SASDC62

Basic domain of telomeric repeat-binding factor 2 (TRF2)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2022-03-31T22:26:26.370859+02:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Basic domain of telomeric repeat-binding factor 2 (TRF2)

浓度— – 1.2 缓冲液 / pH50 mM NaPi, 50 mM NaCl / 7.0
实验温度4.0 设备 / 束线CEITEC / Rigaku BioSAXS-1000
波长1.54 nm曝光3600.0 s × 6

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Basic domain of telomeric repeat-binding factor 2
查看序列
GPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
proteinHomo sapiensQ1555442–86monomer分子数 14.587 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
1445[3]0.0109205–0.650319 1/A含误差列缺失 06sasbdb/entries/62/sasdc62/source/SASDC62.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)7.06—Å
i0Guinier0.1032870.000861426—
i0P(r)0.1060.001—
mwExperimental4.587—kDa
mwPorod2.3—kDa
porod_volumePorod3.69—ų
rgGuinier1.6570.168Å
rgP(r)1.8190.03Å

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

该条目没有来源拟合记录。

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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50 mM NaPi, 50 mM NaCl缓冲液浓度—
pH7.0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2015-03-05储存 / 测量温度4.0 / 4.0
曝光时间3600.0帧数6
波长1.54样品-探测器距离0.48
光源X-ray in house探测器Pilatus 100K
机构 / 束线CEITEC / Rigaku BioSAXS-1000 · Brno, Czech Republic
q 范围0.109 – 6.503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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curve:来源记录
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full_entry_zip:来源记录与 ZIP 内部目录(2 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:134 个字段值
字段路径原始值
codeSASDC62
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.author_listNecasová I, Janoušková E, Klumpler T, Hofr C
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkx812
project.publication.pmid28981702
project.publication.published_date2017 Dec 1
project.statusreleased
project.submitted_date2017-01-06
project.released_date2017-09-18
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experiment.instrument.detector.typenull
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experiment.instrument.detector.resolution172.0
experiment.instrument.nameCEITEC
experiment.instrument.cityBrno
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometry
experiment.instrument.type_of_sourceX-ray in house
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_nameBasic domain of telomeric repeat-binding factor 2
experiment.sample.molecule[0].short_nameTRF2
experiment.sample.molecule[0].sequenceGPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ15554
experiment.sample.molecule[0].uniprot_range_first42
experiment.sample.molecule[0].uniprot_range_last86
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRR ASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQ IRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEM IKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNI IREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDK QPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQ ALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLN SSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDE DSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLG MN
experiment.sample.molecule[0].mw4.587
experiment.sample.molecule[0].total_mw4.587
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_stateFalse
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experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name50 mM NaPi, 50 mM NaCl
experiment.sample.buffer.concentration_unitnull
experiment.sample.buffer.commentnull
experiment.sample.buffer.additivenull
experiment.sample.buffer.concentrationnull
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameBasic domain of telomeric repeat-binding factor 2 (TRF2)
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
experiment.sample.dry_volnull
experiment.sample.absorbptionnull
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experiment.sample.mixturenull
experiment.contributor[0].affiliation[0].short_namenull
experiment.contributor[0].affiliation[0].addressnull
experiment.contributor[0].affiliation[0].full_nameCEITEC - Central European Institute of Technology, Masaryk University
experiment.contributor[0].affiliation[0].webpagehttps://www.ceitec.eu/
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameKlumpler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2015-03-05
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time3600.0
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experiment.s_min0.109
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experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionprimus/qt r8972
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 1.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.
tags[0]idp
intensity_unitnull
experimental_mw4.587
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw2.3
porod_mw_errornull
pddf_i00.106
pddf_i0_error0.001
guinier_i00.103287
guinier_i0_error0.000861426
pddf_rg1.819
pddf_rg_error0.03
guinier_rg1.657
guinier_rg_error0.168
pddf_dmax7.06
pddf_dmax_errornull
porod_volume3.69
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first6
guinier_point_last48
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDC62_datloglog_img.png
symmetrynull
last_modified2022-03-31T22:26:26.370859+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDC62
statussuccess
started_at2026-08-11T13:31:12.464729+00:00
finished_at2026-08-11T13:31:19.977441+00:00
source_last_modified2022-03-31T22:26:26.370859+02:00
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查看完整 summary.json 原文
{
  "code": "SASDC62",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.",
    "publication": {
      "title": "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.",
      "author_list": "Necasová I, Janoušková E, Klumpler T, Hofr C",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkx812",
      "pmid": "28981702",
      "published_date": "2017 Dec 1"
    },
    "status": "released",
    "submitted_date": "2017-01-06",
    "released_date": "2017-09-18"
  },
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  "experiment_description": "SAXS data from solutions of the basic domain of telomeric repeat-binding factor 2 (TRF2) in 50 mM sodium phosphate, 50 mM NaCl, pH 7, were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 1.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.",
  "tags": [
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  "experimental_mw_error": null,
  "guinier_i0_mw": null,
  "guinier_i0_mw_error": null,
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  "pddf_i0_error": 0.001,
  "guinier_i0": 0.103287,
  "guinier_i0_error": 0.000861426,
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  "pddf_rg_error": 0.03,
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  "pddf_dmax": 7.06,
  "pddf_dmax_error": null,
  "porod_volume": 3.69,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 6,
  "guinier_point_last": 48,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDC62_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2022-03-31T22:26:26.370859+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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