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Found 1 Document (0.512 seconds)

BMRB: 20049

7SAV

NMR solution structure of Mu-KIIIA[C1A,C9A]

Authors

Khoo, K.K., Feng, Z., Norton, R.S.

Assembly

Mu-KIIIA[C1A,C9A]

Entity

1. Mu-KIIIA[C1A,C9A] (polymer, Thiol state: all disulfide bound), 16 monomers, 1827.057 Da Detail

ACNCSSKWAR DHSRCC

Formula weight

1827.057 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS2:SG	1:CYS15:SG
2	disulfide	sing	1:CYS4:SG	1:CYS16:SG

Source organism

Conus kinoshitai

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 67.3 %, Completeness (bb): 62.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	67.3 % (113 of 168)	95.5 % (84 of 88)	27.4 % (17 of 62)	66.7 % (12 of 18)
Backbone	62.5 % (60 of 96)	96.9 % (31 of 32)	35.4 % (17 of 48)	75.0 % (12 of 16)
Sidechain	61.4 % (54 of 88)	94.6 % (53 of 56)	3.3 % (1 of 30)	0.0 % (0 of 2)
Aromatic	31.3 % (5 of 16)	62.5 % (5 of 8)	0.0 % (0 of 7)	0.0 % (0 of 1)
Methyl	50.0 % (2 of 4)	100.0 % (2 of 2)	0.0 % (0 of 2)

1. KIIIA[Ala1,9]

ACNCSSKWAR DHSRCC

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Temperature 278 K, pH 5.3

#	Name	Isotope labeling	Type	Concentration
1	KIIIA[Ala1,9]	natural abundance		3.7 mM

Sample #2

Solvent system 100% D2O, Temperature 278 K, pH 5.3

#	Name	Isotope labeling	Type	Concentration
2	KIIIA[Ala1,9]	natural abundance		3.7 mM

Release date

2009-04-03

Citation

Structure of the analgesic mu-conotoxin KIIIA and effects on the structure and function of disulfide deletion
Khoo, K.K., Feng, Z., Smith, B.J., Zhang, M., Yoshikami, D., Olivera, B.M., Bulaj, G., Norton, R.S.
Biochemistry (2009), 48, 1210-1219, PubMed 19170536 , DOI 10.1021/bi801998a , Abstract

Related entities 1. Mu-KIIIA[C1A,C9A], : 1 : 4 : 9 entities Detail

Experiments performed 10 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr20049_3.str
Input source #2: Coordindates	bmr20049.coor.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	None
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)
1:2:CYS:SG	1:15:CYS:SG	unknown, CA 56.3 ppm	unknown, CA 57.2 ppm	2.021
1:4:CYS:SG	1:16:CYS:SG	unknown	unknown, CA 55.9 ppm	2.019

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

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): 1 vs Auth_asym_ID (model): A

--------10------ 
ACNCSSKWARDHSRCC 
|||||||||||||||| 
ACNCSSKWARDHSRCCX
--------10-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
1	A	17	1	0	94.1

Content subtype: bmr20049_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	121		100.0 (chain: 1, length: 16)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 16, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 94
  - ¹³C chemical shifts: 15
  - ¹⁵N chemical shifts: 12
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
5	SER	HG	6.15
6	SER	HG	6.31
7	LYS	HZ1	7.81
7	LYS	HZ2	7.81
7	LYS	HZ3	7.81
13	SER	HG	6.01

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	88	84	95.5
¹³C chemical shifts	62	15	24.2
¹⁵N chemical shifts	20	12	60.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	32	31	96.9
¹³C chemical shifts	32	15	46.9
¹⁵N chemical shifts	16	12	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	56	53	94.6
¹³C chemical shifts	30	0	0.0
¹⁵N chemical shifts	4	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	2	2	100.0
¹³C chemical shifts	2	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	5	62.5
¹³C chemical shifts	7	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords disulfide deletion, Mu-conotoxin, sodium channel blocker, toxin

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Found 1 Document (0.512 seconds)

BMRB: 20049

Sample #1

Sample #2

Related entities 1. Mu-KIIIA[C1A,C9A], : 1 : 4 : 9 entities Detail

Experiments performed 10 experiments Detail

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Chemical shift validation 3 contents Detail