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- PDB-6t3o: Crystal structure of the human myomesin domain 10 -

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Basic information

Entry
Database: PDB / ID: 6t3o
TitleCrystal structure of the human myomesin domain 10
ComponentsMyomesin-1
KeywordsCONTRACTILE PROTEIN / small protein domain / scaffold structure
Function / homology
Function and homology information


extraocular skeletal muscle development / striated muscle myosin thick filament / M band / structural constituent of muscle / sarcomere organization / protein kinase A signaling / positive regulation of protein secretion / kinase binding / positive regulation of gene expression / protein homodimerization activity / identical protein binding
Similarity search - Function
Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype ...Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
AZIDE ION / Myomesin-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsDuskova, J. / Petrokova, H. / Maly, P.
Funding support Czech Republic, 1items
OrganizationGrant numberCountry
Ministry of Education, Youth and Sports of the Czech RepublicCZ.02.1.01/0.0/0.0/16_025/0007397 Czech Republic
CitationJournal: Virulence / Year: 2021
Title: Myomedin scaffold variants targeted to 10E8 HIV-1 broadly neutralizing antibody mimic gp41 epitope and elicit HIV-1 virus-neutralizing sera in mice.
Authors: Kuchar, M. / Kosztyu, P. / Daniel Liskova, V. / Cerny, J. / Petrokova, H. / Vroblova, E. / Maly, M. / Vankova, L. / Krupka, M. / Raskova Kafkova, L. / Turanek Knotigova, P. / Duskova, J. / ...Authors: Kuchar, M. / Kosztyu, P. / Daniel Liskova, V. / Cerny, J. / Petrokova, H. / Vroblova, E. / Maly, M. / Vankova, L. / Krupka, M. / Raskova Kafkova, L. / Turanek Knotigova, P. / Duskova, J. / Dohnalek, J. / Masek, J. / Turanek, J. / Raska, M. / Maly, P.
History
DepositionOct 11, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 17, 2021Provider: repository / Type: Initial release
Revision 1.1Sep 29, 2021Group: Data collection / Database references / Structure summary
Category: citation / citation_author ...citation / citation_author / database_2 / pdbx_database_proc / struct
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct.title
Revision 1.2Jan 24, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Myomesin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)15,4372
Polymers15,3951
Non-polymers421
Water1,56787
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area120 Å2
ΔGint1 kcal/mol
Surface area6670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.599, 58.599, 62.821
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Components on special symmetry positions
IDModelComponents
11A-201-

AZI

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Components

#1: Protein Myomesin-1 / 190 kDa connectin-associated protein / 190 kDa titin-associated protein / Myomesin family member 1


Mass: 15395.444 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MYOM1 / Production host: Escherichia coli (E. coli) / References: UniProt: P52179
#2: Chemical ChemComp-AZI / AZIDE ION


Mass: 42.020 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: N3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 87 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.09 Å3/Da / Density % sol: 41.12 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.4
Details: 0.1 M citrate/phosphate buffer pH 5.4, 30 % PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.918409 Å
DetectorType: DECTRIS PILATUS 300K / Detector: PIXEL / Date: May 30, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918409 Å / Relative weight: 1
ReflectionResolution: 1.8→42.85 Å / Num. all: 55419 / Num. obs: 10591 / % possible obs: 99.7 % / Redundancy: 5.2 % / Biso Wilson estimate: 30.9 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.025 / Rpim(I) all: 0.017 / Rrim(I) all: 0.031 / Χ2: 1 / Net I/av σ(I): 2.5 / Net I/σ(I): 2.5
Reflection shellResolution: 1.8→1.84 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.572 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 3310 / CC1/2: 0.829 / Rpim(I) all: 0.408 / Rrim(I) all: 0.706 / Χ2: 0.99 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0238refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2Y23
Resolution: 1.8→42.85 Å / Cor.coef. Fo:Fc: 0.955 / SU B: 5.418 / SU ML: 0.086 / Cross valid method: FREE R-VALUE / ESU R: 0.145 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rfree0.244 -5 %
Rwork0.1983 --
obs0.20471 10572 99.33 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 38.438 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å20 Å20 Å2
2---0.04 Å20 Å2
3---0.08 Å2
Refinement stepCycle: LAST / Resolution: 1.8→42.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms908 0 3 87 998
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.013932
X-RAY DIFFRACTIONr_bond_other_d0.0020.018873
X-RAY DIFFRACTIONr_angle_refined_deg1.9951.6481246
X-RAY DIFFRACTIONr_angle_other_deg1.5211.5872037
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.5475110
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.96824.44454
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.21615185
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.221154
X-RAY DIFFRACTIONr_chiral_restr0.0930.2116
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.021029
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02191
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.8072.451437
X-RAY DIFFRACTIONr_mcbond_other1.8022.447436
X-RAY DIFFRACTIONr_mcangle_it2.473.672545
X-RAY DIFFRACTIONr_mcangle_other2.4683.676546
X-RAY DIFFRACTIONr_scbond_it2.1992.705494
X-RAY DIFFRACTIONr_scbond_other2.192.692492
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.3343.959699
X-RAY DIFFRACTIONr_long_range_B_refined6.39947.4954122
X-RAY DIFFRACTIONr_long_range_B_other6.32246.6434041
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.8→1.847 Å
RfactorNum. reflection% reflection
Rfree0.318 -5 %
Rwork0.289 765 -
obs--99.87 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.0084-0.0988-0.04461.63661.90055.9911-0.02010.0025-0.01710.3432-0.19710.25070.6573-0.15120.21710.1807-0.06440.10980.1498-0.04450.177214.3048-0.00219.4933
21.98310.0451-0.04082.59422.01892.6367-0.003-0.29630.19830.2407-0.39010.32670.219-0.3110.39320.082-0.06030.05030.1965-0.11770.1514.25698.934819.6684
31.8106-0.0185-4.47891.1014-0.641511.806-0.22-0.1833-0.01470.17230.07680.05880.42480.26030.14320.0910.03010.02270.1248-0.0490.09622.45745.556625.6296
46.29152.57992.91143.91952.37684.8334-0.09610.20.1473-0.23310.02030.3189-0.0690.14650.07570.04680.00980.00940.02380.01620.103817.00753.56271.5526
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A22 - 48
2X-RAY DIFFRACTION2A49 - 97
3X-RAY DIFFRACTION3A98 - 108
4X-RAY DIFFRACTION4A109 - 130

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