BMRBj - BMREntryMaster

Found 1 Document (0.572 seconds)

BMRB: 25516

2N07

Design of a Highly Stable Disulfide-Deleted Mutant of Analgesic Cyclic alpha-Conotoxin Vc1.1

Authors

Yu, R., Seymour, V., Berecki, G., Jia, X., Akcan, M., Adams, D., Kaas, Q., Craik, D.

Assembly

Disulfide-Deleted Mutant of Analgesic Cyclic alpha-Conotoxin Vc1.1

Entity

1. Disulfide-Deleted Mutant of Analgesic Cyclic alpha-Conotoxin Vc1.1 (polymer, Thiol state: all free), 22 monomers, 2260.382 Da Detail

GHCSDPRFNY DHPEICGGAA GG

Formula weight

2260.382 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 61.2 %, Completeness (bb): 50.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	61.2 % (120 of 196)	95.5 % (107 of 112)	15.5 % (13 of 84)
Backbone	50.9 % (55 of 108)	97.9 % (46 of 47)	14.8 % (9 of 61)
Sidechain	66.7 % (70 of 105)	93.8 % (61 of 65)	22.5 % (9 of 40)
Aromatic	50.0 % (13 of 26)	100.0 % (13 of 13)	0.0 % (0 of 13)
Methyl	75.0 % (6 of 8)	100.0 % (4 of 4)	50.0 % (2 of 4)

1. entity

GHCSDPRFNY DHPEICGGAA GG

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 280 K, pH 4.5

#	Name	Isotope labeling	Concentration
1	cVc 1.1 mutant	natural abundance	1.7 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2N07, Strand ID: X Detail

Release date

2016-04-11

Citation

Less is More: Design of a Highly Stable Disulfide-Deleted Mutant of Analgesic Cyclic α-Conotoxin Vc1.1
Yu, R., Seymour, V., Berecki, G., Jia, X., Akcan, M., Adams, D., Kaas, Q., Craik, D.
Sci. Rep. (2015), 5, 13264-13264, PubMed 26290113 , DOI 10.1038/srep13264 , Abstract

Related entities 1. Disulfide-Deleted Mutant of Analgesic Cyclic alpha-Conotoxin Vc1.1, : 1 : 2 : 6 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_25516_2n07.nef
Input source #2: Coordindates	2n07.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	True (see coodinates for details)
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
X:3:CYS:SG	X:16:CYS:SG	unknown	unknown	2.031

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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:22:GLY:C	1:1:GLY:N	unknown	unknown	n/a

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): X vs Auth_asym_ID (model): X

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
X	X	22	0	0	100.0

Content subtype: combined_25516_2n07.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	121		100.0 (chain: X, length: 22)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	77 (77)	.	95.5 (chain: X, length: 22)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: X, Chain length: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 108
  - ¹³C chemical shifts: 13
- Completeness of assignments
  - Entity_assemble_ID: X
- 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: X

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
10	TYR	HH	6.82

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	112	107	95.5
¹³C chemical shifts	84	13	15.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	46	97.9
¹³C chemical shifts	44	4	9.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	65	61	93.8
¹³C chemical shifts	40	9	22.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	2	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: X, Chain length: 22, Sequence coverage: 95.5%
- Total number of restraints: 77
- Total number of restraints per polymer type: 77
- Weight of restraints: 1.0 (77)
- Potential type of restraints: square-well-parabolic (77)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: X

Keywords Disulfide-Deleted Mutant cVc1.1

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 (0.572 seconds)

BMRB: 25516

Sample

Related entities 1. Disulfide-Deleted Mutant of Analgesic Cyclic alpha-Conotoxin Vc1.1, : 1 : 2 : 6 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail