SASDVN5

NT17 peptide

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新:2024-08-18T16:49:40.573540+02:00

The sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · NT17 peptide

浓度0.5 – 1.0 缓冲液 / pHSodium phosphate buffer / 7.4
实验温度10.0 设备 / 束线NSRRC / TPS13A
波长0.08265 nm曝光2.0 s × 5

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
NT17
查看序列
MATLEKLMKAFESLKSF
proteinsynthetic construct——–—monomer分子数 11.974 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
1422[3]0.01243–1.00168 1/A含误差列缺失 00sasbdb/entries/n5/sasdvn5/source/SASDVN5.dat
▼

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)4.0—Å
i0Guinier0.00537077—1/cm
mwExperimental1.4—kDa
porod_volumePorod4.5—ų
rgGuinier1.20.175Å

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

▶

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“—”;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Sodium phosphate buffer缓冲液浓度—
pH7.4添加剂—
缓冲液说明(PB) solution (containing 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% TFA)
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2021-10-21储存 / 测量温度10.0 / 10.0
曝光时间2.0帧数5
波长0.08265样品-探测器距离2.5
光源X-ray synchrotron探测器Eiger X 1M & 9M
机构 / 束线NSRRC / TPS13A · Hsinchu, Taiwan
q 范围0.124 – 10.017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

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/n5/sasdvn5/source/SASDVN5.outnot_listed——下载查看原文件
sascifsasbdb/entries/n5/sasdvn5/source/SASDVN5.sascifnot_available——下载查看原文件源站
summarysasbdb/entries/n5/sasdvn5/source/summary.jsondownloaded716931f1ee8b8c76498c7023028662b7e7d36a68a52370434ae2e41d6a8e296d2efe下载查看原文件源站
curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(3 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:156 个字段值
字段路径原始值
codeSASDVN5
statusPublished
type_of_curveMerged
angular_unit1/A
project.titleBinding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.
project.publication.titleBinding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.
project.publication.author_listLin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
project.publication.journalIUCrJ
project.publication.doi10.1107/S2052252524006341
project.publication.pmid39120045
project.publication.published_date2024 Sep 1
project.statusreleased
project.submitted_date2024-08-01
project.released_date2024-08-07
pddf_datanull
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pddf_plotnull
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experiment.instrument.detector.nameEiger X 1M & 9M
experiment.instrument.detector.resolution0.001
experiment.instrument.nameNSRRC
experiment.instrument.cityHsinchu
experiment.instrument.countryTaiwan
experiment.instrument.beamline_nameTPS13A
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray synchrotron
experiment.instrument.point_sourcenull
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experiment.instrument.xray_energynull
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experiment.sample.molecule[0].long_nameNT17
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMATLEKLMKAFESLKSF
experiment.sample.molecule[0].organismsynthetic construct
experiment.sample.molecule[0].uniprot_codenull
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_sequence
experiment.sample.molecule[0].mw1.974
experiment.sample.molecule[0].total_mw1.974
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_description
experiment.sample.buffer.nameSodium phosphate buffer
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.comment(PB) solution (containing 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% TFA)
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.4
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameNT17 peptide
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].addressHsinchu City, Taiwan
experiment.contributor[0].affiliation[0].full_nameNational Synchrotron Radiation Research Center
experiment.contributor[0].affiliation[0].webpagehttps://www.nsrrc.org.tw/
experiment.contributor[0].contributor_nameOrion
experiment.contributor[0].contributor_surnameShih
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2021-10-21
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time2.0
experiment.number_of_frames5
experiment.wavelength0.08265
experiment.sample_detector_distance2.5
experiment.concentration_min0.5
experiment.concentration_max1.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.124
experiment.s_max10.017
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].softwareRosetta
fits[0].models[0].pdb_link[]
fits[0].models[0].model_titlenull
fits[0].models[0].type_of_modelatomic
fits[0].models[0].software_versionnull
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fits[0].models[0].model_mw1.974
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fits[0].chi_square_value4.585
fits[0].p_value0.0
fits[0].fit_residual_plotSASDVN5_fit1_fitresiduals_img.png
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pddf_softwarenull
pddf_software_versionnull
i0_calibration_standardnull
descriptionThe sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).
experiment_descriptionSynchrotron SAXS data from solutions of NT17 peptide in sodium phosphate buffer, pH 7.4 were collected on the TPS13A beam line at the NSRRC (Hsinchu, Taiwan) using a Eiger X 1M & 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.08265 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 1 mg/ml were measured at 10°C. Five successive 2 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
tags[]
intensity_unit1/cm
experimental_mw1.4
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guinier_i0_mwnull
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pddf_dmax_errornull
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porod_volume_errornull
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guinier_point_first69
guinier_point_last148
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDVN5_datloglog_img.png
symmetrynull
last_modified2024-08-18T16:49:40.573540+02:00
bragg_peak[]
manifest.json:31 个字段值
字段路径原始值
codeSASDVN5
statussuccess
started_at2026-08-11T14:52:12.329301+00:00
finished_at2026-08-11T14:52:17.592243+00:00
source_last_modified2024-08-18T16:49:40.573540+02:00
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查看完整 summary.json 原文
{
  "code": "SASDVN5",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/A",
  "project": {
    "title": "Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.",
    "publication": {
      "title": "Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.",
      "author_list": "Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US",
      "journal": "IUCrJ",
      "doi": "10.1107/S2052252524006341",
      "pmid": "39120045",
      "published_date": "2024 Sep 1"
    },
    "status": "released",
    "submitted_date": "2024-08-01",
    "released_date": "2024-08-07"
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  "description": "The sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).",
  "experiment_description": "Synchrotron SAXS data from solutions of NT17 peptide in sodium phosphate buffer, pH 7.4 were collected on the TPS13A beam line at the NSRRC (Hsinchu, Taiwan) using a Eiger X 1M & 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.08265 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 1 mg/ml were measured at 10°C. Five successive 2 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.",
  "tags": [],
  "intensity_unit": "1/cm",
  "experimental_mw": 1.4,
  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
  "porod_mw": null,
  "porod_mw_error": null,
  "pddf_i0": null,
  "pddf_i0_error": null,
  "guinier_i0": 0.00537077,
  "guinier_i0_error": null,
  "pddf_rg": null,
  "pddf_rg_error": null,
  "guinier_rg": 1.2,
  "guinier_rg_error": 0.175,
  "pddf_dmax": 4.0,
  "pddf_dmax_error": null,
  "porod_volume": 4.5,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 69,
  "guinier_point_last": 148,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDVN5_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2024-08-18T16:49:40.573540+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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