BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18982

Title: Transcriptional regulatory protein   PubMed: 24155902

Deposition date: 2013-01-28 Original release date: 2013-12-09

Authors: de Chiara, Cesira; Kelly, Geoff; Pastore, Annalisa

Citation: de Chiara, Cesira; Menon, Rajesh; Kelly, Geoff; Pastore, Annalisa. "Protein-Protein Interactions as a Strategy towards Protein-Specific Drug Design: The Example of Ataxin-1"  PLoS One 8, e76456-e76456 (2013).

Assembly members:
CIC_polypeptide, polymer, 15 residues, 1726.026 Da.
Ataxin-1_AXH, polymer, 126 residues, 13517.461 Da.

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: chemical synthesis   Host organism: Escherichia coli

Entity Sequences (FASTA):
CIC_polypeptide: VFPWHSLVPFLAPSQ
Ataxin-1_AXH: GAMAPPTLPPYFMKGSIIQL ANGELKKVEDLKTEDFIQSA EISNDLKIDSSTVERIEDSH SPGVAVIQFAVGEHRAQVSV EVLVEYPFFVFGQGWSSCCP ERTSQLFDLPCSKLSVGDVC ISLTLK

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts124
1H chemical shifts906

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CIC_polypeptide1
2Ataxin-1_AXH2

Entities:

Entity 1, CIC_polypeptide 15 residues - 1726.026 Da.

1   VALPHEPROTRPHISSERLEUVALPROPHE
2   LEUALAPROSERGLN

Entity 2, Ataxin-1_AXH 126 residues - 13517.461 Da.

1   GLYALAMETALAPROPROTHRLEUPROPRO
2   TYRPHEMETLYSGLYSERILEILEGLNLEU
3   ALAASNGLYGLULEULYSLYSVALGLUASP
4   LEULYSTHRGLUASPPHEILEGLNSERALA
5   GLUILESERASNASPLEULYSILEASPSER
6   SERTHRVALGLUARGILEGLUASPSERHIS
7   SERPROGLYVALALAVALILEGLNPHEALA
8   VALGLYGLUHISARGALAGLNVALSERVAL
9   GLUVALLEUVALGLUTYRPROPHEPHEVAL
10   PHEGLYGLNGLYTRPSERSERCYSCYSPRO
11   GLUARGTHRSERGLNLEUPHEASPLEUPRO
12   CYSSERLYSLEUSERVALGLYASPVALCYS
13   ILESERLEUTHRLEULYS

Samples:

sample_1: Ataxin-1 AXH domain, [U-100% 13C; U-100% 15N], 0.5 mM; CIC polypeptide 0.6 mM; H2O 90 mM; D2O 10 mM

sample_2: Ataxin-1 AXH domain, [U-100% 15N], 0.5 mM; CIC polypeptide 0.6 mM; H2O 90 mM; D2O 10 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 15N-13C-filtered, 15N-13C-edited NOESYsample_1isotropicsample_conditions_1
2D 15N-13C-rejected NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O, . - automated NOEs assignment, refinement, structure solution

XEASY, Bartels et al. - data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP Q96RK0 P54253
PDB
DBJ BAE27813 BAE27978 BAI45609 BAP18650 BAC33290
GB AAI40444 AAI52805 AAK73515 AAK73516 ABD61704 AAH58178 AAI17126 ADR83271 AIC49678 EAW55372
REF NP_001289740 NP_001291744 NP_055940 NP_082158 XP_001153776 NP_000323 NP_001121636 NP_001186233 NP_033150 NP_036858
SP Q924A2 Q96RK0 P54253 P54254 Q63540
EMBL CAA55793 CAA58533 CAA62822
PRF 2210312A

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts