BMRB Entry 18963

Name: 1H, 13C, 15N chemical shift assignments of Dido PHD domain
Published: 2013-08-05

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PDB ID: 2m3h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18963
MolProbity Validation Chart

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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:

1H, 13C, 15N chemical shift assignments of Dido PHD domain

Deposition date:

2013-01-19

Original release date:

2013-08-05

Authors:

Santiveri, Clara; Perez-Canadillas, Jose; Jimenez, M Angeles

Citation:

Citation: Santiveri, Clara; Garcia-Mayoral, Maria; Perez-Canadillas, Jose; Jimenez, M Angeles. "NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3" J. Biomol. NMR 56, 183-190 (2013).
PubMed: 23579637

Assembly members:

Assembly members:
Dido_PHD, polymer, 61 residues, 7048.059 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dido_PHD: GSMDPNALYCICRQPHNNRF MICCDRCEEWFHGDCVGISE ARGRLLERNGEDYICPNCTI L

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	268
15N chemical shifts	68
1H chemical shifts	808

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Dido_PHD	1
2	ZINC ION_1	2
3	ZINC ION_2	2

Entities:

Entity 1, Dido_PHD 61 residues - 7048.059 Da.

Residues 1-3, GSM, are the cloning tag. Residues 4-61 correspond to residues 265-322 from human Dido or to residues 262-319 from mouse Dido.

1

GLY

SER

MET

ASP

PRO

ASN

ALA

LEU

TYR

CYS

2

ILE

CYS

ARG

GLN

PRO

HIS

ASN

ARG

PHE

3

MET

ILE

CYS

ASP

ARG

CYS

GLU

TRP

4

PHE

HIS

GLY

ASP

CYS

VAL

GLY

ILE

SER

GLU

5

ALA

ARG

GLY

ARG

LEU

GLU

ARG

ASN

GLY

6

GLU

ASP

TYR

ILE

CYS

PRO

ASN

CYS

THR

ILE

7

LEU

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1

ZN

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

UNP	Q9BTC0 Q8C9B9
BMRB	19074
PDB	1WEM 2M3H 4L7X
DBJ	BAA20791 BAA92094 BAC31270 BAC97927 BAE88140
EMBL	CAB48401 CAG31367 CAH89967
GB	AAH00770 AAH04237 AAH14489 AAH29110 AAH96662
REF	NP_001124926 NP_001180298 NP_001180299 NP_001278361 NP_001278362
SP	Q8C9B9 Q9BTC0
AlphaFold	Q9UFB6 Q9WV00 Q8C9B9 Q9BTC0

BMRB Entry 18963

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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