SASDB36

Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00

Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization by removing an N-linked glycan that clashes with its symmetry mate.

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant

Concentration— – 2.12 Buffer / pH20 mM HEPES 150 mM NaCl / 7.5
Experimental temperature20.0 Facility / beamlineESRF / BM29
Wavelength0.0992 nmExposure1.0 s × 9

Molecular Components

ComponentType / organismUniProt and ConstructOligomeric StateMolecular weight
Myelin-associated glycoprotein (20-508; N406Q mutant)
View sequence
GHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFQLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQSLELPFQGAHR
proteinMus musculusP2091720–508monomerMolecule count 153.978 kDa

Experimental Curves

CurvePoints / columnsq rangeUncertainty qualityNegative-intensity pointsSource file
11043[3]0.03286978–4.944755 1/nmHas uncertainty columnMissing 01sasbdb/entries/36/sasdb36/source/SASDB36.dat
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2. Measurements Reported by SASBDB Reported Results

MetricMethodValueUncertaintyUnit
dmaxP(r)25.6—nm
i0Guinier82.0——
i0P(r)82.23——
mwExperimental63.7—kDa
mwGuinier I(0)82.0—kDa
mwPorod112.74—kDa
porod_volumePorod193.23—nm³
rgGuinier7.3—nm
rgP(r)7.6—nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

Fit 1 · —

χ²: 11.89CorMap p: 0.0Unit: 1/A
ModelName / TypeSoftwareSymmetryModel MWPDB DeclarationSource file
1—atomicPDB (Protein Data Bank) 2.8.3—112.15LFUModel Image
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4. Source File Index Source Files

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5. Experiment Description and Publication Experiment & Publication

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6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name20 mM HEPES 150 mM NaClBuffer concentration20.0 mM
pH7.5Additives150 mM NaCl
Buffer description—
Purity measurement method—Extinction coefficient—
Absorbance—Scattering contrast—
Specific volume / dry volume— / —Mixture / deuteration— / —

Acquisition Conditions and Instrument

Measurement date2016-02-05Storage / measurement temperature20.0 / 20.0
Exposure time1.0Frames9
Wavelength0.0992Sample-to-detector distance2.87
SourceX-ray synchrotronDetectorPilatus 1M
Facility / beamlineESRF / BM29 · Grenoble, France
q range0.033 – 4.945Sample volume / flow rate— / —

Original SASBDB Plots

Experimental I(q)
Experimental I(q)
Experimental I(q), log-log
Experimental I(q), log-log
Guinier plot
Guinier plot
Kratky plot
Kratky plot
P(r) plot
P(r) plot

