BMRB Entry 17014

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17014
MolProbity Validation Chart

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Title:
Backbone 1H,13C and 15N assignments of ChxR
Deposition date:
2010-06-22
Original release date:
2014-03-24
Authors:
Hickey, John; Hefty, Scott
Citation:

Citation: Barta, Michael; Hickey, John; Anbanandam, Asokan; Dyer, Kevin; Hammel, Michal; Hefty, P Scott. "Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding."  PLoS ONE 9, e91760-e91760 (2014).
PubMed: 24646934

Assembly members:

Assembly members:
ChxR_effector_domain, polymer, 116 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ChxR_effector_domain: HSVPESIRFGPNVFYVLKLT VETPEGSVHLTPSESGILKR LLINKGQLCLRKHLLEEIKN HAKAIVARNVDVHIASLRKK LGAYGSRIVTLRGVGYLFSD DGDKKFSQQDTKLSLE

Data sets:
Data typeCount
13C chemical shifts452
15N chemical shifts111
1H chemical shifts728

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1ChxR monomer1

Entities:

Entity 1, ChxR monomer 116 residues - Formula weight is not available

1   HISSERVALPROGLUSERILEARGPHEGLY
2   PROASNVALPHETYRVALLEULYSLEUTHR
3   VALGLUTHRPROGLUGLYSERVALHISLEU
4   THRPROSERGLUSERGLYILELEULYSARG
5   LEULEUILEASNLYSGLYGLNLEUCYSLEU
6   ARGLYSHISLEULEUGLUGLUILELYSASN
7   HISALALYSALAILEVALALAARGASNVAL
8   ASPVALHISILEALASERLEUARGLYSLYS
9   LEUGLYALATYRGLYSERARGILEVALTHR
10   LEUARGGLYVALGLYTYRLEUPHESERASP
11   ASPGLYASPLYSLYSPHESERGLNGLNASP
12   THRLYSLEUSERLEUGLU

Samples:

sample_1: ChxR effector domain, [U-100% 13C; U-100% 15N], 1.0 mM; NaCl 400 mM; Na2HPO4 20 mM; KH2PO4 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAP04331 CAP07285 CAX09301 CAX10195 CAX11088
GB AAC68234 AAX50907 ADH17418 ADH18341 ADH19265
REF NP_220147 WP_009871999 WP_009872804 WP_009873961 WP_010725282
SP A0A0H3MDW1
AlphaFold A0A0H3MDW1

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