BMRBj - BMREntryMaster

Found 1 Document (0.2 seconds)

BMRB: 34559

Capra hircus Cathelicidin-1

Authors

Myshkin, M.Y., Mironov, P.A., Shenkarev, Z.O.

Assembly

Capra hircus Cathelicidin-1

Entity

1. Capra hircus Cathelicidin-1 (polymer, Thiol state: all disulfide bound), 12 monomers, 1505.895 × 2 Da Detail

RICQFVLIRV CR

Total weight

3011.79 Da

Max. entity weight

1505.895 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS3:SG	1:CYS11:SG
2	disulfide	sing	1:CYS11:SG	1:CYS3:SG

Source organism

Capra hircus

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 88.7 %, Completeness (bb): 79.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.7 % (142 of 160)	98.8 % (82 of 83)	73.8 % (45 of 61)	93.8 % (15 of 16)
Backbone	79.2 % (57 of 72)	95.8 % (23 of 24)	63.9 % (23 of 36)	91.7 % (11 of 12)
Sidechain	97.0 % (97 of 100)	100.0 % (59 of 59)	91.9 % (34 of 37)	100.0 % (4 of 4)
Aromatic	80.0 % (8 of 10)	100.0 % (5 of 5)	60.0 % (3 of 5)
Methyl	95.0 % (19 of 20)	100.0 % (10 of 10)	90.0 % (9 of 10)

1. entity 1

RICQFVLIRV CR

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 4.0, Details 0.43 mM Capra hircus Catelicidin-1, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	Capra hircus Catelicidin-1	natural abundance		0.43 mM

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 4.0, Details 0.2 mM [U-15N] Capra hircus Catelicidin-1, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
2	Capra hircus Catelicidin-1	[U-15N]		0.2 mM

Release date

2020-10-04

Citation

Dodecapeptide Cathelicidins of Cetartiodactyla: Structure, Mechanism of Antimicrobial Action, and Synergistic Interaction With Other Cathelicidins
Bolosov, I.A., Panteleev, P.V., Sychev, S.V., Sukhanov, S.V., Mironov, P.A., Myshkin, M.Y., Shenkarev, Z.O., Ovchinnikova, T.V.
Front. Microbiol. (2021), 12, 725526-725526, PubMed 34484167 , DOI 10.3389/fmicb.2021.725526 , Abstract

Experiments performed 4 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34559_3.str
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	OK

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:3:CYS:SG	2:11:CYS:SG	oxidized, CA 52.696, CB 44.78 ppm	unknown	n/a
1:11:CYS:SG	2:3:CYS:SG	oxidized, CA 52.499, CB 44.949 ppm	unknown	n/a

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

None

Non-standard residues

None

Content subtype: bmr34559_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	159		100.0 (chain: 1, length: 12)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 12, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 102
  - ¹³C chemical shifts: 42
  - ¹⁵N chemical shifts: 15
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	83	82	98.8
¹³C chemical shifts	61	42	68.9
¹⁵N chemical shifts	16	15	93.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	24	23	95.8
¹³C chemical shifts	24	10	41.7
¹⁵N chemical shifts	12	11	91.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	59	59	100.0
¹³C chemical shifts	37	32	86.5
¹⁵N chemical shifts	4	4	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	10	100.0
¹³C chemical shifts	10	9	90.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	5	5	100.0
¹³C chemical shifts	5	1	20.0

Keywords ANTIMICROBIAL PROTEIN, PROTEIN

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 (0.2 seconds)

BMRB: 34559

Sample #1

Sample #2

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail