SASDA77

Surface Protein G (SasG) EG5 repeat protein G51-G56

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2023-06-21T07:56:39.492710+02:00

SAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.

1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Surface Protein G (SasG) EG5 repeat protein G51-G56

浓度— – 4.0 缓冲液 / pH20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl / 7.5
实验温度10.0 设备 / 束线PETRA III / EMBL P12
波长0.12 nm曝光0.05 s × 20

分子组分

组分类型 / 物种UniProt 与构建体寡聚状态分子量
Surface protein G
查看序列
GPAMAPKTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETWSHPQFEK
proteinStaphylococcus aureusQ2G2B2419–1141monomer分子数 180.922 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
11687[3]0.0475023–4.48844 1/nm含误差列缺失 08sasbdb/entries/77/sasda77/source/SASDA77.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)57.0nm
i0Guinier10488.6
i0P(r)13550.0
mwExperimental69.7kDa
mwGuinier I(0)69.7kDa
mwPorod74.0kDa
porod_volumePorod89.2nm³
rgGuinier14.1nm
rgP(r)15.48nm

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。

3. 来源拟合与模型 Source Fits & Models

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20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl缓冲液浓度20.0 mM
pH7.5添加剂200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl
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2013-11-12储存 / 测量温度10.0 / 10.0
曝光时间0.05帧数20
波长0.12样品-探测器距离3.1
光源X-ray synchrotron探测器Pilatus 2M
机构 / 束线PETRA III / EMBL P12 · DESY; Hamburg, Germany
q 范围0.048 – 4.488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/77/sasda77/source/SASDA77.zipdownloaded1674952e245634122f938e6cabed6a8201eca22a663d5946443478687827e27417f638下载查看原文件源站
pddfsasbdb/entries/77/sasda77/source/SASDA77.outdownloaded35648858e7cddf7c2920f2374c777a03416a833a80fb19a2c3f3fb5be4f7fc615e46e下载查看原文件源站
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summarysasbdb/entries/77/sasda77/source/summary.jsondownloaded9943a2e81b61e0f85ef25b59536b0b26beed39cc9fb9ae3d6cf14631c754226cae58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(6 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:179 个字段值
字段路径原始值
codeSASDA77
statusPublished
type_of_curveSingle concentration
angular_unit1/nm
project.titleCooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
project.publication.titleCooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
project.publication.author_listGruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
project.publication.journalNat Commun
project.publication.doi10.1038/ncomms8271
project.publication.pmid26027519
project.publication.published_date2015 Jun 1
project.statusreleased
project.submitted_date2014-11-27
project.released_date2015-07-07
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experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 2M
experiment.instrument.detector.resolutionnull
experiment.instrument.namePETRA III
experiment.instrument.cityDESY; Hamburg
experiment.instrument.countryGermany
experiment.instrument.beamline_nameEMBL P12
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_nameSurface protein G
experiment.sample.molecule[0].short_nameSasG
experiment.sample.molecule[0].sequenceGPAMAPKTITELEK KVEEIPFKKE RKFNPDLAPG TEKVTREGQK GEKTITTPTL KNPLTGVIIS KGEPKEEITK DPINELTEYG PETIAPGHRD EFDPKLPTGE KEEVPGKPGI KNPETGDVVR PPVDSVTKYG PVKGDSIVEK EEIPFEKERK FNPDLAPGTE KVTREGQKGE KTITTPTLKN PLTGEIISKG ESKEEITKDP INELTEYGPE TITPGHRDEF DPKLPTGEKE EVPGKPGIKN PETGDVVRPP VDSVTKYGPV KGDSIVEKEE IPFEKERKFN PDLAPGTEKV TREGQKGEKT ITTPTLKNPL TGVIISKGEP KEEITKDPIN ELTEYGPETI TPGHRDEFDP KLPTGEKEEV PGKPGIKNPE TGDVVRPPVD SVTKYGPVKG DSIVEKEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG EIISKGESKE EITKDPINEL TEYGPETITP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG QKGEKTITTP TLKNPLTGEI ISKGESKEEI TKDPINELTE YGPETITPGH RDEFDPKLPT GEKEEVPGKP GIKNPETGDV VRPPVDSVTK YGPVKGDSIV EKEEIPFKKE RKFNPDLAPG TEKVTREGQK GEKTITTPTL KNPLTGEIIS KGESKEEITK DPINELTEYG PETWSHPQFEK
experiment.sample.molecule[0].organismStaphylococcus aureus
experiment.sample.molecule[0].uniprot_codeQ2G2B2
experiment.sample.molecule[0].uniprot_range_first419
experiment.sample.molecule[0].uniprot_range_last1141
