BMRB Entry 30773

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PDB ID:
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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Title:
Intrinsically disordered bacterial polar organizing protein Z, PopZ, interacts with protein binding partners through an N-terminal Molecular Recognition Feature
Deposition date:
2020-07-14
Original release date:
2020-10-30
Authors:
Nordyke, C.; Ahmed, Y.; Puterbaugh, R.; Bowman, G.; Varga, K.
Citation:

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).
PubMed: 33058876

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts104
1H chemical shifts480

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 141 residues - 14988.290 Da.

1   METSERASPGLNSERGLNGLUPROTHRMET
2   GLUGLUILELEUALASERILEARGARGILE
3   ILESERGLUASPASPALAPROALAGLUPRO
4   ALAALAGLUALAALAPROPROPROPROPRO
5   GLUPROGLUPROGLUPROVALSERPHEASP
6   ASPGLUVALLEUGLULEUTHRASPPROILE
7   ALAPROGLUPROGLULEUPROPROLEUGLU
8   THRVALGLYASPILEASPVALTYRSERPRO
9   PROGLUPROGLUSERGLUPROALATYRTHR
10   PROPROPROALAALAPROVALPHEASPARG
11   ASPGLUVALALAGLUGLNLEUVALGLYVAL
12   SERALAALASERALAALAALASERALAPHE
13   GLYSERLEUSERSERALALEULEUMETPRO
14   LYSASPGLYLEUGLUHISHISHISHISHIS
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_2
2D 1H-15N HSQCsample_3anisotropicsample_conditions_3
2D 1H-15N HSQCsample_4isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks