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 19477

Title: Backbone 1H and 15N Chemical Shift Assignments for P130 Cas substrate domain   PubMed: 24052412

Deposition date: 2013-09-05 Original release date: 2014-02-12

Authors: Liu, Xiao

Citation: Liu, Xiao; Yang, Daiwen. "HN(CA)N and HN(COCA)N experiments for assignment of large disordered proteins."  J. Biomol. NMR 57, 83-89 (2013).

Assembly members:
P130Cas_substrate_domian, polymer, 306 residues, Formula weight is not available

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
P130Cas_substrate_domian: PDNVYLVPTPSKTQQGLYQA PGPNPQFQSPPAKQTSTFSK QTPHHSFPSPATDLYQVPPG PGSPAQDIYQVPPSAGTGHD IYQVPPSLDTRSWEGTKPPA KVVVPTRVGQGYVYEASQAE QDEYDTPRHLLAPGSQDIYD VPPVRGLLPNQYGQEVYDTP PMAVKGPNGRDPLLDVYDVP PSVEKGLPPSNHHSVYDVPP SVSKDVPDGPLLREETYDVP PAFAKPKPFDPTRHPLILAA PPPDSPPAEDVYDVPPPAPD LYDVPPGLRRPGPGTLYDVP RERVLPPEVADGSVIDDGVY AVPPPA

Data sets:
Data typeCount
15N chemical shifts238
1H chemical shifts238

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P130Cas SD, chain 11
2P130Cas SD, chain 21

Entities:

Entity 1, P130Cas SD, chain 1 306 residues - Formula weight is not available

1   PROASPASNVALTYRLEUVALPROTHRPRO
2   SERLYSTHRGLNGLNGLYLEUTYRGLNALA
3   PROGLYPROASNPROGLNPHEGLNSERPRO
4   PROALALYSGLNTHRSERTHRPHESERLYS
5   GLNTHRPROHISHISSERPHEPROSERPRO
6   ALATHRASPLEUTYRGLNVALPROPROGLY
7   PROGLYSERPROALAGLNASPILETYRGLN
8   VALPROPROSERALAGLYTHRGLYHISASP
9   ILETYRGLNVALPROPROSERLEUASPTHR
10   ARGSERTRPGLUGLYTHRLYSPROPROALA
11   LYSVALVALVALPROTHRARGVALGLYGLN
12   GLYTYRVALTYRGLUALASERGLNALAGLU
13   GLNASPGLUTYRASPTHRPROARGHISLEU
14   LEUALAPROGLYSERGLNASPILETYRASP
15   VALPROPROVALARGGLYLEULEUPROASN
16   GLNTYRGLYGLNGLUVALTYRASPTHRPRO
17   PROMETALAVALLYSGLYPROASNGLYARG
18   ASPPROLEULEUASPVALTYRASPVALPRO
19   PROSERVALGLULYSGLYLEUPROPROSER
20   ASNHISHISSERVALTYRASPVALPROPRO
21   SERVALSERLYSASPVALPROASPGLYPRO
22   LEULEUARGGLUGLUTHRTYRASPVALPRO
23   PROALAPHEALALYSPROLYSPROPHEASP
24   PROTHRARGHISPROLEUILELEUALAALA
25   PROPROPROASPSERPROPROALAGLUASP
26   VALTYRASPVALPROPROPROALAPROASP
27   LEUTYRASPVALPROPROGLYLEUARGARG
28   PROGLYPROGLYTHRLEUTYRASPVALPRO
29   ARGGLUARGVALLEUPROPROGLUVALALA
30   ASPGLYSERVALILEASPASPGLYVALTYR
31   ALAVALPROPROPROALA

Samples:

P130CasSD_1: P130Cas substrate domian, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCP130CasSD_1isotropicsample_conditions_1
3D HN(CA)NP130CasSD_1isotropicsample_conditions_1
3D HN(COCA)NP130CasSD_1isotropicsample_conditions_1

Software:

NMRspy, Zheng, Liu and Yang - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

DBJ BAA06169 BAA06170
GB EDL92583 EDL92584 EDL92585
REF NP_037063 XP_006255690 XP_006255691
SP Q63767

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