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Biological Magnetic Resonance Data Bank


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BMRB Entry 18673

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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/BMR18673
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Title: Solution NMR structure of a potential acylphosphatase from Giardia lamblia, Seattle Structural Genomics Center for Infectious Disease target GilaA.01396.a

Deposition date: 2012-08-20 Original release date: 2012-09-25

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephan; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Solution structure of an acylphosphatase from Giardia lamblia, the etiological agent responsible for giardiasis"  Not known ., .-..

Assembly members:
entity, polymer, 121 residues, 13221.998 Da.

Natural source:   Common Name: Giardia intestinalis ATCC 50803   Taxonomy ID: 184922   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Giardia lamblia

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

Entity Sequences (FASTA):
entity: MAHHHHHHMGTLEAQTQGPG SMQGSMPSSSEDVTTLCYRV TGKVQGVFFRKYTKKEADAL SLVGYVTNNEDGSVSGVVQG PKEQVDAFVKYLHKGSPKSV VKKVSIHASSRVDADGFEIR R

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts99
1H chemical shifts598

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1potential acylphosphatase from Giardia lamblia1

Entities:

Entity 1, potential acylphosphatase from Giardia lamblia 121 residues - 13221.998 Da.

Residues 1-21 are non-native residues added to the protein to facilitate purification.

1   METALAHISHISHISHISHISHISMETGLY
2   THRLEUGLUALAGLNTHRGLNGLYPROGLY
3   SERMETGLNGLYSERMETPROSERSERSER
4   GLUASPVALTHRTHRLEUCYSTYRARGVAL
5   THRGLYLYSVALGLNGLYVALPHEPHEARG
6   LYSTYRTHRLYSLYSGLUALAASPALALEU
7   SERLEUVALGLYTYRVALTHRASNASNGLU
8   ASPGLYSERVALSERGLYVALVALGLNGLY
9   PROLYSGLUGLNVALASPALAPHEVALLYS
10   TYRLEUHISLYSGLYSERPROLYSSERVAL
11   VALLYSLYSVALSERILEHISALASERSER
12   ARGVALASPALAASPGLYPHEGLUILEARG
13   ARG

Samples:

sample_1: GilaA, [U-99% 13C; U-99% 15N], 1.5 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; H2O 93%; D2O 7%

sample_2: GilaA, [U-99% 13C; U-99% 15N], 1.5 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - data analysis, peak picking

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

FELIX v2007, Accelrys Software Inc. - processing

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

PSVS v1.3, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
GB EDO78469 ESU35281
REF XP_001706143

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