BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	86.3 % (252 of 292)	97.4 % (152 of 156)	72.1 % (80 of 111)	80.0 % (20 of 25)
Backbone	77.5 % (110 of 142)	93.6 % (44 of 47)	65.3 % (47 of 72)	82.6 % (19 of 23)
Sidechain	95.4 % (166 of 174)	99.1 % (108 of 109)	90.5 % (57 of 63)	50.0 % (1 of 2)
Aromatic	96.4 % (27 of 28)	100.0 % (14 of 14)	100.0 % (13 of 13)	0.0 % (0 of 1)
Methyl	100.0 % (12 of 12)	100.0 % (6 of 6)	100.0 % (6 of 6)

1. entity 1

CQTWRXVSPE ECRKYKEEYX CVRCTE

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_EHE_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	design peptide NC_EHE_D1	natural abundance		1.0 mg/mL

Sample #2

Solvent system 100% D2O, Pressure 1 null, Temperature 298 (±0.1) K, pH 3.0 (±0.1), Details 1.0 mg/mL design peptide NC_EHE_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	design peptide NC_EHE_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KWO, Strand ID: A Detail

Release date

2016-09-15

Citation

Accurate de novo design of hyperstable constrained peptides
Bhardwaj, G., Mulligan, V.K., Bahl, C.D., Gilmore, J.M., Harvey, P.J., Cheneval, O., Buchko, G.W., Pulavarti, S.V., Kaas, Q., Eletsky, A., Huang, P.S., Johnsen, W.A., Greisen, P.J., Rocklin, G.J., Song, Y., Linsky, T.W., Watkins, A., Rettie, S.A., Xu, X., Carter, L.P., Bonneau, R., Olson, J.M., Coutsias, E., Correnti, C.E., Szyperski, T., Craik, D.J., Baker, D.
Nature (2016), 538, 329-335, PubMed 27626386 , DOI 10.1038/nature19791 , Abstract

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30140_5kwo.nef
Input source #2: Coordindates	5kwo.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:1:CYS:SG	A:21:CYS:SG	oxidized, CA 56.294, CB 45.578 ppm	oxidized, CA 57.017, CB 41.812 ppm	2.031
A:12:CYS:SG	A:24:CYS:SG	oxidized, CB 41.097 ppm	oxidized, CA 53.832, CB 46.157 ppm	2.009

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)
1:5:ARG:C	1:6:DAR:N	unknown	unknown	n/a
1:6:DAR:C	1:7:VAL:N	unknown	unknown	n/a
1:19:TYR:C	1:20:DSG:N	unknown	unknown	n/a
1:20:DSG:C	1:21:CYS:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	6	DAR	D-ARGININE	Assigned chemical shifts, Coordinates
A	20	DSG	D-ASPARAGINE	Assigned chemical shifts, Coordinates

Sequence alignments

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

--------10--------20------
CQTWRXVSPEECRKYKEEYXCVRCTE
||||||||||||||||||||||||||
CQTWRXVSPEECRKYKEEYXCVRCTE

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_30140_5kwo.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	6		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	280		100.0 (chain: A, length: 26)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	277 (1)	noe	92.3 (chain: A, length: 26)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	18 (1)	hbond	53.8 (chain: A, length: 26)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	44 (44)	.	92.3 (chain: A, length: 26)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 173
  - ¹³C chemical shifts: 85
  - ¹⁵N chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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
6	DAR
20	DSG

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
16	LYS	HZ1	7.608
16	LYS	HZ2	7.608
16	LYS	HZ3	7.608

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	156	155	99.4
¹³C chemical shifts	111	80	72.1
¹⁵N chemical shifts	28	20	71.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	47	46	97.9
¹³C chemical shifts	48	23	47.9
¹⁵N chemical shifts	23	19	82.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	109	109	100.0
¹³C chemical shifts	63	57	90.5
¹⁵N chemical shifts	5	1	20.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	6	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	13	13	100.0
¹⁵N chemical shifts	1	0	0.0

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: 26, Sequence coverage: 92.3%
- Total number of restraints: 276
- Weight of restraints: 1.0 (276)
- Potential type of restraints: square-well-parabolic (276)
- Range of distance target values: 2.35, 3.65 (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_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 53.8%
  - Total number of restraints: 18
  - Weight of restraints: 1.0 (18)
  - Potential type of restraints: square-well-parabolic (18)
  - Range of distance target values: 1.0, 1.5 (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_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 92.3%
- Total number of restraints: 44
- Total number of restraints per polymer type: 44
- Weight of restraints: 1.0 (44)
- Potential type of restraints: square-well-parabolic (44)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords De novo protein, designed peptide

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BMRB: 30140

Sample #1

Sample #2

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail