BMRBj - BMREntryMaster

Found 1 Document (1.863 seconds)

BMRB: 19602

2MGT

Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide with Alzheimer`s disease pathogenic English mutation H6R

Authors

Polshakov, V., Istrate, A., Kozin, S.

Assembly

dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc

Entity

1. dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc, entity 1 (polymer, Thiol state: not present), 18 monomers, 1998.099 × 2 Da Detail

XDAEFRRDSG YEVHHQKX

2. ZINC ION (non-polymer), 65.409 Da

Total weight

4061.607 Da

Max. entity weight

1998.099 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 88.9 %, Completeness: 91.0 %, Completeness (bb): 84.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	91.0 % (172 of 189)	100.0 % (100 of 100)	77.8 % (56 of 72)	94.1 % (16 of 17)
Backbone	84.4 % (81 of 96)	100.0 % (33 of 33)	68.1 % (32 of 47)	100.0 % (16 of 16)
Sidechain	98.1 % (106 of 108)	100.0 % (67 of 67)	97.5 % (39 of 40)	0.0 % (0 of 1)
Aromatic	100.0 % (26 of 26)	100.0 % (13 of 13)	100.0 % (13 of 13)
Methyl	83.3 % (5 of 6)	100.0 % (3 of 3)	66.7 % (2 of 3)

1. entity 1

XDAEFRRDSG YEVHHQKX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 7.2

#	Name	Isotope labeling	Concentration
6	entity_1	natural abundance	2 mM
7	bis-Tris	[U-99% 2H]	20 mM
8	TSP	d4 (100%)	40 uM
9	D2O	natural abundance	100 %

Chem. Shift Complete2

Sequence coverage: 88.9 %, Completeness: 87.8 %, Completeness (bb): 79.7 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	87.8 % (332 of 378)	100.0 % (200 of 200)	72.9 % (105 of 144)	79.4 % (27 of 34)
Backbone	79.7 % (153 of 192)	100.0 % (66 of 66)	63.8 % (60 of 94)	84.4 % (27 of 32)
Sidechain	95.4 % (206 of 216)	100.0 % (134 of 134)	90.0 % (72 of 80)	0.0 % (0 of 2)
Aromatic	92.3 % (48 of 52)	100.0 % (26 of 26)	84.6 % (22 of 26)
Methyl	91.7 % (11 of 12)	100.0 % (6 of 6)	83.3 % (5 of 6)

1. entity 1

XDAEFRRDSG YEVHHQKX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pD 7.2

#	Name	Isotope labeling	Concentration
16	entity_1	natural abundance	2 mM
17	zinc cloride	natural abundance	1 mM
18	bis-Tris	[U-99% 2H]	20 mM
19	TSP	d4 (100%)	40 uM
20	D2O	natural abundance	100 %

Chem. Shift Complete3

Sequence coverage: 88.9 %, Completeness: 86.9 %, Completeness (bb): 78.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	86.9 % (493 of 567)	100.0 % (300 of 300)	71.8 % (155 of 216)	74.5 % (38 of 51)
Backbone	78.8 % (227 of 288)	100.0 % (99 of 99)	63.8 % (90 of 141)	79.2 % (38 of 48)
Sidechain	94.8 % (307 of 324)	100.0 % (201 of 201)	88.3 % (106 of 120)	0.0 % (0 of 3)
Aromatic	89.7 % (70 of 78)	100.0 % (39 of 39)	79.5 % (31 of 39)
Methyl	88.9 % (16 of 18)	100.0 % (9 of 9)	77.8 % (7 of 9)

1. entity 1

XDAEFRRDSG YEVHHQKX

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pD 7.2

#	Name	Isotope labeling	Concentration
16	entity_1	natural abundance	2 mM
17	zinc cloride	natural abundance	1 mM
18	bis-Tris	[U-99% 2H]	20 mM
19	TSP	d4 (100%)	40 uM
20	D2O	natural abundance	100 %

Protein Blocks Logo

Calculated from 20 models in PDB: 2MGT, Strand ID: A, B Detail

Release date

2014-11-09

Citation

[Optimization of the methods for small peptide solution structure determination by NMR spectroscopy]
Istrate, A.N., Makarov, A.A., Kozin, S.A., Polshakov, V.I.
Mol. Biol (Mosk). (2010), 44, 1075-1085, PubMed 21290829 , DOI: , Abstract