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMRDKKGPVNKRVDFLSNKLNKYSIRKFTVGTASILIGSLMYLGTQQEAEAAENNIENPTT LKDNVQSKEVKIEEVTNKDTAPQGVEAKSEVTSNKDTIEHEPSVKAEDISKKEDTPKEVA DVAEVQPKSSVTHNAETPKVRKARSVDEGSFDITRDSKNVVESTPITIQGKEHFEGYGSV DIQKKPTDLGVSEVTRFNVGNESNGLIGALQLKNKIDFSKDFNFKVRVANNHQSNTTGAD GWGFLFSKGNAEEYLTNGGILGDKGLVNSGGFKIDTGYIYTSSMDKTEKQAGQGYRGYGA FVKNDSSGNSQMVGENIDKSKTNFLNYADNSTNTSDGKFHGQRLNDVILTYVASTGKMRA EYAGKTWETSITDLGLSKNQAYNFLITSSQRWGLNQGINANGWMRTDLKGSEFTFTPEAP KTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKG EPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPP VDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPL TGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPE TGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTIT TPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETITPGHRDEFDPKLPTGEKEEVPG KPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERKFNPDLAPGTEKVTREG QKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRDEFDPKLPT GEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPG TEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPETITPGHRD EFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFKKERK FNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPE TITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEE IPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPIN ELTEYGPETITPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKG DSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKE EITKDPVNELTEFGGEKIPQGHKDIFDPNLPTDQTEKVPGKPGIKNPDTGKVIEEPVDDV IKHGPKTGTPETKTVEIPFETKREFNPKLQPGEERVKQEGQPGSKTITTPITVNPLTGEK VGEGQPTEEITKQPVDKIVEFGGEKPKDPKGPENPEKPSRPTHPSGPVNPNNPGLSKDRA KPNGPVHSMDKNDKVKKSKIAKESVANQEKKRAELPKTGLESTQKGLIFSSIIGIAGLML LARRRKN
experiment.sample.molecule[0].mw80.922
experiment.sample.molecule[0].total_mw80.922
experiment.sample.molecule[0].number_molecules1
experiment.sample.molecule[0].complex_statenull
experiment.sample.molecule[0].deuterationnull
experiment.sample.molecule[0].molecule_sourcebiological
experiment.sample.molecule[0].molecule_descriptionnull
experiment.sample.buffer.name20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl
experiment.sample.buffer.concentration_unitmM
experiment.sample.buffer.commentnull
experiment.sample.buffer.additive200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl
experiment.sample.buffer.concentration20.0
experiment.sample.buffer.pkanull
experiment.sample.buffer.ph7.5
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameSurface Protein G (SasG) EG5 repeat protein G51-G56
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[]
experiment.contributor[0].contributor_nameFiona
experiment.contributor[0].contributor_surnameWhelan
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2013-11-12
experiment.storage_temperature10.0
experiment.cell_temperature10.0
experiment.exposure_time0.05
experiment.number_of_frames20
experiment.wavelength0.12
experiment.sample_detector_distance3.1
experiment.concentration_minnull
experiment.concentration_max4.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.048
experiment.s_max4.488
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[1].descriptionnull
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pddf_softwareATSAS GNOM
pddf_software_versionnull
i0_calibration_standardnull
descriptionSAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.
experiment_descriptionnull
tags[]
intensity_unitnull
experimental_mw69.7
experimental_mw_errornull
guinier_i0_mw69.7
guinier_i0_mw_errornull
porod_mw74.0
porod_mw_errornull
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pddf_i0_errornull
guinier_i010488.6
guinier_i0_errornull
pddf_rg15.48
pddf_rg_errornull
guinier_rg14.1
guinier_rg_errornull
pddf_dmax57.0
pddf_dmax_errornull
porod_volume89.2
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last13
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDA77_datloglog_img.png
symmetrynull
last_modified2023-06-21T07:56:39.492710+02:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDA77
statussuccess
started_at2026-08-11T15:23:19.960687+00:00
finished_at2026-08-11T15:23:29.480736+00:00
source_last_modified2023-06-21T07:56:39.492710+02:00
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查看完整 summary.json 原文
{
  "code": "SASDA77",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/nm",
  "project": {
    "title": "Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.",
    "publication": {
      "title": "Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.",
      "author_list": "Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J",
      "journal": "Nat Commun",
      "doi": "10.1038/ncomms8271",
      "pmid": "26027519",
      "published_date": "2015 Jun 1"
    },
    "status": "released",
    "submitted_date": "2014-11-27",
    "released_date": "2015-07-07"
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}
查看完整 manifest.json 原文
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  "code": "SASDA77",
  "status": "success",
  "started_at": "2026-08-11T15:23:19.960687+00:00",
  "finished_at": "2026-08-11T15:23:29.480736+00:00",
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