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Solution structure for human HSP70 substrate binding domain L542Y mutant
Authors
Hoshikawa, M., Tochio, N., Tate, S.
Assembly
Heat shock 70 kDa protein 1A
Entity
1. Heat shock 70 kDa protein 1A (polymer, Thiol state: not present), 185 monomers, 20349.68 Da Detail

HMGDKSENVQ DLLLLDVAPL SLGLETAGGV MTALIKRNST IPTKQTQIFT TYSDNQPGVL IQVYEGERAM TKDNNLLGRF ELSGIPPAPR GVPQIEVTFD IDANGILNVT ATDKSTGKAN KITITNDKGR LSKEEIERMV QEAEKYKAED EVQRERVSAK NAYESYAFNM KSAVEDEGLK GKISE


Formula weight
20349.68 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 97.8 %, Completeness: 88.0 %, Completeness (bb): 95.8 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All88.0 % (1860 of 2113)81.8 % (902 of 1103)94.6 % (769 of 813)95.9 % (189 of 197)
Backbone95.8 % (1050 of 1096)93.6 % (353 of 377)96.9 % (524 of 541)97.2 % (173 of 178)
Sidechain82.2 % (976 of 1188)75.6 % (549 of 726)92.8 % (411 of 443)84.2 % (16 of 19)
Aromatic95.2 % (80 of 84)95.2 % (40 of 42)95.2 % (40 of 42)
Methyl92.0 % (195 of 212)90.6 % (96 of 106)93.4 % (99 of 106)

1. Heat shock 70 kDa protein 1A

HMGDKSENVQ DLLLLDVAPL SLGLETAGGV MTALIKRNST IPTKQTQIFT TYSDNQPGVL IQVYEGERAM TKDNNLLGRF ELSGIPPAPR GVPQIEVTFD IDANGILNVT ATDKSTGKAN KITITNDKGR LSKEEIERMV QEAEKYKAED EVQRERVSAK NAYESYAFNM KSAVEDEGLK GKISE

Sample

Solvent system 94% H2O/6% D2O, Pressure 1 atm, Temperature 310 K, pH 7.0, Details 50 mM potassium phosphate, 50 mM potassium chloride, 10 mM DTT, 94% H2O/6% D2O


#NameIsotope labelingTypeConcentration
1human HSP70 substrate binding domain L542Y mutantprotein0.0 ~ 0.0 mM
2DTTnatural abundance10 mM
3potassium chloridenatural abundance50 mM
4potassium phosphatenatural abundance50 mM

LACS Plot; CA
Referencing offset: -0.06 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.06 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: -0.04 ppm, Outliers: 2 Detail
LACS Plot; CO
Referencing offset: 0.23 ppm, Outliers: 2 Detail
Release date
2017-07-05
Citation
Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication
Umehara, K., Hoshikawa, M., Tochio, N., Tate, S.I.
Molecules (2018), 23, E528-E528, PubMed 29495458 , DOI 10.3390/molecules23030528 ,
Related entities 1. Heat shock 70 kDa protein 1A, : 1 : 7 : 285 entities Detail
Interaction partners 1. Heat shock 70 kDa protein 1A, : 2 interactors Detail
Experiments performed 15 experiments Detail
NMR combined restraints 4 contents Detail
Keywords apo state, heat shock protein 70 kDa