BMRB Entry 27191

Name: ProXp-ala bound to microhelixPro
Published: 2017-08-21

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27191

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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:

ProXp-ala bound to microhelixPro

Deposition date:

2017-07-21

Original release date:

2017-08-21

Authors:

Danhart, Eric

Citation:

Citation: Danhart, Eric; Bakhtina, Marina; Cantara, William; Kuzmishin, Alexandra; Ma, Xiao; Sanford, Brianne; Kosutic, Marija; Goto, Yuki; Suga, Hiroaki; Nakanishi, Kotaro; Micura, Ronald; Foster, Mark; Musier-Forsyth, Karin. "Conformational and chemical selection by a trans-acting editing domain." Proc. Natl. Acad. Sci. U.S.A. 114, E6774-E6783 (2017).
PubMed: 28768811

Assembly members:

Assembly members:
ProXp-ala, polymer, 171 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Caulobacter vibrioides Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ProXp-ala: GSHMKTRADLFAFFDAHGVD HKTLDHPPVFRVEEGLEIKA AMPGGHTKNLFLKDAKGQLW LISALGETTIDLKKLHHVIG SGRLSFGPQEMMLETLGVTP GSVTAFGLINDTEKRVRFVL DKALADSDPVNFHPLKNDAT TAVSQAGLRRFLAALGVEPM IVDFAAMEVVG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	451
15N chemical shifts	152
1H chemical shifts	152

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ProXp-ala	1

Entities:

Entity 1, ProXp-ala 171 residues - Formula weight is not available

1

GLY

SER

HIS

MET

LYS

THR

ARG

ALA

ASP

LEU

2

PHE

ALA

PHE

ASP

ALA

HIS

GLY

VAL

ASP

3

HIS

LYS

THR

LEU

ASP

HIS

PRO

VAL

PHE

4

ARG

VAL

GLU

GLY

LEU

GLU

ILE

LYS

ALA

5

ALA

MET

PRO

GLY

HIS

THR

LYS

ASN

LEU

6

PHE

LEU

LYS

ASP

ALA

LYS

GLY

GLN

LEU

TRP

7

LEU

ILE

SER

ALA

LEU

GLY

GLU

THR

ILE

8

ASP

LEU

LYS

LEU

HIS

VAL

ILE

GLY

9

SER

GLY

ARG

LEU

SER

PHE

GLY

PRO

GLN

GLU

10

MET

LEU

GLU

THR

LEU

GLY

VAL

THR

PRO

11

GLY

SER

VAL

THR

ALA

PHE

GLY

LEU

ILE

ASN

12

ASP

THR

GLU

LYS

ARG

VAL

ARG

PHE

VAL

LEU

13

ASP

LYS

ALA

LEU

ALA

ASP

SER

ASP

PRO

VAL

14

ASN

PHE

HIS

PRO

LEU

LYS

ASN

ASP

ALA

THR

15

THR

ALA

VAL

SER

GLN

ALA

GLY

LEU

ARG

16

PHE

LEU

ALA

LEU

GLY

VAL

GLU

PRO

MET

17

ILE

VAL

ASP

PHE

ALA

MET

GLU

VAL

18

GLY

Samples:

sample_1: ProXp-ala, [U-100% 13C; U-100% 15N], 0.65 mM

sample_conditions_1: ionic strength: 0.16 M; pH: 7.5; 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

Bruker DRX 600 MHz

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