SASDB79

Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex

数据类型:SASBDB 实验数据 状态:Published 曲线类型:Single concentration 最后更新:2019-12-06T13:07:15.624532+01:00

The two-phase bead model of the protein-DNA complex was generated using MONSA refinement from SAXS data measured from the complex (top data-model fit) in parallel with data measured from the isolated telomeric DNA duplex (bottom data-model fit; refer to SASBDB entry SASDB89).

1. 样品、组分与实验条件 Sample & Experiment

样品 1 · Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex

浓度— – 2.9 缓冲液 / pH20 mM Tris-HCl, 50 mM LiCl / 7.5
Experimental temperature4.0 设备 / 束线CEITEC / Rigaku BioSAXS-1000
波长0.154 nm曝光3600.0 s × 6

分子组分

组分类型 / OrganismUniProt 与Construct寡聚状态Molecular weight
Basic domain of telomeric repeat-binding factor 2
查看序列
GPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
proteinHomo sapiensQ1555442–86monomer分子数 14.587 kDa
telomere DNA duplex
查看序列
GTTAGGGTTAGGGTTAGCAATCCCAATCCCAATC
DNA—–—monomer分子数 110.522 kDa

实验曲线

曲线点数 / 列q range误差质量负强度点来源文件
1188[3]0.0310836–0.300399 1/A含误差列缺失 012sasbdb/entries/79/sasdb79/source/SASDB79.dat

2. SASBDB 报告的指标 Reported Results

指标方法数值误差单位
dmaxP(r)5.95Å
i0Guinier0.220.0018
i0P(r)0.22780.001668
mwExperimental15.1kDa
porod_volumePorod20.3ų
rgGuinier1.7110.058Å
rgP(r)1.7760.017Å

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-HCl, 50 mM LiCl缓冲液浓度
pH7.5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2016-05-03储存 / 测量温度4.0 / 4.0
曝光时间3600.0帧数6
波长0.154样品-探测器距离0.4791
光源X-ray in house探测器Pilatus 100K
机构 / 束线CEITEC / Rigaku BioSAXS-1000 · Brno, Czech Republic
q range0.311 – 3.004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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full_entry_zip:来源记录与 ZIP 内部目录(5 项)
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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:184 个字段值
字段路径原始值
codeSASDB79
statusPublished
type_of_curveSingle concentration
angular_unit1/A
project.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.titleBasic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.
project.publication.author_listNecasová I, Janoušková E, Klumpler T, Hofr C
project.publication.journalNucleic Acids Res
project.publication.doi10.1093/nar/gkx812
project.publication.pmid28981702
project.publication.published_date2017 Dec 1
project.statusreleased
project.submitted_date2017-01-06
project.released_date2017-09-18
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experiment.instrument.detector.resolution172.0
experiment.instrument.nameCEITEC
experiment.instrument.cityBrno
experiment.instrument.countryCzech Republic
experiment.instrument.beamline_nameRigaku BioSAXS-1000
experiment.instrument.beam_geometry
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
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experiment.instrument.beam_profile_ahnull
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experiment.sample.molecule[0].long_nameBasic domain of telomeric repeat-binding factor 2
experiment.sample.molecule[0].short_nameTRF2
experiment.sample.molecule[0].sequenceGPPGSMAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAG
experiment.sample.molecule[0].organismHomo sapiens
experiment.sample.molecule[0].uniprot_codeQ15554
experiment.sample.molecule[0].uniprot_range_first42
experiment.sample.molecule[0].uniprot_range_last86
experiment.sample.molecule[0].oligomerizationmonomer
experiment.sample.molecule[0].molecular_typeprotein
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experiment.sample.molecule[1].long_nametelomere DNA duplex
experiment.sample.molecule[1].short_namenull
experiment.sample.molecule[1].sequenceGTTAGGGTTAGGGTTAG CAATCCCAATCCCAATC
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experiment.sample.contrastnull
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experiment.contributor[0].affiliation[0].webpagehttps://www.ceitec.eu/
experiment.contributor[0].contributor_nameTomas
experiment.contributor[0].contributor_surnameKlumpler
experiment.contributor[0].orcidnull
experiment.concentration_methodnull
experiment.concentration_unitnull
experiment.date2016-05-03
experiment.storage_temperature4.0
experiment.cell_temperature4.0
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experiment.wavelength0.154
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experiment.sample_volumenull
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experiment.total_exposure_timenull
experiment.seccolumnnull
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estimated_volume_methodnull
pddf_softwareATSAS GNOM
pddf_software_versionGNOM Version 5.0
i0_calibration_standardnull
descriptionThe two-phase bead model of the protein-DNA complex was generated using MONSA refinement from SAXS data measured from the complex (top data-model fit) in parallel with data measured from the isolated telomeric DNA duplex (bottom data-model fit; refer to SASBDB entry SASDB89).
experiment_descriptionSAXS data from solutions of the basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with a telomeric DNA duplex in 20 mM Tris-HCl, 50 mM LiCl, pH 7.5 were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4πsinθ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 2.9 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.
tags[]
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pddf_point_firstnull
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i0_calibration_standard_datanull
intensities_log_log_plotSASDB79_datloglog_img.png
symmetrynull
last_modified2019-12-06T13:07:15.624532+01:00
bragg_peak[]
manifest.json:36 个字段值
字段路径原始值
codeSASDB79
statussuccess
started_at2026-08-11T16:07:29.352291+00:00
finished_at2026-08-11T16:07:40.561932+00:00
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查看完整 summary.json 原文
{
  "code": "SASDB79",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.",
    "publication": {
      "title": "Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it.",
      "author_list": "Necasová I, Janoušková E, Klumpler T, Hofr C",
      "journal": "Nucleic Acids Res",
      "doi": "10.1093/nar/gkx812",
      "pmid": "28981702",
      "published_date": "2017 Dec 1"
    },
    "status": "released",
    "submitted_date": "2017-01-06",
    "released_date": "2017-09-18"
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          "long_name": "Basic domain of telomeric repeat-binding factor 2",
          "short_name": "TRF2",
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          "organism": "Homo sapiens",
          "uniprot_code": "Q15554",
          "uniprot_range_first": 42,
          "uniprot_range_last": 86,
          "oligomerization": "monomer",
          "molecular_type": "protein",
          "uniprot_sequence": "MAAGAGTAGPASGPGVVRDPAASQPRKRPGREGGEGARRSDTMAGGGGSSDGSGRAAGRR\nASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQ\nIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEM\nIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNI\nIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDK\nQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQ\nALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRLVLEEDSQSTEPSAGLN\nSSQEAASAPPSKPTVLNQPLPGEKNPKVPKGKWNSSNGVEEKETWVEEDELFQVQAAPDE\nDSTTNITKKQKWTVEESEWVKAGVQKYGEGNWAAISKNYPFVNRTAVMIKDRWRTMKRLG\nMN",
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          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        },
        {
          "long_name": "telomere DNA duplex",
          "short_name": null,
          "sequence": "GTTAGGGTTAGGGTTAG\r\nCAATCCCAATCCCAATC",
          "organism": null,
          "uniprot_code": null,
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          "oligomerization": "monomer",
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          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
      "buffer": {
        "name": "20 mM Tris-HCl, 50 mM LiCl",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.5,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with telomeric DNA duplex",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "CEITEC - Central European Institute of Technology, Masaryk University",
            "webpage": "https://www.ceitec.eu/"
          }
        ],
        "contributor_name": "Tomas",
        "contributor_surname": "Klumpler",
        "orcid": null
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2016-05-03",
    "storage_temperature": 4.0,
    "cell_temperature": 4.0,
    "exposure_time": 3600.0,
    "number_of_frames": 6,
    "wavelength": 0.154,
    "sample_detector_distance": 0.4791,
    "concentration_min": null,
    "concentration_max": 2.9,
    "sample_volume": null,
    "flow_rate": null,
    "s_min": 0.311,
    "s_max": 3.004,
    "total_exposure_time": null,
    "seccolumn": null
  },
  "fits": [
    {
      "models": [
        {
          "model_plot": "https://www.sasbdb.org/media/pdb_file/images/SASDB79_fit1_model1_img.png",
          "software": "MONSA",
          "pdb_link": [],
          "model_title": null,
          "type_of_model": "dummy",
          "software_version": "",
          "model_data": "https://www.sasbdb.org/media/pdb_file/SASDB79_fit1_model1.pdb",
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          "log": "https://www.sasbdb.org/media/log_files/yCB0Wg_ABxuwwo_wY51QbU.log",
          "symmetry": "",
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          "user": 195
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      "fit_unit": "1/A",
      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDB79_fit1_fit_img.png",
      "software": "MONSA",
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      "p_value": 0.955,
      "fit_residual_plot": "SASDB79_fit1_fitresiduals_img.png",
      "fit_data": "https://www.sasbdb.org/media/fitting_files/SASDB79_fit1.fit",
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      "fit_plot": "https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDB79_fit2_fit_img.png",
      "software": "MONSA",
      "chi_square_value": 1.22,
      "p_value": 0.002,
      "fit_residual_plot": "SASDB79_fit2_fitresiduals_img.png",
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  "description": "The two-phase bead model of the protein-DNA complex was generated using MONSA refinement from SAXS data measured from the complex (top data-model fit) in parallel with data measured from the isolated telomeric DNA duplex (bottom data-model fit; refer to SASBDB entry SASDB89).",
  "experiment_description": "SAXS data from solutions of the basic domain of human telomeric repeat-binding factor 2 (TRF2) in complex with a telomeric DNA duplex in 20 mM Tris-HCl, 50 mM LiCl, pH 7.5 were collected using a Rigaku BioSAXS-1000 instrument at CEITEC (Brno, Czech Republic) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m (I(s) vs s, where = 4πsinθ/λ; 2θ is the scattering angle and λ = 0.154 nm). Six successive 3600 second frames were collected at a sample temperature of 4°C using a solute concentration of 2.9 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged and the corresponding scattering from the solvent-blank was subtracted to produced the scattering profile displayed in this entry.",
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  "intensities_log_log_plot": "SASDB79_datloglog_img.png",
  "symmetry": null,
  "last_modified": "2019-12-06T13:07:15.624532+01:00",
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}
查看完整 manifest.json 原文
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