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Found 1 Document (0.375 seconds)

BMRB: 30260

5V11

Solution structure of arenicin-3 synthetic analog.

Authors

Edwards, I.A., Mobli, M.

Assembly

AA139

Entity

1. AA139 (polymer), 21 monomers, 2553.972 Da Detail

GFCWYVCARR NGARVCYRRC N

Formula weight

2553.972 Da

Source organism

Arenicola marina

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 84.6 %, Completeness (bb): 79.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.6 % (209 of 247)	95.4 % (124 of 130)	66.7 % (62 of 93)	95.8 % (23 of 24)
Backbone	79.4 % (100 of 126)	95.5 % (42 of 44)	62.3 % (38 of 61)	95.2 % (20 of 21)
Sidechain	90.0 % (126 of 140)	95.3 % (82 of 86)	80.4 % (41 of 51)	100.0 % (3 of 3)
Aromatic	84.2 % (32 of 38)	100.0 % (19 of 19)	66.7 % (12 of 18)	100.0 % (1 of 1)
Methyl	91.7 % (11 of 12)	100.0 % (6 of 6)	83.3 % (5 of 6)

1. entity 1

GFCWYVCARR NGARVCYRRC N

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.01) atm, Temperature 298 (±0.2) K, pH 3.3 (±0.05), Details 2.5 mM AA139, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	AA139	natural abundance		2.5 mM

Release date

2017-12-12

Citation

Elucidating the Lipid Binding Properties of Membrane-Active Peptides Using Cyclised Nanodiscs
Zhang, A.H., Edwards, I.A., Mishra, B.P., Sharma, G., Healy, M.D., Elliott, A.G., Blaskovich, M., Cooper, M.A., Collins, B.M., Jia, X., Mobli, M.
Front. Chem. (2019), 7, 238-238, PubMed 31058133 , DOI 10.3389/fchem.2019.00238 , Abstract

Related entities 1. AA139, : 1 : 1 : 4 entities Detail

Experiments performed 4 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_30260_5v11.nef
Input source #2: Coordindates	5v11.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:3:CYS:SG	A:20:CYS:SG	oxidized, CA 55.824, CB 48.185 ppm	oxidized, CA 55.202, CB 48.455 ppm	1.986
A:7:CYS:SG	A:16:CYS:SG	oxidized, CA 55.228, CB 48.214 ppm	oxidized, CA 55.141, CB 48.823 ppm	2.079

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

None

Non-standard residues

None

Sequence alignments

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

--------10--------20-
GFCWYVCARRNGARVCYRRCN
|||||||||||||||||||||
GFCWYVCARRNGARVCYRRCN

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0

Content subtype: combined_30260_5v11.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	209		100.0 (chain: A, length: 21)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	Warning	12 (1)	undefined	19.0 (chain: A, length: 21)
2	Distance restraints	DYANA/DIANA_distance_constraints_3	Warning	20 (1)	hbond	28.6 (chain: A, length: 21)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 125
  - ¹³C chemical shifts: 61
  - ¹⁵N chemical shifts: 23
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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	130	125	96.2
¹³C chemical shifts	93	61	65.6
¹⁵N chemical shifts	29	23	79.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	43	97.7
¹³C chemical shifts	42	20	47.6
¹⁵N chemical shifts	21	20	95.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	86	82	95.3
¹³C chemical shifts	51	41	80.4
¹⁵N chemical shifts	8	3	37.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	5	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	19	100.0
¹³C chemical shifts	18	12	66.7
¹⁵N chemical shifts	1	1	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: Warning
- Experiment type: undefined
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 19.0%
- Total number of restraints: 12
- Weight of restraints: 1.0 (12)
- Potential type of restraints: upper-bound-parabolic (12)
- Range of distance target values: 1.98, 3.1 (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: DYANA/DIANA_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 28.6%
  - Total number of restraints: 20
  - Weight of restraints: 1.0 (20)
  - Potential type of restraints: upper-bound-parabolic (20)
  - Range of distance target values: 1.7, 3.2 (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

Keywords ANTIMICROBIAL PROTEIN, antimicrobial peptide, b-hairpin

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Found 1 Document (0.375 seconds)

BMRB: 30260

Sample

Related entities 1. AA139, : 1 : 1 : 4 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail