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NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310
Authors
Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G.
Assembly
E. coli Trigger Factor in complex with unfolded PhoA220-310
Entity
1. E. coli Trigger Factor in complex with unfolded PhoA220-310, entity 1 (polymer, Thiol state: all free), 93 monomers, 9854.951 Da Detail

HMARADVTLG GGAKTFAETA TAGEWQGKTL REQAQARGYQ LVSDAASLNS VTEANQQKPL LGLFADGNMP VRWLGPKATY HGNIDKPAVT CTP


2. E. coli Trigger Factor in complex with unfolded PhoA220-310, entity 2 (polymer, Thiol state: not present), 443 monomers, 49624.62 Da Detail

MNHKVHHHHH HMQVSVETTQ GLGRRVTITI AADSIETAVK SELVNVAKKV RIDGFRKGKV PMNIVAQRYG ASVRQDVLGD LMSRNFIDAI IKEKINPAGA PTYVPGEYKL GEDFTYSVEF EVYPEVELQG LEAIEVEKPI VEVTDADVDG MLDTLRKQQA TWKEKDGAVE AEDRVTIDFT GSVDGEEFEG GKASDFVLAM GQGRMIPGFE DGIKGHKAGE EFTIDVTFPE EYHAENLKGK AAKFAINLKK VEERELPELT AEFIKRFGVE DGSVEGLRAE VRKNMERELK SAIRNRVKSQ AIEGLVKAND IDVPAALIDS EIDVLRRQAA QRFGGNEKQA LELPRELFEE QAKRRVVVGL LLGEVIRTNE LKADEERVKG LIEEMASAYE DPKEVIEFYS KNKELMDNMR NVALEEQAVE AVLAKAKVTE KETTFNELMN QQA


Total weight
59479.57 Da
Max. entity weight
49624.62 Da
Source organism
Escherichia coli BL21(DE3)
Exptl. method
solution NMR
Refine. method
molecular dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 79.7 %, Completeness: 40.7 %, Completeness (bb): 45.8 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All40.7 % (2507 of 6162)40.1 % (1288 of 3210)33.5 % (799 of 2387)74.3 % (420 of 565)
Backbone45.8 % (1458 of 3182)53.3 % (585 of 1097)29.4 % (461 of 1566)79.4 % (412 of 519)
Sidechain35.1 % (1221 of 3474)32.9 % (695 of 2113)39.4 % (518 of 1315)17.4 % (8 of 46)
Aromatic28.9 % (101 of 350)29.1 % (51 of 175)28.5 % (49 of 172)33.3 % (1 of 3)
Methyl70.7 % (437 of 618)70.9 % (219 of 309)70.6 % (218 of 309)

1. entity 1

HMARADVTLG GGAKTFAETA TAGEWQGKTL REQAQARGYQ LVSDAASLNS VTEANQQKPL LGLFADGNMP VRWLGPKATY HGNIDKPAVT CTP

2. entity 2

MNHKVHHHHH HMQVSVETTQ GLGRRVTITI AADSIETAVK SELVNVAKKV RIDGFRKGKV PMNIVAQRYG ASVRQDVLGD LMSRNFIDAI IKEKINPAGA PTYVPGEYKL GEDFTYSVEF EVYPEVELQG LEAIEVEKPI VEVTDADVDG MLDTLRKQQA TWKEKDGAVE AEDRVTIDFT GSVDGEEFEG GKASDFVLAM GQGRMIPGFE DGIKGHKAGE EFTIDVTFPE EYHAENLKGK AAKFAINLKK VEERELPELT AEFIKRFGVE DGSVEGLRAE VRKNMERELK SAIRNRVKSQ AIEGLVKAND IDVPAALIDS EIDVLRRQAA QRFGGNEKQA LELPRELFEE QAKRRVVVGL LLGEVIRTNE LKADEERVKG LIEEMASAYE DPKEVIEFYS KNKELMDNMR NVALEEQAVE AVLAKAKVTE KETTFNELMN QQA

