BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	78.7 % (196 of 249)	78.0 % (103 of 132)	76.5 % (75 of 98)	94.7 % (18 of 19)
Backbone	79.5 % (89 of 112)	97.4 % (37 of 38)	62.5 % (35 of 56)	94.4 % (17 of 18)
Sidechain	80.6 % (125 of 155)	70.2 % (66 of 94)	96.7 % (58 of 60)	100.0 % (1 of 1)
Aromatic	100.0 % (10 of 10)	100.0 % (5 of 5)	100.0 % (5 of 5)
Methyl	97.1 % (33 of 34)	100.0 % (17 of 17)	94.1 % (16 of 17)

1. entity

PKILNKILGK ILRLAAAFK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	TSP	natural abundance	5 %
2	D2O	natural abundance	10 %
3	H2O	natural abundance	90 %
4	SDS	natural abundance	100 mM
5	sodium phosphate	natural abundance	30 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 2N9R, Strand ID: A Detail

Release date

2016-02-16

Citation

Novel antimicrobial peptide PaDBS1R1 designed from the ribosomal protein L39E from Pyrobaculum aerophilum using bioinformatics
Alves, E.S.F., Matos, C.O., Liao, L.M.
Not known

Experiments performed 4 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_25916_2n9r.nef
Input source #2: Coordindates	2n9r.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)
1:19:LYS:C	1:20:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	20	NH2	AMINO GROUP	Coordinates

Sequence alignments

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

--------10--------20
PKILNKILGKILRLAAAFKX
||||||||||||||||||||
PKILNKILGKILRLAAAFKX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	20	0	0	100.0

Content subtype: combined_25916_2n9r.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	194		95.0 (chain: A, length: 20)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	34 (34)	.	95.0 (chain: A, length: 20)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 95.0%
- Total number of assignments
  - ¹H chemical shifts: 101
  - ¹³C chemical shifts: 75
  - ¹⁵N chemical shifts: 18
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
13	ARG	HH21	7.21
13	ARG	HH22	7.184

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	134	99	73.9
¹³C chemical shifts	98	75	76.5
¹⁵N chemical shifts	21	18	85.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	37	97.4
¹³C chemical shifts	38	17	44.7
¹⁵N chemical shifts	19	17	89.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	96	62	64.6
¹³C chemical shifts	60	58	96.7
¹⁵N chemical shifts	2	1	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0
¹³C chemical shifts	17	16	94.1

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

Covalent bonds

Saveframe: assembly
- Status: OK

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 20, Sequence coverage: 95.0%
- Total number of restraints: 34
- Total number of restraints per polymer type: 34
- Weight of restraints: 1.0 (34)
- Potential type of restraints: square-well-parabolic (34)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords PaDBS1R1, peptide

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BMRB: 25916

Sample

Experiments performed 4 experiments Detail

Instrument

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Instrument

Sample

Instrument

Sample

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Sample

NMR combined restraints 3 contents Detail