BMRBj - BMREntryMaster

Found 1 Document (0.593 seconds)

BMRB: 30834

6LQA

NMR solution structure of Nav1.5 DIV S3b-S4a paddle motif in DPC micelle

Authors

Hussein, A.K., Bhuiyan, M.H., Arshava, B., Zhuang, J., Poget, S.F.

Assembly

Sodium channel protein type 5 subunit alpha

Entity

1. Sodium channel protein type 5 subunit alpha (polymer, Thiol state: not present), 37 monomers, 4204.097 Da Detail

VVVILSIVGT VLSDIIQKYF FSPTLFRVIR LARIGRI

Formula weight

4204.097 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 91.9 %, Completeness: 62.2 %, Completeness (bb): 73.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	62.2 % (290 of 466)	79.7 % (188 of 236)	38.1 % (72 of 189)	73.2 % (30 of 41)
Backbone	73.6 % (162 of 220)	88.0 % (66 of 75)	61.5 % (67 of 109)	80.6 % (29 of 36)
Sidechain	56.9 % (160 of 281)	75.8 % (122 of 161)	32.2 % (37 of 115)	20.0 % (1 of 5)
Aromatic	26.3 % (10 of 38)	52.6 % (10 of 19)	0.0 % (0 of 19)
Methyl	48.6 % (36 of 74)	81.1 % (30 of 37)	16.2 % (6 of 37)

1. entity 1

VVVILSIVGT VLSDIIQKYF FSPTLFRVIR LARIGRI

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 7 (±.05), Details 1 mM [U-13C; U-15N] Nav1.5 DIV S3bS4a motif, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	Nav1.5 DIV S3bS4a motif	[U-13C; U-15N]	1 (±0.1) mM
2	Nacl	natural abundance	10 mM
3	potassium phosphate	natural abundance	10 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 310 K, pH 7 (±.05), Details 0.5 mM [U-13C; U-15N] Nav1.5 DIV S3bS4a motif, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
4	Nav1.5 DIV S3bS4a motif	[U-13C; U-15N]	0.5 (±0.1) mM
5	Nacl	natural abundance	10 mM
6	potassium phosphate	natural abundance	10 mM

Heteronucl. T₁

33 T₁ values in 1 lists
Coherence Sz, Field strength (¹H) 800 MHz, Pressure 1 atm, Temperature 310 K, pH 7 (±.05) Detail

Heteronucl. T₂

33 T₂ values in 1 lists
Coherence S(+,-), Field strength (¹H) 800 MHz, Pressure 1 atm, Temperature 310 K, pH 7 (±.05) Detail

Heteronucl. NOE

33 NOE values in 1 lists
Value type peak height, Field strength (¹H) 800 MHz, Pressure 1 atm, Temperature 310 K, pH 7 (±.05) Detail

Heteronucl. T₁/T₂

33 T₁/T₂ values in 1 lists
Field strength (¹H) 800 MHz, Pressure 1 atm, Temperature 310 K, pH 7 (±.05) Detail

Release date

2021-01-28

Citation

NMR solution structure of the S3b-S4a paddle motif from repeat IV of the human cardiac sodium channel
Hussein, A.K., Bhuiyan, M.H., Arshava, B., Zhuang, J., Poget, S.F.

Related entities 1. Sodium channel protein type 5 subunit alpha, : 1 : 11 : 90 entities Detail

Interaction partners 1. Sodium channel protein type 5 subunit alpha, : 10 interactors Detail

More details for 10 interactors identified by 7 citations

Experiments performed 5 experiments Detail

Chemical shift validation 5 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data, Spectral peak lists	bmr30834_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr30834_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	349		91.9 (chain: 1, length: 37)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information
1	Spectral peak lists	spectral_peak_list_1	Error	219	.	86.5 (chain: 1, length: 37)
2	Spectral peak lists	spectral_peak_list_2	Error	3027	.	91.9 (chain: 1, length: 37)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 37, Sequence coverage: 91.9%
- Total number of assignments
  - ¹H chemical shifts: 248
  - ¹³C chemical shifts: 71
  - ¹⁵N chemical shifts: 30
- Completeness of assignments
  - Entity_assemble_ID: 1
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	236	188	79.7
¹³C chemical shifts	189	71	37.6
¹⁵N chemical shifts	41	30	73.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	75	66	88.0
¹³C chemical shifts	74	34	45.9
¹⁵N chemical shifts	36	29	80.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	161	122	75.8
¹³C chemical shifts	115	37	32.2
¹⁵N chemical shifts	5	1	20.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	37	30	81.1
¹³C chemical shifts	37	6	16.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	10	52.6
¹³C chemical shifts	19	0	0.0

Spectral peak lists

Saveframe: spectral_peak_list_1
- Status: Error
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 37, Sequence coverage: 86.5%
- Number of spectral dimensions: 3
- Total number of spectral peaks: 219
Saveframe: spectral_peak_list_2
- Status: Error
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 37, Sequence coverage: 91.9%
- Number of spectral dimensions: 3
- Total number of spectral peaks: 3027

Keywords MEMBRANE PROTEIN, Sodium channel, voltage sensing

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.593 seconds)

BMRB: 30834

Sample #1

Sample #2

Related entities 1. Sodium channel protein type 5 subunit alpha, : 1 : 11 : 90 entities Detail

Interaction partners 1. Sodium channel protein type 5 subunit alpha, : 10 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 5 contents Detail