BMRBj - BMREntryMaster

	Total	¹H	¹³C
All	75.3 % (134 of 178)	90.3 % (93 of 103)	54.7 % (41 of 75)
Backbone	70.2 % (66 of 94)	92.1 % (35 of 38)	55.4 % (31 of 56)
Sidechain	81.4 % (83 of 102)	89.2 % (58 of 65)	67.6 % (25 of 37)
Methyl	88.9 % (16 of 18)	100.0 % (9 of 9)	77.8 % (7 of 9)

1. entity 1

SPEERAQLCT AAEKADELG

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 4, Details 0.7 mM non-label 1, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	entity_1	natural abundance		0.7 (±0.05) mM

Protein Blocks Logo

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

Release date

2017-09-26

Citation

De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures
Dang, B., Wu, H., Mulligan, V.K., Mravic, M., Wu, Y., Lemmin, T., Ford, A., Silva, D.A., Baker, D., DeGrado, W.F.
Proc. Natl. Acad. Sci. U. S. A. (2017), 114, 10852-10857, PubMed 28973862 , DOI 10.1073/pnas.1710695114 , Abstract

Entries sharing articles BMRB: 2 entries Detail

  BMRB: 30320 released on 2017-09-26
    Title De Novo Design of Covalently Constrained Meso-size Protein Scaffolds with Unique Tertiary Structures
  BMRB: 30267 released on 2017-06-19
    Title De Novo Design of Novel Covalent Constrained Meso-size Peptide Scaffolds with Unique Tertiary Structures

Experiments performed 3 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30319_5woc.nef
Input source #2: Coordindates	5woc.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)
1:9:CYS:SG	3:1:B74:CB1	unknown	unknown	n/a
2:9:CYS:SG	3:1:B74:CB2	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
C	1	B74	(3-methylphenyl)methanol	None

Sequence alignments

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

--------10---------
SPEERAQLCTAAEKADELG
|||||||||||||||||||
SPEERAQLCTAAEKADELG

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

--------10---------
SPEERAQLCTAAEKADELG
|||||||||||||||||||
SPEERAQLCTAAEKADELG

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	19	0	0	100.0
B	B	19	0	0	100.0

Content subtype: combined_30319_5woc.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	301		100.0 (chain: A, length: 19), 100.0 (chain: B, length: 19)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	578 (1)	noe	100.0 (chain: A, length: 19), 100.0 (chain: B, length: 19)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	40 (40)	.	84.2 (chain: A, length: 19), 84.2 (chain: B, length: 19)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 19, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 19, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 214
  - ¹³C chemical shifts: 87
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- 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
  - Chain_ID: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
1	SER	HG	4.87
14	LYS	HZ1	7.61
14	LYS	HZ2	7.61
14	LYS	HZ3	7.61

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	103	102	99.0
¹³C chemical shifts	75	44	58.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	37	97.4
¹³C chemical shifts	38	16	42.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	65	65	100.0
¹³C chemical shifts	37	28	75.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0
¹³C chemical shifts	9	7	77.8

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
1	SER	HG	4.87
14	LYS	HZ1	7.61
14	LYS	HZ2	7.61
14	LYS	HZ3	7.61

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	103	102	99.0
¹³C chemical shifts	75	43	57.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	38	37	97.4
¹³C chemical shifts	38	15	39.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	65	65	100.0
¹³C chemical shifts	37	28	75.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	9	9	100.0
¹³C chemical shifts	9	7	77.8

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 19, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 19, Sequence coverage: 100.0%
- Total number of restraints: 574
- Weight of restraints: 1.0 (574)
- Potential type of restraints: square-well-parabolic (574)
- Range of distance target values: 2.13, 4.6 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 19, Sequence coverage: 84.2%
  - Entity_assembly_ID: B, Chain length: 19, Sequence coverage: 84.2%
- Total number of restraints: 40
- Total number of restraints per polymer type: 40
- Weight of restraints: 1.0 (40)
- Potential type of restraints: square-well-parabolic (40)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords Covalent Constrained Peptide, DE NOVO PROTEIN, De Novo design

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BMRB: 30319

Sample

Entries sharing articles BMRB: 2 entries Detail

Experiments performed 3 experiments Detail

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Instrument

Sample

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Sample

NMR combined restraints 4 contents Detail