BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16428

Title: The structure of the KlcA and ArdB proteins show a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro.   PubMed: 20007596

Deposition date: 2009-07-28 Original release date: 2010-02-02

Authors: Serfiotis-Mitsa, Dimitra; Herbert, Andrew; Roberts, Gareth; Soares, Dinesh; White, John; Blakely, Garry; Uhrin, Dusan; Dryden, David

Citation: Serfiotis-Mitsa, Dimitra; Herbert, Andrew; Roberts, Gareth; Soares, Dinesh; White, John; Blakely, Garry; Uhrin, Dusan; Dryden, David. "The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro."  Nucleic Acids Res. 38, 1723-1737 (2010).

Assembly members:
KlcA and ArdB proteins, polymer, 142 residues, Formula weight is not available

Natural source:   Common Name: B. pertussis   Taxonomy ID: 520   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bordetella pertussis

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

Entity Sequences (FASTA):
KlcA and ArdB proteins: MNTEEQPVTASLVAEAQRLD FLPTYFGPRLMMRGEALVYA WMRRLCERYNGAYWHYYALS DGGFYMAPDLAGRLEIEVNG NGFRGELSADAAGIVATLFA LGQLAAEIADTDAADALIDR YHFLRGFAAGHPEAAAIYRA ID

Data sets:
Data typeCount
13C chemical shifts559
15N chemical shifts149
1H chemical shifts897
residual dipolar couplings110

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KlcA and ArdB proteins1

Entities:

Entity 1, KlcA and ArdB proteins 142 residues - Formula weight is not available

1   METASNTHRGLUGLUGLNPROVALTHRALA
2   SERLEUVALALAGLUALAGLNARGLEUASP
3   PHELEUPROTHRTYRPHEGLYPROARGLEU
4   METMETARGGLYGLUALALEUVALTYRALA
5   TRPMETARGARGLEUCYSGLUARGTYRASN
6   GLYALATYRTRPHISTYRTYRALALEUSER
7   ASPGLYGLYPHETYRMETALAPROASPLEU
8   ALAGLYARGLEUGLUILEGLUVALASNGLY
9   ASNGLYPHEARGGLYGLULEUSERALAASP
10   ALAALAGLYILEVALALATHRLEUPHEALA
11   LEUGLYGLNLEUALAALAGLUILEALAASP
12   THRASPALAALAASPALALEUILEASPARG
13   TYRHISPHELEUARGGLYPHEALAALAGLY
14   HISPROGLUALAALAALAILETYRARGALA
15   ILEASP

Samples:

sample_1: KlcA, [U-98% 13C; U-98% 15N], 0.7 mM; sodium acetate, [U-100% 2H], 20 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_2: KlcA, [U-98% 15N], 0.7 mM; sodium acetate, [U-100% 2H], 20 mM; sodium azide 0.05%; Pf1 phage 6.25 mg; H2O 90%; D2O 10%

sample_3: KlcA, [U-98% 15N], 0.7 mM; sodium acetate, [U-100% 2H], 20 mM; sodium azide 0.05%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (Aromatic Selective)sample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
T1sample_3isotropicsample_conditions_1
T2sample_3isotropicsample_conditions_1
Heteronuclear NOEsample_3isotropicsample_conditions_1
IPAP for RDC measurementsample_2anisotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ANALYSIS v1.0.15, CCPN - chemical shift assignment, data analysis, peak picking

AZARA v2.7, Boucher - processing

ProcheckNMR v3.5, Laskowski and MacArthur - Structure Validation

WhatIF, Vriend - Structure Validation

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

EMBL BAF33451.1
UNP Q08L07
PDB
DBJ BAF33451
REF WP_011666376 YP_787932

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