BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17177

Title: Partial backbone 1H,15N chemical shift of arrestin-1   PubMed: 21050017

Deposition date: 2010-09-10 Original release date: 2010-11-19

Authors: Zhuang, Tiandi; Vishnivetskiy, Sergey; Gurevich, Vsevolod; Sanders, Charles

Citation: Zhuang, Tiandi; Vishnivetskiy, Sergey; Gurevich, Vsevolod; Sanders, Charles. "Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance."  Biochemistry 49, 10473-10485 (2010).

Assembly members:
arrestin-1, polymer, 404 residues, Formula weight is not available

Natural source:   Common Name: cattle   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
arrestin-1: MKANKPAPNHVIFKKISRDK SVTIYLGKRDYIDHVERVEP VDGVVLVDPELVKGKRVYVS LTCAFRYGQEDIDVMGLSFR RDLYASQVQVFPPVGASGAT TRLQESLIKKLGANTYPFLL TFPDYLPCSVMLQPAPQDVG KSCGVDFEIKAFATHSTDVE EDKIPKKSSVRLLIRKVQHA PRDMGPQPRAEASWQFAMSD KPLRLAVSLSKEIYYHGEPI PVTVAVTNSTEKTVKKIKVL VEQVTNVVLYSSDYYIKTVA AEEAQEKVPPNSSLTKTLTL VPLLANNRERRGIALDGKIK HEDTNLASSTIIKEGIDKTV MGILVSYQIKVKLTVSGLLG ELTSSEVATEVPFRLMHPQP EDPDTAKESFQDENFVFEEF ARQNLKDAGEYKEEKTDQEA AMDE

Data sets:
Data typeCount
15N chemical shifts146
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1visual arrestin1

Entities:

Entity 1, visual arrestin 404 residues - Formula weight is not available

1   METLYSALAASNLYSPROALAPROASNHIS
2   VALILEPHELYSLYSILESERARGASPLYS
3   SERVALTHRILETYRLEUGLYLYSARGASP
4   TYRILEASPHISVALGLUARGVALGLUPRO
5   VALASPGLYVALVALLEUVALASPPROGLU
6   LEUVALLYSGLYLYSARGVALTYRVALSER
7   LEUTHRCYSALAPHEARGTYRGLYGLNGLU
8   ASPILEASPVALMETGLYLEUSERPHEARG
9   ARGASPLEUTYRALASERGLNVALGLNVAL
10   PHEPROPROVALGLYALASERGLYALATHR
11   THRARGLEUGLNGLUSERLEUILELYSLYS
12   LEUGLYALAASNTHRTYRPROPHELEULEU
13   THRPHEPROASPTYRLEUPROCYSSERVAL
14   METLEUGLNPROALAPROGLNASPVALGLY
15   LYSSERCYSGLYVALASPPHEGLUILELYS
16   ALAPHEALATHRHISSERTHRASPVALGLU
17   GLUASPLYSILEPROLYSLYSSERSERVAL
18   ARGLEULEUILEARGLYSVALGLNHISALA
19   PROARGASPMETGLYPROGLNPROARGALA
20   GLUALASERTRPGLNPHEALAMETSERASP
21   LYSPROLEUARGLEUALAVALSERLEUSER
22   LYSGLUILETYRTYRHISGLYGLUPROILE
23   PROVALTHRVALALAVALTHRASNSERTHR
24   GLULYSTHRVALLYSLYSILELYSVALLEU
25   VALGLUGLNVALTHRASNVALVALLEUTYR
26   SERSERASPTYRTYRILELYSTHRVALALA
27   ALAGLUGLUALAGLNGLULYSVALPROPRO
28   ASNSERSERLEUTHRLYSTHRLEUTHRLEU
29   VALPROLEULEUALAASNASNARGGLUARG
30   ARGGLYILEALALEUASPGLYLYSILELYS
31   HISGLUASPTHRASNLEUALASERSERTHR
32   ILEILELYSGLUGLYILEASPLYSTHRVAL
33   METGLYILELEUVALSERTYRGLNILELYS
34   VALLYSLEUTHRVALSERGLYLEULEUGLY
35   GLULEUTHRSERSERGLUVALALATHRGLU
36   VALPROPHEARGLEUMETHISPROGLNPRO
37   GLUASPPROASPTHRALALYSGLUSERPHE
38   GLNASPGLUASNPHEVALPHEGLUGLUPHE
39   ALAARGGLNASNLEULYSASPALAGLYGLU
40   TYRLYSGLUGLULYSTHRASPGLNGLUALA
41   ALAMETASPGLU

Samples:

sample_1: arrestin-1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.1 – 0.5 mM; Bis-Tris 25 mM; sodium chloride 150 mM; beta-mercaptoethanol 5 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection

Sparta, Yang Shen, Ad Bax - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
EMBL CAA27179
GB AAA20465 AAA30377 AAA30378 AAB31037 ELR56916
REF NP_851343 XP_005895068 XP_005895069 XP_006041822 XP_006041824
SP P08168
TPG DAA30932

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