SASDA37

Surface Protein G (SasG) EG5 repeat protein G51-G52

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-G52

浓度— – 7.5 mg/ml缓冲液 / pH20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl / 7.5
Experimental temperature10.0 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 / OrganismUniProt 与Construct寡聚状态Molecular weight
Surface protein G
查看序列
GPHMAPKTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPET
proteinStaphylococcus aureusQ2G2B2420–629monomer分子数 123.729 kDa

实验曲线

曲线点数 / 列q range误差质量负强度点来源文件
11679[3]0.0685743–4.48844 1/nm含误差列缺失 00sasbdb/entries/37/sasda37/source/SASDA37.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)19.0nm
i0Guinier4140.4
i0P(r)4206.0
mwExperimental20.3kDa
mwGuinier I(0)20.3kDa
mwPorod23.7kDa
porod_volumePorod28.6nm³
rgGuinier4.72nm
rgP(r)5.08nm

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“—”;Not declared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
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 range0.069 – 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Download文件

类别文件状态大小校验值Download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(6 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:183 个字段值
字段路径原始值
codeSASDA37
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].sequenceGPHMAPKTITELEKKVEEIPFKKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGVIISKGEPKEEITKDPINELTEYGPETIAPGHRDEFDPKLPTGEKEEVPGKPGIKNPETGDVVRPPVDSVTKYGPVKGDSIVEKEEIPFEKERKFNPDLAPGTEKVTREGQKGEKTITTPTLKNPLTGEIISKGESKEEITKDPINELTEYGPET
experiment.sample.molecule[0].organismStaphylococcus aureus
experiment.sample.molecule[0].uniprot_codeQ2G2B2
experiment.sample.molecule[0].uniprot_range_first420
experiment.sample.molecule[0].uniprot_range_last629
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].mw23.729
experiment.sample.molecule[0].total_mw23.729
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-G52
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_unitmg/ml
experiment.date2013-11-12
experiment.storage_temperaturenull
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_max7.5
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.069
experiment.s_max4.488
experiment.total_exposure_timenull
experiment.seccolumnnull
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fits[0].softwarenull
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fits[0].p_value0.003173
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fits[1].p_value0.811058
fits[1].fit_residual_plotSASDA37_fit2_fitresiduals_img.png
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fits[1].descriptionnull
estimated_volume_methodnull
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_mw20.3
experimental_mw_errornull
guinier_i0_mw20.3
guinier_i0_mw_errornull
porod_mw23.7
porod_mw_errornull
pddf_i04206.0
pddf_i0_errornull
guinier_i04140.4
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pddf_rg_errornull
guinier_rg4.72
guinier_rg_errornull
pddf_dmax19.0
pddf_dmax_errornull
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porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
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guinier_point_lastnull
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDA37_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
codeSASDA37
statussuccess
started_at2026-08-11T15:20:43.866820+00:00
finished_at2026-08-11T15:20:53.093707+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": "SASDA37",
  "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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  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDA37.dat",
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}
查看完整 manifest.json 原文
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