SASDB55

Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2019-12-06T13:07:15.624532+01:00

The model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.

1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

浓度— – 3.38 mg/ml缓冲液 / pH25 mM HEPES 150 mM NaCl / 7.5
Experimental temperature20.0 设备 / 束线ESRF / BM29
波长0.93 nm曝光2.0 s × 9

分子组分

组分类型 / OrganismUniProt 与Construct寡聚状态Molecular weight
Myelin-associated glycoprotein Ig domains 1-5
查看序列
GHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGEDGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIFKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQAQAPPRVICTSRNLYGTQSLELPFQGAHR
proteinMus musculusP2091720–508dimer分子数 253.963 kDa

实验曲线

曲线点数 / 列q range误差质量负强度点来源文件
11043[3]0.0363402–4.969332 1/nm含误差列缺失 01sasbdb/entries/55/sasdb55/source/SASDB55.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)23.79nm
i0Guinier76.790.098
i0P(r)76.610.08
mwExperimental77.0kDa
porod_volumePorod177.0nm³
rgGuinier6.80.22nm
rgP(r)6.990.009nm

这些数值是 SASBDB 来源记录,不是 SAXSdb 对实验曲线重新计算的结果。

3. 来源拟合与模型 Source Fits & Models

4. 来源文件索引 Source Files

5. 实验说明与论文 Experiment & Publication

6. 完整来源记录 Complete Source Record

下列内容直接来自 SASBDB 条目。字段没有值时显示“—”;Not declared的单位不会由 SAXSdb 猜测。

打开 SASBDB 原始条目

缓冲液与样品属性

缓冲液名称25 mM HEPES 150 mM NaCl缓冲液浓度25.0 mM
pH7.5添加剂150 mM NaCl
缓冲液说明
纯度测定方法消光系数
吸收值散射对比度
比体积 / 干体积— / —混合物 / 氘代— / —

采集条件与仪器

测量日期2014-09-11储存 / 测量温度20.0 / 20.0
曝光时间2.0帧数9
波长0.93样品-探测器距离2.43
光源X-ray synchrotron探测器Pilatus 1M
机构 / 束线ESRF / BM29 · Grenoble, France
q range0.036 – 4.969样品体积 / 流速— / —

SASBDB 原始图

实验 I(q)
实验 I(q)
实验 I(q) log-log
实验 I(q) log-log
Guinier 图
Guinier 图
Kratky 图
Kratky 图
P(r) 图
P(r) 图

可Download文件

类别文件状态大小校验值Download与查看
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curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(5 项)
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pddf:来源记录
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全部来源字段(无筛选)

