BMRB Entry 16520

Name: Solution structure of humar Par-3b PDZ2 (residues 451-549)
Published: 2010-01-28

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PDB ID: 2kom
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16520
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of humar Par-3b PDZ2 (residues 451-549)

Deposition date:

2009-09-24

Original release date:

2010-01-28

Authors:

Volkman, B.; Tyler, R.; Peterson, F.

Citation:

Citation: Jensen, Davin; Woytovich, Christopher; Li, Margie; Duvnjak, Petar; Cassidy, Michael; Frederick, Ronnie; Bergeman, Lai; Peterson, Francis; Volkman, Brian. "Rapid, robotic, small-scale protein production for NMR screening and structure determination." Protein Sci. 19, 570-578 (2010).
PubMed: 20073081

Assembly members:

Assembly members:
hPar-3_PDZ2, polymer, 121 residues, 13394.356 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: pQE30-8HT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hPar-3_PDZ2: MRGSHHHHHHHHGSENLYFQ GSYNTKKIGKRLNIQLKKGT EGLGFSITSRDVTIGGSAPI YVKNILPRGAAIQDGRLKAG DRLIEVNGVDLVGKSQEEVV SLLRSTKMEGTVSLLVFRQE D

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	393
15N chemical shifts	99
1H chemical shifts	616

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hPar3 PDZ2	1

Entities:

Entity 1, hPar3 PDZ2 121 residues - 13394.356 Da.

Residues 429-450 (MRGSHHHHHHHHGSENLYFQGS) are a octa-His tag that was not removed from the protein prior to structure determination.

1

MET

ARG

GLY

SER

HIS

2

HIS

GLY

SER

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

SER

TYR

ASN

THR

LYS

ILE

GLY

LYS

4

ARG

LEU

ASN

ILE

GLN

LEU

LYS

GLY

THR

5

GLU

GLY

LEU

GLY

PHE

SER

ILE

THR

SER

ARG

6

ASP

VAL

THR

ILE

GLY

SER

ALA

PRO

ILE

7

TYR

VAL

LYS

ASN

ILE

LEU

PRO

ARG

GLY

ALA

8

ALA

ILE

GLN

ASP

GLY

ARG

LEU

LYS

ALA

GLY

9

ASP

ARG

LEU

ILE

GLU

VAL

ASN

GLY

VAL

ASP

10

LEU

VAL

GLY

LYS

SER

GLN

GLU

VAL

11

SER

LEU

ARG

SER

THR

LYS

MET

GLU

GLY

12

THR

VAL

SER

LEU

VAL

PHE

ARG

GLN

GLU

13

ASP

Samples:

sample_1: hPar-3 PDZ2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%; sodium azide 0.02%

sample_conditions_1: ionic strength: 53 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

Bruker Avance III 500 MHz

BMRB	16515
PDB	2KOJ 2KOM
GB	EPQ12192
REF	XP_011836158