BMRB Entry 18191

Name: Solution structure of Sgf11(63-99) zinc finger domain
Published: 2012-03-23

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PDB ID: 2lo2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18191
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Sgf11(63-99) zinc finger domain

Deposition date:

2012-01-10

Original release date:

2012-03-23

Authors:

Gao, Xiaojun; Koehler, Christian; Bonnet, Jacques; Devys, Didier; Kieffer, Bruno

Citation:

Citation: KOEHLER, CHRISTIAN; GAO, XIAOJUN; BONNET, JACQUES; DEVYS, DIDIER; KIEFFER, BRUNO. "Insights into the role of SGF11 and SGF73 for the interaction between SAGA and nucleosomes" .

Assembly members:

Assembly members:
sgf11, polymer, 38 residues, 8599.688 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGex4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sgf11: GKQQESSQYIHCENCGRDVS ANRLAAHLQRCLSRGARR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	45
1H chemical shifts	232
heteronuclear NOE values	36
T1 relaxation values	36
T2 relaxation values	36

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SGF11	1
2	ZINC ION	2

Entities:

Entity 1, SGF11 38 residues - 8599.688 Da.

1

GLY

LYS

GLN

GLU

SER

GLN

TYR

ILE

2

HIS

CYS

GLU

ASN

CYS

GLY

ARG

ASP

VAL

SER

3

ALA

ASN

ARG

LEU

ALA

HIS

LEU

GLN

ARG

4

CYS

LEU

SER

ARG

GLY

ALA

ARG

Entity 2, ZINC ION - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: sgf11, [U-99% 13C; U-98% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 75 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions: ionic strength: 0.115 M; pH: 7.0; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions
2D 1H-1H COSY	sample_1	isotropic	sample_conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions
3D HNCO	sample_1	isotropic	sample_conditions
3D HNCA	sample_1	isotropic	sample_conditions
3D HNCACB	sample_1	isotropic	sample_conditions
3D HN(CO)CA	sample_1	isotropic	sample_conditions
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions
3D HNCACO	sample_1	isotropic	sample_conditions
2D 1H-15N HSQC R1 edited	sample_1	isotropic	sample_conditions
2D 1H-15N HSQC R2 edited	sample_1	isotropic	sample_conditions
2D 1H-15N heteronuclear NOE	sample_1	isotropic	sample_conditions

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz

PDB	2LO2 3M99 3MHH 3MHS 4FJC 4FK5 4W4U 4WA6
DBJ	GAA26924
EMBL	CAY86913
GB	AAB68174 AAS56656 AHY78128 AJP42096 AJV91186
REF	NP_015278
SP	A6ZWK1 B3LL20 Q03067
TPG	DAA11383
AlphaFold	A6ZWK1 B3LL20 Q03067