BMRBj - BMREntryMaster

Found 1 Document (0.381 seconds)

BMRB: 16332

2KJN

pH dependent structures of LAH4 in micellar environmnet:mode of acting

Authors

Georgescu, J., Bechinger, B.

Assembly

lah4

Entity

1. lah4 (polymer, Thiol state: not present), 26 monomers, 2779.456 Da Detail

KKALLALALH HLAHLALHLA LALKKA

Formula weight

2779.456 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 83.5 %, Completeness (bb): 98.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	83.5 % (132 of 158)	83.5 % (132 of 158)
Backbone	98.1 % (51 of 52)	98.1 % (51 of 52)
Sidechain	76.4 % (81 of 106)	76.4 % (81 of 106)
Aromatic	100.0 % (8 of 8)	100.0 % (8 of 8)
Methyl	85.7 % (24 of 28)	85.7 % (24 of 28)

1. lah4

KKALLALALH HLAHLALHLA LALKKA

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 317 K, pH 4.1 (±0.1), Details DPC in PBS

#	Name	Isotope labeling	Concentration
1	lah4	natural abundance	2 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %
4	sodium chloride	natural abundance	115 mM
5	sodium phosphate	natural abundance	20 mM
6	potassium dihydrogen phosphate	natural abundance	8 mM

Protein Blocks Logo

Calculated from 20 models in PDB: 2KJN, Strand ID: A Detail

Release date

2009-11-02

Citation

Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection
Georgescu, J., Bechinger, B.
Biophys. J.

Related entities 1. lah4, : 1 : 1 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_16332_2kjn.nef
Input source #2: Coordindates	2kjn.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------
KKALLALALHHLAHLALHLALALKKA
||||||||||||||||||||||||||
KKALLALALHHLAHLALHLALALKKA

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	26	0	0	100.0

Content subtype: combined_16332_2kjn.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	126		100.0 (chain: A, length: 26)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	307 (1)	noe	96.2 (chain: A, length: 26)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	14 (1)	hbond	65.4 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 126
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	158	126	79.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	52	51	98.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	106	75	70.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	24	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 96.2%
- Total number of restraints: 307
- Weight of restraints: 1.0 (307)
- Potential type of restraints: square-well-parabolic (307)
- Range of distance target values: 2.5, 5.1 (Å)
- Histogram of 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: 26, Sequence coverage: 65.4%
  - Total number of restraints: 14
  - Weight of restraints: 1.0 (14)
  - Potential type of restraints: square-well-parabolic (14)
  - Range of distance target values: 1.9, 1.9 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Keywords amphipathic peptide

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Found 1 Document (0.381 seconds)

BMRB: 16332

Sample

Related entities 1. lah4, : 1 : 1 entities Detail

Experiments performed 4 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail