BMRB Entry 16637

Name: Solution Structure of extended PDZ2 Domain from NHERF1 (150-270)
Published: 2010-02-01

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PDB ID: 2kjd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16637
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of extended PDZ2 Domain from NHERF1 (150-270)

Deposition date:

2009-12-18

Original release date:

2010-02-01

Authors:

Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei

Citation:

Citation: Bhattacharya, Shibani; Dai, Zhongping; Li, Jianquan; Baxter, Sabine; Callaway, David; Cowburn, David; Bu, Zimei. "A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation." J. Biol. Chem. 285, 9981-9994 (2010).
PubMed: 20042604

Assembly members:

Assembly members:
PDZ2-270, polymer, 128 residues, 14101.081 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: pET151/D-TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PDZ2-270: GIDPFTMLRPRLCTMKKGPS GYGFNLHSDKSKPGQFIRSV DPDSPAEASGLRAQDRIVEV NGVCMEGKQHGDVVSAIRAG GDETKLLVVDRETDEFFKKC RVIPSQEHLNGPLPVPFTNG EIQKENSR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	495
15N chemical shifts	123
1H chemical shifts	845

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PDZ2-270	1

Entities:

Entity 1, PDZ2-270 128 residues - 14101.081 Da.

Residues 1-7 represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

MET

LEU

ARG

PRO

2

ARG

LEU

CYS

THR

MET

LYS

GLY

PRO

SER

3

GLY

TYR

GLY

PHE

ASN

LEU

HIS

SER

ASP

LYS

4

SER

LYS

PRO

GLY

GLN

PHE

ILE

ARG

SER

VAL

5

ASP

PRO

ASP

SER

PRO

ALA

GLU

ALA

SER

GLY

6

LEU

ARG

ALA

GLN

ASP

ARG

ILE

VAL

GLU

VAL

7

ASN

GLY

VAL

CYS

MET

GLU

GLY

LYS

GLN

HIS

8

GLY

ASP

VAL

SER

ALA

ILE

ARG

ALA

GLY

9

GLY

ASP

GLU

THR

LYS

LEU

VAL

ASP

10

ARG

GLU

THR

ASP

GLU

PHE

LYS

CYS

11

ARG

VAL

ILE

PRO

SER

GLN

GLU

HIS

LEU

ASN

12

GLY

PRO

LEU

PRO

VAL

PRO

PHE

THR

ASN

GLY

13

GLU

ILE

GLN

LYS

GLU

ASN

SER

ARG

Samples:

sample_1: PDZ2-270, [U-100% 13C; U-100% 15N], 550 uM; HEPES 20 mM; DTT 0.5 mM; PMSF 0.1 mM; sodium chloride 150 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v1.3, Guntert, Mumenthaler and Wuthrich - structure solution

ARIA v2.2, Linge, O'Donoghue and Nilges - refinement, structure solution

CARA v1.5, Keller and Wuthrich - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - Dihedral Angle Calculation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 900 MHz

BMRB	15567 16638 18826
PDB	2JXO 2KJD 2KRG 2M0V 2OZF 4Q3H
DBJ	BAG54683
GB	EAW89189 EHH58322