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 27135

Title: Backbone 1H, 15N and 13C assignments of the Sec63 unit of human Brr2   PubMed: 28838205

Deposition date: 2017-06-12 Original release date: 2017-06-14

Authors: Henning, Lisa; Sticht, Jana; Freund, Christian

Citation: Henning, Lisa; Santos, Karine; Sticht, Jana; Jehle, Stefanie; Lee, Chung-Tien; Wittwer, Malte; Urlaub, Henning; Stelzl, Ulrich; Wahl, Markus; Freund, Christian. "A new role for FBP21 as regulator of Brr2 helicase activity."  Nucleic Acids Res. 45, 7922-7937 (2017).

Assembly members:
Brr2_C-terminal_Sec63_unit, polymer, 305 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Brr2_C-terminal_Sec63_unit: GPLGSPEFTKVRGLIEIISN AAEYENIPIRHHEDNLLRQL AQKVPHKLNNPKFNDPHVKT NLLLQAHLSRMQLSAELQSD TEEILSKAIRLIQACVDVLS SNGWLSPALAAMELAQMVTQ AMWSKDSYLKQLPHFTSEHI KRCTDKGVESVFDIMEMEDE ERNALLQLTDSQIADVARFC NRYPNIELSYEVVDKDSIRS GGPVVVLVQLEREEEVTGPV IAPLFPQKREEGWWVVIGDA KSNSLISIKRLTLQQKAKVK LDFVAPATGAHNYTLYFMSD AYMGCDQEYKFSVDVKEAET DSDSD

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts231
1H chemical shifts231

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sec631

Entities:

Entity 1, Sec63 305 residues - Formula weight is not available

Residues 1-8 represent a non-native linker that was used for affinity purification; Residues 9-305 represent the C-terminal Sec63 unit of Brr2, including the Helical Bundle, the helix-loop-helix and the immunoglobulin-like domain.

1   GLYPROLEUGLYSERPROGLUPHETHRLYS
2   VALARGGLYLEUILEGLUILEILESERASN
3   ALAALAGLUTYRGLUASNILEPROILEARG
4   HISHISGLUASPASNLEULEUARGGLNLEU
5   ALAGLNLYSVALPROHISLYSLEUASNASN
6   PROLYSPHEASNASPPROHISVALLYSTHR
7   ASNLEULEULEUGLNALAHISLEUSERARG
8   METGLNLEUSERALAGLULEUGLNSERASP
9   THRGLUGLUILELEUSERLYSALAILEARG
10   LEUILEGLNALACYSVALASPVALLEUSER
11   SERASNGLYTRPLEUSERPROALALEUALA
12   ALAMETGLULEUALAGLNMETVALTHRGLN
13   ALAMETTRPSERLYSASPSERTYRLEULYS
14   GLNLEUPROHISPHETHRSERGLUHISILE
15   LYSARGCYSTHRASPLYSGLYVALGLUSER
16   VALPHEASPILEMETGLUMETGLUASPGLU
17   GLUARGASNALALEULEUGLNLEUTHRASP
18   SERGLNILEALAASPVALALAARGPHECYS
19   ASNARGTYRPROASNILEGLULEUSERTYR
20   GLUVALVALASPLYSASPSERILEARGSER
21   GLYGLYPROVALVALVALLEUVALGLNLEU
22   GLUARGGLUGLUGLUVALTHRGLYPROVAL
23   ILEALAPROLEUPHEPROGLNLYSARGGLU
24   GLUGLYTRPTRPVALVALILEGLYASPALA
25   LYSSERASNSERLEUILESERILELYSARG
26   LEUTHRLEUGLNGLNLYSALALYSVALLYS
27   LEUASPPHEVALALAPROALATHRGLYALA
28   HISASNTYRTHRLEUTYRPHEMETSERASP
29   ALATYRMETGLYCYSASPGLNGLUTYRLYS
30   PHESERVALASPVALLYSGLUALAGLUTHR
31   ASPSERASPSERASP

Samples:

sample_Val: Brr2 C-terminal Sec63 unit, [U-15N]-Val, 130 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Ile: Brr2 C-terminal Sec63 unit, [U-15N]-Ile, 100 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Trp-Phe: Brr2 C-terminal Sec63 unit, [U-15N]-Trp, [U-15N]-Phe, 130 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Tyr-Phe: Brr2 C-terminal Sec63 unit, [U-15N]-Tyr, [U-15N]-Phe, 530 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Gly: Brr2 C-terminal Sec63 unit, [U-15N]-Gly, 100 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_1: Brr2 C-terminal Sec63 unit, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2-0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Leu: Brr2 C-terminal Sec63 unit, [U-15N]-Leu, 480 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_Ala: Brr2 C-terminal Sec63 unit, [U-15N]-Ala, 140 uM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_Leuisotropicsample_conditions_1
2D 1H-15N HSQCsample_Alaisotropicsample_conditions_1
2D 1H-15N HSQCsample_Valisotropicsample_conditions_1
2D 1H-15N HSQCsample_Ileisotropicsample_conditions_1
2D 1H-15N HSQCsample_Trp-Pheisotropicsample_conditions_1
2D 1H-15N HSQCsample_Tyr-Pheisotropicsample_conditions_1
2D 1H-15N HSQCsample_Glyisotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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