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Found 1 Document (0.536 seconds)

BMRB: 19979

2MPI

Solution structure of B24G insulin

Authors

Yang, Y., Wickramasinghe, N.P., Hua, Q., Weiss, M.A.

Assembly

B24G insulin

Entity

1. B24G insulin (polymer, Thiol state: all disulfide bound), 51 monomers, 5683.427 Da Detail

GIVEQCCTSI CSLYQLENYC NFVNQHLCGS DLVEALYLVC GERGGFYTKP T

Formula weight

5683.427 Da

Entity Connection

disulfide 3 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS6:SG	1:CYS11:SG
2	disulfide	sing	1:CYS7:SG	1:CYS28:SG
3	disulfide	sing	1:CYS20:SG	1:CYS40:SG

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 96.1 %, Completeness: 75.5 %, Completeness (bb): 73.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	75.5 % (222 of 294)	75.5 % (222 of 294)
Backbone	73.6 % (78 of 106)	73.6 % (78 of 106)
Sidechain	76.6 % (144 of 188)	76.6 % (144 of 188)
Aromatic	42.9 % (12 of 28)	42.9 % (12 of 28)
Methyl	82.1 % (23 of 28)	82.1 % (23 of 28)

1. entity

GIVEQCCTSI CSLYQLENYC NFVNQHLCGS DLVEALYLVC GERGGFYTKP T

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 8, Details 32 degree, PH 8.0

#	Name	Isotope labeling	Type	Concentration
1	entity	natural abundance		0.3 mM

Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 273 K, pH 8

#	Name	Isotope labeling	Type	Concentration
2	entity	natural abundance		0.3 mM

Protein Blocks Logo

Calculated from 18 models in PDB: 2MPI, Strand ID: A, B Detail

Release date

2014-12-21

Citation

Protective hinge in insulin opens to enable its receptor engagement
Menting, J.G., Yang, Y., Chan, S.JIN., Phillips, N.B., Smith, B.J., Whittaker, J., Wickramasinghe, N.P., Whittaker, L.J., Pandyarajan, V., Wan, Z., Yadav, S.P., Carroll, J.M., Strokes, N., Roberts, C.T., Ismail-Beigi, F., Milewski, W., Steiner, D.F., Chauhan, V.S., Ward, C.W., Weiss, M.A., Lawrence, M.C.
Proc. Natl. Acad. Sci. U. S. A. (2014), 111, E3395-E3404, PubMed 25092300 , DOI 10.1073/pnas.1412897111 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 19822 released on 2014-08-24
Title NMR structure of B25-(alpha, beta)-dehydro-phenylalanine insulin

Related entities 1. B24G insulin, : 2 entities Detail

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_19979_2mpi.nef
Input source #2: Coordindates	2mpi.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	None
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)
A:6:CYS:SG	A:11:CYS:SG	unknown	unknown	2.02
A:7:CYS:SG	B:28:CYS:SG	unknown	unknown	2.017
A:20:CYS:SG	B:40:CYS:SG	unknown	unknown	2.019

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-
GIVEQCCTSICSLYQLENYCN
|||||||||||||||||||||
GIVEQCCTSICSLYQLENYCN

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

-------30--------40--------50-
FVNQHLCGSDLVEALYLVCGERGGFYTKPT
||||||||||||||||||||||||||||||
FVNQHLCGSDLVEALYLVCGERGGFYTKPT
--------10--------20--------30

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0
B	B	30	0	0	100.0

Content subtype: combined_19979_2mpi.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	3		No information
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	215		95.2 (chain: A, length: 21), 90.0 (chain: B, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	658 (1)	noe	100.0 (chain: A, length: 21), 100.0 (chain: B, length: 30)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	38 (1)	hbond	42.9 (chain: A, length: 21), 43.3 (chain: B, length: 30)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_3	OK	42 (42)	.	81.0 (chain: A, length: 21), 60.0 (chain: B, length: 30)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 95.2%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 90.0%
- Total number of assignments
  - ¹H chemical shifts: 215
- Completeness of assignments
  - Entity_assemble_ID: A
  - Entity_assemble_ID: B
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A
  - Chain_ID: B

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	82	68.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	28	65.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	54	70.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	9	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	4	50.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	174	133	76.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	63	43	68.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	111	90	81.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	14	82.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	8	40.0

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: A, Chain length: 21, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 100.0%
- Total number of restraints: 658
- Weight of restraints: 1.0 (658)
- Potential type of restraints: square-well-parabolic (658)
- Range of distance target values: 1.35, 5.5 (Å)
- Histogram of distance target values
- Distance restraints per residue
  - Chain_ID: A
  - Chain_ID: B
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 42.9%
    - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 43.3%
  - Total number of restraints: 38
  - Weight of restraints: 1.0 (38)
  - Potential type of restraints: square-well-parabolic (38)
  - Range of distance target values: 1.45, 1.95 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
    - Chain_ID: B
  - 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: 21, Sequence coverage: 81.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 60.0%
- Total number of restraints: 42
- Total number of restraints per polymer type: 42
- Weight of restraints: 1.0 (42)
- Potential type of restraints: square-well-parabolic (42)
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords NMR, insulin structure, insulin mutant

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Found 1 Document (0.536 seconds)

BMRB: 19979

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. B24G insulin, : 2 entities Detail

Experiments performed 6 experiments Detail

Instrument

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Instrument

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Instrument

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Sample

NMR combined restraints 5 contents Detail