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Found 1 Document (0.469 seconds)

BMRB: 30497

6E5I

Heterogeneous-Backbone Mimics of a Designed Disulfide-Rich Protein: Orn turn

Authors

Cabalteja, C.C., Mihalko, D.S., Horne, W.S.

Assembly

Designed peptide NC HEE D1: Orn turn mutant

Entity

1. Designed peptide NC HEE D1: Orn turn mutant (polymer, Thiol state: all disulfide bound), 27 monomers, 3224.738 Da Detail

NDKCKELKKR YXCEVRCDXP RYEVHCX

Formula weight

3224.738 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS4:SG	1:CYS17:SG
2	disulfide	sing	1:CYS13:SG	1:CYS26:SG

Source organism

synthetic construct

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 88.9 %, Completeness: 99.4 %, Completeness (bb): 97.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	99.4 % (160 of 161)	99.4 % (160 of 161)
Backbone	97.9 % (46 of 47)	97.9 % (46 of 47)
Sidechain	100.0 % (114 of 114)	100.0 % (114 of 114)
Aromatic	100.0 % (10 of 10)	100.0 % (10 of 10)
Methyl	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

NDKCKELKKR YXCEVRCDXP RYEVHCX

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 275 K, pH 4.0, Details 0.2 mM NA DSS, 5.7 mM NA Designed peptide NC_HEE_D1: Orn turn mutant, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	DSS	natural abundance		0.2 mM
2	Designed peptide NC_HEE_D1: Orn turn mutant	natural abundance		5.7 mM

Release date

2018-07-30

Citation

Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein
Cabalteja, C.C., Mihalko, D.S., Horne, W.S.
Chembiochem. (2018), 20, 103-110, PubMed 30326175 , DOI 10.1002/cbic.201800558 , Abstract

Related entities 1. Designed peptide NC HEE D1: Orn turn mutant, : 1 : 6 entities Detail

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30497_6e5i.nef
Input source #2: Coordindates	6e5i.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:4:CYS:SG	A:17:CYS:SG	unknown	unknown	2.026
A:13:CYS:SG	A:26:CYS:SG	unknown	unknown	2.03

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)
1:11:TYR:C	1:12:ORN:NE	unknown	unknown	n/a
1:12:ORN:C	1:13:CYS:N	unknown	unknown	n/a
1:18:ASP:C	1:19:DPR:N	unknown	unknown	n/a
1:19:DPR:C	1:20:PRO:N	unknown	unknown	n/a
1:26:CYS:C	1:27:NH2:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	12	ORN	L-ornithine	Assigned chemical shifts, Distance restraints, Coordinates
A	19	DPR	D-PROLINE	Assigned chemical shifts, Distance restraints, Coordinates
A	27	NH2	AMINO GROUP	Assigned chemical shifts, Coordinates

Sequence alignments

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

--------10--------20-------
NDKCKELKKRYXCEVRCDXPRYEVHCX
|||||||||||||||||||||||||||
NDKCKELKKRYXCEVRCDXPRYEVHCX

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	27	0	0	100.0

Content subtype: combined_30497_6e5i.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	7		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	189		100.0 (chain: A, length: 27)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	735 (1)	noe	96.3 (chain: A, length: 27)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	24 (1)	hbond	63.0 (chain: A, length: 27)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	16 (16)	.	74.1 (chain: A, length: 27)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 189
- 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

Comp_index_ID	Comp_ID
19	DPR

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
3	LYS	HZ1	7.587
3	LYS	HZ2	7.587
3	LYS	HZ3	7.587
5	LYS	HZ1	7.567
5	LYS	HZ2	7.567
5	LYS	HZ3	7.567
8	LYS	HZ1	7.616
8	LYS	HZ2	7.616
8	LYS	HZ3	7.616
9	LYS	HZ1	7.567
9	LYS	HZ2	7.567
9	LYS	HZ3	7.567
12	ORN	HE1	7.702

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	171	169	98.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	49	47	95.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	122	122	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	10	10	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 96.3%
- Total number of restraints: 706
- Weight of restraints: 1.0 (706)
- Potential type of restraints: square-well-parabolic (706)
- Range of distance target values: 1.69, 5.15 (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_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 63.0%
  - Total number of restraints: 24
  - Weight of restraints: 1.0 (24)
  - Potential type of restraints: square-well-parabolic (24)
  - Range of distance target values: 1.9, 2.9 (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_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 27, Sequence coverage: 74.1%
- Total number of restraints: 16
- Total number of restraints per polymer type: 16
- Weight of restraints: 1.0 (16)
- Potential type of restraints: square-well-parabolic (16)
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords DE NOVO PROTEIN, heterogeneous backbone foldamer

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Found 1 Document (0.469 seconds)

BMRB: 30497

Sample

Related entities 1. Designed peptide NC HEE D1: Orn turn mutant, : 1 : 6 entities Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail