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- PDB-4ibu: Human p53 core domain with hot spot mutation R273C and second-sit... -

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Basic information

Entry
Database: PDB / ID: 4ibu
TitleHuman p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R in sequence-specific complex with DNA
Components
  • Cellular tumor antigen p53
  • DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')
KeywordsDNA BINDING PROTEIN/DNA / METAL-BINDING / LOOP-SHEET-HELIX MOTIF / TRANSCRIPTION / ACTIVATOR / ANTI-ONCOGENE / APOPTOSIS / CELL CYCLE / DISEASE MUTATION / RESCUE MUTATION / TUMOR SUPPRESSOR / DNA BINDING PROTEIN-DNA complex
Function / homology
Function and homology information


negative regulation of helicase activity / signal transduction by p53 class mediator / Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / regulation of cell cycle G2/M phase transition / negative regulation of G1 to G0 transition / Transcriptional activation of cell cycle inhibitor p21 / negative regulation of pentose-phosphate shunt / Activation of NOXA and translocation to mitochondria / ATP-dependent DNA/DNA annealing activity ...negative regulation of helicase activity / signal transduction by p53 class mediator / Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / regulation of cell cycle G2/M phase transition / negative regulation of G1 to G0 transition / Transcriptional activation of cell cycle inhibitor p21 / negative regulation of pentose-phosphate shunt / Activation of NOXA and translocation to mitochondria / ATP-dependent DNA/DNA annealing activity / oligodendrocyte apoptotic process / positive regulation of thymocyte apoptotic process / oxidative stress-induced premature senescence / bone marrow development / cellular response to actinomycin D / circadian behavior / positive regulation of programmed necrotic cell death / RUNX3 regulates CDKN1A transcription / TP53 Regulates Transcription of Death Receptors and Ligands / Activation of PUMA and translocation to mitochondria / TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / mRNA transcription / Regulation of TP53 Activity through Association with Co-factors / Urea cycle / ER overload response / hematopoietic stem cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / TP53 Regulates Transcription of Caspase Activators and Caspases / intrinsic apoptotic signaling pathway by p53 class mediator / entrainment of circadian clock by photoperiod / Zygotic genome activation (ZGA) / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / PI5P Regulates TP53 Acetylation / positive regulation of release of cytochrome c from mitochondria / Association of TriC/CCT with target proteins during biosynthesis / hematopoietic progenitor cell differentiation / negative regulation of telomere maintenance via telomerase / SUMOylation of transcription factors / TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / replicative senescence / Transcriptional Regulation by VENTX / TFIID-class transcription factor complex binding / viral process / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / determination of adult lifespan / Pyroptosis / positive regulation of RNA polymerase II transcription preinitiation complex assembly / general transcription initiation factor binding / negative regulation of fibroblast proliferation / positive regulation of execution phase of apoptosis / type II interferon-mediated signaling pathway / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / cellular response to glucose starvation / core promoter sequence-specific DNA binding / cis-regulatory region sequence-specific DNA binding / Regulation of TP53 Activity through Acetylation / intrinsic apoptotic signaling pathway / mitotic G1 DNA damage checkpoint signaling / positive regulation of intrinsic apoptotic signaling pathway / 14-3-3 protein binding / response to gamma radiation / MDM2/MDM4 family protein binding / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / protein phosphatase 2A binding / DNA damage response, signal transduction by p53 class mediator / transcription initiation-coupled chromatin remodeling / molecular function activator activity / Regulation of PTEN gene transcription / tumor necrosis factor-mediated signaling pathway / cellular response to ionizing radiation / cellular response to xenobiotic stimulus / TP53 Regulates Metabolic Genes / TP53 Regulates Transcription of DNA Repair Genes / cellular response to gamma radiation / Regulation of NF-kappa B signaling / mRNA 3'-UTR binding / protein tetramerization / molecular condensate scaffold activity / promoter-specific chromatin binding / Stabilization of p53 / negative regulation of cell growth / nucleotide-excision repair / G2/M Checkpoints / receptor tyrosine kinase binding / Autodegradation of the E3 ubiquitin ligase COP1 / PML body / cellular senescence / PKR-mediated signaling / positive regulation of miRNA transcription / Oncogene Induced Senescence / DNA-binding transcription repressor activity, RNA polymerase II-specific / Regulation of TP53 Activity through Methylation / G2/M DNA damage checkpoint / DNA Damage/Telomere Stress Induced Senescence / Pre-NOTCH Transcription and Translation / intracellular protein localization / transcription coactivator binding / positive regulation of reactive oxygen species metabolic process / histone deacetylase binding
Similarity search - Function
Immunoglobulin-like - #720 / Cellular tumor antigen p53, transactivation domain 2 / Transactivation domain 2 / p53 transactivation domain / P53 transactivation motif / : / p53 family signature. / p53, tetramerisation domain / P53 tetramerisation motif / p53, DNA-binding domain ...Immunoglobulin-like - #720 / Cellular tumor antigen p53, transactivation domain 2 / Transactivation domain 2 / p53 transactivation domain / P53 transactivation motif / : / p53 family signature. / p53, tetramerisation domain / P53 tetramerisation motif / p53, DNA-binding domain / P53 DNA-binding domain / p53 tumour suppressor family / p53-like tetramerisation domain superfamily / p53/RUNT-type transcription factor, DNA-binding domain superfamily / p53-like transcription factor, DNA-binding / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / DNA / DNA (> 10) / Cellular tumor antigen p53
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.7 Å
AuthorsEldar, A. / Rozenberg, H. / Diskin-Posner, Y. / Shakked, Z.
CitationJournal: Nucleic Acids Res. / Year: 2013
Title: Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions.
Authors: Eldar, A. / Rozenberg, H. / Diskin-Posner, Y. / Rohs, R. / Shakked, Z.
History
DepositionDec 9, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 14, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 28, 2013Group: Derived calculations
Revision 1.2Oct 23, 2013Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software
Revision 1.4Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cellular tumor antigen p53
B: Cellular tumor antigen p53
C: Cellular tumor antigen p53
D: Cellular tumor antigen p53
E: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')
F: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')
G: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')
H: DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)106,06130
Polymers104,6888
Non-polymers1,37322
Water17,276959
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.537, 58.158, 77.968
Angle α, β, γ (deg.)82.960, 87.780, 73.570
Int Tables number1
Space group name H-MP1

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Components

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Protein / DNA chain , 2 types, 8 molecules ABCDEFGH

#1: Protein
Cellular tumor antigen p53 / Antigen NY-CO-13 / Phosphoprotein p53 / Tumor suppressor p53


Mass: 22507.621 Da / Num. of mol.: 4 / Fragment: DNA binding domain / Mutation: R273C, T284R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: P53, TP53 / Plasmid: pET-27-b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P04637
#2: DNA chain
DNA (5'-D(*CP*GP*GP*GP*CP*AP*TP*GP*CP*CP*CP*G)-3')


Mass: 3664.380 Da / Num. of mol.: 4 / Source method: obtained synthetically

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Non-polymers , 4 types, 981 molecules

#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 959 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.25 Å3/Da / Density % sol: 45.3 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.1
Details: 1:2 PROTEIN/DNA RATIO, 14% PEG 3350, 0.14M Li-Acetate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 25, 2008 / Details: TOROIDAL MIRROR
RadiationMonochromator: DIAMOND (111), GE(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 1.69→40 Å / Num. obs: 96978 / % possible obs: 94.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rmerge(I) obs: 0.047 / Χ2: 1.087 / Net I/σ(I): 15
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
1.69-1.723.70.35532800.842164.4
1.72-1.753.70.29538060.842174.8
1.75-1.783.60.25447430.91192.2
1.78-1.823.90.2250010.908196.7
1.82-1.8640.19349260.95196.6
1.86-1.940.16349470.974196.7
1.9-1.953.90.13249971.028197
1.95-23.90.10849481.088197.1
2-2.063.90.09449721.114197.2
2.06-2.133.90.08249791.218197.5
2.13-2.213.90.0750231.251197.5
2.21-2.293.90.0649931.224197.7
2.29-2.43.90.05650291.158198
2.4-2.523.90.0550181.193198.1
2.52-2.683.90.04550481.084198.3
2.68-2.893.90.0450471.131198.6
2.89-3.183.90.03550301.141198.7
3.18-3.643.90.0351021.126198.9
3.64-4.593.90.03350611.169199.1
4.59-403.80.04250281.188198.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
PHENIX1.8.1_1168refinement
PDB_EXTRACT3.11data extraction
DNAdata collection
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2AC0, chain A

