SASDCJ2

Solution structure of recombinant prion protein (89–230) in complex with Fab-P

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新:2019-12-06T13:07:15.624532+01:00
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1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Solution structure of recombinant prion protein (89–230) in complex with Fab-P

浓度1.0 – 3.7 缓冲液 / pHsodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl) / 5.1
实验温度9.8 设备 / 束线Stanford Synchrotron Radiation Lightsource (SSRL) / BL4-2
波长0.113 nm曝光1.0 s × 10

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Major prion protein
查看序列
KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRS
proteinMus musculusP0492523–230monomer分子数 122.932 kDa
P-Clone Fab, Chimera
查看序列
ATQAYAELVMTQTPSSLSASLGERVSLTCRASQDIGNNLNWIQQKPDGTIKRLIYATSSLDSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQHDTFPLTFGGGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRAYAEVQLLEQSGAELVKPGASVKLSCTASGFNIEDSYIHWVKQRPEQGLEWIGRIDPEDGETKYAPKFQGKATITADTSSNTAYLHLRRLTSEDTAIYYCGRGAYYIKEDFWGQGTTLTVSSASTKGPSVFPLAPSSKAGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPA
proteinHomo sapiens——–—monomer分子数 147.386 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
1498[3]0.0124103–0.472414 1/A含误差列缺失 00sasbdb/entries/j2/sasdcj2/source/SASDCJ2.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)14.50.5Å
i0Guinier1087.129.23—
i0P(r)1066.02.78—
mwExperimental73.8—kDa
porod_volumePorod106.0—ų
rgGuinier3.920.02Å
rgP(r)3.830.13Å

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

拟合 1 · FoXS

χ²:1.13CorMap p:0.058单位:1/A
模型名称 / 类型软件对称性模型 MWPDB 声明来源文件
1—atomicPDB (Protein Data Bank) —69.122HH0模型 图片
2—atomicPDB (Protein Data Bank) —69.12—模型 图片

