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BMRB: 34087

5MWQ

Biosynthetic engineered A21K-B31K-B32R human insulin monomer structure in water/acetonitrile solution

Authors

Bocian, W., Kozerski, L.

Assembly

Insulin

Entity

1. Insulin (polymer), 21 monomers, 2397.765 Da Detail

GIVEQCCTSI CSLYQLENYC K

2. Insulin (polymer), 32 monomers, 3714.277 Da Detail

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT KR

Total weight

6112.042 Da

Max. entity weight

3714.277 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	2:CYS7:SG
3	disulfide	sing	1:CYS20:SG	2:CYS19:SG

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 43.4 %, Completeness: 42.5 %, Completeness (bb): 41.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	42.5 % (138 of 325)	42.5 % (138 of 325)
Backbone	41.3 % (45 of 109)	41.3 % (45 of 109)
Sidechain	43.1 % (93 of 216)	43.1 % (93 of 216)
Aromatic	22.9 % (8 of 35)	22.9 % (8 of 35)
Methyl	39.3 % (11 of 28)	39.3 % (11 of 28)

1. Insulin

GIVEQCCTSI CSLYQLENYC K

2. Insulin

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT KR

Show sample condition

Sample #1

Solvent system 73% H2O/27% CD3CN, Pressure 1 atm, Temperature 298 K, pH 2.5, Details 2.5 mM insulin, 73% H2O/27% CD3CN

#	Name	Isotope labeling	Concentration
1	insulin	natural abundance	2.5 mM
2	H2O	natural abundance	73 %
3	CD3CN	natural abundance	27 %

Sample #2

Solvent system 73% D2O/27% CD3CN, Pressure 1 atm, Temperature 298 K, pH 2.5, Details 2.5 mM insulin, 73% D2O/27% CD3CN

#	Name	Isotope labeling	Concentration
4	insulin	natural abundance	2.5 mM
5	H2O	natural abundance	73 %
6	CD3CN	natural abundance	27 %

Chem. Shift Complete2

Sequence coverage: 62.3 %, Completeness: 50.0 %, Completeness (bb): 50.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	50.0 % (325 of 650)	50.0 % (325 of 650)
Backbone	50.9 % (111 of 218)	50.9 % (111 of 218)
Sidechain	49.5 % (214 of 432)	49.5 % (214 of 432)
Aromatic	40.0 % (28 of 70)	40.0 % (28 of 70)
Methyl	50.0 % (28 of 56)	50.0 % (28 of 56)

1. Insulin

GIVEQCCTSI CSLYQLENYC K

2. Insulin

FVNQHLCGSH LVEALYLVCG ERGFFYTPKT KR

Show sample condition

Sample #1

Solvent system 73% H2O/27% CD3CN, Pressure 1 atm, Temperature 298 K, pH 2.5, Details 2.5 mM insulin, 73% H2O/27% CD3CN

#	Name	Isotope labeling	Concentration
1	insulin	natural abundance	2.5 mM
2	H2O	natural abundance	73 %
3	CD3CN	natural abundance	27 %

Sample #2

Solvent system 73% D2O/27% CD3CN, Pressure 1 atm, Temperature 298 K, pH 2.5, Details 2.5 mM insulin, 73% D2O/27% CD3CN

#	Name	Isotope labeling	Concentration
4	insulin	natural abundance	2.5 mM
5	H2O	natural abundance	73 %
6	CD3CN	natural abundance	27 %

Protein Blocks Logo

Calculated from 20 models in PDB: 5MWQ, Strand ID: A, B Detail

Release date

2017-01-22

Citation

Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli
Stadnik, D., Bierczynska-Krzysik, A., Zielinska, J., Antosik, J., Borowicz, P., Bocian, W., Sitkowski, J., Bednarek, E., Kozerski, L.
Pharm. Res. (2019), 36, 79-79, PubMed 30949841 , DOI 10.1007/s11095-019-2601-z , Abstract

Related entities 1. Insulin, : 1 : 118 : 102 entities Detail

Related entities 2. Insulin, : 1 : 2 : 30 : 88 : 90 entities Detail

Interaction partners 1. Insulin, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. Insulin, : 6 : 1 interactors Detail

More details for 7 interactors identified by 7 citations

Experiments performed 3 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_34087_5mwq.nef
Input source #2: Coordindates	5mwq.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	2.033
A:7:CYS:SG	B:7:CYS:SG	unknown	unknown	2.043
A:20:CYS:SG	B:19:CYS:SG	unknown	unknown	2.031

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-
GIVEQCCTSICSLYQLENYCK
|||||||||||||||||||||
GIVEQCCTSICSLYQLENYCK

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

--------10--------20--------30--
FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR
||||||||||||||||||||||||||||||||
FVNQHLCGSHLVEALYLVCGERGFFYTPKTKR

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	21	0	0	100.0
B	B	32	0	0	100.0

Content subtype: combined_34087_5mwq.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_chemical_shifts_1	OK	121		95.2 (chain: A, length: 21)
2	Assigned chemical shifts	assigned_chemical_shifts_2	OK	186		100.0 (chain: B, length: 32)
1	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	954 (1)	noe	95.2 (chain: A, length: 21), 100.0 (chain: B, length: 32)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	498 (498)	.	100.0 (chain: A, length: 21), 100.0 (chain: B, length: 32)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 95.2%
- Total number of assignments
  - ¹H chemical shifts: 121
- 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
Saveframe: assigned_chemical_shifts_2
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: B, Chain length: 32, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 186
- Completeness of assignments
  - Entity_assemble_ID: B
- 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	124	121	97.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	40	93.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	81	81	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	11	11	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	8	8	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	201	186	92.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	66	65	98.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	135	121	89.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	17	17	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	27	20	74.1

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_3
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 95.2%
  - Entity_assembly_ID: B, Chain length: 32, Sequence coverage: 100.0%
- Total number of restraints: 954
- Weight of restraints: 1.0 (954)
- Potential type of restraints: square-well-parabolic (954)
- Range of distance target values: 2.6, 5.52 (Å)
- Histogram of distance target values
- Histogram of discrepancy in 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_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 100.0%
  - Entity_assembly_ID: B, Chain length: 32, Sequence coverage: 100.0%
- Total number of restraints: 498
- Total number of restraints per polymer type: 498
- Weight of restraints: 1.0 (498)
- Potential type of restraints: square-well-parabolic (498)
- Plot of Phi-Psi angle restraints
- Plot of Chi1-Chi2 angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A
  - Chain_ID: B

Keywords BIOSYNTHETIC PROTEIN, Human Insulin, mutant, water/acetonitrile solution

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Found 1 Document (0.931 seconds)

BMRB: 34087

Sample #1

Sample #2

Sample #1

Sample #2

Related entities 1. Insulin, : 1 : 118 : 102 entities Detail

Related entities 2. Insulin, : 1 : 2 : 30 : 88 : 90 entities Detail

Interaction partners 1. Insulin, : 1 : 1 interactors Detail

Interaction partners 2. Insulin, : 6 : 1 interactors Detail

Experiments performed 3 experiments Detail

Instrument

Sample

Instrument

Sample

Instrument

Sample

NMR combined restraints 5 contents Detail