BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	85.6 % (357 of 417)	90.4 % (197 of 218)	76.1 % (121 of 159)	97.5 % (39 of 40)
Backbone	82.2 % (176 of 214)	95.9 % (71 of 74)	67.6 % (71 of 105)	97.1 % (34 of 35)
Sidechain	90.7 % (214 of 236)	87.5 % (126 of 144)	95.4 % (83 of 87)	100.0 % (5 of 5)
Aromatic	93.8 % (45 of 48)	100.0 % (24 of 24)	87.0 % (20 of 23)	100.0 % (1 of 1)
Methyl	80.0 % (16 of 20)	70.0 % (7 of 10)	90.0 % (9 of 10)

1. ShK-like peptide

VCEDLNAHCE MWQQLGHCQY SPKYMGHYCK KACGLCX

Show sample condition

Sample #1

Solvent system 100% D2O, Pressure 1 atm, Temperature 293 K, pH 5.8

#	Name	Isotope labeling	Concentration
1	ShK-like_peptide	natural abundance	0.8 mM
2	sodium phosphate	natural abundance	10 mM
3	D2O	natural abundance	100 %

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 293 K, pH 5.8

#	Name	Isotope labeling	Concentration
4	ShK-like_peptide	natural abundance	0.8 mM
5	sodium phosphate	natural abundance	10 mM
6	H2O	natural abundance	90 %
7	D2O	natural abundance	10 %

Protein Blocks Logo

Calculated from 30 models in PDB: 2MCR, Strand ID: A Detail

Release date

2014-06-29

Citation

Kv1.3 channel-blocking immunomodulatory peptides from parasitic worms: implications for autoimmune diseases
Chhabra, S., Chang, S., Nguyen, H.M., Londono, L.M., Huq, R., Tanner, M.R., Estrada, R., Dhawan, V., Chauhan, S., Upadhyay, S.K., Swarbrick, J.D., Mohanty, B., Wulff, H., Iadonato, S.P., Gutman, G.A., Beeton, C., Pennington, M.W., Chandy, G.K., Norton, R.S.
FASEB J. (2014), 28, 3952-3964, PubMed 24891519 , DOI 10.1096/fj.14-251967 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 19460 released on 2014-06-29
Title Solution structure of ShK-like immunomodulatory peptide from Ancylostoma caninum (hookworm)

Related entities 1. ShK-like immunomodulatory peptide from Brugia malayi, : 1 : 101 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19450_2mcr.nef
Input source #2: Coordindates	2mcr.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)
A:2:CYS:SG	A:36:CYS:SG	oxidized, CB 38.89 ppm	oxidized, CA 54.051, CB 39.326 ppm	2.02
A:9:CYS:SG	A:29:CYS:SG	oxidized, CA 59.789, CB 36.932 ppm	oxidized, CA 51.384, CB 37.055 ppm	2.019
A:18:CYS:SG	A:33:CYS:SG	oxidized, CA 59.405, CB 37.937 ppm	oxidized, CA 54.274, CB 37.793 ppm	2.018

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

None

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	37	NH2	AMINO GROUP	Assigned chemical shifts, Coordinates

Sequence alignments

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

--------10--------20--------30-------
VCEDLNAHCEMWQQLGHCQYSPKYMGHYCKKACGLCX
|||||||||||||||||||||||||||||||||||||
VCEDLNAHCEMWQQLGHCQYSPKYMGHYCKKACGLCX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	37	0	0	100.0

Content subtype: combined_19450_2mcr.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	354		100.0 (chain: A, length: 37)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	736 (1)	noe	97.3 (chain: A, length: 37)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	18 (1)	hbond	37.8 (chain: A, length: 37)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	50 (50)	.	91.9 (chain: A, length: 37)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 196
  - ¹³C chemical shifts: 118
  - ¹⁵N chemical shifts: 40
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	220	196	89.1
¹³C chemical shifts	159	118	74.2
¹⁵N chemical shifts	41	40	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	74	70	94.6
¹³C chemical shifts	72	35	48.6
¹⁵N chemical shifts	36	35	97.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	146	126	86.3
¹³C chemical shifts	87	83	95.4
¹⁵N chemical shifts	5	5	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	9	75.0
¹³C chemical shifts	12	11	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	24	100.0
¹³C chemical shifts	23	20	87.0
¹⁵N chemical shifts	1	1	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 97.3%
- Total number of restraints: 735
- Weight of restraints: 1.0 (735)
- Potential type of restraints: square-well-parabolic (735)
- Range of distance target values: 1.95, 3.65 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 37.8%
  - Total number of restraints: 18
  - Weight of restraints: 1.0 (18)
  - Potential type of restraints: square-well-parabolic (18)
  - Range of distance target values: 1.9, 2.4 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 91.9%
- Total number of restraints: 50
- Total number of restraints per polymer type: 50
- Weight of restraints: 1.0 (50)
- Potential type of restraints: square-well-parabolic (50)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords BmK1, Kv1.3, NMR, ShK-like peptide, worms

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Found 1 Document (0.787 seconds)

BMRB: 19450

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. ShK-like immunomodulatory peptide from Brugia malayi, : 1 : 101 entities Detail

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail