BMRB Entry 17005

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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/BMR17005
MolProbity Validation Chart

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Title:
Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from Escherichia coli
Deposition date:
2010-06-17
Original release date:
2011-05-31
Authors:
Setiyaputra, Surya; Mackay, Joel; Patrick, Wayne
Citation:

Citation: Setiyaputra, Surya; Mackay, Joel; Patrick, Wayne. "The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the ()8 barrel fold."  J. Mol. Biol. 408, 291-303 (2011).
PubMed: 21354426

Assembly members:

Assembly members:
trPRAI, polymer, 134 residues, 14308.270 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pWP107

Entity Sequences (FASTA):

Entity Sequences (FASTA):
trPRAI: MGENKVCGLTRGQDAKAAYD AGAIYGGLIFVATSPRCVNV EQAQEVMAAAPLQYVGVFRN HDIADVVDKAKVLSLAAVQL HGNEEQLYIDTLREALPAHV AIWKALSVGETLPAREFQHV DKYVLDNGQGGAGS

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts137
1H chemical shifts842
coupling constants74

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1trPRAI1

Entities:

Entity 1, trPRAI 134 residues - 14308.270 Da.

Residue 132-134 are cloning artifacts from the plasmid display selection and not part of the original sequence of PRAI from E.coli

1   METGLYGLUASNLYSVALCYSGLYLEUTHR
2   ARGGLYGLNASPALALYSALAALATYRASP
3   ALAGLYALAILETYRGLYGLYLEUILEPHE
4   VALALATHRSERPROARGCYSVALASNVAL
5   GLUGLNALAGLNGLUVALMETALAALAALA
6   PROLEUGLNTYRVALGLYVALPHEARGASN
7   HISASPILEALAASPVALVALASPLYSALA
8   LYSVALLEUSERLEUALAALAVALGLNLEU
9   HISGLYASNGLUGLUGLNLEUTYRILEASP
10   THRLEUARGGLUALALEUPROALAHISVAL
11   ALAILETRPLYSALALEUSERVALGLYGLU
12   THRLEUPROALAARGGLUPHEGLNHISVAL
13   ASPLYSTYRVALLEUASPASNGLYGLNGLY
14   GLYALAGLYSER

Samples:

sample_1: trPRAI 0.8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_2: trPRAI, [U-99% 15N], .6 – 1 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_3: trPRAI, [U-98% 13C; U-98% 15N], .6 – .8 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; H2O 95%; D2O 5%

sample_4: trPRAI, [U-98% 13C; U-98% 15N], 0.7 mM; HEPES 20 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D 1H-13C NOESY AROMATICsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - automated NOE peak assignments, NOE peaks calibration

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

TALOS vTALOS+, Cornilescu, Delaglio and Bax - prediction of protein backbone torsion angles from NMR chemical shifts

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution, water refinement

ProcheckNMR v3.5.3, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA14794 BAG66423 BAG76835 BAI25111 BAI30254
EMBL CAA23664 CAQ31763 CAQ98141 CAU97277 CBJ00867
GB AAA57299 AAA65138 AAA65144 AAA65150 AAA65156
REF NP_415778 NP_707171 WP_000983871 WP_000983893 WP_001195309
SP P00909
AlphaFold P00909

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