BMRB Entry 15393
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15393
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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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 979 |
15N chemical shifts | 251 |
1H chemical shifts | 1439 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | H2A.Z-H2B | 1 |
2 | Chz1 | 2 |
Entities:
Entity 1, H2A.Z-H2B 200 residues - 27270.035 Da.
as polymer sequence
1 | ARG | LYS | GLU | THR | TYR | SER | SER | TYR | ILE | TYR | |
2 | LYS | VAL | LEU | LYS | GLN | THR | HIS | PRO | ASP | THR | |
3 | GLY | ILE | SER | GLN | LYS | SER | MET | SER | ILE | LEU | |
4 | ASN | SER | PHE | VAL | ASN | ASP | ILE | PHE | GLU | ARG | |
5 | ILE | ALA | THR | GLU | ALA | SER | LYS | LEU | ALA | ALA | |
6 | TYR | ASN | LYS | LYS | SER | THR | ILE | SER | ALA | ARG | |
7 | GLU | ILE | GLN | THR | ALA | VAL | ARG | LEU | ILE | LEU | |
8 | PRO | GLY | GLU | LEU | ALA | LYS | HIS | ALA | VAL | SER | |
9 | GLU | GLY | THR | ARG | ALA | VAL | THR | LYS | TYR | SER | |
10 | SER | SER | THR | GLN | ALA | GLN | SER | SER | SER | ALA | |
11 | ARG | ALA | GLY | LEU | GLN | PHE | PRO | VAL | GLY | ARG | |
12 | ILE | LYS | ARG | TYR | LEU | LYS | ARG | HIS | ALA | THR | |
13 | GLY | ARG | THR | ARG | VAL | GLY | SER | LYS | ALA | ALA | |
14 | ILE | TYR | LEU | THR | ALA | VAL | LEU | GLU | TYR | LEU | |
15 | THR | ALA | GLU | VAL | LEU | GLU | LEU | ALA | GLY | ASN | |
16 | ALA | ALA | LYS | ASP | LEU | LYS | VAL | LYS | ARG | ILE | |
17 | THR | PRO | ARG | HIS | LEU | GLN | LEU | ALA | ILE | ARG | |
18 | GLY | ASP | ASP | GLU | LEU | ASP | SER | LEU | ILE | ARG | |
19 | ALA | THR | ILE | ALA | SER | GLY | GLY | VAL | LEU | PRO | |
20 | HIS | ILE | ALA | GLU | GLU | LEU | ASP | LYS | LYS | GLU |
Entity 2, Chz1 62 residues - 161.126 Da.
as polymer sequence
1 | THR | VAL | GLU | ASP | SER | GLU | SER | ASP | MET | ASP | ||||
2 | ASP | ALA | LYS | LEU | ASP | ALA | LEU | MET | GLY | ASN | ||||
3 | GLU | GLY | GLU | GLU | GLU | GLU | ASP | ASP | LEU | ALA | ||||
4 | GLU | ILE | ASP | THR | SER | ASN | ILE | ILE | THR | SER | ||||
5 | GLY | ARG | ARG | THR | ARG | GLY | LYS | VAL | ILE | ASP | ||||
6 | TYR | LYS | LYS | THR | ALA | GLU | GLU | LEU | ASP | LYS | ||||
7 | LYS | GLU |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | not available | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | not available | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | not available | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | not available | isotropic | sample_conditions_1 |
3D HNCACB | not available | isotropic | sample_conditions_1 |
3D HNCACB | not available | isotropic | sample_conditions_1 |
3D HNCO | not available | isotropic | sample_conditions_1 |
3D HNCO | not available | isotropic | sample_conditions_1 |
3D HNCA | not available | isotropic | sample_conditions_1 |
3D HN(CO)CA | not available | isotropic | sample_conditions_1 |
3D H(CCO)NH | not available | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | not available | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | not available | isotropic | sample_conditions_1 |
3D HNHA | not available | isotropic | sample_conditions_1 |
3D HNCANNH | not available | isotropic | sample_conditions_1 |
3D TOCSY-HSQC | not available | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | not available | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | not available | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | not available | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | not available | isotropic | sample_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