BMRBj - BMREntryMaster

	Total	¹³C	¹⁵N
All	83.0 % (137 of 165)	80.6 % (108 of 134)	93.5 % (29 of 31)
Backbone	98.3 % (114 of 116)	97.7 % (85 of 87)	100.0 % (29 of 29)
Sidechain	64.5 % (49 of 76)	66.2 % (49 of 74)	0.0 % (0 of 2)
Aromatic	0.0 % (0 of 23)	0.0 % (0 of 22)	0.0 % (0 of 1)
Methyl	100.0 % (13 of 13)	100.0 % (13 of 13)

1. HNP-1

ACYCRIPACI AGERRYGTCI YQGRLWAFCC

Show sample condition

Sample

Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 268 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

Protein Blocks Logo

Calculated from 10 models in PDB: 2KHT, Strand ID: A Detail

Release date

2010-01-11

Citation

3D (13)C-(13)C-(13)C correlation NMR for de novo distance determination of solid proteins and application to a human alpha-defensin
Li, S., Zhang, Y., Hong, M.
J. Magn. Reson. (2010), 202, 203-210, PubMed 19963419 , DOI 10.1016/j.jmr.2009.11.011 , Abstract

Related entities 1. Microcrystalline HNP-1, : 1 : 4 : 1 : 22 : 85 entities Detail

Interaction partners 1. Microcrystalline HNP-1, : 5 interactors Detail

More details for 5 interactors identified by 5 citations

Experiments performed 7 experiments Detail

1 2D 13C-13C DARR 40 ms, 100 ms & 200 ms

Instrument

Bruker Avance - 600 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 268 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

2 2D 15N-15N PDSD 3 s

Instrument

Bruker Avance - 600 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 268 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

3 2D CM5RR 0.8 ms & 1.5 ms

Instrument

Bruker Avance - 900 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 253 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

4 2D CHHC 200 us & 300 us

Instrument

Bruker Avance - 600 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 253 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

5 3D 15N-13C-13C NCACX

Instrument

Bruker Avance - 600 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 268 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

6 3D 15N-13C-13C NCOCX

Instrument

Bruker Avance - 600 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 268 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

7 2D 15N-13C NCX

Instrument

Bruker Avance - 900 MHz

Sample

State solid, Solvent system 40% H2O, 60% PEG400, Pressure 1 atm, Temperature 253 K, pH 6.5

#	Name	Isotope labeling	Concentration
1	HNP-1
2	PEG400	natural abundance	60% w/v
3	Cacodylate	natural abundance	30 mM
4	Lithium Sulfate	natural abundance	60 mM

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_16254_2kht.nef
Input source #2: Coordindates	2kht.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

--------10--------20--------30
ACYCRIPACIAGERRYGTCIYQGRLWAFCC
||||||||||||||||||||||||||||||
ACYCRIPACIAGERRYGTCIYQGRLWAFCC

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	30	0	0	100.0

Content subtype: combined_16254_2kht.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	145		100.0 (chain: A, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	3 (1)	disulfide_bond	20.0 (chain: A, length: 30)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	129 (1)	undefined	100.0 (chain: A, length: 30)
3	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	207 (1)	undefined	100.0 (chain: A, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_5	OK	52 (52)	.	100.0 (chain: A, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 115
  - ¹⁵N chemical shifts: 30
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- 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: A

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
5	ARG	CZ	159.9
7	PRO	N	134.4
13	GLU	CD	183.45
15	ARG	CZ	158.8
16	TYR	CG	133.2
21	TYR	CG	128.5
22	GLN	CD	178.2
28	PHE	CG	130.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	134	108	80.6
¹⁵N chemical shifts	35	29	82.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	60	59	98.3
¹⁵N chemical shifts	29	29	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	74	49	66.2
¹⁵N chemical shifts	6	0	0.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	22	0	0.0
¹⁵N chemical shifts	1	0	0.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: disulfide_bond
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 20.0%
- Total number of restraints: 3
- Weight of restraints: 1.0 (3)
- Potential type of restraints: square-well-parabolic (3)
- Range of distance target values: 1.9, 1.9 (Å)
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
  - Total number of restraints: 129
  - Weight of restraints: 1.0 (129)
  - Potential type of restraints: square-well-parabolic (129)
  - Range of distance target values: 3.8, 5.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map
  - Saveframe: CNS/XPLOR_distance_constraints_4
    - Status: OK
    - Experiment type: undefined
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
    - Total number of restraints: 207
    - Weight of restraints: 1.0 (207)
    - Potential type of restraints: square-well-parabolic (207)
    - Range of distance target values: 5.0, 5.0 (Å)
    - Distance restraints per residue
      - Chain_ID: A
    - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_5
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 30, Sequence coverage: 100.0%
- Total number of restraints: 52
- Total number of restraints per polymer type: 52
- Weight of restraints: 1.0 (52)
- Potential type of restraints: square-well-parabolic (52)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords human alpha defensin, microcrystalline protein, resonance assignment, solid state NMR, structure determination

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Found 1 Document (0.648 seconds)

BMRB: 16254

Sample

Related entities 1. Microcrystalline HNP-1, : 1 : 4 : 1 : 22 : 85 entities Detail

Interaction partners 1. Microcrystalline HNP-1, : 5 interactors Detail

Experiments performed 7 experiments Detail

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NMR combined restraints 6 contents Detail