Search

Backbone and side chain chemical shift assignments of apo calmodulin bound to the NaV1.2 IQ motif peptide
Authors
Mahling, R., Kilpatrick, A.M., Shea, M.A.
Assembly
CaM NaV1.2 IQ motif
Entity
1. Calmodulin (polymer, Thiol state: not present), 148 monomers, 16706.21 × 2 Da Detail

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK


2. Voltage-gated sodium channel NaV1-2 IQ motif peptide (polymer, Thiol state: not present), 31 monomers, 3672.329 × 2 Da Detail

GPGSKRKQEE VSAIIIQRAY RRYLLKQKVK K


Total weight
40757.08 Da
Max. entity weight
16706.21 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
molecular dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 83.2 %, Completeness: 75.4 %, Completeness (bb): 81.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All75.4 % (1563 of 2074)71.6 % (778 of 1087)79.5 % (633 of 796)79.6 % (152 of 191)
Backbone81.4 % (869 of 1068)80.7 % (297 of 368)81.9 % (429 of 524)81.3 % (143 of 176)
Sidechain70.9 % (831 of 1172)66.9 % (481 of 719)77.9 % (341 of 438)60.0 % (9 of 15)
Aromatic81.9 % (95 of 116)84.5 % (49 of 58)79.3 % (46 of 58)
Methyl80.5 % (140 of 174)81.6 % (71 of 87)79.3 % (69 of 87)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. Voltage-gated sodium channel NaV1-2 IQ motif peptide

GPGSKRKQEE VSAIIIQRAY RRYLLKQKVK K

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1Calmodulin[U-99% 13C; U-99% 15N]0.95 mM
2Voltage-gated sodium channel NaV1.2 IQ motif peptide[U-99% 13C; U-99% 15N]0.95 mM
3imidazole[U-99% 2H]10 mM
4potassium chloridenatural abundance100 mM
5EDTAnatural abundance0.1 mM
6sodium azidenatural abundance0.01 %

Chem. Shift Complete2
Sequence coverage: 35.2 %, Completeness: 52.6 %, Completeness (bb): 57.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All52.6 % (2180 of 4148)50.1 % (1089 of 2174)55.1 % (877 of 1592)56.0 % (214 of 382)
Backbone57.3 % (1224 of 2136)56.8 % (418 of 736)57.5 % (603 of 1048)57.7 % (203 of 352)
Sidechain48.9 % (1147 of 2344)46.7 % (671 of 1438)53.1 % (465 of 876)36.7 % (11 of 30)
Aromatic48.3 % (112 of 232)50.0 % (58 of 116)46.6 % (54 of 116)
Methyl52.0 % (181 of 348)52.9 % (92 of 174)51.1 % (89 of 174)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. Voltage-gated sodium channel NaV1-2 IQ motif peptide

GPGSKRKQEE VSAIIIQRAY RRYLLKQKVK K

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1Calmodulin[U-99% 13C; U-99% 15N]0.95 mM
2Voltage-gated sodium channel NaV1.2 IQ motif peptide[U-99% 13C; U-99% 15N]0.95 mM
3imidazole[U-99% 2H]10 mM
4potassium chloridenatural abundance100 mM
5EDTAnatural abundance0.1 mM
6sodium azidenatural abundance0.01 %

Chem. Shift Complete3
Sequence coverage: 30.7 %, Completeness: 42.1 %, Completeness (bb): 46.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All42.1 % (2618 of 6222)40.6 % (1323 of 3261)43.5 % (1038 of 2388)44.9 % (257 of 573)
Backbone46.3 % (1483 of 3204)46.1 % (509 of 1104)46.3 % (728 of 1572)46.6 % (246 of 528)
Sidechain38.9 % (1367 of 3516)37.7 % (814 of 2157)41.2 % (542 of 1314)24.4 % (11 of 45)
Aromatic36.5 % (127 of 348)40.2 % (70 of 174)32.8 % (57 of 174)
Methyl41.8 % (218 of 522)42.9 % (112 of 261)40.6 % (106 of 261)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. Voltage-gated sodium channel NaV1-2 IQ motif peptide

GPGSKRKQEE VSAIIIQRAY RRYLLKQKVK K

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1Calmodulin[U-99% 13C; U-99% 15N]0.95 mM
2Voltage-gated sodium channel NaV1.2 IQ motif peptide[U-99% 13C; U-99% 15N]0.95 mM
3imidazole[U-99% 2H]10 mM
4potassium chloridenatural abundance100 mM
5EDTAnatural abundance0.1 mM
6sodium azidenatural abundance0.01 %

Chem. Shift Complete4
Sequence coverage: 27.4 %, Completeness: 36.3 %, Completeness (bb): 40.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All36.3 % (3009 of 8296)35.4 % (1538 of 4348)36.7 % (1170 of 3184)39.4 % (301 of 764)
Backbone40.2 % (1718 of 4272)40.9 % (602 of 1472)39.5 % (827 of 2096)41.1 % (289 of 704)
Sidechain33.3 % (1559 of 4688)32.5 % (936 of 2876)34.9 % (611 of 1752)20.0 % (12 of 60)
Aromatic31.9 % (148 of 464)35.8 % (83 of 232)28.0 % (65 of 232)
Methyl35.8 % (249 of 696)37.1 % (129 of 348)34.5 % (120 of 348)

1. Calmodulin

ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE VDEMIREADI DGDGQVNYEE FVQMMTAK

2. Voltage-gated sodium channel NaV1-2 IQ motif peptide

GPGSKRKQEE VSAIIIQRAY RRYLLKQKVK K

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.5


#NameIsotope labelingTypeConcentration
1Calmodulin[U-99% 13C; U-99% 15N]0.95 mM
2Voltage-gated sodium channel NaV1.2 IQ motif peptide[U-99% 13C; U-99% 15N]0.95 mM
3imidazole[U-99% 2H]10 mM
4potassium chloridenatural abundance100 mM
5EDTAnatural abundance0.1 mM
6sodium azidenatural abundance0.01 %

Protein Blocks Logo
Calculated from 20 models in PDB: 6BUT, Strand ID: A, B Detail


Release date
2017-05-07
Citation
Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaV1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin
Mahling, R., Kilpatrick, A.M., Shea, M.A.
Biomol. NMR Assign. (2017), 11, 297-303, PubMed 28823028 , DOI 10.1007/s12104-017-9767-2 ,
Related entities 1. Calmodulin, : 11 : 88 entities Detail
Related entities 2. Voltage-gated sodium channel NaV1-2 IQ motif peptide, : 1 : 3 : 71 entities Detail
Experiments performed 4 experiments Detail
null