BMRB Entry 27821

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments of ITSN1 SH3D20_L
Deposition date:
2019-03-04
Original release date:
2019-03-15
Authors:
Gerth, Fabian; Jaepel, Maria; Sticht, Jana; Schmitt, Xiao; Kuropka, Benno; Driller, Jan; Loll, Bernhard; Wahl, Markus; Pagel, Kevin; Haucke, Volker; Freund, Christian
Citation:

Citation: Gerth, Fabian; Jaepel, Maria; Sticht, Jana; Schmitt, Xiao; Kuropka, Benno; Driller, Jan; Loll, Bernhard; Wahl, Markus; Pagel, Kevin; Haucke, Volker; Freund, Christian. "Exon Inclusion Modulates Conformational Plasticity and Autoinhibition of the Intersectin 1 SH3A Domain."  Structure 27, 977-987 (2019).
PubMed: 31031201

Assembly members:

Assembly members:
ITSN1_SH3AD20-L, polymer, 95 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: pET28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts59
15N chemical shifts54
1H chemical shifts54

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3AD20-L1

Entities:

Entity 1, SH3AD20-L 95 residues - Formula weight is not available

This is the short splice isoform of the SH3A domain (SH3AD20) with C-terminal extension, residues GSHM at the N-terminus are non-native.

1   GLYSERHISMETLYSVALVALTYRTYRARG
2   ALALEUTYRPROPHEGLUSERARGSERHIS
3   ASPGLUILETHRILEGLNPROGLYASPILE
4   VALMETVALASPGLUSERGLNTHRGLYGLU
5   PROGLYTRPLEUGLYGLYGLULEULYSGLY
6   LYSTHRGLYTRPPHEPROALAASNTYRALA
7   GLULYSILEPROGLUASNGLUVALPROALA
8   PROVALLYSPROVALTHRASPSERTHRSER
9   ALAPROALAPROLYSLEUALALEUARGGLU
10   THRPROALAPROLEU

Samples:

sample_1: ITSN1 SH3AD20-L, [U-100% 13C; U-100% 15N], 400 uM; NaCl 50 mM

all_samples_conditions: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicall_samples_conditions
3D HNCAsample_1isotropicall_samples_conditions
3D HN(CO)CAsample_1isotropicall_samples_conditions

Software:

CcpNMR_Analysis, CCPN - chemical shift assignment

TOPSPIN v3, Bruker - collection, processing, refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP Q15811-3
AlphaFold Q9UQ92

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