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BMRB: 34315

6HNG

Peptide-membrane interaction between targeting and lysis

Authors

Schneider, G., Blatter, M., Mueller, A.

Assembly

TRP-TYR-HIS-ARG-LEU-SER-HIS-ILE-HIS-SER-ARG-LEU-GLN-ASP-NH2

Entity

1. TRP-TYR-HIS-ARG-LEU-SER-HIS-ILE-HIS-SER-ARG-LEU-GLN-ASP-NH2 (polymer, Thiol state: not present), 15 monomers, 1690.315 Da Detail

KLLKLLKKLL KLLKX

Formula weight

1690.315 Da

Source organism

synthetic construct

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.3 %, Completeness: 92.5 %, Completeness (bb): 78.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C
All	92.5 % (185 of 200)	99.1 % (115 of 116)	83.3 % (70 of 84)
Backbone	78.6 % (55 of 70)	96.4 % (27 of 28)	66.7 % (28 of 42)
Sidechain	100.0 % (144 of 144)	100.0 % (88 of 88)	100.0 % (56 of 56)
Methyl	100.0 % (32 of 32)	100.0 % (16 of 16)	100.0 % (16 of 16)

1. entity 1

KLLKLLKKLL KLLKX

Show sample condition

Sample

Solvent system trifluoroethanol/water, Pressure 1 Pa, Temperature 291 K, pH 5, Details 10 mM peptide, trifluoroethanol/water

#	Name	Isotope labeling	Type	Concentration
1	peptide	natural abundance		10 mM

Release date

2018-10-16

Citation

Peptide-Membrane Interaction between Targeting and Lysis
Blatter, M., Schneider, G.
ACS Chem. Biol. (2017), 12, 2254-2259, PubMed 28763193 , DOI 10.1021/acschembio.7b00504 , Abstract

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 34314 released on 2018-10-16
    Title Peptide-membrane interaction between targeting and lysis
  BMRB: 34316 released on 2018-10-16
    Title Peptide-membrane interaction between targeting and lysis
  BMRB: 34090 released on 2017-02-13
    Title Peptide-membrane interaction between targeting and lysis
  BMRB: 34091 released on 2017-02-13
    Title Peptide-membrane interaction between targeting and lysis
  BMRB: 34092 released on 2017-02-13
    Title Peptide-membrane interaction between targeting and lysis

Experiments performed 3 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_34315_6hng.nef
Input source #2: Coordindates	6hng.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	True (see coodinates for details)
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)

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:14:LYS:C	1:15:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	15	NH2	AMINO GROUP	Assigned chemical shifts, Coordinates

Sequence alignments

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

--------10-----
KLLKLLKKLLKLLKX
|||||||||||||||
KLLKLLKKLLKLLKX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	15	0	0	100.0

Content subtype: combined_34315_6hng.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	186		100.0 (chain: A, length: 15)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	224 (1)	noe	93.3 (chain: A, length: 15)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 15, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 116
  - ¹³C chemical shifts: 70
- Completeness of assignments
  - Entity_assemble_ID: A
- 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	118	116	98.3
¹³C chemical shifts	84	70	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	26	92.9
¹³C chemical shifts	28	14	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	90	90	100.0
¹³C chemical shifts	56	56	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	16	16	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 15, Sequence coverage: 93.3%
- Total number of restraints: 224
- Weight of restraints: 1.0 (224)
- Potential type of restraints: upper-bound-parabolic (224)
- Range of distance target values: 2.51, 5.5 (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 CELL CYCLE, PROTEIN

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Found 1 Document (0.4 seconds)

BMRB: 34315

Sample

Entries sharing articles BMRB: 5 entries Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail