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Backbone 1H, 13C and 15N Chemical Shift Assignments of Ezrin C ERMAD in a non-covalent complex with Ezrin N FERM
Authors
Jayaraman, B., Nicholson, L.K.
Assembly
Ezrin FERM C ERMAD Complex
Entity
1. C ERMAD (polymer, Thiol state: not present), 112 monomers, 13140.15 Da Detail

PPVYEPVSYH VQESLQDEGA EPTGYSAELS SEGIRDDRNE EKRITEAEKN ERVQRQLLTL SSELSQARDE NKRTHNDIIH NENMRQGRDK YKTLRQIRQG NTKQRIDEFE AL


2. N FERM (polymer, Thiol state: unknown), 295 monomers, 34797.82 Da Detail

PKPINVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTIGLRE VWYFGLHYVD NKGFPTWLKL DKKVSAQEVR KENPLQFKFR AKFYPEDVAE ELIQDITQKL FFLQVKEGIL SDEIYCPPET AVLLGSYAVQ AKFGDYNKEV HKSGYLSSER LIPQRVMDQH KLTRDQWEDR IQVWHAEHRG MLKDNAMLEY LKIAQDLEMY GINYFEIKNK KGTDLWLGVD ALGLNIYEKD DKLTPKIGFP WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL QLCMGNHELY MRRRK


Total weight
47937.97 Da
Max. entity weight
34797.82 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 28.7 %, Completeness: 11.5 %, Completeness (bb): 21.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All11.5 % (579 of 5028) 5.9 % (158 of 2657)16.4 % (317 of 1932)23.7 % (104 of 439)
Backbone21.9 % (526 of 2406)14.2 % (116 of 816)25.5 % (306 of 1201)26.7 % (104 of 389)
Sidechain 4.9 % (147 of 3009) 2.3 % (43 of 1841) 9.3 % (104 of 1118) 0.0 % (0 of 50)
Aromatic 0.0 % (0 of 414) 0.0 % (0 of 207) 0.0 % (0 of 201) 0.0 % (0 of 6)
Methyl 3.9 % (16 of 412) 2.9 % (6 of 206) 4.9 % (10 of 206)

1. C ERMAD

PPVYEPVSYH VQESLQDEGA EPTGYSAELS SEGIRDDRNE EKRITEAEKN ERVQRQLLTL SSELSQARDE NKRTHNDIIH NENMRQGRDK YKTLRQIRQG NTKQRIDEFE AL

2. N FERM

PKPINVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTIGLRE VWYFGLHYVD NKGFPTWLKL DKKVSAQEVR KENPLQFKFR AKFYPEDVAE ELIQDITQKL FFLQVKEGIL SDEIYCPPET AVLLGSYAVQ AKFGDYNKEV HKSGYLSSER LIPQRVMDQH KLTRDQWEDR IQVWHAEHRG MLKDNAMLEY LKIAQDLEMY GINYFEIKNK KGTDLWLGVD ALGLNIYEKD DKLTPKIGFP WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL QLCMGNHELY MRRRK

Sample

Temperature 303 (±2) K, pH 5.7 (±0.1)


#NameIsotope labelingTypeConcentration
1C ERMAD[U-99% 13C; U-99% 15N; U-95% 2H]protein0.5 mM
2N FERMnatural abundanceprotein0.5 mM
3Acetic Acidnatural abundancebuffer10 mM
4Sodium Acetatenatural abundancebuffer90 mM
5DTTnatural abundancebuffer5 mM
6Sodium Azidenatural abundancebuffer15 mM
7Protease inhibitorsnatural abundance0.0 ~ 0.0 mM

LACS Plot; CA
Referencing offset: -0.37 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.37 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: -0.17 ppm, Outliers: 1 Detail
Release date
2006-10-01
Citation
Backbone resonance assignments of Ezrin C ERMAD in a non-covalent complex with Ezrin N FERM
Jayaraman, B., Nicholson, L.K.
J. Biomol. NMR (2006), 36 Suppl 1, 63-63, PubMed 17131035 , DOI 10.1007/s10858-006-9049-2 ,
Related entities 1. C ERMAD, : 2 : 20 entities Detail
Related entities 2. N FERM, : 1 : 94 entities Detail
Interaction partners 1. C ERMAD, : 51 interactors Detail
Experiments performed 7 experiments Detail
Chemical shift validation 4 contents Detail