BMRB Entry 15064

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15064

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Title:
apo-WT chicken Triosephosphate Isomerase (TIM)
Deposition date:
2006-12-05
Original release date:
2007-02-22
Authors:
Kempf, James; Jung, Ju-yeon; Ragain, Christina; Sampson, Nicole; Loria, Pat
Citation:

Citation: Kempf, James; Jung, Ju-yeon; Ragain, Christina; Sampson, Nicole; Loria, J.. "Dynamic Requirements for a Functional Protein Hinge"  J. Mol. Biol. 368, 131-149 (2007).
PubMed: 17336327

Assembly members:

Assembly members:
triosephosphate_isomerase, polymer, 248 residues, 26620 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b/cTIM

Entity Sequences (FASTA):

Entity Sequences (FASTA):
triosephosphate_isomerase: MAPRKFFVGGNWKMNGDKKS LGELIHTLNGAKLSADTEVV CGAPSIYLDFARQKLDAKIG VAAQNCYKVPKGAFTGEISP AMIKDIGAAWVILGHSERRH VFGESDELIGQKVAHALAEG LGVIACIGEKLDEREAGITE KVVFEQTKAIADNVKDWSKV VLAYEPVWAIGTGKTATPQQ AQEVHEKLRGWLKSHVSDAV AQSTRIIYGGSVTGGNCKEL ASQHDVDGFLVGGASLKPEF VDIINAKH

Data sets:
Data typeCount
13C chemical shifts688
15N chemical shifts226
1H chemical shifts226
heteronuclear NOE values362
T1 relaxation values362
T2 relaxation values362

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WT TIM chain 11
2WT TIM chain 21

Entities:

Entity 1, WT TIM chain 1 248 residues - 26620 Da.

26.6kDa monomer of 53.1 kDa homodimer reported

1   METALAPROARGLYSPHEPHEVALGLYGLY
2   ASNTRPLYSMETASNGLYASPLYSLYSSER
3   LEUGLYGLULEUILEHISTHRLEUASNGLY
4   ALALYSLEUSERALAASPTHRGLUVALVAL
5   CYSGLYALAPROSERILETYRLEUASPPHE
6   ALAARGGLNLYSLEUASPALALYSILEGLY
7   VALALAALAGLNASNCYSTYRLYSVALPRO
8   LYSGLYALAPHETHRGLYGLUILESERPRO
9   ALAMETILELYSASPILEGLYALAALATRP
10   VALILELEUGLYHISSERGLUARGARGHIS
11   VALPHEGLYGLUSERASPGLULEUILEGLY
12   GLNLYSVALALAHISALALEUALAGLUGLY
13   LEUGLYVALILEALACYSILEGLYGLULYS
14   LEUASPGLUARGGLUALAGLYILETHRGLU
15   LYSVALVALPHEGLUGLNTHRLYSALAILE
16   ALAASPASNVALLYSASPTRPSERLYSVAL
17   VALLEUALATYRGLUPROVALTRPALAILE
18   GLYTHRGLYLYSTHRALATHRPROGLNGLN
19   ALAGLNGLUVALHISGLULYSLEUARGGLY
20   TRPLEULYSSERHISVALSERASPALAVAL
21   ALAGLNSERTHRARGILEILETYRGLYGLY
22   SERVALTHRGLYGLYASNCYSLYSGLULEU
23   ALASERGLNHISASPVALASPGLYPHELEU
24   VALGLYGLYALASERLEULYSPROGLUPHE
25   VALASPILEILEASNALALYSHIS

Samples:

2H_15N_sample: triosephosphate isomerase, [U-99% 15N; U-99%2H], 0.9 mM; D2O 7.5%; sodium azide 0.02%; sodium chloride 10 mM; MES, [U-2H], 10 mM

2H_13C_15N_sample: triosephosphate isomerase, [U-99% 13C; U-99% 15N; 70% 2H], 0.9 mM; D2O 7.5%; sodium azide 0.02%; sodium chloride 10 mM; MES, [U-2H], 10 mM

standard_conditions: pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCA2H_13C_15N_sampleisotropicstandard_conditions
3D HN(CO)CA2H_13C_15N_sampleisotropicstandard_conditions
3D HNCACB2H_13C_15N_sampleisotropicstandard_conditions
3D HN(CO)CACB2H_13C_15N_sampleisotropicstandard_conditions
3D HN(CA)CO2H_13C_15N_sampleisotropicstandard_conditions
3D HNCO2H_13C_15N_sampleisotropicstandard_conditions
1H-15N ssNOE2H_15N_sampleisotropicstandard_conditions
1H-15N T12H_15N_sampleisotropicstandard_conditions
1H-15N T22H_15N_sampleisotropicstandard_conditions

Software:

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

PISTACHIO, Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15065 15066 15067
PDB
EMBL CAE45562 CAE45563 CAE45564
GB AAA49094 AAA49095 ACH45461 ACH45462 ACH45463
REF NP_001232159 NP_990782 XP_005016819 XP_005235418 XP_005434378
SP P00940
AlphaFold P00940

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