拟合 2 · FoXS

χ²:2.13CorMap p:0.0单位:1/A
模型名称 / 类型软件对称性模型 MWPDB 声明来源文件
1—atomicPDB (Protein Data Bank) —69.12—模型 图片
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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sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl)缓冲液浓度—
pH5.1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2013-12-05储存 / 测量温度4.0 / 9.8
曝光时间1.0帧数10
波长0.113样品-探测器距离1.7
光源X-ray synchrotron探测器Rayonix MX225-HE
机构 / 束线Stanford Synchrotron Radiation Lightsource (SSRL) / BL4-2 · Menlo Park, CA, USA
q 范围0.124 – 4.724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(7 项)
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pddf:来源记录
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sascif: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:212 个字段值
字段路径原始值
codeSASDCJ2
statusPublished
type_of_curveMerged
angular_unit1/A
project.titlePrion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.
project.publication.titlePrion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.
project.publication.author_listCarter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A
project.publication.journalBiophys J
project.publication.doi10.1016/j.bpj.2015.06.065
project.publication.pmid26287631
project.publication.published_date2015 Aug 18
project.statusreleased
project.submitted_date2017-04-04
project.released_date2017-06-09
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intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDCJ2.dat
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intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCJ2_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDCJ2.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.nameRayonix MX225-HE
experiment.instrument.detector.resolutionnull
experiment.instrument.nameStanford Synchrotron Radiation Lightsource (SSRL)
experiment.instrument.cityMenlo Park, CA
experiment.instrument.countryUSA
experiment.instrument.beamline_nameBL4-2
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_nameMajor prion protein
experiment.sample.molecule[0].short_nameprion
experiment.sample.molecule[0].sequenceKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWG QPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFG NDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETD VKMMERVVEQMCVTQYQKESQAYYDGRRS
experiment.sample.molecule[0].organismMus musculus
experiment.sample.molecule[0].uniprot_codeP04925
experiment.sample.molecule[0].uniprot_range_first23
experiment.sample.molecule[0].uniprot_range_last230
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPH GGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAV VGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVN ITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPP VILLISFLIFLIVG
experiment.sample.molecule[0].mw22.932
experiment.sample.molecule[0].total_mw22.932
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.molecule[1].long_nameP-Clone Fab, Chimera
experiment.sample.molecule[1].short_nameFab-P
experiment.sample.molecule[1].sequenceATQAYAELVMTQTPSSLSASLGERVSLTCRASQDIGNNLNWIQQKPDGTIKRLIYATSS LDSGVPKRFSGSRSGSDYSLTISSLESEDFADYYCLQHDTFPLTFGGGTKLEIKRTVAAP SVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTY SLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR AYAEVQLLEQSGAELVKPGASVKLSCTASGFNIEDSYIHWVKQRPEQGLEWIGRIDPED GETKYAPKFQGKATITADTSSNTAYLHLRRLTSEDTAIYYCGRGAYYIKEDFWGQGTTLT VSSASTKGPSVFPLAPSSKAGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPA
experiment.sample.molecule[1].organismHomo sapiens
experiment.sample.molecule[1].uniprot_codenull
experiment.sample.molecule[1].uniprot_range_firstnull
experiment.sample.molecule[1].uniprot_range_lastnull
experiment.sample.molecule[1].oligomerizationmonomer
experiment.sample.molecule[1].molecular_typeprotein
experiment.sample.molecule[1].uniprot_sequencenull
experiment.sample.molecule[1].mw47.386
experiment.sample.molecule[1].total_mw47.386
experiment.sample.molecule[1].number_molecules1
experiment.sample.molecule[1].complex_stateFalse
experiment.sample.molecule[1].deuterationnull
experiment.sample.molecule[1].molecule_sourcebiological
experiment.sample.molecule[1].molecule_descriptionnull
experiment.sample.buffer.namesodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 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.ph5.1
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSolution structure of recombinant prion protein (89–230) in complex with Fab-P
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].addressJerusalem, Israel
experiment.contributor[0].affiliation[0].full_nameThe Hebrew University of Jerusalem
experiment.contributor[0].affiliation[0].webpagehttp://new.huji.ac.il
experiment.contributor[0].contributor_nameDina
experiment.contributor[0].contributor_surnameSchneidman
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-12-05
experiment.storage_temperature4.0
experiment.cell_temperature9.8
experiment.exposure_time1.0
experiment.number_of_frames10
experiment.wavelength0.113
experiment.sample_detector_distance1.7
experiment.concentration_min1.0
experiment.concentration_max3.7
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.124
experiment.s_max4.724
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].models[0].user206
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fits[0].models[1].comment
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fits[0].chi_square_value1.13
fits[0].p_value0.058
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fits[1].chi_square_value2.13
fits[1].p_value0.0
fits[1].fit_residual_plotnull
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fits[1].fit_lognull
fits[1].software_version
fits[1].descriptionnull
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM V5.0 (r8972)
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of recombinant prion protein (89–230) in complex with Fab-P in 20 mM sodium acetate, 150 mM NaCl, pH 5.1 were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL, Stanford, CA, USA) using a Rayonix MX225-HE detector at a sample-detector distance of 1.7 m and at a wavelength of λ = 0.113 nm (I(s) vs s, where s = 4πsin θ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 3.7 mg/ml were measured at 9.8°C. 10 successive 1 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 difference curves were scaled for protein concentration. 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_unitnull
experimental_mw73.8
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mwnull
porod_mw_errornull
pddf_i01066.0
pddf_i0_error2.78
guinier_i01087.12
guinier_i0_error9.23
pddf_rg3.83
pddf_rg_error0.13
guinier_rg3.92
guinier_rg_error0.02
pddf_dmax14.5
pddf_dmax_error0.5
porod_volume106.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first4
guinier_point_last15
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDCJ2_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDCJ2
statussuccess
started_at2026-08-11T13:39:21.785098+00:00
finished_at2026-08-11T13:39:31.675310+00:00
source_last_modified2019-12-06T13:07:15.624532+01:00
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查看完整 summary.json 原文
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    "title": "Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.",
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      "title": "Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.",
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      "doi": "10.1016/j.bpj.2015.06.065",
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查看完整 manifest.json 原文
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