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BMRB: 30848

7LHC

NMR Solution Structure of [T20K]kalata B1

Authors

Harvey, P.J., Craik, D.J., Gruber, C.W.

Assembly

Kalata-B1

Entity

1. Kalata-B1 (polymer, Thiol state: all disulfide bound), 29 monomers, 2943.403 Da Detail

GLPVCGETCV GGTCNTPGCK CSWPVCTRN

Formula weight

2943.403 Da

Entity Connection

disulfide 3, covalent 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS5:SG	1:CYS19:SG
2	disulfide	sing	1:CYS9:SG	1:CYS21:SG
3	disulfide	sing	1:CYS14:SG	1:CYS26:SG
4	covalent	sing	1:GLY1:N	1:ASN29:C

Source organism

Oldenlandia affinis

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 85.6 %, Completeness (bb): 82.1 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	85.6 % (249 of 291)	98.0 % (146 of 149)	67.0 % (75 of 112)	93.3 % (28 of 30)
Backbone	82.1 % (138 of 168)	100.0 % (60 of 60)	63.4 % (52 of 82)	100.0 % (26 of 26)
Sidechain	91.8 % (135 of 147)	96.6 % (86 of 89)	87.0 % (47 of 54)	50.0 % (2 of 4)
Aromatic	25.0 % (3 of 12)	50.0 % (3 of 6)	0.0 % (0 of 5)	0.0 % (0 of 1)
Methyl	91.7 % (22 of 24)	100.0 % (12 of 12)	83.3 % (10 of 12)

1. entity 1

GLPVCGETCV GGTCNTPGCK CSWPVCTRN

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 3.3, Details 1.0 mM peptide, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	peptide	natural abundance		1.0 (±0.1) mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 298 K, pH 3.3, Details 1.0 mM peptide, 100% D2O

#	Name	Isotope labeling	Type	Concentration
2	peptide	natural abundance		1.0 (±0.1) mM

Release date

2021-02-07

Citation

Importance of the Cyclic Cystine Knot Structural Motif for Immunosuppressive Effects of Cyclotides
Hellinger, R., Muratspahic, E., Devi, S., Koehbach, J., Vasileva, M., Harvey, P.J., Craik, D.J., Grundemann, C., Gruber, C.W.
ACS Chem. Biol. (2021), 16, 2373-2386, PubMed 34592097 , DOI 10.1021/acschembio.1c00524 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 30935 released on 2021-07-29
Title NMR Solution structure of linear [T20K]kalataB1

Related entities 1. Kalata-B1, : 1 : 17 : 103 entities Detail

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr30848_3.str
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	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)
1:5:CYS:SG	1:19:CYS:SG	oxidized, CA 59.335, CB 49.002 ppm	oxidized, CA 58.137, CB 49.983 ppm	n/a
1:9:CYS:SG	1:21:CYS:SG	oxidized, CA 54.674, CB 47.686 ppm	oxidized, CA 56.35, CB 39.907 ppm	n/a
1:14:CYS:SG	1:26:CYS:SG	oxidized, CA 55.253, CB 45.325 ppm	oxidized, CA 56.784, CB 44.002 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr30848_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	273		100.0 (chain: 1, length: 29)
1	Chemical shift references	chem_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 29, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 173
  - ¹³C chemical shifts: 72
  - ¹⁵N chemical shifts: 28
- Completeness of assignments
  - Entity_assemble_ID: 1
- 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: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
20	LYS	HZ1	7.506
20	LYS	HZ2	7.506
20	LYS	HZ3	7.506

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	149	146	98.0
¹³C chemical shifts	112	72	64.3
¹⁵N chemical shifts	30	28	93.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	60	60	100.0
¹³C chemical shifts	58	25	43.1
¹⁵N chemical shifts	26	26	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	89	86	96.6
¹³C chemical shifts	54	47	87.0
¹⁵N chemical shifts	4	2	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	12	12	100.0
¹³C chemical shifts	12	10	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	6	3	50.0
¹³C chemical shifts	5	0	0.0
¹⁵N chemical shifts	1	0	0.0

Keywords CCK motif, PLANT PROTEIN, cyclic peptide, cyclotide, knottin

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Found 1 Document (0.525 seconds)

BMRB: 30848

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Kalata-B1, : 1 : 17 : 103 entities Detail

Experiments performed 6 experiments Detail

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Chemical shift validation 3 contents Detail