BMRB Entry 17818

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17818
MolProbity Validation Chart

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Title:
Solution NMR structure of a FKBP-type peptidyl-prolyl cis-trans isomerase from Giardia lamblia. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target GilaA.00840.a
Deposition date:
2011-07-29
Original release date:
2011-08-17
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Hewitt, Stephen; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia."  J. Biomol. NMR 57, 369-374 (2013).
PubMed: 24293257

Assembly members:

Assembly members:
FKBP, polymer, 130 residues, 14160.289 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP: MAHHHHHHMGTLEAQTQGPG SMSAQLEKKVLTPGDGVTKP QAGKKVTVHYDGRFPDGKQF DSSRSRGKPFQFTLGAGEVI KGWDQGVATMTLGEKALFTI PYQLAYGERGYPPVIPPKAT LVFEVELLAV

Data sets:
Data typeCount
13C chemical shifts378
15N chemical shifts116
1H chemical shifts726

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP1

Entities:

Entity 1, FKBP 130 residues - 14160.289 Da.

The first 21 residues are a tag for protein isolation (MAHHHHHHMGTLEAQTQGPGS). The first native residue is M22.

1   METALAHISHISHISHISHISHISMETGLY
2   THRLEUGLUALAGLNTHRGLNGLYPROGLY
3   SERMETSERALAGLNLEUGLULYSLYSVAL
4   LEUTHRPROGLYASPGLYVALTHRLYSPRO
5   GLNALAGLYLYSLYSVALTHRVALHISTYR
6   ASPGLYARGPHEPROASPGLYLYSGLNPHE
7   ASPSERSERARGSERARGGLYLYSPROPHE
8   GLNPHETHRLEUGLYALAGLYGLUVALILE
9   LYSGLYTRPASPGLNGLYVALALATHRMET
10   THRLEUGLYGLULYSALALEUPHETHRILE
11   PROTYRGLNLEUALATYRGLYGLUARGGLY
12   TYRPROPROVALILEPROPROLYSALATHR
13   LEUVALPHEGLUVALGLULEULEUALAVAL

Samples:

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

sample_2: FKBP, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 mM; TRIS 20 mM; DTT 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
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_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
deuterium exchangesample_2isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D HBCBCGCDCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

FELIX v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

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

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAM33435 EDO81467 EET00236 EFO62827 ESU38634
REF XP_001709141

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