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 7


#NameIsotope labelingTypeConcentration
1entity_1[U-100% 13C; U-100% 15N]0.5 mM
2entity_2[U-100% 13C; U-100% 15N]0.5 mM
3potassium chloridenatural abundance100 mM
4BMEnatural abundance3 mM
5potassium phosphatenatural abundance20 mM
6H2Onatural abundance90 %
7D2Onatural abundance10 %

Chem. Shift Complete2
Sequence coverage: 32.1 %, Completeness: 28.8 %, Completeness (bb): 33.0 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All28.8 % (3547 of 12324)28.6 % (1838 of 6420)23.9 % (1143 of 4774)50.1 % (566 of 1130)
Backbone33.0 % (2099 of 6364)38.5 % (844 of 2194)22.3 % (698 of 3132)53.7 % (557 of 1038)
Sidechain24.2 % (1681 of 6948)23.2 % (980 of 4226)26.3 % (692 of 2630) 9.8 % (9 of 92)
Aromatic18.9 % (132 of 700)20.6 % (72 of 350)17.2 % (59 of 344)16.7 % (1 of 6)
Methyl47.6 % (588 of 1236)48.2 % (298 of 618)46.9 % (290 of 618)

1. entity 1

HMARADVTLG GGAKTFAETA TAGEWQGKTL REQAQARGYQ LVSDAASLNS VTEANQQKPL LGLFADGNMP VRWLGPKATY HGNIDKPAVT CTP

2. entity 2

MNHKVHHHHH HMQVSVETTQ GLGRRVTITI AADSIETAVK SELVNVAKKV RIDGFRKGKV PMNIVAQRYG ASVRQDVLGD LMSRNFIDAI IKEKINPAGA PTYVPGEYKL GEDFTYSVEF EVYPEVELQG LEAIEVEKPI VEVTDADVDG MLDTLRKQQA TWKEKDGAVE AEDRVTIDFT GSVDGEEFEG GKASDFVLAM GQGRMIPGFE DGIKGHKAGE EFTIDVTFPE EYHAENLKGK AAKFAINLKK VEERELPELT AEFIKRFGVE DGSVEGLRAE VRKNMERELK SAIRNRVKSQ AIEGLVKAND IDVPAALIDS EIDVLRRQAA QRFGGNEKQA LELPRELFEE QAKRRVVVGL LLGEVIRTNE LKADEERVKG LIEEMASAYE DPKEVIEFYS KNKELMDNMR NVALEEQAVE AVLAKAKVTE KETTFNELMN QQA

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 7


#NameIsotope labelingTypeConcentration
1entity_1[U-100% 13C; U-100% 15N]0.5 mM
2entity_2[U-100% 13C; U-100% 15N]0.5 mM
3potassium chloridenatural abundance100 mM
4BMEnatural abundance3 mM
5potassium phosphatenatural abundance20 mM
6H2Onatural abundance90 %
7D2Onatural abundance10 %

Protein Blocks Logo
Calculated from 10 models in PDB: 2MLX, Strand ID: A, B Detail


Release date
2014-05-19
Citation
Structural basis for protein antiaggregation activity of the trigger factor chaperone
Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G.
Science (2014), 344, 1250494-1250494, PubMed 24812405 , DOI 10.1126/science.1250494 ,
Entries sharing articles BMRB: 2 entries Detail
  BMRB: 19836 released on 2014-05-19
    Title NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150
  BMRB: 19837 released on 2014-05-19
    Title NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471
Related entities 1. E. coli Trigger Factor in complex with unfolded PhoA220-310, entity 1, : 1 : 37 : 19 entities Detail
Related entities 2. E. coli Trigger Factor in complex with unfolded PhoA220-310, entity 2, : 2 : 4 entities Detail
Interaction partners 1. E. coli Trigger Factor in complex with unfolded PhoA220-310, entity 1, : 8 interactors Detail
Experiments performed 9 experiments Detail
NMR combined restraints 6 contents Detail
Keywords molecular chaperone, protein complex, solution NMR, unfolded protein