Peptide-membrane interaction between targeting and lysis
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 KLLKXSolvent 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 |
Bruker AvanceIII - 500 MHz
State isotropic, 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 |
Bruker AvanceIII - 500 MHz
State isotropic, 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 |
Bruker AvanceIII - 500 MHz
State isotropic, 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 |
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
NoneOther 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
--------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
Assigned chemical shifts
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 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|
Covalent bonds
Distance restraints
--------10----- KLLKLLKKLLKLLKX |||||||||||||| KLLKLLKKLLKLLK --------10----