BMRB Entry 30773

Name: Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature
Published: 2020-10-30

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PDB ID: 6xry
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30773
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature PubMed: 33058876

Deposition date: 2020-07-14 Original release date: 2020-10-30

Authors: Nordyke, C.; Ahmed, Y.; Puterbaugh, R.; Bowman, G.; Varga, K.

Citation: Nordyke, C.; Ahmed, Y.; Puterbaugh, R.; Bowman, G.; Varga, K.. "Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature" J. Mol. Biol. 432, 6092-6107 (2020).

Assembly members:
entity_1, polymer, 141 residues, 14988.290 Da.

Natural source: Common Name: Caulobacter vibrioides Taxonomy ID: 190650 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter vibrioides

Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: MSDQSQEPTMEEILASIRRI ISEDDAPAEPAAEAAPPPPP EPEPEPVSFDDEVLELTDPI APEPELPPLETVGDIDVYSP PEPESEPAYTPPPAAPVFDR DEVAEQLVGVSAASAAASAF GSLSSALLMPKDGLEHHHHH H

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	423
15N chemical shifts	104
1H chemical shifts	480

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 141 residues - 14988.290 Da.

1

MET

SER

ASP

GLN

SER

GLN

GLU

PRO

THR

MET

2

GLU

ILE

LEU

ALA

SER

ILE

ARG

ILE

3

ILE

SER

GLU

ASP

ALA

PRO

ALA

GLU

PRO

4

ALA

GLU

ALA

PRO

5

GLU

PRO

GLU

PRO

GLU

PRO

VAL

SER

PHE

ASP

6

ASP

GLU

VAL

LEU

GLU

LEU

THR

ASP

PRO

ILE

7

ALA

PRO

GLU

PRO

GLU

LEU

PRO

LEU

GLU

8

THR

VAL

GLY

ASP

ILE

ASP

VAL

TYR

SER

PRO

9

PRO

GLU

PRO

GLU

SER

GLU

PRO

ALA

TYR

THR

10

PRO

ALA

PRO

VAL

PHE

ASP

ARG

11

ASP

GLU

VAL

ALA

GLU

GLN

LEU

VAL

GLY

VAL

12

SER

ALA

SER

ALA

SER

ALA

PHE

13

GLY

SER

LEU

SER

ALA

LEU

MET

PRO

14

LYS

ASP

GLY

LEU

GLU

HIS

15

HIS

Samples:

sample_1: Polar organizing protein Z, [U-99% 13C; U-99% 15N], 913 uM; NaCl 20 mM

sample_2: Polar organizing protein Z, [U-99% 15N], 142 uM; acrylamide gel with 5.4 mm outer diameter 5.4%; NaCl 20 mM

sample_3: Polar organizing protein Z, [U-99% 15N], 142 uM; acrylamide gel with 6.0 mm outer diameter 5.4%; NaCl 20 mM

sample_4: Polar organizing protein Z, [U-99% 15N], 142 uM; NaCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1.0 atm; temperature: 298 K

sample_conditions_2: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHANH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	anisotropic	sample_conditions_2
2D 1H-15N HSQC	sample_3	anisotropic	sample_conditions_3
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_4

Software:

TopSpin, Bruker Biospin - collection

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

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

NMRFAM-SPARKY v1.41, Lee, Tonelli, and Markley - chemical shift assignment

PONDEROSA-C/S, Lee, Stark, and Markley - data analysis, refinement, structure calculation

NMRFAM-SPARKY, Lee, Tonelli, and Markley - peak picking

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 700 MHz

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