BMRB Entry 25350

Name: Solution structure of PsbQ from spinacia oleracea
Published: 2015-07-27

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PDB ID: 2mwq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25350
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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 PsbQ from spinacia oleracea

Deposition date:

2014-11-19

Original release date:

2015-07-27

Authors:

Rathner, Petr; Mueller, Norbert; Wimmer, Reinhard; Chandra, Kousik

Citation:

Citation: Rathner, Petr; Walnerova, Adriana; Hornicakova, Michaela; Wohlschlager, Christian; Chandra, Kousik; Kohoutova, Jaroslava; Ettrich, Ruediger; Wimmer, Reinhard; Mueller, Norbert. "Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants" Proteins 83, 1677-1686 (2015).
PubMed: 26138376

Assembly members:

Assembly members:
PsbQ, polymer, 149 residues, 16544.906 Da.

Natural source:

Natural source: Common Name: spinach Taxonomy ID: 3562 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: spinacia oleracea

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: JR2592

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PsbQ: EARPIVVGPPPPLSGGLPGT ENSDQARDGTLPYTKDRFYL QPLPPTEAAQRAKVSASEIL NVKQFIDRKAWPSLQNDLRL RASYLRYDLKTVISAKPKDE KKSLQELTSKLFSSIDNLDH AAKIKSPTEAEKYYGQTVSN INEVLAKLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	638
15N chemical shifts	148
1H chemical shifts	924

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PsbQ	1

Entities:

Entity 1, PsbQ 149 residues - 16544.906 Da.

1

GLU

ALA

ARG

PRO

ILE

VAL

GLY

PRO

2

PRO

LEU

SER

GLY

LEU

PRO

GLY

THR

3

GLU

ASN

SER

ASP

GLN

ALA

ARG

ASP

GLY

THR

4

LEU

PRO

TYR

THR

LYS

ASP

ARG

PHE

TYR

LEU

5

GLN

PRO

LEU

PRO

THR

GLU

ALA

GLN

6

ARG

ALA

LYS

VAL

SER

ALA

SER

GLU

ILE

LEU

7

ASN

VAL

LYS

GLN

PHE

ILE

ASP

ARG

LYS

ALA

8

TRP

PRO

SER

LEU

GLN

ASN

ASP

LEU

ARG

LEU

9

ARG

ALA

SER

TYR

LEU

ARG

TYR

ASP

LEU

LYS

10

THR

VAL

ILE

SER

ALA

LYS

PRO

LYS

ASP

GLU

11

LYS

SER

LEU

GLN

GLU

LEU

THR

SER

LYS

12

LEU

PHE

SER

ILE

ASP

ASN

LEU

ASP

HIS

13

ALA

LYS

ILE

LYS

SER

PRO

THR

GLU

ALA

14

GLU

LYS

TYR

GLY

GLN

THR

VAL

SER

ASN

15

ILE

ASN

GLU

VAL

LEU

ALA

LYS

LEU

GLY

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HC(C)H-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)C(C)(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HC(C)H-COSY	sample_1	isotropic	sample_conditions_1
3D TOCSY-HSQC	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 25350

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: