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Found 1 Document (1.071 seconds)

BMRB: 25261

2MVD

Solution structure of [GlnB22]-insulin mutant at pH 1.9

Authors

Hexnerova, R., Krizkova, K., Maletinska, L., Jiracek, J., Brzozowski, A.M., Zakova, L., Veverka, V.

Assembly

[GlnB22]-insulin mutant

Entity

1. [GlnB22]-insulin mutant, entity 1 (polymer, Thiol state: all disulfide bound), 21 monomers, 2383.696 Da Detail

GIVEQCCTSI CSLYQLENYC N

2. [GlnB22]-insulin mutant, entity 2 (polymer, Thiol state: all disulfide bound), 30 monomers, 3401.862 Da Detail

FVNQHLCGSH LVEALYLVCG EQGFFYTPKT

Total weight

5785.558 Da

Max. entity weight

3401.862 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

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 95.7 %, Completeness (bb): 95.2 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	95.7 % (288 of 301)	95.7 % (288 of 301)
Backbone	95.2 % (100 of 105)	95.2 % (100 of 105)
Sidechain	95.9 % (188 of 196)	95.9 % (188 of 196)
Aromatic	97.1 % (34 of 35)	97.1 % (34 of 35)
Methyl	100.0 % (28 of 28)	100.0 % (28 of 28)

1. entity 1

GIVEQCCTSI CSLYQLENYC N

2. entity 2

FVNQHLCGSH LVEALYLVCG EQGFFYTPKT

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 1.9

#	Name	Isotope labeling	Concentration
1	entity_1	natural abundance	0.2 mM
2	entity_2	natural abundance	0.2 mM
3	acetic acid	[U-99% 2H]	20 %
4	H2O	natural abundance	95 %
5	D2O	[U-99% 2H]	5 %

Protein Blocks Logo

Calculated from 40 models in PDB: 2MVD, Strand ID: A, B Detail

Release date

2016-09-12

Citation

Structural and functional study of the GlnB22-insulin mutant responsible for maturity-onset diabetes of the young
Krizkova, K., Veverka, V., Maletinska, L., Hexnerova, R., Brzozowski, A., Jiracek, J.M., Zakova, L.
PLoS One (2014), 9, e112883-e112883, PubMed 25423173 , DOI 10.1371/journal.pone.0112883 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 25260 released on 2016-09-12
Title Solution structure of human insulin at pH 1.9

Related entities 1. [GlnB22]-insulin mutant, entity 1, : 112 : 13 : 7 : 90 entities Detail

Related entities 2. [GlnB22]-insulin mutant, entity 2, : 1 : 113 : 1 : 106 entities Detail

Interaction partners 1. [GlnB22]-insulin mutant, entity 1, : 1 : 1 interactors Detail

More details for 2 interactors identified by 2 citations

Interaction partners 2. [GlnB22]-insulin mutant, entity 2, : 6 : 1 interactors Detail

More details for 7 interactors identified by 7 citations

Experiments performed 2 experiments Detail

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_25261_2mvd.nef
Input source #2: Coordindates	2mvd.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	2.036
A:7:CYS:SG	B:37:CYS:SG	unknown	unknown	2.048
A:20:CYS:SG	B:49:CYS:SG	unknown	unknown	2.007

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

--------40--------50--------60
FVNQHLCGSHLVEALYLVCGEQGFFYTPKT
||||||||||||||||||||||||||||||
FVNQHLCGSHLVEALYLVCGEQGFFYTPKT
--------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_25261_2mvd.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	288		100.0 (chain: A, length: 21), 100.0 (chain: B, length: 30)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	Warning	834 (1)	noe	100.0 (chain: A, length: 21), 96.7 (chain: B, length: 30)
2	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	30 (1)	noe	57.1 (chain: A, length: 21), 30.0 (chain: B, length: 30)
3	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	32 (1)	hbond	66.7 (chain: A, length: 21), 40.0 (chain: B, length: 30)
4	Distance restraints	CNS/XPLOR_distance_constraints_5	Warning	32 (1)	hbond	66.7 (chain: A, length: 21), 40.0 (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: 100.0%
  - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 100.0%
- Total number of assignments
  - ¹H chemical shifts: 288
- 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	113	94.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	43	39	90.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	77	74	96.1

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	181	175	96.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	62	61	98.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	119	114	95.8

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	26	96.3

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: 96.7%
- Total number of restraints: 834
- Weight of restraints: 1.0 (834)
- Potential type of restraints: square-well-parabolic (834)
- Range of distance target values: 1.05, 2.83 (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
- Saveframe: CNS/XPLOR_distance_constraints_4
  - Status: Warning
  - Experiment type: noe
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 57.1%
    - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 30.0%
  - Total number of restraints: 30
  - Weight of restraints: 1.0 (30)
  - Potential type of restraints: square-well-parabolic (30)
  - Range of distance target values: 2.5, 4.5 (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_3
    - Status: OK
    - Experiment type: hbond
    - Sequence coverage of experimental data
      - Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 66.7%
      - Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 40.0%
    - Total number of restraints: 32
    - Weight of restraints: 1.0 (32)
    - Potential type of restraints: square-well-parabolic (32)
    - Range of distance target values: 1.0, 1.5 (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_5
      - Status: Warning
      - Experiment type: hbond
      - Sequence coverage of experimental data
        Entity_assembly_ID: A, Chain length: 21, Sequence coverage: 66.7%
        --------10--------20- GIVEQCCTSICSLYQLENYCN ||| ||| || |||||| GIV.QCC....SL.QLENYC --------10--------20
        Entity_assembly_ID: B, Chain length: 30, Sequence coverage: 40.0%
      - Total number of restraints: 32
        Total hydrogen bond restraints: 32
        O...H-x (too far!): 16
        O...h-N (too far!): 16
      - Weight of restraints: 1.0 (32)
        Total hydrogen bond restraints: 1.0 (32)
        O...H-x (too far!): 1.0 (16)
        O...h-N (too far!): 1.0 (16)
      - Potential type of restraints: square-well-parabolic (32)
        Total hydrogen bond restraints: square-well-parabolic (32)
        O...H-x (too far!): square-well-parabolic (16)
        O...h-N (too far!): square-well-parabolic (16)
      - Range of distance target values: 2.7, 4.05 (Å)
      - Histogram of distance target values
      - Distance restraints per residue
        Chain_ID: A
        Chain_ID: B
      - Distance restraints on contact map
        Chain_ID_1: A - Chain_ID_2: A

Keywords MODY, insulin

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Found 1 Document (1.071 seconds)

BMRB: 25261

Sample

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. [GlnB22]-insulin mutant, entity 1, : 112 : 13 : 7 : 90 entities Detail

Related entities 2. [GlnB22]-insulin mutant, entity 2, : 1 : 113 : 1 : 106 entities Detail

Interaction partners 1. [GlnB22]-insulin mutant, entity 1, : 1 : 1 interactors Detail

Interaction partners 2. [GlnB22]-insulin mutant, entity 2, : 6 : 1 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

NMR combined restraints 6 contents Detail