SASDXL3

Alkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Merged 最后更新:2025-06-23T08:56:50.963067+02:00

1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Alkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)

浓度0.25 – 2.0 缓冲液 / pH20 mM Tris, 150 mM NaCl / 8.0
Experimental temperature20.0 设备 / 束线PETRA III / EMBL P12
波长0.124 nm曝光0.05 s × 20

分子组分

组分类型 / OrganismUniProt 与Construct寡聚状态Molecular weight
Alkaline serine protease (Δ1-150)
查看序列
LAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYSFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYIKVVGEAAYNGVSILATQ
proteinStenotrophomonas maltophiliaQ93IQ4151–617monomer分子数 147.476 kDa

实验曲线

曲线点数 / 列q range误差质量负强度点来源文件
12651[3]0.0243063–7.37124 1/nm含误差列缺失 021sasbdb/entries/l3/sasdxl3/source/SASDXL3.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)10.0nm
i0Guinier0.1424561/cm
mwExperimental62.4kDa
mwPorod70.0kDa
porod_volumePorod112.0nm³
rgGuinier2.870.007nm

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

该条目没有来源拟合记录。

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, 150 mM NaCl缓冲液浓度
pH8.0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2021-11-25储存 / 测量温度20.0 / 20.0
曝光时间0.05帧数20
波长0.124样品-探测器距离3.1
光源X-ray synchrotron探测器Pilatus 6M
机构 / 束线PETRA III / EMBL P12 · DESY; Hamburg, Germany
q range0.024 – 7.371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

