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 15393

Title: Structure of Chz1 Complexed with H2A.Z-H2B and Eviction of Nucleosomal H2A-H2B   PubMed: 18641662

Deposition date: 2007-07-19 Original release date: 2008-07-29

Authors: Zhou, Zheng; Feng, Hanqiao; Hansen, Flemming; Luk, Ed; Kato, Hidenori; Freedberg, Daron; Key, Lewis; Wu, Carl; Bai, Yawen

Citation: Zhou, Zheng; Feng, Hanqiao; Hansen, Flemming; Kato, Hidenori; Luk, Ed; Freedberg, Daron; Key, Lewis; Wu, Carl; Bai, Yawen. "NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B"  Nat. Struct. Mol. Biol. 15, 868-869 (2008).

Assembly members:
H2A.Z-H2B, polymer, 200 residues, 27270.035 Da.
Chz1, polymer, 62 residues, 161.126 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):
H2A.Z-H2B: RKETYSSYIYKVLKQTHPDT GISQKSMSILNSFVNDIFER IATEASKLAAYNKKSTISAR EIQTAVRLILPGELAKHAVS EGTRAVTKYSSSTQAQSSSA RAGLQFPVGRIKRYLKRHAT GRTRVGSKAAIYLTAVLEYL TAEVLELAGNAAKDLKVKRI TPRHLQLAIRGDDELDSLIR ATIASGGVLPHIAEELDKKE
Chz1: TVEDSESDMDDAKLDALMGN EGEEEEDDLAEIDTSNIITS GRRTRGKVIDYKKTAEELDK KE

Data sets:
Data typeCount
13C chemical shifts979
15N chemical shifts251
1H chemical shifts1439

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1H2A.Z-H2B1
2Chz12

Entities:

Entity 1, H2A.Z-H2B 200 residues - 27270.035 Da.

as polymer sequence

1   ARGLYSGLUTHRTYRSERSERTYRILETYR
2   LYSVALLEULYSGLNTHRHISPROASPTHR
3   GLYILESERGLNLYSSERMETSERILELEU
4   ASNSERPHEVALASNASPILEPHEGLUARG
5   ILEALATHRGLUALASERLYSLEUALAALA
6   TYRASNLYSLYSSERTHRILESERALAARG
7   GLUILEGLNTHRALAVALARGLEUILELEU
8   PROGLYGLULEUALALYSHISALAVALSER
9   GLUGLYTHRARGALAVALTHRLYSTYRSER
10   SERSERTHRGLNALAGLNSERSERSERALA
11   ARGALAGLYLEUGLNPHEPROVALGLYARG
12   ILELYSARGTYRLEULYSARGHISALATHR
13   GLYARGTHRARGVALGLYSERLYSALAALA
14   ILETYRLEUTHRALAVALLEUGLUTYRLEU
15   THRALAGLUVALLEUGLULEUALAGLYASN
16   ALAALALYSASPLEULYSVALLYSARGILE
17   THRPROARGHISLEUGLNLEUALAILEARG
18   GLYASPASPGLULEUASPSERLEUILEARG
19   ALATHRILEALASERGLYGLYVALLEUPRO
20   HISILEALAGLUGLULEUASPLYSLYSGLU

Entity 2, Chz1 62 residues - 161.126 Da.

as polymer sequence

1   THRVALGLUASPSERGLUSERASPMETASP
2   ASPALALYSLEUASPALALEUMETGLYASN
3   GLUGLYGLUGLUGLUGLUASPASPLEUALA
4   GLUILEASPTHRSERASNILEILETHRSER
5   GLYARGARGTHRARGGLYLYSVALILEASP
6   TYRLYSLYSTHRALAGLUGLULEUASPLYS
7   LYSGLU

Samples:

sample_1: H2A.Z-H2B, [U-35% 2H], 1.0 – 1.2 mM; Chz1, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_2: H2A.Z-H2B, [U-100% 15N; U-100% 2H], 1.0 – 1.2 mM; Chz1, [U-30%2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_3: H2A.Z-H2B, [U-100% 13C; U-30% 2H], 1.0 – 1.2 mM; Chz1, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_4: H2A.Z-H2B, [U-13C; U-15N; U-2H], 1.0 – 1.2 mM; Chz1, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_5: H2A.Z-H2B, [U-100% 15N; U-30%2H], 1.0 – 1.2 mM; Chz1, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_6: H2A.Z-H2B, [U-100% 13C;U-35%2H]/[U-100% 2H], 1.0 – 1.2 mM; Chz1, [U-100% 13C;U-35%2H]/[U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_7: H2A.Z-H2B, [U-100% 15N; U-100%2H], 1.0 – 1.2 mM; Chz1, [U-30% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_8: Chz1, [U-100% 13C; U-35%2H], 1.0 – 1.2 mM; H2A.Z-H2B, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_9: Chz1, [U-100% 15N; U-30%2H], 1.0 – 1.2 mM; H2A.Z-H2B, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_10: Chz1, [U-100% 13C; U-35%2H], 1.0 – 1.2 mM; H2A.Z-H2B, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_11: Chz1, [U-100%15N; U-100% 2H], 1.0 – 1.2 mM; H2A.Z-H2B, [U-100%15N; U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_12: H2A.Z-H2B, [U-100% 13C; U-100% 15N; U-100%2H], 1.0 – 1.2 mM; Chz1, [U-100% 13C; U-100% 15N; U-100%2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_13: Chz1, [U-10% 13C; U-100% 15N], 1.0 – 1.2 mM; H2A.Z-H2B, [U-100% 2H], 1.0 – 1.2 mM; MES 25 mM; KCl 200 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availableisotropicsample_conditions_1
2D 1H-1H NOESYnot availableisotropicsample_conditions_1
3D CBCA(CO)NHnot availableisotropicsample_conditions_1
3D CBCA(CO)NHnot availableisotropicsample_conditions_1
3D HNCACBnot availableisotropicsample_conditions_1
3D HNCACBnot availableisotropicsample_conditions_1
3D HNCOnot availableisotropicsample_conditions_1
3D HNCOnot availableisotropicsample_conditions_1
3D HNCAnot availableisotropicsample_conditions_1
3D HN(CO)CAnot availableisotropicsample_conditions_1
3D H(CCO)NHnot availableisotropicsample_conditions_1
3D HCCH-TOCSYnot availableisotropicsample_conditions_1
3D HBHA(CO)NHnot availableisotropicsample_conditions_1
3D HNHAnot availableisotropicsample_conditions_1
3D HNCANNHnot availableisotropicsample_conditions_1
3D TOCSY-HSQCnot availableisotropicsample_conditions_1
3D 1H-15N NOESYnot availableisotropicsample_conditions_1
3D 1H-15N NOESYnot availableisotropicsample_conditions_1
3D 1H-13C NOESYnot availableisotropicsample_conditions_1
3D 1H-13C NOESYnot availableisotropicsample_conditions_1

Software:

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment, NMR data process and analysis, peak picking

X-PLOR NIH v2.16, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMRPipe v2004, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, processing

PIPP v4.3.3, Garrett - chemical shift assignment, peak picking

TALOS v2004, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR v3.5.4, Laskowski and MacArthur - structure analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker DRX 700 MHz

Related Database Links:

BMRB 17114 17114
PDB
DBJ GAA22856
EMBL CAY79198
GB AAB64563 AHY75583 EDN62999 EDV08859 EDZ72631
REF NP_010947
SP A6ZQX9 P40019
TPG DAA07683

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