BMRBj - BMREntryMaster

	Total	¹³C
All	58.7 % (27 of 46)	58.7 % (27 of 46)
Backbone	84.6 % (22 of 26)	84.6 % (22 of 26)
Sidechain	42.9 % (12 of 28)	42.9 % (12 of 28)
Aromatic	50.0 % (5 of 10)	50.0 % (5 of 10)

1. entity 1

RPPGFSPFR

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Sample #1

Solvent system 100% H2O, Pressure 1 atm, Temperature 200 K, pH 7.4, Details 0.36 ug/uL [U-13C, 15N]-F8R9 Bradykinin (BK), 21.4 mg/mL unlabeled hB2R, 50 mM unlabeled HEPES, 100 mM unlabeled NaCl, 2 mM unlabeled EDTA, 4 % w/v unlabeled DDM, 100% H2O

#	Name	Isotope labeling	Concentration
1	Bradykinin (BK)	[U-13C; 15N]-F8R9	0.36 ug/uL
2	hB2R	natural abundance	21.4 mg/mL
3	HEPES	natural abundance	50 mM
4	NaCl	natural abundance	100 mM
5	EDTA	natural abundance	2 mM
6	DDM	natural abundance	4 % w/v

Sample #2

Solvent system 100% H2O, Pressure 1 atm, Temperature 200 K, pH 7.4, Details 0.36 ug/uL [U-13C, 15N]-P2P3G4F5S6P7F8 Bradykinin (BK), 21.4 mg/mL unlabeled hB2R, 50 mM unlabeled HEPES, 100 mM unlabeled NaCl, 2 mM unlabeled EDTA, 4 % w/v unlabeled DDM, 100% H2O

#	Name	Isotope labeling	Concentration
7	Bradykinin (BK)	[U-13C, 15N]-P2P3G4F5S6P7F8	0.36 ug/uL
8	hB2R	natural abundance	21.4 mg/mL
9	HEPES	natural abundance	50 mM
10	NaCl	natural abundance	100 mM
11	EDTA	natural abundance	2 mM
12	DDM	natural abundance	4 % w/v

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Calculated from 10 models in PDB: 6F3V, Strand ID: A Detail

Release date

2018-01-02

Citation 1

The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy
Lopez, J.J., Shukla, A.K., Reinhart, C., Schwalbe, H., Michel, H., Glaubitz, C.
Angew. Chem Int Ed Engl. (2008), 47, 1668-1671, PubMed 18236494 , DOI 10.1002/anie.200704282 , Abstract

Show more 1 citaion

Citation 2

The molecular basis of subtype selectivity of human kinin G-protein-coupled receptors
Joedicke, L., Mao, J., Kuenze, G., Reinhart, C., Kalavacherla, T., Jonker, H., Richter, C., Schwalbe, H., Meiler, J., Preu, J., Michel, H., Glaubitz, C.
Nat. Chem. Biol. (2018), 14, 284-290, PubMed 29334381 , DOI 10.1038/nchembio.2551 , Abstract

Hide non-primary 1 citaion

Related entities 1. Bradykinin (BK), : 17 : 1 entities Detail

Interaction partners 1. Bradykinin (BK), : 10 interactors Detail

More details for 10 interactors identified by 7 citations

Experiments performed 2 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Dihedral angle restraints	combined_34206_6f3v.nef
Input source #2: Coordindates	6f3v.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	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

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

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RPPGFSPFR
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RPPGFSPFR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	9	0	0	100.0

Content subtype: combined_34206_6f3v.nef

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	22		88.9 (chain: A, length: 9)
1	Dihedral angle restraints	DYANA/DIANA_dihedral_2	OK	10 (10)	.	77.8 (chain: A, length: 9)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 9, Sequence coverage: 88.9%
- Total number of assignments
  - ¹³C chemical shifts: 22
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- 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	46	22	47.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	18	15	83.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	28	7	25.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	10	0	0.0

Dihedral angle restraints

Saveframe: DYANA/DIANA_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 9, Sequence coverage: 77.8%
- Total number of restraints: 10
- Total number of restraints per polymer type: 10
- Weight of restraints: 1.0 (10)
- Potential type of restraints: square-well-parabolic (10)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords GPCR, MEMBRANE PROTEIN

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Found 1 Document (0.648 seconds)

BMRB: 34206

Sample #1

Sample #2

Related entities 1. Bradykinin (BK), : 17 : 1 entities Detail

Interaction partners 1. Bradykinin (BK), : 10 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 3 contents Detail