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BMRB: 15876

2K6O

Human LL-37 Structure

Authors

Assembly

LL-37

Entity

1. LL-37 (polymer, Thiol state: not present), 37 monomers, 4493.261 Da Detail

LLGDFFRKSK EKIGKEFKRI VQRIKDFLRN LVPRTES

Formula weight

4493.261 Da

Source organism

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 39.6 %, Completeness (bb): 81.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	39.6 % (195 of 492)	18.9 % (50 of 265)	57.7 % (109 of 189)	94.7 % (36 of 38)
Backbone	81.4 % (179 of 220)	49.3 % (37 of 75)	97.2 % (106 of 109)	100.0 % (36 of 36)
Sidechain	16.6 % (51 of 307)	6.8 % (13 of 190)	33.0 % (38 of 115)	0.0 % (0 of 2)
Aromatic	15.0 % (6 of 40)	25.0 % (5 of 20)	5.0 % (1 of 20)
Methyl	0.0 % (0 of 38)	0.0 % (0 of 19)	0.0 % (0 of 19)

1. LL-37

LLGDFFRKSK EKIGKEFKRI VQRIKDFLRN LVPRTES

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

Protein Blocks Logo

Calculated from 4 models in PDB: 2K6O, Strand ID: A Detail

Release date

2008-10-07

Citation

Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
Wang, G.
J. Biol. Chem. (2008), 283, 32637-32643, PubMed 18818205 , DOI 10.1074/jbc.M805533200 , Abstract

Entries sharing articles Swiss-Prot: 1 entries Detail

Swiss-Prot: P49913 released on 1996-10-01
Title CAMP_HUMAN Entity Cathelicidin antimicrobial peptide

Related entities 1. LL-37, : 1 : 9 : 2 : 21 entities Detail

Interaction partners 1. LL-37, : 2 interactors Detail

More details for 2 interactors identified by 2 citations

Experiments performed 10 experiments Detail

1 2D 1H-15N HSQC

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

2 3D CBCA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

3 3D HNCACB

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

4 3D HBHA(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

5 3D HN(CO)CA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

6 3D H(CCO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

7 3D HNCO

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

8 3D C(CO)NH

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

9 3D HCCH-TOCSY

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

10 3D HNHA

Instrument

Varian INOVA - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 5.4, Details in the presence of 80-fold SDS

#	Name	Isotope labeling	Type	Concentration
1	LL-37	[U-100% 15N]		0.50 mM
2	LL-37	[U-100% 13C; U-100% 15N]		0.5 mM
3	LL-37	natural abundance		2 mM
4	H2O	natural abundance		90 %
5	D2O	[U-100% 2H]		10 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15876_2k6o.nef
Input source #2: Coordindates	2k6o.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

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--------30-------
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
|||||||||||||||||||||||||||||||||||||
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES

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_15876_2k6o.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	179		100.0 (chain: A, length: 37)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	302 (1)	noe	100.0 (chain: A, length: 37)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	38 (1)	hbond	70.3 (chain: A, length: 37)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	58 (58)	.	83.8 (chain: A, length: 37)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 37
  - ¹³C chemical shifts: 106
  - ¹⁵N chemical shifts: 36
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 100.0%
- Total number of restraints: 302
- Weight of restraints: 1.0 (302)
- Potential type of restraints: square-well-parabolic (302)
- Range of distance target values: 2.35, 4.4 (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_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 70.3%
  - Total number of restraints: 38
  - Weight of restraints: 1.0 (38)
  - Potential type of restraints: square-well-parabolic (38)
  - Range of distance target values: 1.75, 3.0 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 37, Sequence coverage: 83.8%
- Total number of restraints: 58
- Total number of restraints per polymer type: 58
- Weight of restraints: 1.0 (58)
- Potential type of restraints: square-well-parabolic (58)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords antimicrobial peptide, Bacterial membrane targeting, Human cathelicidin, Human host defense peptide, LL-37