BMRB Entry 15481

Title:
15N and 1HN assignments of the EVH1 domain of human HOMER3A
Deposition date:
2007-09-20
Original release date:
2007-09-27
Authors:
Higman, Victoria; Schmieder, Peter; Diehl, Anne; Bishop, Shurene; Oschkinat, Hartmut; Arrowsmith, Cheryl; Wiegelt, Johan; Edwards, Aled; Sundstrom, Michael; Ball, Linda
Citation:

Citation: Higman, Victoria; Schmieder, Peter; Bishop, Shurene; Diehl, Anne; Oschkinat, Hartmut; Arrowsmith, Cheryl; Edwards, Aled; Sundstrom, Michael; Wiegelt, Johan; Ball, Linda. "15N and 1HN assignments of the EVH1 domain of human HOMER3A"  Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
HOMER3A_EVH1_domain, polymer, 117 residues, Formula weight is not available

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   Vector: pNIC28-Bsa4

Data sets:
Data typeCount
15N chemical shifts114
1H chemical shifts114
T1 relaxation values91
T2 relaxation values91

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HOMER3A EVH1 domain1

Entities:

Entity 1, HOMER3A EVH1 domain 117 residues - Formula weight is not available

The first two residues (SM) are from the vector.

1   SERMETALAARGGLUGLNPROILEPHESER
2   THRARGALAHISVALPHEGLNILEASPPRO
3   ALATHRLYSARGASNTRPILEPROALAGLY
4   LYSHISALALEUTHRVALSERTYRPHETYR
5   ASPALATHRARGASNVALTYRARGILEILE
6   SERILEGLYGLYALALYSALAILEILEASN
7   SERTHRVALTHRPROASNMETTHRPHETHR
8   LYSTHRSERGLNLYSPHEGLYGLNTRPALA
9   ASPSERARGALAASNTHRVALTYRGLYLEU
10   GLYPHEALASERGLUGLNHISLEUTHRGLN
11   PHEALAGLULYSPHEGLNGLUVALLYSGLU
12   ALAALAARGLEUALAARGGLU

Samples:

sample_1: HOMER3A EVH1 domain, [U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.15 mM; DTT 1 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 297 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC - T1 seriessample_1isotropicsample_conditions_1
2D 1H-15N HSQC - T2 seriessample_1isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

TOPSPIN v1.3, Bruker Biospin - processing

ANALYSIS v1.0.15, CCPNMR - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

SWS Q9NSC5
PDB
NCBI gi:21361157
DBJ BAA35110 BAG36707 BAG54040
EMBL CAB75536 CAB75543 CAB75544 CAB75545 CAC35223
GB AAB81545 AAC71025 AAC71029 AAH05773 AAH12113
REF NP_001139193 NP_001139194 NP_001139196 NP_001139625 NP_001244618
SP Q99JP6 Q9NSC5 Q9Z2X5
AlphaFold Q9Z2X5 Q99JP6 Q9NSC5

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