SASDXK3

Alkaline serine protease (36 kDa peptidase core domain, StmPr1)

Data type: SASBDB experimental data Status: Published Curve type: Merged Last updated: 2025-06-23T08:56:50.911866+02:00

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · Alkaline serine protease (36 kDa peptidase core domain, StmPr1)

Concentration	1.0 – 10.0	Buffer / pH	20 mM Tris, 150 mM NaCl / 8.0
Experimental temperature	20.0	Facility / beamline	PETRA III / EMBL P12
Wavelength	0.124 nm	Exposure	0.05 s × 40

Molecular Components

Component	Type / organism	UniProt and Construct	Oligomeric State	Molecular weight
Alkaline serine protease View sequence LAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEE	proteinStenotrophomonas maltophilia	Q93IQ4151–509	monomerMolecule count 1	36.335 kDa

Experimental Curves

Curve	Points / columns	q range	Uncertainty quality	Negative-intensity points	Source file
1	1536[3]	0.02304513–4.432072 1/nm	Has uncertainty columnMissing 0	3	sasbdb/entries/k3/sasdxk3/source/SASDXK3.dat

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2. Measurements Reported by SASBDB Reported Results

Metric	Method	Value	Uncertainty	Unit
dmax	P(r)	5.5	—	nm
i0	Guinier	0.28287	—	1/cm
i0	P(r)	0.2812	—	1/cm
mw	Experimental	39.2	—	kDa
mw	Porod	28.0	—	kDa
porod_volume	Porod	44.0	—	nm³
rg	Guinier	1.933	0.001	nm
rg	P(r)	1.896	—	nm

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

This entry has no source fit record.

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4. Source File Index Source Files

Category	Path	Download status	Size
curve	sasbdb/entries/k3/sasdxk3/source/SASDXK3.dat	downloaded	85203
full_entry_zip	sasbdb/entries/k3/sasdxk3/source/SASDXK3.zip	downloaded	50999
pddf	sasbdb/entries/k3/sasdxk3/source/SASDXK3.out	downloaded	102825
sascif	sasbdb/entries/k3/sasdxk3/source/SASDXK3.sascif	not_available	—
summary	sasbdb/entries/k3/sasdxk3/source/summary.json	downloaded	7031

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5. Experiment Description and Publication Experiment & Publication

▼

6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name	20 mM Tris, 150 mM NaCl	Buffer concentration	—
pH	8.0	Additives	—
Buffer description	—
Purity measurement method	—	Extinction coefficient	—
Absorbance	—	Scattering contrast	—
Specific volume / dry volume	— / —	Mixture / deuteration	— / —

Acquisition Conditions and Instrument

Measurement date	2023-06-10	Storage / measurement temperature	20.0 / 20.0
Exposure time	0.05	Frames	40
Wavelength	0.124	Sample-to-detector distance	3.1
Source	X-ray synchrotron	Detector	Pilatus 6M
Facility / beamline	PETRA III / EMBL P12 · DESY; Hamburg, Germany
q range	0.023 – 4.432	Sample volume / flow rate	— / —

Original SASBDB Plots

Downloadable Files

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full_entry_zip	sasbdb/entries/k3/sasdxk3/source/SASDXK3.zip	downloaded	50999	63c03d850d12813a4bc2b3553c464671267e66c980addf6aa8c178e614feedff	DownloadView source fileSource site
pddf	sasbdb/entries/k3/sasdxk3/source/SASDXK3.out	downloaded	102825	f553c0352fc05329d813c471e23fc667e02591ba4c6099fe97c8f23bea55d7b2	DownloadView source fileSource site
sascif	sasbdb/entries/k3/sasdxk3/source/SASDXK3.sascif	not_available	—	—	DownloadView source fileSource site
summary	sasbdb/entries/k3/sasdxk3/source/summary.json	downloaded	7031	0dd344f9668bcd6085f87673f8bf3a65b8e6d282ff6bb1c164c6d303635afaca	DownloadView source fileSource site

curve：source record

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full_entry_zip：source record and ZIP contents (2 items)

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pddf：source record

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sascif：source record

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summary：source record

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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json：134 field values

Field path	Raw value
code	SASDXK3
status	Published
type_of_curve	Merged
angular_unit	1/nm
project.title	Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
project.publication.title	Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
project.publication.author_list	Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
project.publication.journal	Sci Rep
project.publication.doi	10.1038/s41598-025-06177-5
project.publication.pmid	40542111
project.publication.published_date	2025 Jun 20
project.status	released
project.submitted_date	2025-04-13
project.released_date	2025-06-23
pddf_data	https://www.sasbdb.org/media/p_of_R_files/SASDXK3.out
intensities_data	https://www.sasbdb.org/media/intensities_files/SASDXK3.dat
intensities_log_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_dat_img.png
intensities_kratky_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_kratky_img.png
pddf_plot	https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXK3_pofr_img.png
intensities_guinier_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_guinier_img.png
sascif_data	https://www.sasbdb.org/media/sascif/sascif_files/SASDXK3.sascif
experiment.instrument.detector.type	null
experiment.instrument.detector.name	Pilatus 6M
experiment.instrument.detector.resolution	null
experiment.instrument.name	PETRA III
experiment.instrument.city	DESY; Hamburg
experiment.instrument.country	Germany
experiment.instrument.beamline_name	EMBL P12
experiment.instrument.beam_geometry	null
experiment.instrument.type_of_source	X-ray synchrotron
experiment.instrument.point_source	null
experiment.instrument.line_collimation	null
experiment.instrument.sample_path_length	null
experiment.instrument.line_collimation_slitlength	null
experiment.instrument.line_collimation_integrationwidth	null
experiment.instrument.xray_energy	null
experiment.instrument.beam_profile_ah	null
experiment.instrument.beam_profile_al	null
experiment.sample.molecule[0].long_name	Alkaline serine protease
experiment.sample.molecule[0].short_name	StmPr1
experiment.sample.molecule[0].sequence	LAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEE
experiment.sample.molecule[0].organism	Stenotrophomonas maltophilia
experiment.sample.molecule[0].uniprot_code	Q93IQ4
experiment.sample.molecule[0].uniprot_range_first	151
experiment.sample.molecule[0].uniprot_range_last	509
experiment.sample.molecule[0].oligomerization	monomer
experiment.sample.molecule[0].molecular_type	protein
experiment.sample.molecule[0].uniprot_sequence	MIKKQNLRINVLAAAVLSMTAVGAVHAAGLPTREPVRQASAAQPGTDRIIVKYRAGSAAA GDRSAKLSTVQSALTRASLAGGTARASTLGPQVVRRLGVGADVIRLQGRLAPAELQRVLK ELKADPAVQYAEADVKLRRSELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDV SQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVEND NECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIAD AITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETD NASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSD AATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPF PVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYS FEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYI KVVGEAAYNGVSILATQ
experiment.sample.molecule[0].mw	36.335
experiment.sample.molecule[0].total_mw	36.335
experiment.sample.molecule[0].number_molecules	1
experiment.sample.molecule[0].complex_state	False
experiment.sample.molecule[0].deuteration	null
experiment.sample.molecule[0].molecule_source	biological
experiment.sample.molecule[0].molecule_description
experiment.sample.buffer.name	20 mM Tris, 150 mM NaCl
experiment.sample.buffer.concentration_unit	null
experiment.sample.buffer.comment	null
experiment.sample.buffer.additive	null
experiment.sample.buffer.concentration	null
experiment.sample.buffer.pka	null
experiment.sample.buffer.ph	8.0
experiment.sample.buffer.deuteration	null
experiment.sample.purity_method	null
experiment.sample.name	Alkaline serine protease (36 kDa peptidase core domain, StmPr1)
experiment.sample.ext_coefficient	null
experiment.sample.contrast	null
experiment.sample.specific_vol	null
experiment.sample.dry_vol	null
experiment.sample.absorbption	null
experiment.sample.deuteration	null
experiment.sample.mixture	null
experiment.contributor[0].affiliation[0].short_name	null
experiment.contributor[0].affiliation[0].address	Hamburg, Germany
experiment.contributor[0].affiliation[0].full_name	University of Hamburg
experiment.contributor[0].affiliation[0].webpage	https://www.uni-hamburg.de/
experiment.contributor[0].contributor_name	Max
experiment.contributor[0].contributor_surname	Sommer
experiment.contributor[0].orcid	https://orcid.org/0009-0001-8293-0177
experiment.concentration_method	null
experiment.concentration_unit	null
experiment.date	2023-06-10
experiment.storage_temperature	20.0
experiment.cell_temperature	20.0
experiment.exposure_time	0.05
experiment.number_of_frames	40
experiment.wavelength	0.124
experiment.sample_detector_distance	3.1
experiment.concentration_min	1.0
experiment.concentration_max	10.0
experiment.sample_volume	null
experiment.flow_rate	null
experiment.s_min	0.023
experiment.s_max	4.432
experiment.total_exposure_time	null
experiment.seccolumn	null
fits	[]
estimated_volume_method	null
pddf_software	ATSAS GNOM
pddf_software_version	5.0
i0_calibration_standard	null
description	null
experiment_description	Synchrotron SAXS data from solutions of alkaline serine protease (peptidase core domain) 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 1 and 10 mg/ml were measured at 20°C. 40 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_unit	1/cm
experimental_mw	39.2
experimental_mw_error	null
guinier_i0_mw	null
guinier_i0_mw_error	null
porod_mw	28.0
porod_mw_error	null
pddf_i0	0.2812
pddf_i0_error	null
guinier_i0	0.28287
guinier_i0_error	null
pddf_rg	1.896
pddf_rg_error	null
guinier_rg	1.933
guinier_rg_error	0.001
pddf_dmax	5.5
pddf_dmax_error	null
porod_volume	44.0
porod_volume_error	null
estimated_volume	null
estimated_volume_error	null
guinier_point_first	69
guinier_point_last	226
pddf_point_first	null
pddf_point_last	null
i0_calibration_standard_data	null
intensities_log_log_plot	SASDXK3_datloglog_img.png
symmetry	null
last_modified	2025-06-23T08:56:50.911866+02:00
bragg_peak	[]

manifest.json：34 field values

Field path	Raw value
code	SASDXK3
status	success
started_at	2026-08-11T14:02:33.013072+00:00
finished_at	2026-08-11T14:02:41.379475+00:00
source_last_modified	2025-06-23T08:56:50.911866+02:00
files[0].status	downloaded
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files[0].size	7031
files[0].sha256	0dd344f9668bcd6085f87673f8bf3a65b8e6d282ff6bb1c164c6d303635afaca
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View the complete summary.json source

{
  "code": "SASDXK3",
  "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": "https://www.sasbdb.org/media/p_of_R_files/SASDXK3.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDXK3.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXK3_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXK3_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDXK3.sascif",
  "experiment": {
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      "detector": {
        "type": null,
        "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",
          "short_name": "StmPr1",
          "sequence": "LAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPTATPIGTGIVDAKAALAKALEE",
          "organism": "Stenotrophomonas maltophilia",
          "uniprot_code": "Q93IQ4",
          "uniprot_range_first": 151,
          "uniprot_range_last": 509,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MIKKQNLRINVLAAAVLSMTAVGAVHAAGLPTREPVRQASAAQPGTDRIIVKYRAGSAAA\nGDRSAKLSTVQSALTRASLAGGTARASTLGPQVVRRLGVGADVIRLQGRLAPAELQRVLK\nELKADPAVQYAEADVKLRRSELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDV\nSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVEND\nNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIAD\nAITWASGGTVAGVPANANPAEVINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETD\nNASKYRPASCDGVVTVGATRITGGITYYSNYGSRVDLSGPGGGGSVDGNPGGYVWQSGSD\nAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPF\nPVSIPTATPIGTGIVDAKAALAKALEEPCTENCGPVATPLTNKTAVGGLNGTAGSSRLYS\nFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYI\nKVVGEAAYNGVSILATQ",
          "mw": 36.335,
          "total_mw": 36.335,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": ""
        }
      ],
      "buffer": {
        "name": "20 mM Tris, 150 mM NaCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Alkaline serine protease (36 kDa peptidase core domain, StmPr1)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "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",
        "contributor_surname": "Sommer",
        "orcid": "https://orcid.org/0009-0001-8293-0177"
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  "last_modified": "2025-06-23T08:56:50.911866+02:00",
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View the complete manifest.json source

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Title	Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence.
Authors	Sommer M, Negm A, Outzen L, Windhorst S, Gabdulkhakov A, Weber W, Betzel C
DOI / PMID	10.1038/s41598-025-06177-5 / 40542111