Downloadable Files

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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json:159 field values
Field pathRaw value
codeSASDB36
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleStructural basis of myelin-associated glycoprotein adhesion and signalling.
project.publication.titleStructural basis of myelin-associated glycoprotein adhesion and signalling.
project.publication.author_listPronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
project.publication.journalNat Commun
project.publication.doi10.1038/ncomms13584
project.publication.pmid27922006
project.publication.published_date2016 Dec 6
project.statusreleased
project.submitted_date2016-07-24
project.released_date2016-12-13
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDB36.out
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experiment.instrument.detector.typeDectris
experiment.instrument.detector.namePilatus 1M
experiment.instrument.detector.resolution172.0
experiment.instrument.nameESRF
experiment.instrument.cityGrenoble
experiment.instrument.countryFrance
experiment.instrument.beamline_nameBM29
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
experiment.instrument.line_collimationnull
experiment.instrument.sample_path_lengthnull
experiment.instrument.line_collimation_slitlengthnull
experiment.instrument.line_collimation_integrationwidthnull
experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
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experiment.sample.molecule[0].long_nameMyelin-associated glycoprotein (20-508; N406Q mutant)
experiment.sample.molecule[0].short_nameMAG
experiment.sample.molecule[0].sequenceGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY FNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD LGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL GEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP VIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED GVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF KEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFQ LSVEFAPIILLESH CAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA QAPPRVICTSRNLYGTQSLELPFQGAHR
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeP20917
experiment.sample.molecule[0].uniprot_range_first20
experiment.sample.molecule[0].uniprot_range_last508
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY FNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD LGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL GEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP VIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED GVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF KEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH CAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA QAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK NVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH SDLGKRPTKDSYTLTEELAEYAEIRVK
experiment.sample.molecule[0].mw53.978
experiment.sample.molecule[0].total_mw53.978
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_stateFalse
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name20 mM HEPES 150 mM NaCl
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
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experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameGlycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
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experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressUtrecht, Netherlands
experiment.contributor[0].affiliation[0].full_nameUtrecht University
experiment.contributor[0].affiliation[0].webpagehttp://www.uu.nl/
experiment.contributor[0].contributor_nameMatti
experiment.contributor[0].contributor_surnamePronker
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-02-05
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time1.0
experiment.number_of_frames9
experiment.wavelength0.0992
experiment.sample_detector_distance2.87
experiment.concentration_minnull
experiment.concentration_max2.12
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.033
experiment.s_max4.945
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwarePDB (Protein Data Bank)
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fits[0].models[0].user52
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fits[0].softwarenull
fits[0].chi_square_value11.89
fits[0].p_value0.0
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGnom 4.5a
i0_calibration_standardnull
descriptionMyelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization by removing an N-linked glycan that clashes with its symmetry mate.
experiment_descriptionSynchrotron SAXS data from solutions of glycosylated myelin-associated glycoprotein (full extracellular domain (Ig1-5) N406Q mutant) in HEPES, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 2.12 mg/ml was measured at 20°C. Nine successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration.
tags[]
intensity_unitnull
experimental_mw63.7
experimental_mw_errornull
guinier_i0_mw82.0
guinier_i0_mw_errornull
porod_mw112.74
porod_mw_errornull
pddf_i082.23
pddf_i0_errornull
guinier_i082.0
guinier_i0_errornull
pddf_rg7.6
pddf_rg_errornull
guinier_rg7.3
guinier_rg_errornull
pddf_dmax25.6
pddf_dmax_errornull
porod_volume193.23
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first13
guinier_point_last27
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB36_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 field values
Field pathRaw value
codeSASDB36
statussuccess
started_at2026-08-11T16:36:57.415859+00:00
finished_at2026-08-11T16:37:07.122935+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source
{
  "code": "SASDB36",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
    "publication": {
      "title": "Structural basis of myelin-associated glycoprotein adhesion and signalling.",
      "author_list": "Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ",
      "journal": "Nat Commun",
      "doi": "10.1038/ncomms13584",
      "pmid": "27922006",
      "published_date": "2016 Dec 6"
    },
    "status": "released",
    "submitted_date": "2016-07-24",
    "released_date": "2016-12-13"
  },
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    "sample": {
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          "long_name": "Myelin-associated glycoprotein (20-508; N406Q mutant)",
          "short_name": "MAG",
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          "organism": "Mus musculus",
          "uniprot_code": "P20917",
          "uniprot_range_first": 20,
          "uniprot_range_last": 508,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY\nFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD\nLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL\nGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP\nVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED\nGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF\nKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH\nCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA\nQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK\nNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH\nSDLGKRPTKDSYTLTEELAEYAEIRVK",
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "20 mM HEPES 150 mM NaCl",
        "concentration_unit": "mM",
        "comment": null,
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        "concentration": 20.0,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Utrecht, Netherlands",
            "full_name": "Utrecht University",
            "webpage": "http://www.uu.nl/"
          }
        ],
        "contributor_name": "Matti",
        "contributor_surname": "Pronker",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2016-02-05",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 1.0,
    "number_of_frames": 9,
    "wavelength": 0.0992,
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    "concentration_min": null,
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    "s_max": 4.945,
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    "seccolumn": null
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          "software": "PDB (Protein Data Bank)",
          "pdb_link": [
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              "pdb_code": "5lfu",
              "ext_code": "5LFU",
              "ext_type": "pdb",
              "difference_with_model": "derived"
            }
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          "software_version": "2.8.3",
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          "model_mw": 112.1,
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          "log": null,
          "symmetry": "",
          "comment": "",
          "user": 52
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDB36_fit1_fit_img.png",
      "software": null,
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      "fit_residual_plot": null,
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDB36_fit1.fit",
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      "software_version": null,
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  "description": "Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an N406Q mutation that should, based on the crystal structure, enhance MAG dimerization by removing an N-linked glycan that clashes with its symmetry mate.",
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  "tags": [],
  "intensity_unit": null,
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  "experimental_mw_error": null,
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  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDB36_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
View the complete manifest.json source
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