BMRB Entry 5555

Name: Solution structure of the 2nd PHD domain from Mi2b
Published: 2003-08-01

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PDB ID: 1mm2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5555
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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 the 2nd PHD domain from Mi2b

Deposition date:

2002-10-10

Original release date:

2003-08-01

Authors:

Kwan, A.; Gell, D.; Mackay, J.

Citation:

Citation: Kwan, A.; Gell, D.; Verger, A.; Crossley, M.; Matthews, J.; Mackay, J.. "Engineering a Protein Scaffold from a PHD Finger" Structure 11, 803-813 (2003).
PubMed: 12842043

Assembly members:

Assembly members:
PHD, polymer, 61 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: plasmid PGEX-6p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHD: GPLGSDHHMEFCRVCKDGGE LLCCDTCPSSYHIHCLNPPL PEIPNGEWLCPRCTCPALKG K

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	367
15N chemical shifts	50

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mi2-beta	1
2	ZINC ION 1	2
3	ZINC ION 2	2

Entities:

Entity 1, Mi2-beta 61 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

ASP

HIS

MET

GLU

2

PHE

CYS

ARG

VAL

CYS

LYS

ASP

GLY

GLU

3

LEU

CYS

ASP

THR

CYS

PRO

SER

4

TYR

HIS

ILE

HIS

CYS

LEU

ASN

PRO

LEU

5

PRO

GLU

ILE

PRO

ASN

GLY

GLU

TRP

LEU

CYS

6

PRO

ARG

CYS

THR

CYS

PRO

ALA

LEU

LYS

GLY

7

LYS

Entity 2, ZINC ION 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: PHD 1 mM; DTT 1 mM; sodium phosphate buffer 10 mM; NaCl 150 mM; H2O 95%; D2O 5%

sample_2: PHD, [U-15N], 0.2 mM; DTT 1 mM; sodium phosphate buffer 10 mM; NaCl 150 mM; H2O 95%; D2O 5%

sample_cond_1: pH: 7.5; temperature: 298 K; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	not available	not available	sample_cond_1
2D TOCSY	not available	not available	sample_cond_1
DQF-COSY	not available	not available	sample_cond_1
N15-HSQC	not available	not available	sample_cond_1

Software:

XWINNMR v2.5 - processing

XEASY v1.3.13 - data analysis

DYANA v1.5 - refinement

ARIA v1.1.2 - structure solution

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1MM2
DBJ	BAE32198