BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	84.5 % (218 of 258)	91.7 % (122 of 133)	72.3 % (73 of 101)	95.8 % (23 of 24)
Backbone	75.0 % (96 of 128)	93.2 % (41 of 44)	57.8 % (37 of 64)	90.0 % (18 of 20)
Sidechain	84.0 % (126 of 150)	82.0 % (73 of 89)	86.0 % (49 of 57)	100.0 % (4 of 4)
Aromatic	67.9 % (19 of 28)	71.4 % (10 of 14)	61.5 % (8 of 13)	100.0 % (1 of 1)
Methyl	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)

1. O2 contryphan Vc1 prepropeptide

QWCQPGYAYN PVLGICTITL SR

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Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 293 K, pH 4.0, Details 500 uM Con-Vc1R, 93% H2O/7% D2O

#	Name	Isotope labeling	Concentration
1	Con-Vc1R	natural abundance	500 (±0.2) uM
2	H2O	natural abundance	93 %
3	D2O	natural abundance	7 %

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

Release date

2016-11-10

Citation

The Single Disulfide-Directed β-Hairpin Fold. Dynamics, Stability, and Engineering
Chittoor, B., Krishnarjuna, B., Morales, R., MacRaild, C.A., Sadek, M., Leung, E., Robinson, S.D., Pennington, M.W., Norton, R.S.
Biochemistry (2017), 56, 2455-2466, PubMed 28437072 , DOI 10.1021/acs.biochem.7b00120 , Abstract

Related entities 1. O2 contryphan Vc1 prepropeptide, : 1 : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 2 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts	combined_30124_5kkm.nef
Input source #2: Coordindates	5kkm.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	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:3:CYS:SG	A:16:CYS:SG	oxidized, CA 51.873, CB 42.124 ppm	oxidized, CA 56.217, CB 42.948 ppm	2.02

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

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

--------10--------20--
QWCQPGYAYNPVLGICTITLSR
||||||||||||||||||||||
QWCQPGYAYNPVLGICTITLSR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	22	0	0	100.0

Content subtype: combined_30124_5kkm.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	219		100.0 (chain: A, length: 22)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 22, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 122
  - ¹³C chemical shifts: 73
  - ¹⁵N chemical shifts: 24
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	133	122	91.7
¹³C chemical shifts	101	73	72.3
¹⁵N chemical shifts	25	24	96.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	44	43	97.7
¹³C chemical shifts	44	19	43.2
¹⁵N chemical shifts	20	19	95.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	89	79	88.8
¹³C chemical shifts	57	54	94.7
¹⁵N chemical shifts	5	5	100.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	14	14	100.0
¹³C chemical shifts	13	12	92.3
¹⁵N chemical shifts	1	1	100.0

Covalent bonds

Saveframe: assembly
- Status: OK

Keywords Single disulfide-directed beta hairpin, UNKNOWN FUNCTION, contryphan-Vc1, peptide scaffold, stability

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BMRB: 30124

Sample

Related entities 1. O2 contryphan Vc1 prepropeptide, : 1 : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

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NMR combined restraints 2 contents Detail