这里自动展开来源记录中的每一个字段,包括空值、列表成员和页面上方已展示过的字段。

summary.json:169 个字段值
字段路径原始值
codeSASDB55
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
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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
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_nameMyelin-associated glycoprotein Ig domains 1-5
experiment.sample.molecule[0].short_nameMAG
experiment.sample.molecule[0].sequenceGHWGAWMPSTI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED GVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTIRGQA QAPPRVICTS RNLYGTQSLE LPFQGAHR
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].oligomerizationdimer
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].mw53.963
experiment.sample.molecule[0].total_mw107.927
experiment.sample.molecule[0].number_molecules2
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.name25 mM HEPES 150 mM NaCl
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive150 mM NaCl
experiment.sample.buffer.concentration25.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameGlycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
experiment.sample.deuterationnull
experiment.sample.mixturenull
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_unitmg/ml
experiment.date2014-09-11
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time2.0
experiment.number_of_frames9
experiment.wavelength0.93
experiment.sample_detector_distance2.43
experiment.concentration_minnull
experiment.concentration_max3.38
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.036
experiment.s_max4.969
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].p_value0.0
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fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.
experiment_descriptionX-ray synchrotron radiation scattering data from solutions of myelin-associated glycoprotein in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle). One solute concentration of 3.38 mg/ml was measured from nine successive 2 second frames. 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. The low angle data collected were obtained from a single concentration scattering curve.
tags[]
intensity_unitnull
experimental_mw77.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i076.61
pddf_i0_error0.08
guinier_i076.79
guinier_i0_error0.098
pddf_rg6.99
pddf_rg_error0.009
guinier_rg6.8
guinier_rg_error0.22
pddf_dmax23.79
pddf_dmax_errornull
porod_volume177.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first11
guinier_point_last28
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDB55_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDB55
statussuccess
started_at2026-08-11T16:25:33.886494+00:00
finished_at2026-08-11T16:25:43.915204+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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查看完整 summary.json 原文
{
  "code": "SASDB55",
  "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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          "long_name": "Myelin-associated glycoprotein Ig domains 1-5",
          "short_name": "MAG",
          "sequence": "GHWGAWMPSTI SAFEGTCVSI PCRFDFPDEL\r\nRPAVVHGVWY FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC\r\nTLLLSTLSPE LGGKYYFRGD LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV\r\nAGTEVEVSCM VPDNCPELRP ELSWLGHEGL GEPTVLGRLR EDEGTWVQVS\r\nLLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP VIVEMNSSVE\r\nAIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED\r\nGVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ\r\nSNPDPILTIF KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ\r\nRATAFNLSVE FAPIILLESH CAAARDTVQC LCVVKSNPEP SVAFELPSRN\r\nVTVNETEREF VYSERSGLLL TSILTIRGQA QAPPRVICTS RNLYGTQSLE\r\nLPFQGAHR",
          "organism": "Mus musculus",
          "uniprot_code": "P20917",
          "uniprot_range_first": 20,
          "uniprot_range_last": 508,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MIFLATLPLFWIMISASRGGHWGAWMPSTISAFEGTCVSIPCRFDFPDELRPAVVHGVWY\nFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSTLSPELGGKYYFRGD\nLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGL\nGEPTVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQAAFPNTTLQFEGYASLDVKYPP\nVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGMVLREAVAKSLYLDLEEVTPGED\nGVYACLAENAYGQDNRTVELSVMYAPWKPTVNGTVVAVEGETVSILCSTQSNPDPILTIF\nKEKQILATVIYESQLQLELPAVTPEDDGEYWCVAENQYGQRATAFNLSVEFAPIILLESH\nCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNETEREFVYSERSGLLLTSILTIRGQA\nQAPPRVICTSRNLYGTQSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKK\nNVTESSSFSGGDNPHVLYSPEFRISGAPDKYESEKQRLGSERRLLGLRGESPELDLSYSH\nSDLGKRPTKDSYTLTEELAEYAEIRVK",
          "mw": 53.963,
          "total_mw": 107.927,
          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "25 mM HEPES 150 mM NaCl",
        "concentration_unit": "mM",
        "comment": null,
        "additive": "150 mM NaCl",
        "concentration": 25.0,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)",
      "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": "mg/ml",
    "date": "2014-09-11",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 2.0,
    "number_of_frames": 9,
    "wavelength": 0.93,
    "sample_detector_distance": 2.43,
    "concentration_min": null,
    "concentration_max": 3.38,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.036,
    "s_max": 4.969,
    "total_exposure_time": null,
    "seccolumn": null
  },
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    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDB55_fit1_model1_img.png",
          "software": "OLIGOMER",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "mix",
          "software_version": "",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDB55_fit1_model1.pdb",
          "model_mw": 112.1,
          "bead_radius": 1.9,
          "log": null,
          "symmetry": "",
          "comment": "",
          "user": 52
        },
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDB55_fit1_model2_img.png",
          "software": "OLIGOMER",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "atomic",
          "software_version": "",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDB55_fit1_model2.pdb",
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          "bead_radius": 1.9,
          "log": null,
          "symmetry": "",
          "comment": "",
          "user": 52
        }
      ],
      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDB55_fit1_fit_img.png",
      "software": null,
      "chi_square_value": 16.4,
      "p_value": 0.0,
      "fit_residual_plot": "SASDB55_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDB55_fit1.fit",
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  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": null,
  "i0_calibration_standard": null,
  "description": "The model fit displayed in this entry represents the volume fraction weighted contributions of the myelin-associated glycoprotein monomer and dimer structures (determined from X-ray crystallography) present in the sample.",
  "experiment_description": "X-ray synchrotron radiation scattering data from solutions of myelin-associated glycoprotein in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle). One solute concentration of 3.38 mg/ml was measured from nine successive 2 second frames. 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. The low angle data collected were obtained from a single concentration scattering curve.",
  "tags": [],
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  "experimental_mw_error": null,
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  "porod_volume": 177.0,
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  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 11,
  "guinier_point_last": 28,
  "pddf_point_first": null,
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDB55_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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