SASDBX7

Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Extrapolated to infinite dilution 最后更新:2023-05-25T11:22:08.798758+02:00

The chromo-ATPase domains of Saccharomyces cerevisiae Chd1 protein.

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)

浓度0.8 – 13.6 缓冲液 / pH50mM Hepes 150mM NaCl / 7.5
实验温度10.0 设备 / 束线DORIS III, DESY / EMBL X33
波长0.154 nm曝光120.0 s × —

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
chromodomain helicase DNA binding domain
查看序列
QNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGIDIVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLKRLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLEDGTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPRFEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIFARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGKKTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLITGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKKDVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASNHPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQMVRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINLMTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILEYAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAEDHVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQLEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSI
proteinSaccharomyces cerevisiaeP32657133–1010monomer分子数 1101.724 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
11462[3]0.1605–3.523 1/nm含误差列缺失 00sasbdb/entries/x7/sasdbx7/source/SASDBX7.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)16.1—nm
i0Guinier1.440.0021—
i0P(r)1.4340.001—
mwExperimental104.0—kDa
porod_volumePorod190.0—nm³
rgGuinier4.130.01nm
rgP(r)4.190.006nm

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50mM Hepes 150mM NaCl缓冲液浓度—
pH7.5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2008-11-30储存 / 测量温度10.0 / 10.0
曝光时间120.0帧数—
波长0.154样品-探测器距离5.0
光源X-ray synchrotron探测器Pilatus 2M
机构 / 束线DORIS III, DESY / EMBL X33 · Hamburg, Germany
q 范围0.161 – 3.523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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full_entry_zipsasbdb/entries/x7/sasdbx7/source/SASDBX7.zipdownloaded93128b56d56e09a307ccb7b62f2527fb3edecfc22a60cb98dd11705c424de542dac65下载查看原文件源站
pddfsasbdb/entries/x7/sasdbx7/source/SASDBX7.outdownloaded974787c23488671fcce7c9d9d03453edb9dab3b875656c73aef5808c8092a55ed1929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(4 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
codeSASDBX7
statusPublished
type_of_curveExtrapolated to infinite dilution
angular_unit1/nm
project.titleStructural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.
project.publication.titleStructural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.
project.publication.author_listSundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T
project.publication.journalElife
project.publication.doi10.7554/eLife.22510
project.publication.pmid28332978
project.publication.published_date2017 Mar 23
project.statusreleased
project.submitted_date2016-11-26
project.released_date2017-05-02
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.nameDORIS III, DESY
experiment.instrument.cityHamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL X33
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_namechromodomain helicase DNA binding domain
experiment.sample.molecule[0].short_nameChd1
experiment.sample.molecule[0].sequenceQNKTVNYNID YSDDDLLESE DDYGSEEALS EENVHEASAN PQPEDFHGID IVINHRLKTS LEEGKVLEKT VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK RLDNYCKQFI IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY SSNYTSQRPR FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF ARRQNGPHII VVPLSTMPAW LDTFEKWAPD LNCICYMGNQ KSRDTIREYE FYTNPRAKGK KTMKFNVLLT TYEYILKDRA ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK RKDEEYVKEQ LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR RARANDMDSI
experiment.sample.molecule[0].organismSaccharomyces cerevisiae
experiment.sample.molecule[0].uniprot_codeP32657
experiment.sample.molecule[0].uniprot_range_first133
experiment.sample.molecule[0].uniprot_range_last1010
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMAAKDISTEVLQNPELYGLRRSHRAAAHQQNYFNDSDDEDDEDNIKQSRRKRMTTIEDDE DEFEDEEGEEDSGEDEDEEDFEEDDDYYGSPIKQNRSKPKSRTKSKSKSKPKSQSEKQST VKIPTRFSNRQNKTVNYNIDYSDDDLLESEDDYGSEEALSEENVHEASANPQPEDFHGID IVINHRLKTSLEEGKVLEKTVPDLNNCKENYEFLIKWTDESHLHNTWETYESIGQVRGLK RLDNYCKQFIIEDQQVRLDPYVTAEDIEIMDMERERRLDEFEEFHVPERIIDSQRASLED GTSQLQYLVKWRRLNYDEATWENATDIVKLAPEQVKHFQNRENSKILPQYSSNYTSQRPR FEKLSVQPPFIKGGELRDFQLTGINWMAFLWSKGDNGILADEMGLGKTVQTVAFISWLIF ARRQNGPHIIVVPLSTMPAWLDTFEKWAPDLNCICYMGNQKSRDTIREYEFYTNPRAKGK KTMKFNVLLTTYEYILKDRAELGSIKWQFMAVDEAHRLKNAESSLYESLNSFKVANRMLI TGTPLQNNIKELAALVNFLMPGRFTIDQEIDFENQDEEQEEYIHDLHRRIQPFILRRLKK DVEKSLPSKTERILRVELSDVQTEYYKNILTKNYSALTAGAKGGHFSLLNIMNELKKASN HPYLFDNAEERVLQKFGDGKMTRENVLRGLIMSSGKMVLLDQLLTRLKKDGHRVLIFSQM VRMLDILGDYLSIKGINFQRLDGTVPSAQRRISIDHFNSPDSNDFVFLLSTRAGGLGINL MTADTVVIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLVSKDTVEEEVLERARKKMILE YAIISLGVTDGNKYTKKNEPNAGELSAILKFGAGNMFTATDNQKKLEDLNLDDVLNHAED HVTTPDLGESHLGGEEFLKQFEVTDYKADIDWDDIIPEEELKKLQDEEQKRKDEEYVKEQ LEMMNRRDNALKKIKNSVNGDGTAANSDSDDDSTSRSSRRRARANDMDSIGESEVRALYK AILKFGNLKEILDELIADGTLPVKSFEKYGETYDEMMEAAKDCVHEEEKNRKEILEKLEK HATAYRAKLKSGEIKAENQPKDNPLTRLSLKKREKKAVLFNFKGVKSLNAESLLSRVEDL KYLKNLINSNYKDDPLKFSLGNNTPKPVQNWSSNWTKEEDEKLLIGVFKYGYGSWTQIRD DPFLGITDKIFLNEVHNPVAKKSASSSDTTPTPSKKGKGITGSSKKVPGAIHLGRRVDYL LSFLRGGLNTKSPSADIGSKKLPTGPSKKRQRKPANHSKSMTPEITSSEPANGPPSKRMK ALPKGPAALINNTRLSPNSPTPPLKSKVSRDNGTRQSSNPSSGSAHEKEYDSMDEEDCRH TMSAIRTSLKRLRRGGKSLDRKEWAKILKTELTTIGNHIESQKGSSRKASPEKYRKHLWS YSANFWPADVKSTKLMAMYDKITESQKK
experiment.sample.molecule[0].mw101.724
