHESERSERGLUHISHISLEULEU
11   LYSPHEALAGLULYSPHEGLNGLUPHELYS
12   GLUALAALAARGLEUALALYSGLULYSSER
13   GLN

Samples:

sample_1: Homer1 EVH1 S97L mutant, [U-13C; U-15N], 560 uM; Sodium phosphate buffer 50 mM; sodium chloride 20 mM; NaN3 0.02%

sample_2: Homer1 EVH1 S97L mutant, [U-15N], 228 uM; Sodium phosphate buffer 50 mM; sodium chloride 20 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 215 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
T1/R1 relaxationsample_2isotropicsample_conditions_1
T2/R2 relaxationsample_2isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.5.2 - peak picking

NMRFAM-SPARKY v1.413 - data analysis

Tensor v2 - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz

Related Database Links:

SP Q9Z2Y3

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