BMRB Entry 17832

Name: 1H, 15N and 13C resonance assignments for the N-terminal dimeric region of budding yeast histone chaperone Rtt106
Published: 2012-01-25

Click here to enlarge.

PDB ID: 2lh0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17832
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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: 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:
HISTONE_CHAPERONE_RTT106, polymer, 70 residues, 8129.245 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):
HISTONE_CHAPERONE_RTT106: GHMMSKLFLDELPESLSRKI GTVVRVLPSSLEIFEELYKY ALNENSNDRSEHHKKPRIDD SSDLLKTDEI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	286
15N chemical shifts	66
1H chemical shifts	451

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Entity Assembly ID	Entity Name	Entity ID
1	HISTONE CHAPERONE RTT106_1	1
2	HISTONE CHAPERONE RTT106_2	1

1	GLY	HIS	MET	MET	SER	LYS	LEU	PHE	LEU	ASP
2	GLU	LEU	PRO	GLU	SER	LEU	SER	ARG	LYS	ILE
3	GLY	THR	VAL	VAL	ARG	VAL	LEU	PRO	SER	SER
4	LEU	GLU	ILE	PHE	GLU	GLU	LEU	TYR	LYS	TYR
5	ALA	LEU	ASN	GLU	ASN	SER	ASN	ASP	ARG	SER
6	GLU	HIS	HIS	LYS	LYS	PRO	ARG	ILE	ASP	ASP
7	SER	SER	ASP	LEU	LEU	LYS	THR	ASP	GLU	ILE

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H- 15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 13C- FILTERED-EDITED NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

PDB	2LH0
DBJ	GAA25899
GB	AJT01944 AJT02319 AJT04929 AJT05307 AJT07909

Biological Magnetic Resonance Data Bank

BMRB Entry 17832

Title: 1H, 15N and 13C resonance assignments for the N-terminal dimeric region of budding yeast histone chaperone Rtt106 PubMed: 22307274

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	HIS	MET	MET	SER	LYS	LEU	PHE	LEU	ASP
2	GLU	LEU	PRO	GLU	SER	LEU	SER	ARG	LYS	ILE
3	GLY	THR	VAL	VAL	ARG	VAL	LEU	PRO	SER	SER
4	LEU	GLU	ILE	PHE	GLU	GLU	LEU	TYR	LYS	TYR
5	ALA	LEU	ASN	GLU	ASN	SER	ASN	ASP	ARG	SER
6	GLU	HIS	HIS	LYS	LYS	PRO	ARG	ILE	ASP	ASP
7	SER	SER	ASP	LEU	LEU	LYS	THR	ASP	GLU	ILE

1	GLY	HIS	MET	MET	SER	LYS	LEU	PHE	LEU	ASP
2	GLU	LEU	PRO	GLU	SER	LEU	SER	ARG	LYS	ILE
3	GLY	THR	VAL	VAL	ARG	VAL	LEU	PRO	SER	SER
4	LEU	GLU	ILE	PHE	GLU	GLU	LEU	TYR	LYS	TYR
5	ALA	LEU	ASN	GLU	ASN	SER	ASN	ASP	ARG	SER
6	GLU	HIS	HIS	LYS	LYS	PRO	ARG	ILE	ASP	ASP
7	SER	SER	ASP	LEU	LEU	LYS	THR	ASP	GLU	ILE

1	GLY	HIS	MET	MET	SER	LYS	LEU	PHE	LEU	ASP
2	GLU	LEU	PRO	GLU	SER	LEU	SER	ARG	LYS	ILE
3	GLY	THR	VAL	VAL	ARG	VAL	LEU	PRO	SER	SER
4	LEU	GLU	ILE	PHE	GLU	GLU	LEU	TYR	LYS	TYR
5	ALA	LEU	ASN	GLU	ASN	SER	ASN	ASP	ARG	SER
6	GLU	HIS	HIS	LYS	LYS	PRO	ARG	ILE	ASP	ASP
7	SER	SER	ASP	LEU	LEU	LYS	THR	ASP	GLU	ILE