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 18713

Title: The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the centromere-specific Cse4/H4 histone variant

Authors: Hong, Jingjun; Feng, Hanqiao; Zhou, Zheng; Ghirlando, Rodolfo; Bai, Yawen

Citation: Hong, Jingjun; Feng, Hanqiao; Zhou, Zheng; Ghirlando, Rodolfo; Bai, Yawen. "The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the"  J. Mol. Biol. ., .-..

Assembly members:
sC4, polymer, 121 residues, 13718.007 Da.

Natural source:   Common Name: Baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
sC4: LISKIPFARLVKEVTDEFTT KDQDLRWQSMAIMALQEASE AYLVGLLEHTNLLALHLVPR GSKRISGLIYEEVRAVLKSF LESVIRDSVTYTEHAKRKTV TSLDVVYALKRQGRTLYGFG G

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts116
1H chemical shifts843

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sC41

Entities:

Entity 1, sC4 121 residues - 13718.007 Da.

The segment LVPRGS (L57-S62 in the sequence) is a thrombin cutting site.

1   LEUILESERLYSILEPROPHEALAARGLEU
2   VALLYSGLUVALTHRASPGLUPHETHRTHR
3   LYSASPGLNASPLEUARGTRPGLNSERMET
4   ALAILEMETALALEUGLNGLUALASERGLU
5   ALATYRLEUVALGLYLEULEUGLUHISTHR
6   ASNLEULEUALALEUHISLEUVALPROARG
7   GLYSERLYSARGILESERGLYLEUILETYR
8   GLUGLUVALARGALAVALLEULYSSERPHE
9   LEUGLUSERVALILEARGASPSERVALTHR
10   TYRTHRGLUHISALALYSARGLYSTHRVAL
11   THRSERLEUASPVALVALTYRALALEULYS
12   ARGGLNGLYARGTHRLEUTYRGLYPHEGLY
13   GLY

Samples:

sample_1: sC4, [U-100% 15N], 0.8 ± 0.05 mM; sC4, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; sC4, [U-13C; U-15N; U-2H], 0.8 ± 0.05 mM; sC4, [U-13C; U-15N; U-2H], 0.8 ± 0.05 mM; H2O 90 ± 0.05 %; D2O 10 ± 0.05 %

sample_2: sC4, [U-100% 13C; U-100% 15N], 0.8 ± 0.05 mM; D2O 100 ± 0.05 %

sample_3: sC4 0.8 ± 0.05 mM; D2O 100 ± 0.05 %

sample_conditions_1: pH: 5.4; pressure: 1 atm; temperature: 308.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1

Software:

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

NMRView vupdated, Johnson, One Moon Scientific - chemical shift assignment

X-PLOR NIH vupdated, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMRDraw, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR vupdated, Laskowski and MacArthur - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ GAA21560 GAA26073
EMBL CAA25311 CAA25313 CAA84947 CAA95892 CAY77793
GB AAA34660 AAT92979 AHY74495 AHY77062 AJP37096
REF NP_009563 NP_014368
SP P02309
TPG DAA07130 DAA10515