BMRB Entry 19751

Name: Solution structure of ORF2
Published: 2015-03-23

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PDB ID: 2mk4
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/BMR19751
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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 ORF2

Deposition date:

2014-01-24

Original release date:

2015-03-23

Authors:

Miyakawa, Takuya; Kobayashi, Hidetomo; Tashiro, Mitsuru; Yamanaka, Hiroyasu; Tanokura, Masaru

Citation:

Citation: Kobayashi, Hidetomo; Yoshida, Toru; Miyakawa, Takuya; Tashiro, Mitsuru; Okamoto, Keinosuke; Yamanaka, Hiroyasu; Tanokura, Masaru; Tsuge, Hideaki. "Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria" J. Biol. Chem. ., .-. (2015).
PubMed: 25784551

Assembly members:

Assembly members:
entity, polymer, 133 residues, 13751.540 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 646 Superkingdom: Bacteria Kingdom: not available Genus/species: Aeromonas sobria

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPVQESVTMDGKQYSTIEVN GQTYLIPDNGSKKRVARSLD SKVPQQTLRRGDVLMQGAAS PELTVSGTLLVEADDASAKA LATRHGLNFKQSSGGIALLE AKPGTDLNAIATKLKSEGVN VQIELSGAEQQPK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	416
15N chemical shifts	119
1H chemical shifts	794

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ORF2	1

Entities:

Entity 1, ORF2 133 residues - 13751.540 Da.

1

GLY

PRO

VAL

GLN

GLU

SER

VAL

THR

MET

ASP

2

GLY

LYS

GLN

TYR

SER

THR

ILE

GLU

VAL

ASN

3

GLY

GLN

THR

TYR

LEU

ILE

PRO

ASP

ASN

GLY

4

SER

LYS

ARG

VAL

ALA

ARG

SER

LEU

ASP

5

SER

LYS

VAL

PRO

GLN

THR

LEU

ARG

6

GLY

ASP

VAL

LEU

MET

GLN

GLY

ALA

SER

7

PRO

GLU

LEU

THR

VAL

SER

GLY

THR

LEU

8

VAL

GLU

ALA

ASP

ALA

SER

ALA

LYS

ALA

9

LEU

ALA

THR

ARG

HIS

GLY

LEU

ASN

PHE

LYS

10

GLN

SER

GLY

ILE

ALA

LEU

GLU

11

ALA

LYS

PRO

GLY

THR

ASP

LEU

ASN

ALA

ILE

12

ALA

THR

LYS

LEU

LYS

SER

GLU

GLY

VAL

ASN

13

VAL

GLN

ILE

GLU

LEU

SER

GLY

ALA

GLU

GLN

14

GLN

PRO

LYS

Samples:

sample_1: ORF2, [U-99% 13C; U-99% 15N], 0.9 mM; MOPS 18 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, peak picking, refinement, structure solution

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2MK4 3WQB
GB	AEB49524 AHH32619 EKB12965 EKB17107 EKB21458
REF	WP_005333882 WP_005352955 WP_005361466 WP_019445376 WP_021229060