BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	83.7 % (473 of 565)	100.0 % (297 of 297)	65.6 % (141 of 215)	66.0 % (35 of 53)
Backbone	73.8 % (217 of 294)	100.0 % (102 of 102)	58.6 % (85 of 145)	63.8 % (30 of 47)
Sidechain	92.1 % (291 of 316)	100.0 % (195 of 195)	79.1 % (91 of 115)	83.3 % (5 of 6)
Aromatic	96.4 % (54 of 56)	100.0 % (28 of 28)	96.3 % (26 of 27)	0.0 % (0 of 1)
Methyl	100.0 % (32 of 32)	100.0 % (16 of 16)	100.0 % (16 of 16)

1. AhPDF1

XRLCEKPSGT WSGVCGNNGA CRNQCIRLEK ARHGSCNYVF PAHKCICYFP C

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 4.5

#	Name	Isotope labeling	Concentration
1	AhPDF1	natural abundance	1.3 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 4.5

#	Name	Isotope labeling	Type	Concentration
4	AhPDF1	natural abundance		1.3 mM
5	D2O	natural abundance		100 %

Protein Blocks Logo

Calculated from 10 models in PDB: 2M8B, Strand ID: B Detail

Release date

2014-05-11

Citation

Folding and structural studies of the protein AhPDF1
Meindre, F., Paquet, F., Landon, C., Meindre, F., Paquet, F., Landon, C.
Not known

Related entities 1. AhPDF1 from Arabidopsis halleri, : 1 : 84 entities Detail

Experiments performed 7 experiments Detail

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_19237_2m8b.nef
Input source #2: Coordindates	2m8b.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	True (see coodinates for details)
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)
B:4:CYS:SG	B:51:CYS:SG	unknown, CA 60.428 ppm	oxidized, CA 57.632, CB 44.537 ppm	2.03
B:15:CYS:SG	B:36:CYS:SG	oxidized, CA 57.919, CB 39.661 ppm	oxidized, CA 52.833, CB 37.259 ppm	2.028
B:21:CYS:SG	B:45:CYS:SG	oxidized, CA 59.283, CB 37.802 ppm	oxidized, CB 36.42 ppm	2.026
B:25:CYS:SG	B:47:CYS:SG	oxidized, CA 60.365, CB 38.032 ppm	unknown, CA 52.088 ppm	2.034

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)
1:1:PCA:C	1:2:ARG:N	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
B	1	PCA	PYROGLUTAMIC ACID	Assigned chemical shifts, Distance restraints, Coordinates

Sequence alignments

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

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
B	B	51	0	0	100.0

Content subtype: combined_19237_2m8b.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	5		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	470		100.0 (chain: B, length: 51)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	1152 (1)	noe	100.0 (chain: B, length: 51)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 51, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 312
  - ¹³C chemical shifts: 128
  - ¹⁵N chemical shifts: 30
- Completeness of assignments
  - Entity_assemble_ID: B
- 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: B

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
6	LYS	HZ1	7.384
6	LYS	HZ2	7.384
6	LYS	HZ3	7.384
10	THR	HG1	1.144
30	LYS	HZ1	7.566
30	LYS	HZ2	7.566
30	LYS	HZ3	7.566
44	LYS	HZ1	7.656
44	LYS	HZ2	7.656
44	LYS	HZ3	7.656

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	303	302	99.7
¹³C chemical shifts	218	128	58.7
¹⁵N chemical shifts	58	30	51.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	103	99.0
¹³C chemical shifts	101	40	39.6
¹⁵N chemical shifts	48	25	52.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	199	199	100.0
¹³C chemical shifts	117	88	75.2
¹⁵N chemical shifts	10	5	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	16	16	100.0
¹³C chemical shifts	16	16	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	28	28	100.0
¹³C chemical shifts	27	26	96.3
¹⁵N chemical shifts	1	0	0.0

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: B, Chain length: 51, Sequence coverage: 100.0%
- Total number of restraints: 1152
- Weight of restraints: 1.0 (1152)
- Potential type of restraints: square-well-parabolic (1152)
- Range of distance target values: 1.55, 5.76 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: B
- Distance restraints on contact map

Keywords 4 disulfide bridges, CSab, plant defensin

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Found 1 Document (0.642 seconds)

BMRB: 19237

Sample #1

Sample #2

Related entities 1. AhPDF1 from Arabidopsis halleri, : 1 : 84 entities Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 3 contents Detail