SASDBP9

Human Hsp90 co-chaperone Cdc37 protein (CD37)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Extrapolated to infinite dilution 最后更新:2023-06-21T07:56:39.492710+02:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Human Hsp90 co-chaperone Cdc37 protein (CD37)

浓度1.1 – 4.2 缓冲液 / pH25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP / 8.0
实验温度20.0 设备 / 束线PETRA III / EMBL P12
波长0.124 nm曝光0.045 s × 20

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Hsp90 co-chaperone Cdc37
查看序列
MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDGSV
proteinHomo sapiensQ16543—–—monomer分子数 144.426 kDa

实验曲线

曲线点数 / 列q 范围误差质量负强度点来源文件
11818[3]0.0247955–5.0307 1/nm含误差列缺失 024sasbdb/entries/p9/sasdbp9/source/SASDBP9.dat
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2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)15.533.0nm
i0Guinier5968.7417.13—
i0P(r)6042.018.03—
mwExperimental49.1—kDa
mwGuinier I(0)49.15.0kDa
mwPorod52.0—kDa
porod_volumePorod106.46—nm³
rgGuinier3.990.59nm
rgP(r)4.190.02nm

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。

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3. 来源拟合与模型 Source Fits & Models

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4. 来源文件索引 Source Files

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5. 实验说明与论文 Experiment & Publication

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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“—”;未声明的单位不会由 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 Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP缓冲液浓度—
pH8.0添加剂—
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2016-07-10储存 / 测量温度20.0 / 20.0
曝光时间0.045帧数20
波长0.124样品-探测器距离3.1
光源X-ray synchrotron探测器Pilatus 2M
机构 / 束线PETRA III / EMBL P12 · DESY; Hamburg, Germany
q 范围0.025 – 5.031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

可下载文件

类别文件状态大小校验值下载与查看
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pddfsasbdb/entries/p9/sasdbp9/source/SASDBP9.outdownloaded14971441b1f048ccc3a64c1fc0456add0ce37ac02b9c6da7acfd1462e6dc50dd804afe下载查看原文件源站
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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(6 项)
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pddf:来源记录
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sascif:来源记录
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summary: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:182 个字段值
字段路径原始值
codeSASDBP9
statusPublished
type_of_curveExtrapolated to infinite dilution
angular_unit1/nm
project.titleDisease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
project.publication.titleDisease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
project.publication.author_listBunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M
project.publication.journalStructure
project.publication.doi10.1016/j.str.2018.01.016
project.publication.pmid29478821
project.publication.published_date2018 Mar 6
project.statusreleased
project.submitted_date2017-01-18
project.released_date2018-03-20
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
experiment.instrument.beam_geometrynull
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_nameHsp90 co-chaperone Cdc37
experiment.sample.molecule[0].short_nameCDC37
experiment.sample.molecule[0].sequenceMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDGSV
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ16543
experiment.sample.molecule[0].uniprot_range_firstnull
experiment.sample.molecule[0].uniprot_range_lastnull
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRK VAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLS KDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVH LVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTK IKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYES LPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPG DPLLEAVPKTGDEKDVSV
experiment.sample.molecule[0].mw44.426
experiment.sample.molecule[0].total_mw44.426
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.name25 mM Tris.Cl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameHuman Hsp90 co-chaperone Cdc37 protein (CD37)
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_nameEMBL-Hamburg
experiment.contributor[0].affiliation[0].addressNotkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany
experiment.contributor[0].affiliation[0].full_nameEuropean Molecular Biology Laboratory (EMBL) - Hamburg outstation
experiment.contributor[0].affiliation[0].webpagehttp://www.embl-hamburg.de/index.php
experiment.contributor[0].contributor_nameChris
experiment.contributor[0].contributor_surnameKerr
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-07-10
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time0.045
experiment.number_of_frames20
experiment.wavelength0.124
experiment.sample_detector_distance3.1
experiment.concentration_min1.1
experiment.concentration_max4.2
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.025
experiment.s_max5.031
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].pdb_link[0].pdb_code1us7
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fits[0].p_value0.0
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fits[1].softwareMONSA
fits[1].chi_square_value1.635
fits[1].p_value0.0
fits[1].fit_residual_plotSASDBP9_fit2_fitresiduals_img.png
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fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM5 - trunk r8992
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of human Hsp90 co-chaperone Cdc37 protein (CD37) in 25 mM Tris-HCl, 150 mM NaCl, 5% (v/v) glycerol, 1 mM TCEP, pH 8, were collected on the P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.1 and 4.2 mg/ml were measured at 20°C. 20 successive 0.045 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
tags[]
intensity_unitnull
experimental_mw49.1
experimental_mw_errornull
guinier_i0_mw49.1
guinier_i0_mw_error5.0
porod_mw52.0
porod_mw_errornull
pddf_i06042.0
pddf_i0_error18.03
guinier_i05968.74
guinier_i0_error17.13
pddf_rg4.19
pddf_rg_error0.02
guinier_rg3.99
guinier_rg_error0.59
pddf_dmax15.53
pddf_dmax_error3.0
porod_volume106.46
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first25
guinier_point_last110
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBP9_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDBP9
statussuccess
started_at2026-08-11T16:19:01.354279+00:00
finished_at2026-08-11T16:19:13.065156+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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查看完整 summary.json 原文
{
  "code": "SASDBP9",
  "status": "Published",
  "type_of_curve": "Extrapolated to infinite dilution",
  "angular_unit": "1/nm",
  "project": {
    "title": "Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.",
    "publication": {
      "title": "Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.",
      "author_list": "Bunney TD, Inglis AJ, Sanfelice D, Farrell B, Kerr CJ, Thompson GS, Masson GR, Thiyagarajan N, Svergun DI, Williams RL, Breeze AL, Katan M",
      "journal": "Structure",
      "doi": "10.1016/j.str.2018.01.016",
      "pmid": "29478821",
      "published_date": "2018 Mar 6"
    },
    "status": "released",
    "submitted_date": "2017-01-18",
    "released_date": "2018-03-20"
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查看完整 manifest.json 原文
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