BMRBj - BMREntryMaster

Found 1 Document (0.522 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

Search

Query history

Resources

Search for primary databases

Search for subsidiary databases

Display

Hits per page

Statistics

Query Changes will take effect after "OK" button is selected.

Maximum hits

Default conjunction operator

Omni-box

Search filter

Sequence search (BLAST)

E-value

Query sequence coverage

Miscellaneous

The number of previewed publications

Completeness of assigned chemical shift

Sequence chart about top aligned regions

Sequence chart about interacting regions

Hit context with highlight

Link destinations for BMRB, PDB and EMDB

Found 1 Document (0.522 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