BMRBj - BMREntryMaster

Found 1 Document (0.49 seconds)

BMRB: 34298

6H0I

Solution structure of Melampsora larici-populina MlpP4.1

Authors

Tsan, P.

Assembly

Secreted protein

Entity

1. Secreted protein (polymer, Thiol state: free and disulfide bound), 75 monomers, 7965.508 Da Detail

MCEFIEDSED IQGLKSLRKS HTSLEDDDDG SRGGDCEGCS GTACSSDAQC RARGCDGCST SGVCVLSSLH HHHHH

Formula weight

7965.508 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS39:SG	1:CYS55:SG
2	disulfide	sing	1:CYS44:SG	1:CYS58:SG
3	disulfide	sing	1:CYS50:SG	1:CYS64:SG

Source organism

Melampsora larici-populina 98AG31

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.3 %, Completeness: 64.3 %, Completeness (bb): 72.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	64.3 % (480 of 746)	74.7 % (286 of 383)	44.1 % (126 of 286)	88.3 % (68 of 77)
Backbone	72.7 % (327 of 450)	87.4 % (139 of 159)	56.5 % (122 of 216)	88.0 % (66 of 75)
Sidechain	43.9 % (159 of 362)	65.6 % (147 of 224)	7.4 % (10 of 136)	100.0 % (2 of 2)
Aromatic	0.0 % (0 of 38)	0.0 % (0 of 19)	0.0 % (0 of 19)
Methyl	41.7 % (20 of 48)	75.0 % (18 of 24)	8.3 % (2 of 24)

1. entity 1

MCEFIEDSED IQGLKSLRKS HTSLEDDDDG SRGGDCEGCS GTACSSDAQC RARGCDGCST SGVCVLSSLH HHHHH

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 50 mM potassium phosphate, 0.02 % sodium azide, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	entity_1	[U-15N]	1.8 mM
2	potassium phosphate	natural abundance	50 mM
3	sodium azide	natural abundance	0.02 %

Release date

2018-08-14

Citation

Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds
de Guillen, K., Lorrain, C., Tsan, P., Barthe, P., Petre, B., Saveleva, N., Rouhier, N., Duplessis, S., Padilla, A., Hecker, A.
Sci. Rep. (2019), 9, 18084-18084, PubMed 31792250 , DOI 10.1038/s41598-019-53816-9 , Abstract

Related entities 1. Secreted protein, : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34298_6h0i.nef
Input source #2: Coordindates	6h0i.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	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:39:CYS:SG	A:55:CYS:SG	unknown, CA 58.211 ppm	unknown, CA 58.666 ppm	2.033
A:44:CYS:SG	A:58:CYS:SG	unknown, CA 53.993 ppm	unknown, CA 54.368 ppm	2.024
A:50:CYS:SG	A:64:CYS:SG	unknown, CA 56.993 ppm	unknown, CA 54.097 ppm	2.031

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--------30--------40--------50--------60--------70-----
MCEFIEDSEDIQGLKSLRKSHTSLEDDDDGSRGGDCEGCSGTACSSDAQCRARGCDGCSTSGVCVLSSLHHHHHH
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MCEFIEDSEDIQGLKSLRKSHTSLEDDDDGSRGGDCEGCSGTACSSDAQCRARGCDGCSTSGVCVLSSLHHHHHH

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	75	0	0	100.0

Content subtype: combined_34298_6h0i.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	OK	464		88.0 (chain: A, length: 75)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	761 (1)	noe	86.7 (chain: A, length: 75)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	10 (1)	hbond	21.3 (chain: A, length: 75)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	OK	75 (75)	.	72.0 (chain: A, length: 75)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 88.0%
- Total number of assignments
  - ¹³C chemical shifts: 115
  - ¹H chemical shifts: 282
  - ¹⁵N chemical shifts: 67
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- 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 (%)
¹³C chemical shifts	286	115	40.2
¹H chemical shifts	383	282	73.6
¹⁵N chemical shifts	81	67	82.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	150	115	76.7
¹H chemical shifts	159	138	86.8
¹⁵N chemical shifts	75	65	86.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	136	0	0.0
¹H chemical shifts	224	144	64.3
¹⁵N chemical shifts	6	2	33.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	25	0	0.0
¹H chemical shifts	25	18	72.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	19	0	0.0
¹H chemical shifts	19	0	0.0

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: 75, Sequence coverage: 86.7%
- Total number of restraints: 761
- Weight of restraints: 1.0 (761)
- Potential type of restraints: square-well-parabolic (761)
- Range of distance target values: 2.08, 6.08 (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_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 21.3%
  - Total number of restraints: 10
  - Weight of restraints: 1.0 (10)
  - Potential type of restraints: square-well-parabolic (10)
  - Range of distance target values: 2.21, 2.21 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 75, Sequence coverage: 72.0%
- Total number of restraints: 75
- Total number of restraints per polymer type: 75
- Weight of restraints: 1.0 (75)
- Potential type of restraints: square-well-parabolic (75)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords UNKNOWN FUNCTION, cysteine knot protein, effector, poplar rust

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Found 1 Document (0.49 seconds)

BMRB: 34298

Sample

Related entities 1. Secreted protein, : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail