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Found 1 Document (0.513 seconds)

BMRB: 34486

6XYI

NMR solution structure of alpha-AnmTX- Ms11a-3 (Ms11a-3)

Authors

Mineev, K.S., Kornilov, F.D., Lushpa, V.A., Logashina, Y.A., Maleeva, E.E., Andreev, Y.A.

Assembly

AMS9.3.1

Entity

1. AMS9.3.1 (polymer, Thiol state: all disulfide bound), 42 monomers, 4923.782 Da Detail

GCKKLNSYCT RQHRECCHGL VCRRPDYGIG RGILWKCTRA RK

Formula weight

4923.782 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS2:SG	1:CYS17:SG
2	disulfide	sing	1:CYS9:SG	1:CYS22:SG
3	disulfide	sing	1:CYS16:SG	1:CYS37:SG

Source organism

Metridium senile

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.7 %, Completeness (bb): 83.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.7 % (462 of 504)	100.0 % (266 of 266)	78.1 % (146 of 187)	98.0 % (50 of 51)
Backbone	83.2 % (208 of 250)	100.0 % (88 of 88)	66.1 % (80 of 121)	97.6 % (40 of 41)
Sidechain	100.0 % (291 of 291)	100.0 % (178 of 178)	100.0 % (103 of 103)	100.0 % (10 of 10)
Aromatic	100.0 % (36 of 36)	100.0 % (18 of 18)	100.0 % (17 of 17)	100.0 % (1 of 1)
Methyl	100.0 % (30 of 30)	100.0 % (15 of 15)	100.0 % (15 of 15)

1. entity 1

GCKKLNSYCT RQHRECCHGL VCRRPDYGIG RGILWKCTRA RK

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 303 K, pH 4.5, Details 1.4 mM peptide, 95% H2O/5% D2O

#	Name	Isotope labeling	Type	Concentration
1	peptide	natural abundance		1.4 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 6XYI, Strand ID: A Detail

Release date

2020-07-13

Related entities 1. AMS9.3.1, : 1 : 4 entities Detail

Experiments performed 6 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr34486_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	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:2:CYS:SG	1:17:CYS:SG	oxidized, CA 54.247, CB 42.725 ppm	oxidized, CA 54.28, CB 40.587 ppm	n/a
1:9:CYS:SG	1:22:CYS:SG	oxidized, CA 53.735, CB 47.708 ppm	oxidized, CA 55.53, CB 40.856 ppm	n/a
1:16:CYS:SG	1:37:CYS:SG	oxidized, CA 55.113, CB 39.619 ppm	oxidized, CA 54.247, CB 38.973 ppm	n/a

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

None

Non-standard residues

None

Content subtype: bmr34486_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	496		100.0 (chain: 1, length: 42)
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: 42, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 304
  - ¹³C chemical shifts: 142
  - ¹⁵N chemical shifts: 50
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- 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)
4	LYS	HZ1	7.531
4	LYS	HZ2	7.531
4	LYS	HZ3	7.531
4	LYS	NZ	32.39
36	LYS	HZ1	6.856
36	LYS	HZ2	6.856
36	LYS	HZ3	6.856
42	LYS	HZ1	7.52
42	LYS	HZ2	7.52
42	LYS	HZ3	7.52

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	266	265	99.6
¹³C chemical shifts	187	142	75.9
¹⁵N chemical shifts	51	49	96.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	88	87	98.9
¹³C chemical shifts	84	39	46.4
¹⁵N chemical shifts	41	39	95.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	178	178	100.0
¹³C chemical shifts	103	103	100.0
¹⁵N chemical shifts	10	10	100.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	18	18	100.0
¹³C chemical shifts	17	17	100.0
¹⁵N chemical shifts	1	1	100.0

Keywords PROTEIN, TOXIN

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Found 1 Document (0.513 seconds)

BMRB: 34486

Sample

Related entities 1. AMS9.3.1, : 1 : 4 entities Detail

Experiments performed 6 experiments Detail

Instrument

Sample

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Chemical shift validation 3 contents Detail