SASDAB8

Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新:2023-05-25T11:22:16.556436+02:00

Structure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) contributions. To obtain the dimer scattering, two samples were measured at 4.4 and 8,8 mg/ml, and decomposed as described in the reference. Models were fitted to data using a combination of rigid body modelling and EOM, based on structural components defined by NMR and MD simulations. PDB files represent structures found in the optimal ensemble. All data, in addition to that displayed for this entry, are available in the .zip archive.

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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Protein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).

浓度4.2 – 8.8 mg/ml缓冲液 / pH50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100 / 7.4
实验温度4.0 设备 / 束线DORIS III, DESY / EMBL X33
波长— nm曝光40.0 s × 4

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
PRKCA-binding protein
查看序列
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWLKV
proteinRattus norvegicusQ9EP802–416dimer分子数 246.506 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
1116[4]0.0675000018–6.26464963 1/nm含误差列缺失 00sasbdb/entries/b8/sasdab8/source/SASDAB8.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)20.0—nm
i0Guinier1.070.01—
i0P(r)1.0290.01—
mwExperimental92.0—kDa
mwGuinier I(0)92.0—kDa
porod_volumePorod205.0—nm³
rgGuinier6.0170.91nm
rgP(r)6.030.05nm

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50 mM Tris 125 mM NaCl 0.01 vol% reduced TX-100缓冲液浓度50.0 mM
pH7.4添加剂125 mM NaCl, 0.01 vol% reduced TX-100
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2015-05-11储存 / 测量温度— / 4.0
曝光时间40.0帧数4
波长—样品-探测器距离—
光源X-ray synchrotron探测器MAR 345 Image Plate
机构 / 束线DORIS III, DESY / EMBL X33 · Hamburg, Germany
q 范围0.068 – 6.265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(9 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:182 个字段值
字段路径原始值
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statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleStructure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.
project.publication.titleStructure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.
project.publication.author_listKarlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL
project.publication.journalStructure
project.publication.doi10.1016/j.str.2015.04.020
project.publication.pmid26073603
project.publication.published_date2015 Jul 7
project.statusreleased
project.submitted_date2015-05-10
project.released_date2015-07-07
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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
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experiment.instrument.xray_energynull
experiment.instrument.beam_profile_ahnull
experiment.instrument.beam_profile_alnull
experiment.sample.molecule[0].long_namePRKCA-binding protein
experiment.sample.molecule[0].short_namenull
experiment.sample.molecule[0].sequenceMFADLDYDIEEDKLGI PTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGR SIKGKTKVEVAKMIQEVKGEVTIHYNK LQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAIL CNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAAS EAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWLKV
experiment.sample.molecule[0].organismRattus norvegicus
experiment.sample.molecule[0].uniprot_codeQ9EP80
experiment.sample.molecule[0].uniprot_range_first2
experiment.sample.molecule[0].uniprot_range_last416
experiment.sample.molecule[0].oligomerizationdimer
experiment.sample.molecule[0].molecular_typeprotein
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experiment.sample.molecule[0].total_mw93.011
experiment.sample.molecule[0].number_molecules2
experiment.sample.molecule[0].complex_stateFalse
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experiment.sample.buffer.concentration_unitmM
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experiment.sample.buffer.ph7.4
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experiment.sample.nameProtein Interacting with C-kinase 1 (PICK1) LKV, dimer contribution (data decomposition).
experiment.sample.ext_coefficientnull
experiment.sample.contrastnull
experiment.sample.specific_volnull
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experiment.contributor[0].affiliation[0].short_namenull
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experiment.contributor[0].contributor_nameMorten
experiment.contributor[0].contributor_surnameKarlsen
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experiment.concentration_unitmg/ml
experiment.date2015-05-11
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pddf_softwareATSAS GNOM
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i0_calibration_standardBSA
descriptionStructure and flexibility of PICK1 LKV mutant dimer was characterized by SAXS using data obtained by decomposing scattering from two polydisperse samples into dimer (and tetramer) contributions. To obtain the dimer scattering, two samples were measured at 4.4 and 8,8 mg/ml, and decomposed as described in the reference. Models were fitted to data using a combination of rigid body modelling and EOM, based on structural components defined by NMR and MD simulations. PDB files represent structures found in the optimal ensemble. All data, in addition to that displayed for this entry, are available in the .zip archive.
experiment_descriptionnull
tags[0]X33
intensity_unitnull
experimental_mw92.0
experimental_mw_errornull
guinier_i0_mw92.0
guinier_i0_mw_errornull
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pddf_i01.029
pddf_i0_error0.01
guinier_i01.07
guinier_i0_error0.01
pddf_rg6.03
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guinier_rg_error0.91
pddf_dmax20.0
pddf_dmax_errornull
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symmetrynull
last_modified2023-05-25T11:22:16.556436+02:00
bragg_peak[]
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字段路径原始值
codeSASDAB8
statussuccess
started_at2026-08-11T15:49:33.173709+00:00
finished_at2026-08-11T15:49:44.084007+00:00
source_last_modified2023-05-25T11:22:16.556436+02:00
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查看完整 summary.json 原文
{
  "code": "SASDAB8",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.",
    "publication": {
      "title": "Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.",
      "author_list": "Karlsen ML, Thorsen TS, Johner N, Ammendrup-Johnsen I, Erlendsson S, Tian X, Simonsen JB, Høiberg-Nielsen R, Christensen NM, Khelashvili G, Streicher W, Teilum K, Vestergaard B, Weinstein H, Gether U, Arleth L, Madsen KL",
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      "doi": "10.1016/j.str.2015.04.020",
      "pmid": "26073603",
      "published_date": "2015 Jul 7"
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    "released_date": "2015-07-07"
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            "address": "Copenhagen, Denmark",
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}
查看完整 manifest.json 原文
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