Related entities 1. dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc, entity 1, : 1 : 69 : 12 entities Detail

Interaction partners 1. dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc, entity 1, : 94 interactors Detail

More details for 94 interactors identified by 53 citations

Experiments performed 13 experiments Detail

1 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

2 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

3 2D DQF-COSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

4 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

5 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	2 mM
2	bis-Tris	[U-99% 2H]	20 mM
3	TSP	d4 (100%)	40 uM
4	H2O	natural abundance	90 %
5	D2O	natural abundance	10 %

6 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 278 K, Details pH 7.2

#	Name	Isotope labeling	Concentration
6	entity_1	natural abundance	2 mM
7	bis-Tris	[U-99% 2H]	20 mM
8	TSP	d4 (100%)	40 uM
9	D2O	natural abundance	100 %

7 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 278 K, Details pH 7.2

#	Name	Isotope labeling	Concentration
6	entity_1	natural abundance	2 mM
7	bis-Tris	[U-99% 2H]	20 mM
8	TSP	d4 (100%)	40 uM
9	D2O	natural abundance	100 %

8 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

9 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

10 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

11 2D 1H-13C HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 274 K, pH 6.8, Details pH 6.8

#	Name	Isotope labeling	Concentration
10	entity_1	natural abundance	2 mM
11	zinc cloride	natural abundance	1 mM
12	bis-Tris	[U-99% 2H]	20 mM
13	TSP	d4 (100%)	40 uM
14	H2O	natural abundance	90 %
15	D2O	natural abundance	10 %

12 2D 1H-1H NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 278 K, Details pD 7.2

#	Name	Isotope labeling	Concentration
16	entity_1	natural abundance	2 mM
17	zinc cloride	natural abundance	1 mM
18	bis-Tris	[U-99% 2H]	20 mM
19	TSP	d4 (100%)	40 uM
20	D2O	natural abundance	100 %

13 2D 1H-1H TOCSY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 278 K, Details pD 7.2

#	Name	Isotope labeling	Concentration
16	entity_1	natural abundance	2 mM
17	zinc cloride	natural abundance	1 mM
18	bis-Tris	[U-99% 2H]	20 mM
19	TSP	d4 (100%)	40 uM
20	D2O	natural abundance	100 %

NMR combined restraints 7 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19602_2mgt.nef
Input source #2: Coordindates	2mgt.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	Warning

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)
1:1:ACE:C	1:2:ASP:N	unknown	unknown	n/a
1:17:LYS:C	1:18:NH2:N	unknown	unknown	n/a
2:1:ACE:C	2:2:ASP:N	unknown	unknown	n/a
2:17:LYS:C	2:18:NH2:N	unknown	unknown	n/a
1:12:GLU:OE1	3:1:ZN:ZN	unknown	unknown	n/a
2:15:HIS:NE2	3:1:ZN:ZN	unknown	unknown	n/a
1:15:HIS:NE2	3:1:ZN:ZN	unknown	unknown	n/a
2:12:GLU:OE2	3:1:ZN:ZN	unknown	unknown	n/a
1:12:GLU:OE2	3:1:ZN:ZN	unknown	unknown	n/a
2:12:GLU:OE1	3:1:ZN:ZN	unknown	unknown	n/a

Non-standard residues

Chain_ID	Seq_ID	Comp_ID	Chem_comp_name	Experimental evidences
A	0	ACE	ACETYL GROUP	Coordinates
A	17	NH2	AMINO GROUP	Coordinates
B	0	ACE	ACETYL GROUP	Assigned chemical shifts, Coordinates
B	17	NH2	AMINO GROUP	Assigned chemical shifts, Coordinates
C	1	ZN	ZINC ION	Distance restraints, Torsion angle restraints

Sequence alignments

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

0--------10-------
XDAEFRRDSGYEVHHQKX
||||||||||||||||||
XDAEFRRDSGYEVHHQKX
--------10--------

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

0--------10-------
XDAEFRRDSGYEVHHQKX
||||||||||||||||||
XDAEFRRDSGYEVHHQKX
--------10--------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	18	0	0	100.0
B	B	18	0	0	100.0

Content subtype: combined_19602_2mgt.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	10		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	175		94.4 (chain: B, length: 18)
2	Assigned chemical shifts	Assigned_chemical_shifts_2	Warning	166		100.0 (chain: B, length: 18)
3	Assigned chemical shifts	Assigned_chemical_shifts_3	Warning	167		100.0 (chain: B, length: 18)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	424 (1)	noe	88.9 (chain: A, length: 18), 88.9 (chain: B, length: 18)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	6 (1)	undefined	11.1 (chain: A, length: 18), 11.1 (chain: B, length: 18), 100.0 (chain: C, length: 1)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	Warning	19 (19)	.	11.1 (chain: A, length: 18), 11.1 (chain: B, length: 18), 100.0 (chain: C, length: 1)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 94.4%
- Total number of assignments
  - ¹H chemical shifts: 103
  - ¹³C chemical shifts: 56
  - ¹⁵N chemical shifts: 16
- Completeness of assignments
  - Entity_assemble_ID: B
- 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
Saveframe: Assigned_chemical_shifts_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 105
  - ¹³C chemical shifts: 50
  - ¹⁵N chemical shifts: 11
- Completeness of assignments
  - Entity_assemble_ID: B
- 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
Saveframe: Assigned_chemical_shifts_3
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 105
  - ¹³C chemical shifts: 51
  - ¹⁵N chemical shifts: 11
- Completeness of assignments
  - Entity_assemble_ID: B
- 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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	101	97.1
¹³C chemical shifts	74	56	75.7
¹⁵N chemical shifts	20	16	80.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	34	100.0
¹³C chemical shifts	32	16	50.0
¹⁵N chemical shifts	17	16	94.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	70	67	95.7
¹³C chemical shifts	42	40	95.2
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	3	75.0

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

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	103	99.0
¹³C chemical shifts	74	50	67.6
¹⁵N chemical shifts	20	11	55.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	34	100.0
¹³C chemical shifts	32	16	50.0
¹⁵N chemical shifts	17	11	64.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	70	69	98.6
¹³C chemical shifts	42	34	81.0
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	4	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	9	69.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	104	103	99.0
¹³C chemical shifts	74	51	68.9
¹⁵N chemical shifts	20	11	55.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	34	34	100.0
¹³C chemical shifts	32	16	50.0
¹⁵N chemical shifts	17	11	64.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	70	69	98.6
¹³C chemical shifts	42	35	83.3
¹⁵N chemical shifts	3	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	4	4	100.0
¹³C chemical shifts	4	3	75.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	13	13	100.0
¹³C chemical shifts	13	9	69.2

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: 18, Sequence coverage: 88.9%
  - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 88.9%
- Total number of restraints: 424
- Weight of restraints: 1.0 (424)
- Potential type of restraints: square-well-parabolic (424)
- Range of distance target values: 1.25, 3.0 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
  - Chain_ID: C
    None
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: undefined
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 11.1%
    - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 11.1%
    - Entity_assembly_ID: C, Chain length: 1, Sequence coverage: 100.0%
  - Total number of restraints: 6
  - Weight of restraints: 1.0 (6)
  - Potential type of restraints: square-well-parabolic (6)
  - Range of distance target values: 2.1, 2.1 (Å)
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
    - Chain_ID: C
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 18, Sequence coverage: 11.1%
  - Entity_assembly_ID: B, Chain length: 18, Sequence coverage: 11.1%
  - Entity_assembly_ID: C, Chain length: 1, Sequence coverage: 100.0%
- Total number of restraints: 19
- Total number of restraints per polymer type: 19
- Weight of restraints: 1.0 (19)
- Potential type of restraints: square-well-parabolic (19)
- Dihedral angle restraints per residue
  - Chain_ID: C
    None

Keywords Alzheimer`s disease, Human amyloid -peptide, Zinc binding

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Found 1 Document (1.863 seconds)

BMRB: 19602

Sample #1

Sample #2

Sample #1

Sample #2

Sample #1

Sample #2

Related entities 1. dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc, entity 1, : 1 : 69 : 12 entities Detail

Interaction partners 1. dimer of the metal binding domain 1-16 of human amyloid beta-peptide in complex with Zinc, entity 1, : 94 interactors Detail

Experiments performed 13 experiments Detail

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NMR combined restraints 7 contents Detail