BMRBj - BMREntryMaster

Found 1 Document (0.386 seconds)

BMRB: 30434

6COV

CSP2-l14

Authors

Yang, Y.

Assembly

Competence-stimulating peptide type 1

Entity

1. Competence-stimulating peptide type 1 (polymer, Thiol state: not present), 17 monomers, 2178.685 Da Detail

EMRISRIILD FLFLRKK

Formula weight

2178.685 Da

Source organism

Streptococcus pneumoniae

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 61.5 %, Completeness (bb): 77.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	61.5 % (147 of 239)	76.6 % (98 of 128)	35.1 % (33 of 94)	94.1 % (16 of 17)
Backbone	77.5 % (79 of 102)	88.2 % (30 of 34)	64.7 % (33 of 51)	94.1 % (16 of 17)
Sidechain	54.5 % (84 of 154)	72.3 % (68 of 94)	26.7 % (16 of 60)
Aromatic	15.0 % (3 of 20)	30.0 % (3 of 10)	0.0 % (0 of 10)
Methyl	50.0 % (12 of 24)	100.0 % (12 of 12)	0.0 % (0 of 12)

1. Competence-stimulating peptide type 2

EMRISRIILD FLFLRKK

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details 250 mM D DPC, 1.9 mM Competence stimulating peptide type 2 mutant - CSP2l14, 90% H2O/10% D2O

#	Name	Isotope labeling	Type	Concentration
1	DPC	D		250 mM
2	Competence stimulating peptide type 2 mutant - CSP2l14	natural abundance		1.9 mM

Release date

2018-07-16

Citation

Structural Characterization of Competence-Stimulating Peptide Analogues Reveals Key Features for ComD1 and ComD2 Receptor Binding in Streptococcus pneumoniae
Yang, Y., Cornilescu, G., Tal-Gan, Y.
Biochemistry (2018), 57, 5359-5369, PubMed 30125091 , DOI 10.1021/acs.biochem.8b00653 , Abstract

Related entities 1. Competence-stimulating peptide type 1, : 1 : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30434_6cov.nef
Input source #2: Coordindates	6cov.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	True (see coodinates for details)
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Error

Disulfide bonds

None

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

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:13:PHE:C	1:14:DLE:N	unknown	unknown	n/a
1:14:DLE:C	1:15:ARG:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	14	DLE	D-LEUCINE	Coordinates

Sequence alignments

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

--------10-------
EMRISRIILDFLFXRKK
|||||||||||||||||
EMRISRIILDFLFXRKK

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	17	0	0	100.0

Content subtype: combined_30434_6cov.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	2		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Error	145		88.2 (chain: A, length: 17)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	998 (1)	noe	88.2 (chain: A, length: 17)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	23 (23)	.	70.6 (chain: A, length: 17)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Error
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 17, Sequence coverage: 88.2%
- Total number of assignments
  - ¹H chemical shifts: 100
  - ¹³C chemical shifts: 30
  - ¹⁵N chemical shifts: 15
- Completeness of assignments
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 17, Sequence coverage: 88.2%
- Total number of restraints: 946
- Weight of restraints: 1.0 (946)
- Potential type of restraints: square-well-parabolic (946)
- Range of distance target values: 2.2, 4.65 (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

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 17, Sequence coverage: 70.6%
- Total number of restraints: 23
- Total number of restraints per polymer type: 23
- Weight of restraints: 1.0 (23)
- Potential type of restraints: square-well-parabolic (23)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords CSP, SIGNALING PROTEIN, pneumococcus, quorum sensing, signaling molecule

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Found 1 Document (0.386 seconds)

BMRB: 30434

Sample

Related entities 1. Competence-stimulating peptide type 1, : 1 : 1 : 2 entities Detail

Experiments performed 5 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 4 contents Detail