BMRBj - BMREntryMaster

Found 1 Document (0.65 seconds)

BMRB: 25505

2MZX

CCR5-ECL2 helical structure, residues Q186-T195.

Authors

Abayev, M., Anglister, J.

Assembly

CCR5-ECL2 helical structure, residues Q186-T195

Entity

1. CCR5-ECL2 helical structure, residues Q186-T195 (polymer, Thiol state: not present), 10 monomers, 1389.511 Da Detail

QYQFWKNFQT

Formula weight

1389.511 Da

Source organism

Escherichia coli

Exptl. method

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 39.7 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	39.7 % (60 of 151)	25.0 % (20 of 80)	53.6 % (30 of 56)	66.7 % (10 of 15)
Backbone	100.0 % (60 of 60)	100.0 % (20 of 20)	100.0 % (30 of 30)	100.0 % (10 of 10)
Sidechain	9.9 % (10 of 101)	0.0 % (0 of 60)	27.8 % (10 of 36)	0.0 % (0 of 5)
Aromatic	0.0 % (0 of 40)	0.0 % (0 of 20)	0.0 % (0 of 19)	0.0 % (0 of 1)
Methyl	0.0 % (0 of 2)	0.0 % (0 of 1)	0.0 % (0 of 1)

1. entity

QYQFWKNFQT

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

Protein Blocks Logo

Calculated from 11 models in PDB: 2MZX, Strand ID: A Detail

Release date

2015-04-19

Citation

An extended CCR5 ECL2 peptide forms a helix that binds HIV-1 gp120 through non-specific hydrophobic interactions
Anglister, J., Abayev, M., Moseri, A., Tchaicheeyan, O., Kessler, N., Arshava, B., Naider, F., Scherf, T.
FEBS J. (2015), 282, 1906-1921, PubMed 25703038 , DOI 10.1111/febs.13243 , Abstract

Related entities 1. CCR5-ECL2 helical structure, residues Q186-T195, : 1 : 34 : 1 entities Detail

Interaction partners 1. CCR5-ECL2 helical structure, residues Q186-T195, : 15 interactors Detail

More details for 15 interactors identified by 9 citations

Experiments performed 9 experiments Detail

1 3D CBCA(CO)NH

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

2 3D HNCACB

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

3 3D HNCA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

4 3D HN(CO)CA

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

5 2D 1H-15N HSQC

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

6 2D 1H-1H NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

7 3D 1H-15N NOESY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

8 2D 1H-1H TOCSY

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

9 3D HNCO

Instrument

Bruker Avance - 800 MHz

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 277 K, pH 4.8

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-99% 2H]		20 mM
2	Thiomersal	natural abundance		0.005 % v/v
3	H2O	natural abundance		90 %
4	D2O	natural abundance		10 %

NMR combined restraints 4 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_25505_2mzx.nef
Input source #2: Coordindates	2mzx.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

--190-----
QYQFWKNFQT
||||||||||
QYQFWKNFQT
--------10

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	10	0	0	100.0

Content subtype: combined_25505_2mzx.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	60		100.0 (chain: A, length: 10)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	66 (1)	noe	100.0 (chain: A, length: 10)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	6 (6)	.	50.0 (chain: A, length: 10)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 10, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 20
  - ¹³C chemical shifts: 30
  - ¹⁵N chemical shifts: 10
- Completeness of assignments
  - Entity_assemble_ID: A
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 10, Sequence coverage: 100.0%
- Total number of restraints: 66
- Weight of restraints: 1.0 (66)
- Potential type of restraints: square-well-parabolic (66)
- Range of distance target values: 2.33, 3.88 (Å)
- Histogram of 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: 10, Sequence coverage: 50.0%
- Total number of restraints: 6
- Total number of restraints per polymer type: 6
- Weight of restraints: 1.0 (6)
- Potential type of restraints: square-well-parabolic (6)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords CCR5, ECL2, Helical, TM5