可Download文件

类别文件状态大小校验值Download与查看
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pddfsasbdb/entries/l3/sasdxl3/source/SASDXL3.outnot_listedDownload查看原文件
sascifsasbdb/entries/l3/sasdxl3/source/SASDXL3.sascifnot_availableDownload查看原文件源站
summarysasbdb/entries/l3/sasdxl3/source/summary.jsondownloaded70519011e8ff183470e11ce5a283aa5feafc2446fb14c3dc9176f22c71890aced669Download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(1 项)
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pddf:来源记录
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sascif:来源记录
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  "status": "not_available",
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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:134 个字段值
字段路径原始值
codeSASDXL3
statusPublished
type_of_curveMerged
angular_unit1/nm
project.titleUnveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
project.publication.titleUnveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
project.publication.author_listSommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
project.publication.journalSci Rep
project.publication.doi10.1038/s41598-025-06177-5
project.publication.pmid40542111
project.publication.published_date2025 Jun 20
project.statusreleased
project.submitted_date2025-04-13
project.released_date2025-06-23
pddf_datanull
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDXL3.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_kratky_img.png
pddf_plotnull
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDXL3.sascif
experiment.instrument.detector.typenull
experiment.instrument.detector.namePilatus 6M
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_nameAlkaline serine protease (Δ1-150)
experiment.sample.molecule[0].short_nameStmPr1
experiment.sample.molecule[0].sequenceLAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYSFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYIKVVGEAAYNGVSILATQ
experiment.sample.molecule[0].organismStenotrophomonas maltophilia
experiment.sample.molecule[0].uniprot_codeQ93IQ4
experiment.sample.molecule[0].uniprot_range_first151
experiment.sample.molecule[0].uniprot_range_last617
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMIKKQNLRINVLAAAVLSMTAVGAVHAAGLPTREPVRQASAAQPGTDRIIVKYRAGSAAA GDRSAKLSTVQSALTRASLAGGTARASTLGPQVVRRLGVGADVIRLQGRLAPAELQRVLK ELKADPAVQYAEADVKLRRSELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDV SQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVEND NECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIAD AITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETD NASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSD AATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPF PVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYS FEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYI KVVGEAAYNGVSILATQ
experiment.sample.molecule[0].mw47.476
experiment.sample.molecule[0].total_mw47.476
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_description
experiment.sample.buffer.name20 mM Tris, 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.ph8.0
experiment.sample.buffer.deuterationnull
experiment.sample.purity_methodnull
experiment.sample.nameAlkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)
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].addressHamburg, Germany
experiment.contributor[0].affiliation[0].full_nameUniversity of Hamburg
experiment.contributor[0].affiliation[0].webpagehttps://www.uni-hamburg.de/
experiment.contributor[0].contributor_nameMax
experiment.contributor[0].contributor_surnameSommer
experiment.contributor[0].orcidhttps://orcid.org/0009-0001-8293-0177
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2021-11-25
experiment.storage_temperature20.0
experiment.cell_temperature20.0
experiment.exposure_time0.05
experiment.number_of_frames20
experiment.wavelength0.124
experiment.sample_detector_distance3.1
experiment.concentration_min0.25
experiment.concentration_max2.0
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.024
experiment.s_max7.371
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwarenull
pddf_software_versionnull
i0_calibration_standardnull
descriptionnull
experiment_descriptionSynchrotron SAXS data from solutions of alkaline serine protease (peptidase core and C-terminal domains) in 20 mM Tris, 150 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 2 mg/ml were measured at 20°C. 20 successive 0.050 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. 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_unit1/cm
experimental_mw62.4
experimental_mw_errornull
guinier_i0_mwnull
guinier_i0_mw_errornull
porod_mw70.0
porod_mw_errornull
pddf_i0null
pddf_i0_errornull
guinier_i00.142456
guinier_i0_errornull
pddf_rgnull
pddf_rg_errornull
guinier_rg2.87
guinier_rg_error0.007
pddf_dmax10.0
pddf_dmax_errornull
porod_volume112.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first35
guinier_point_last155
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDXL3_datloglog_img.png
symmetrynull
last_modified2025-06-23T08:56:50.963067+02:00
bragg_peak[]
manifest.json:31 个字段值
字段路径原始值
codeSASDXL3
statussuccess
started_at2026-08-11T14:03:14.871345+00:00
finished_at2026-08-11T14:03:21.438914+00:00
source_last_modified2025-06-23T08:56:50.963067+02:00
files[0].statusdownloaded
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查看完整 summary.json 原文
{
  "code": "SASDXL3",
  "status": "Published",
  "type_of_curve": "Merged",
  "angular_unit": "1/nm",
  "project": {
    "title": "Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.",
    "publication": {
      "title": "Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.",
      "author_list": "Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C",
      "journal": "Sci Rep",
      "doi": "10.1038/s41598-025-06177-5",
      "pmid": "40542111",
      "published_date": "2025 Jun 20"
    },
    "status": "released",
    "submitted_date": "2025-04-13",
    "released_date": "2025-06-23"
  },
  "pddf_data": null,
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDXL3.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_kratky_img.png",
  "pddf_plot": null,
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXL3_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDXL3.sascif",
  "experiment": {
    "instrument": {
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        "name": "Pilatus 6M",
        "resolution": null
      },
      "name": "PETRA III",
      "city": "DESY; Hamburg",
      "country": "Germany",
      "beamline_name": "EMBL P12",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
      "point_source": null,
      "line_collimation": null,
      "sample_path_length": null,
      "line_collimation_slitlength": null,
      "line_collimation_integrationwidth": null,
      "xray_energy": null,
      "beam_profile_ah": null,
      "beam_profile_al": null
    },
    "sample": {
      "molecule": [
        {
          "long_name": "Alkaline serine protease (Δ1-150)",
          "short_name": "StmPr1",
          "sequence": "LAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYSFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYIKVVGEAAYNGVSILATQ",
          "organism": "Stenotrophomonas maltophilia",
          "uniprot_code": "Q93IQ4",
          "uniprot_range_first": 151,
          "uniprot_range_last": 617,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MIKKQNLRINVLAAAVLSMTAVGAVHAAGLPTREPVRQASAAQPGTDRIIVKYRAGSAAA\nGDRSAKLSTVQSALTRASLAGGTARASTLGPQVVRRLGVGADVIRLQGRLAPAELQRVLK\nELKADPAVQYAEADVKLRRSELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDV\nSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVEND\nNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIAD\nAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETD\nNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSD\nAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPF\nPVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYS\nFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYI\nKVVGEAAYNGVSILATQ",
          "mw": 47.476,
          "total_mw": 47.476,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": ""
        }
      ],
      "buffer": {
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        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Alkaline serine protease (47 kDa peptidase core and C-terminal domains, StmPr1)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
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        "affiliation": [
          {
            "short_name": null,
            "address": "Hamburg, Germany",
            "full_name": "University of Hamburg",
            "webpage": "https://www.uni-hamburg.de/"
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        ],
        "contributor_name": "Max",
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        "orcid": "https://orcid.org/0009-0001-8293-0177"
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    "concentration_method": null,
    "concentration_unit": null,
    "date": "2021-11-25",
    "storage_temperature": 20.0,
    "cell_temperature": 20.0,
    "exposure_time": 0.05,
    "number_of_frames": 20,
    "wavelength": 0.124,
    "sample_detector_distance": 3.1,
    "concentration_min": 0.25,
    "concentration_max": 2.0,
    "sample_volume": null,
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  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "Synchrotron SAXS data from solutions of alkaline serine protease (peptidase core and C-terminal domains) in 20 mM Tris, 150 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 2 mg/ml were measured at 20°C. 20 successive 0.050 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.",
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  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDXL3_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2025-06-23T08:56:50.963067+02:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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