BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	79.3 % (146 of 184)	96.0 % (97 of 101)	52.2 % (35 of 67)	87.5 % (14 of 16)
Backbone	71.6 % (63 of 88)	100.0 % (29 of 29)	48.9 % (22 of 45)	85.7 % (12 of 14)
Sidechain	83.8 % (93 of 111)	94.4 % (68 of 72)	62.2 % (23 of 37)	100.0 % (2 of 2)
Methyl	100.0 % (10 of 10)	100.0 % (5 of 5)	100.0 % (5 of 5)

1. entity 1

NPELQRKCKE LXTRXXXXXX XXXXSD

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_cHh_DL_D1, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	design peptide NC_cHh_DL_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_cHh_DL_D1, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	design peptide NC_cHh_DL_D1	natural abundance		1.0 mg/mL

Protein Blocks Logo

Calculated from 20 models in PDB: 5KX0, 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_30144_5kx0.nef
Input source #2: Coordindates	5kx0.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	True (see coordinates for details)
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:8:CYS:SG	A:21:DCY:SG	oxidized, CA 56.92, CB 36.067 ppm	oxidized, CA 57.6, CB 37.24 ppm	2.01

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:LEU:C	1:12:DAS:N	unknown	unknown	n/a
1:12:DAS:C	1:13:THR:N	unknown	unknown	n/a
1:14:ARG:C	1:15:DPR:N	unknown	unknown	n/a
1:15:DPR:C	1:16:DGL:N	unknown	unknown	n/a
1:16:DGL:C	1:17:DAL:N	unknown	unknown	n/a
1:17:DAL:C	1:18:DGL:N	unknown	unknown	n/a
1:18:DGL:C	1:19:DAR:N	unknown	unknown	n/a
1:19:DAR:C	1:20:DLY:N	unknown	unknown	n/a
1:20:DLY:C	1:21:DCY:N	unknown	unknown	n/a
1:21:DCY:C	1:22:DAR:N	unknown	unknown	n/a
1:22:DAR:C	1:23:DGL:N	unknown	unknown	n/a
1:23:DGL:C	1:24:DGL:N	unknown	unknown	n/a
1:24:DGL:C	1:25:SER:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	12	DAS	D-ASPARTIC ACID	Assigned chemical shifts, Coordinates
A	15	DPR	D-PROLINE	Assigned chemical shifts, Distance restraints, Coordinates
A	16	DGL	D-GLUTAMIC ACID	Assigned chemical shifts, Coordinates
A	17	DAL	D-ALANINE	Assigned chemical shifts, Coordinates
A	18	DGL	D-GLUTAMIC ACID	Assigned chemical shifts, Coordinates
A	19	DAR	D-ARGININE	Assigned chemical shifts, Coordinates
A	20	DLY	D-LYSINE	Assigned chemical shifts, Coordinates
A	21	DCY	D-CYSTEINE	Assigned chemical shifts, Coordinates
A	22	DAR	D-ARGININE	Assigned chemical shifts, Coordinates
A	23	DGL	D-GLUTAMIC ACID	Assigned chemical shifts, Coordinates
A	24	DGL	D-GLUTAMIC ACID	Assigned chemical shifts, Coordinates

Sequence alignments

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

--------10--------20------
NPELQRKCKELXTRXXXXXXXXXXSD
||||||||||||||||||||||||||
NPELQRKCKELXTRXXXXXXXXXXSD

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_30144_5kx0.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	15		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	234		100.0 (chain: A, length: 26)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	148 (1)	noe	61.5 (chain: A, length: 26)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	6 (1)	hbond	23.1 (chain: A, length: 26)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	22 (22)	.	46.2 (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: 167
  - ¹³C chemical shifts: 46
  - ¹⁵N chemical shifts: 21
- 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
12	DAS
15	DPR
16	DGL
18	DGL
19	DAR
20	DLY
21	DCY
22	DAR
23	DGL
24	DGL

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
9	LYS	HZ1	7.554
9	LYS	HZ2	7.554
9	LYS	HZ3	7.554

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	100	96.2
¹³C chemical shifts	69	31	44.9
¹⁵N chemical shifts	19	15	78.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	31	31	100.0
¹³C chemical shifts	31	8	25.8
¹⁵N chemical shifts	15	13	86.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	73	69	94.5
¹³C chemical shifts	38	23	60.5
¹⁵N chemical shifts	4	2	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	6	100.0
¹³C chemical shifts	6	6	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: 26, Sequence coverage: 61.5%
- Total number of restraints: 148
- Weight of restraints: 1.0 (148)
- Potential type of restraints: square-well-parabolic (148)
- Range of distance target values: 2.38, 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: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 26, Sequence coverage: 23.1%
  - Total number of restraints: 6
  - Weight of restraints: 1.0 (6)
  - Potential type of restraints: square-well-parabolic (6)
  - 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: 46.2%
- Total number of restraints: 22
- Total number of restraints per polymer type: 22
- Weight of restraints: 1.0 (22)
- Potential type of restraints: square-well-parabolic (22)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords de novo protein, designed peptide

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BMRB: 30144

Sample #1

Sample #2

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail