BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15066

Title: apo-PGG/GGG chicken Triosephosphate Isomerase (TIM)   PubMed: 17336327

Authors: Kempf, James; Jung, Ju-yeon; Ragain, Christina; Sampson, Nicole; Loria, Pat

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).

Assembly members:
PGG/GGG_mono, polymer, 248 residues, 26620 Da.

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

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

Entity Sequences (FASTA):
PGG/GGG_mono: MAPRKFFVGGNWKMNGDKKS LGELIHTLNGAKLSADTEVV CGAPSIYLDFARQKLDAKIG VAAQNCYKVPKGAFTGEISP AMIKDIGAAWVILGHSERRH VFGESDELIGQKVAHALAEG LGVIACIGEKLDEREAGITE KVVFEQTKAIADNVKDWSKV VLAYEPGGAIGTGGGGTPQQ AQEVHEKLRGWLKSHVSDAV AQSTRIIYGGSVTGGNCKEL ASQHDVDGFLVGGASLKPEF VDIINAKH

Data sets:
Data typeCount
13C chemical shifts404
15N chemical shifts191
1H chemical shifts191
heteronuclear NOE values381
T1 relaxation values380
T2 relaxation values381

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PGG/GGG monomer 11
2PGG/GGG monomer 21

Entities:

Entity 1, PGG/GGG monomer 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   VALLEUALATYRGLUPROGLYGLYALAILE
18   GLYTHRGLYGLYGLYGLYTHRPROGLNGLN
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; U-99% 2H], 0.9 mM; D2O 7.5%; sodium azide 0.02%; sodium chloride 10 mM; MES, [U-2H], 10 mM

standard_conditions: ionic strength: . M; 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
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

SPARKY, Goddard - data analysis

NMR spectrometers:

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

Related Database Links:

BMRB 15064 15065 15067
PDB
EMBL CAE45562 CAE45563 CAE45564
GB AAA49094 AAA49095 KFP89361 KFP99577 KFQ92375
REF NP_990782 XP_009506417 XP_010147293 XP_010168177 XP_010716134
SP P00940