BMRB Entry 50733

Name: NN206* (P22A and M85A; hereafter NN206*)
Published: 2021-05-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50733

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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:

NN206* (P22A and M85A; hereafter NN206*)

Deposition date:

2021-01-25

Original release date:

2021-05-18

Authors:

Tzeng, Shiou-Ru

Citation:

Citation: Tzeng, Shiou-Ru; Tseng, Yin-Chu; Lin, Chien-Chu; Hsu, Chia-Ying; Huang, Shing-Jong; Kuo, Yi-Ting; Chang, Chung-I. "Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease" elife 10, e64056-e64056 (2021).
PubMed: 33929321

Assembly members:

Assembly members:
entity_1, polymer, 206 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Meiothermus taiwanensis Taxonomy ID: 172827 Superkingdom: Bacteria Kingdom: not available Genus/species: Meiothermus taiwanensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-206*

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MRLELPVIPLRNTVILPHTT TAVDVGRAKSKRAVEEAMGA DRLIFLVAQRDPEVDDPAPD DLYTWGVQAVVKQAMRLPDG TLQVAVEARARAQVTDYIPG PYLRARGEVFSEIFPIDEAV VRVLVEELKEAFEKYVANHK SLRLDRYQLEAVKGTSDPAM LADTIAYHATWTVAEKQEIL ELTDLEARLKKVLGLLSRDL ERFELD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	187
1H chemical shifts	187

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NN206* (P22A and M85A)	1

Entities:

Entity 1, NN206* (P22A and M85A) 206 residues - Formula weight is not available

1

MET

ARG

LEU

GLU

LEU

PRO

VAL

ILE

PRO

LEU

2

ARG

ASN

THR

VAL

ILE

LEU

PRO

HIS

THR

3

THR

ALA

VAL

ASP

VAL

GLY

ARG

ALA

LYS

SER

4

LYS

ARG

ALA

VAL

GLU

ALA

MET

GLY

ALA

5

ASP

ARG

LEU

ILE

PHE

LEU

VAL

ALA

GLN

ARG

6

ASP

PRO

GLU

VAL

ASP

PRO

ALA

PRO

ASP

7

ASP

LEU

TYR

THR

TRP

GLY

VAL

GLN

ALA

VAL

8

VAL

LYS

GLN

ALA

MET

ARG

LEU

PRO

ASP

GLY

9

THR

LEU

GLN

VAL

ALA

VAL

GLU

ALA

ARG

ALA

10

ARG

ALA

GLN

VAL

THR

ASP

TYR

ILE

PRO

GLY

11

PRO

TYR

LEU

ARG

ALA

ARG

GLY

GLU

VAL

PHE

12

SER

GLU

ILE

PHE

PRO

ILE

ASP

GLU

ALA

VAL

13

VAL

ARG

VAL

LEU

VAL

GLU

LEU

LYS

GLU

14

ALA

PHE

GLU

LYS

TYR

VAL

ALA

ASN

HIS

LYS

15

SER

LEU

ARG

LEU

ASP

ARG

TYR

GLN

LEU

GLU

16

ALA

VAL

LYS

GLY

THR

SER

ASP

PRO

ALA

MET

17

LEU

ALA

ASP

THR

ILE

ALA

TYR

HIS

ALA

THR

18

TRP

THR

VAL

ALA

GLU

LYS

GLN

GLU

ILE

LEU

19

GLU

LEU

THR

ASP

LEU

GLU

ALA

ARG

LEU

LYS

20

LYS

VAL

LEU

GLY

LEU

SER

ARG

ASP

LEU

21

GLU

ARG

PHE

GLU

LEU

ASP

Samples:

sample_1: NN206* (P22A and M85A; hereafter NN206*), [U-99% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 328 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMR spectrometers:

Bruker AVIII-800 800MHz Super-Conducting Magnet - 18.79 Tesla MHz

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