experiment.sample.molecule[0].total_mw101.724
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.name50mM Hepes 150mM 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.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameChromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)
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].addressDundee, UK
experiment.contributor[0].affiliation[0].full_nameUniversity of Dundee
experiment.contributor[0].affiliation[0].webpagehttps://www.dundee.ac.uk/
experiment.contributor[0].contributor_nameRamasubramanian
experiment.contributor[0].contributor_surnameSundaramoorthy
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2008-11-30
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time120.0
experiment.number_of_framesnull
experiment.wavelength0.154
experiment.sample_detector_distance5.0
experiment.concentration_min0.8
experiment.concentration_max13.6
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.161
experiment.s_max3.523
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].lognull
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fits[0].models[0].comment
fits[0].models[0].user184
fits[0].fit_unit1/A
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fits[0].softwareGASBOR
fits[0].chi_square_value14.72
fits[0].p_value0.0
fits[0].fit_residual_plotSASDBX7_fit1_fitresiduals_img.png
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fits[0].fit_lognull
fits[0].software_version
fits[0].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionATSAS GNOM
i0_calibration_standardnull
descriptionThe chromo-ATPase domains of Saccharomyces cerevisiae Chd1 protein.
experiment_descriptionSynchrotron SAXS data from solutions of the chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected at the X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsin θ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 13.6 mg/ml were measured at 10°C. 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. Chromo-Helicase domain
tags[0]X33
intensity_unitnull
experimental_mw104.0
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i01.434
pddf_i0_error0.001
guinier_i01.44
guinier_i0_error0.0021
pddf_rg4.19
pddf_rg_error0.006
guinier_rg4.13
guinier_rg_error0.01
pddf_dmax16.1
pddf_dmax_errornull
porod_volume190.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first3
guinier_point_last50
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDBX7_datloglog_img.png
symmetrynull
last_modified2023-05-25T11:22:08.798758+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDBX7
statussuccess
started_at2026-08-11T15:41:49.247003+00:00
finished_at2026-08-11T15:42:01.210791+00:00
source_last_modified2023-05-25T11:22:08.798758+02:00
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查看完整 summary.json 原文
{
  "code": "SASDBX7",
  "status": "Published",
  "type_of_curve": "Extrapolated to infinite dilution",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.",
    "publication": {
      "title": "Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.",
      "author_list": "Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T",
      "journal": "Elife",
      "doi": "10.7554/eLife.22510",
      "pmid": "28332978",
      "published_date": "2017 Mar 23"
    },
    "status": "released",
    "submitted_date": "2016-11-26",
    "released_date": "2017-05-02"
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          "organism": "Saccharomyces cerevisiae",
          "uniprot_code": "P32657",
          "uniprot_range_first": 133,
          "uniprot_range_last": 1010,
          "oligomerization": "monomer",
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          "molecule_source": "biological",
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      "buffer": {
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        "deuteration": null
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      "purity_method": null,
      "name": "Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)",
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    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Dundee, UK",
            "full_name": "University of Dundee",
            "webpage": "https://www.dundee.ac.uk/"
          }
        ],
        "contributor_name": "Ramasubramanian",
        "contributor_surname": "Sundaramoorthy",
        "orcid": null
      }
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2008-11-30",
    "storage_temperature": 10.0,
    "cell_temperature": 10.0,
    "exposure_time": 120.0,
    "number_of_frames": null,
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      "fit_unit": "1/A",
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      "fit_residual_plot": "SASDBX7_fit1_fitresiduals_img.png",
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  "description": "The chromo-ATPase  domains of Saccharomyces cerevisiae Chd1 protein.",
  "experiment_description": "Synchrotron SAXS data from solutions of the chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected at the X33 beam line at the  DORIS III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsin θ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 13.6 mg/ml were measured at 10°C. 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.\r\n\r\nChromo-Helicase domain",
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  "last_modified": "2023-05-25T11:22:08.798758+02:00",
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}
查看完整 manifest.json 原文
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  "status": "success",
  "started_at": "2026-08-11T15:41:49.247003+00:00",
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  "source_last_modified": "2023-05-25T11:22:08.798758+02:00",
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