BMRB Entry 17832

Title:
1H, 15N and 13C resonance assignments for the N-terminal dimeric region of budding yeast histone chaperone Rtt106   PubMed: 22307274
Deposition date:
2011-08-04
Original release date:
2012-01-25
Authors:
Hu, Q.; Cui, G.; Mer, G.
Citation:

Citation: Su, Dan; Hu, Qi; Li, Qing; Thompson, James; Cui, Gaofeng; Fazly, Ahmed; Davies, Brian; Botuyan, Maria; Zhang, Zhiguo; Mer, Georges. "Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106"  Nature 483, 104-107 (2012).

Assembly members:

Assembly members:
HISTONE_CHAPERONE_RTT106, polymer, 70 residues, 8129.245 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PTEV

Experimental source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HISTONE_CHAPERONE_RTT106: GHMMSKLFLDELPESLSRKI GTVVRVLPSSLEIFEELYKY ALNENSNDRSEHHKKPRIDD SSDLLKTDEI

Data sets:
Data typeCount
13C chemical shifts286
15N chemical shifts66
1H chemical shifts451

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HISTONE CHAPERONE RTT106_11
2HISTONE CHAPERONE RTT106_21

Entities:

Entity 1, HISTONE CHAPERONE RTT106_1 70 residues - 8129.245 Da.

1   GLYHISMETMETSERLYSLEUPHELEUASP
2   GLULEUPROGLUSERLEUSERARGLYSILE
3   GLYTHRVALVALARGVALLEUPROSERSER
4   LEUGLUILEPHEGLUGLULEUTYRLYSTYR
5   ALALEUASNGLUASNSERASNASPARGSER
6   GLUHISHISLYSLYSPROARGILEASPASP
7   SERSERASPLEULEULYSTHRASPGLUILE

Samples:

sample_1: HISTONE CHAPERONE RTT106, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; NaCl 30 mM; Sodium Phosphate 20 mM

sample_2: HISTONE CHAPERONE RTT106, [U-100% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 30 mM; Sodium Phosphate 20 mM

sample_3: HISTONE CHAPERONE RTT106, [U-100% 13C; U-100% 15N], 0.6 mM; HISTONE CHAPERONE RTT106 0.6 mM; D2O 100%; NaCl 30 mM; Sodium Phosphate 20 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.95; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H- 15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 13C- FILTERED-EDITED NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • BRUKER AVANCE 700 MHz

Related Database Links:

PDB
DBJ GAA25899
GB AJT01944 AJT02319 AJT04929 AJT05307 AJT07909

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks