SASDXV4

EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2025-11-02T21:11:43.418457+01:00

1. 样品、组分与实验条件 Sample & Experiment

样品 1 · EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml

浓度— – 2.6 缓冲液 / pH20 mM HEPES, 250 mM NaCl, 250 mM KCl / 8.0
Experimental temperature4.0 设备 / 束线Yale University / Rigaku MicroMax-007HF
波长0.1542 nm曝光7200.0 s × 3

分子组分

组分类型 / OrganismUniProt 与Construct寡聚状态Molecular weight
Receptor protein-tyrosine kinase (duplication mutant)
查看序列
HHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
proteinHomo sapiensQ504U8651–993monomer分子数 179.594 kDa

实验曲线

曲线点数 / 列q range误差质量负强度点来源文件
1601[3]0.0069953898–0.500787611 1/A含误差列缺失 097sasbdb/entries/v4/sasdxv4/source/SASDXV4.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)16.4Å
i0Guinier0.278134arbitrary
i0P(r)0.2736arbitrary
mwExperimental86.0kDa
mwGuinier I(0)86.0kDa
mwPorod101.0kDa
porod_volumePorod163.0ų
rgGuinier4.8670.663Å
rgP(r)4.87Å

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 HEPES, 250 mM NaCl, 250 mM KCl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2022-03-22储存 / 测量温度4.0 / 4.0
曝光时间7200.0帧数3
波长0.1542样品-探测器距离0.491
光源X-ray in house探测器Rigaku PSAXS Nano
机构 / 束线Yale University / Rigaku MicroMax-007HF · New Haven, United States
q range0.07 – 5.008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
curvesasbdb/entries/v4/sasdxv4/source/SASDXV4.datdownloaded39701ffe617db2e793bbd14f3bf5e7ae9ec840a4ec7d164488b8d904d2caecc3e5d4cDownload查看原文件源站
full_entry_zipsasbdb/entries/v4/sasdxv4/source/SASDXV4.zipdownloaded224220208ef77bab7ecf7c95447bd72a224b57dcb45352df75c9cf364aebdd344cec5Download查看原文件源站
pddfsasbdb/entries/v4/sasdxv4/source/SASDXV4.outdownloaded27489e610c60ca50c66deb1b24b5db3383e2c5074febb09084f822757eed49897cffaDownload查看原文件源站
sascifsasbdb/entries/v4/sasdxv4/source/SASDXV4.sascifnot_availableDownload查看原文件源站
summarysasbdb/entries/v4/sasdxv4/source/summary.jsondownloaded7773924721796f4e65d482c15cf9d4d531c9727255a571141a6cada54791e8e84665Download查看原文件源站
curve:来源记录
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  "url": "https://www.sasbdb.org/media/intensities_files/SASDXV4.dat"
}
full_entry_zip:来源记录与 ZIP 内部目录(2 项)
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  "zip_member_count": 2,
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pddf:来源记录
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sascif:来源记录
{
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  "role": "sascif",
  "status": "not_available",
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summary:来源记录
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  "size": 7773,
  "status": "downloaded",
  "url": "https://www.sasbdb.org/rest-api/entry/summary/SASDXV4/"
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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:129 个字段值
字段路径原始值
codeSASDXV4
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleThe role of kinase domain dimerization in EGFR activation
project.publicationnull
project.statusreleased
project.submitted_date2025-03-16
project.released_date2025-11-02
pddf_datahttps://www.sasbdb.org/media/p_of_R_files/SASDXV4.out
intensities_datahttps://www.sasbdb.org/media/intensities_files/SASDXV4.dat
intensities_log_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_dat_img.png
intensities_kratky_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_kratky_img.png
pddf_plothttps://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXV4_pofr_img.png
intensities_guinier_plothttps://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_guinier_img.png
sascif_datahttps://www.sasbdb.org/media/sascif/sascif_files/SASDXV4.sascif
experiment.instrument.detector.typeRigaku HyPix - 3000
experiment.instrument.detector.nameRigaku PSAXS Nano
experiment.instrument.detector.resolution100.0
experiment.instrument.nameYale University
experiment.instrument.cityNew Haven
experiment.instrument.countryUnited States
experiment.instrument.beamline_nameRigaku MicroMax-007HF
experiment.instrument.beam_geometrynull
experiment.instrument.type_of_sourceX-ray in house
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_nameReceptor protein-tyrosine kinase (duplication mutant)
experiment.sample.molecule[0].short_nameKDD
experiment.sample.molecule[0].sequenceHHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ504U8
experiment.sample.molecule[0].uniprot_range_first651
experiment.sample.molecule[0].uniprot_range_last993
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
experiment.sample.molecule[0].uniprot_sequenceMRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA VLSNYDANKTGLKELPMRNLQGQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRG KSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKY SFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEF KDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFL LIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISG NKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVS CRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHY IDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS IATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR ILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYV MASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGM NYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALES ILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYM IMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEE DMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSF LQRYSSDPTGALTEDSIDDTFLPVPGEWLVWKQSCSSTSSTHSAAASLQCPSQVLPPASP EGETVADLQTQ
experiment.sample.molecule[0].mw79.594
experiment.sample.molecule[0].total_mw79.594
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_descriptionEGFR kinase domain duplication mutant. The purified construct consists of amino acids 643-976 appended to amino acids 651-993 using mature protein numbering (UniProt Q504U8 numbering: 651-993 followed by a duplicated 643-977 region). The protein construct used for SAXS contains an additional N-terminal non-native 22 amino acid extension and polyhistidine tag (HHHHHHSSGVDLGTENLYFQSM).
experiment.sample.buffer.name20 mM HEPES, 250 mM NaCl, 250 mM KCl
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.nameEGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml
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].addressNew Haven, CT, USA
experiment.contributor[0].affiliation[0].full_nameYale University
experiment.contributor[0].affiliation[0].webpagehttps://www.yale.edu/
experiment.contributor[0].contributor_nameZaritza
experiment.contributor[0].contributor_surnamePetrova
experiment.contributor[0].orcidhttps://orcid.org/0000-0002-4877-4676
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2022-03-22
experiment.storage_temperature4.0
experiment.cell_temperature4.0
experiment.exposure_time7200.0
experiment.number_of_frames3
experiment.wavelength0.1542
experiment.sample_detector_distance0.491
experiment.concentration_minnull
experiment.concentration_max2.6
experiment.sample_volumenull
experiment.flow_ratenull
experiment.s_min0.07
experiment.s_max5.008
experiment.total_exposure_timenull
experiment.seccolumnnull
fits[]
estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_version5.0
i0_calibration_standardnull
descriptionnull
experiment_descriptionSAXS data from solutions of EGFR kinase domain duplication mutant in 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH 8 were collected on the Rigaku MicroMax-007HF instrument (Yale University, New Haven, United States) using a Rigaku PSAXS Nano detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.60 mg/ml was measured at 4°C. Three successive 7200 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.
tags[]
intensity_unitarbitrary
experimental_mw86.0
experimental_mw_errornull
guinier_i0_mw86.0
guinier_i0_mw_errornull
porod_mw101.0
porod_mw_errornull
pddf_i00.2736
pddf_i0_errornull
guinier_i00.278134
guinier_i0_errornull
pddf_rg4.87
pddf_rg_errornull
guinier_rg4.867
guinier_rg_error0.663
pddf_dmax16.4
pddf_dmax_errornull
porod_volume163.0
porod_volume_errornull
estimated_volumenull
estimated_volume_errornull
guinier_point_first2
guinier_point_last25
pddf_point_firstnull
pddf_point_lastnull
i0_calibration_standard_datanull
intensities_log_log_plotSASDXV4_datloglog_img.png
symmetrynull
last_modified2025-11-02T21:11:43.418457+01:00
bragg_peak[]
manifest.json:34 个字段值
字段路径原始值
codeSASDXV4
statussuccess
started_at2026-08-11T14:32:37.719435+00:00
finished_at2026-08-11T14:32:44.789741+00:00
source_last_modified2025-11-02T21:11:43.418457+01:00
files[0].statusdownloaded
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files[3].rolesascif
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files[4].zip_validationcentral_directory_readable
查看完整 summary.json 原文
{
  "code": "SASDXV4",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "The role of kinase domain dimerization in EGFR activation",
    "publication": null,
    "status": "released",
    "submitted_date": "2025-03-16",
    "released_date": "2025-11-02"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDXV4.out",
  "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDXV4.dat",
  "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_dat_img.png",
  "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_kratky_img.png",
  "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDXV4_pofr_img.png",
  "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDXV4_guinier_img.png",
  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDXV4.sascif",
  "experiment": {
    "instrument": {
      "detector": {
        "type": "Rigaku HyPix - 3000",
        "name": "Rigaku PSAXS Nano",
        "resolution": 100.0
      },
      "name": "Yale University",
      "city": "New Haven",
      "country": "United States",
      "beamline_name": "Rigaku MicroMax-007HF",
      "beam_geometry": null,
      "type_of_source": "X-ray in house",
      "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": "Receptor protein-tyrosine kinase (duplication mutant)",
          "short_name": "KDD",
          "sequence": "HHHHHHSSGVDLGTENLYFQSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLLVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG",
          "organism": "Homo sapiens",
          "uniprot_code": "Q504U8",
          "uniprot_range_first": 651,
          "uniprot_range_last": 993,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV\nVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA\nVLSNYDANKTGLKELPMRNLQGQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRG\nKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKY\nSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEF\nKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFL\nLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISG\nNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVS\nCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHY\nIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS\nIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR\nILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYV\nMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGM\nNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALES\nILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYM\nIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEE\nDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSF\nLQRYSSDPTGALTEDSIDDTFLPVPGEWLVWKQSCSSTSSTHSAAASLQCPSQVLPPASP\nEGETVADLQTQ",
          "mw": 79.594,
          "total_mw": 79.594,
          "number_molecules": 1,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "EGFR kinase domain duplication mutant. The purified construct consists of amino acids 643-976 appended to amino acids 651-993 using mature protein numbering (UniProt Q504U8 numbering: 651-993 followed by a duplicated 643-977 region). The protein construct used for SAXS contains an additional N-terminal non-native 22 amino acid extension and polyhistidine tag (HHHHHHSSGVDLGTENLYFQSM)."
        }
      ],
      "buffer": {
        "name": "20 mM HEPES, 250 mM NaCl, 250 mM KCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 8.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "EGFR kinase domain duplication mutant (KDD) at 2.6 mg/ml",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "New Haven, CT, USA",
            "full_name": "Yale University",
            "webpage": "https://www.yale.edu/"
          }
        ],
        "contributor_name": "Zaritza",
        "contributor_surname": "Petrova",
        "orcid": "https://orcid.org/0000-0002-4877-4676"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2022-03-22",
    "storage_temperature": 4.0,
    "cell_temperature": 4.0,
    "exposure_time": 7200.0,
    "number_of_frames": 3,
    "wavelength": 0.1542,
    "sample_detector_distance": 0.491,
    "concentration_min": null,
    "concentration_max": 2.6,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.07,
    "s_max": 5.008,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [],
  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "5.0",
  "i0_calibration_standard": null,
  "description": null,
  "experiment_description": "SAXS data from solutions of EGFR kinase domain duplication mutant in 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH 8 were collected on the Rigaku MicroMax-007HF instrument (Yale University, New Haven, United States) using a Rigaku PSAXS Nano detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.60 mg/ml was measured at 4°C. Three successive 7200 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.",
  "tags": [],
  "intensity_unit": "arbitrary",
  "experimental_mw": 86.0,
  "experimental_mw_error": null,
  "guinier_i0_mw": 86.0,
  "guinier_i0_mw_error": null,
  "porod_mw": 101.0,
  "porod_mw_error": null,
  "pddf_i0": 0.2736,
  "pddf_i0_error": null,
  "guinier_i0": 0.278134,
  "guinier_i0_error": null,
  "pddf_rg": 4.87,
  "pddf_rg_error": null,
  "guinier_rg": 4.867,
  "guinier_rg_error": 0.663,
  "pddf_dmax": 16.4,
  "pddf_dmax_error": null,
  "porod_volume": 163.0,
  "porod_volume_error": null,
  "estimated_volume": null,
  "estimated_volume_error": null,
  "guinier_point_first": 2,
  "guinier_point_last": 25,
  "pddf_point_first": null,
  "pddf_point_last": null,
  "i0_calibration_standard_data": null,
  "intensities_log_log_plot": "SASDXV4_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2025-11-02T21:11:43.418457+01:00",
  "bragg_peak": []
}
查看完整 manifest.json 原文
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  "code": "SASDXV4",
  "status": "success",
  "started_at": "2026-08-11T14:32:37.719435+00:00",
  "finished_at": "2026-08-11T14:32:44.789741+00:00",
  "source_last_modified": "2025-11-02T21:11:43.418457+01:00",
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