2ac0


Resolution: 1.7→30.118 Å / Occupancy max: 1 / Occupancy min: 0.2 / FOM work R set: 0.8729 / SU ML: 0.17 / Cross valid method: THROUGHOUT / σ(F): 1.97 / σ(I): 0 / Phase error: 20.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1971 4783 5 %RANDOM
Rwork0.1628 ---
obs0.1645 95621 95.33 %-
all-95621 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 104.86 Å2 / Biso mean: 26.7876 Å2 / Biso min: 5.75 Å2
Refinement stepCycle: LAST / Resolution: 1.7→30.118 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6119 934 76 959 8088
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0067751
X-RAY DIFFRACTIONf_angle_d1.16610717
X-RAY DIFFRACTIONf_chiral_restr0.0791157
X-RAY DIFFRACTIONf_plane_restr0.0061263
X-RAY DIFFRACTIONf_dihedral_angle_d17.4423040
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.7-1.71930.28111170.22052076219366
1.7193-1.73960.22971220.20572305242773
1.7396-1.76080.23331400.20142694283484
1.7608-1.78310.26841590.20352992315196
1.7831-1.80650.23911890.18733081327097
1.8065-1.83130.25241610.18883079324097
1.8313-1.85740.20471550.18273062321797
1.8574-1.88510.23711670.18273062322997
1.8851-1.91460.20391430.18333048319197
1.9146-1.9460.26021770.18633171334897
1.946-1.97950.21081780.1812988316697
1.9795-2.01550.24441290.17913178330797
2.0155-2.05430.22231540.17053071322597
2.0543-2.09620.21131690.17053117328697
2.0962-2.14180.23041520.17073070322298
2.1418-2.19160.19511700.16783099326998
2.1916-2.24640.20131860.16023083326998
2.2464-2.30710.20831530.16523109326298
2.3071-2.37490.20111660.16873115328198
2.3749-2.45160.21811530.17233131328498
2.4516-2.53910.21321640.17133131329598
2.5391-2.64070.23251630.17353120328398
2.6407-2.76080.20821650.17593126329198
2.7608-2.90630.22711520.1783153330599
2.9063-3.08820.20271570.17253137329499
3.0882-3.32640.19441950.16363095329099
3.3264-3.66060.16861600.14283166332699
3.6606-4.18910.16591590.14233152331199
4.1891-5.27320.14551700.12483140331099
5.2732-30.12280.15741580.15083087324597
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.59783.4058-2.87857.2639-5.14553.87260.3201-0.37520.08940.7359-0.1453-0.2475-0.50040.519-0.11950.2829-0.007-0.02790.156-0.01930.281426.561828.84324.97
22.9935-0.52950.3252.6234-0.08921.40830.0208-0.01960.0025-0.1288-0.05670.2163-0.0329-0.10040.03890.10.0172-0.02360.07-0.01030.13066.294824.58153.2684
32.087-0.09690.02261.8604-0.72732.2614-0.0106-0.0846-0.1303-0.10250.0315-0.09890.1483-0.0657-0.00240.07860.0104-0.00540.0577-0.00580.148419.263115.55283.9718
44.4738-2.4257-1.44585.2034-0.1482.430.02510.6684-0.4483-0.62110.0811-0.02140.2408-0.2832-0.08740.2045-0.037-0.00570.1728-0.07360.157317.549312.3544-6.1708
50.67810.0401-1.70081.22380.20054.3752-0.3413-0.4785-0.42040.0783-0.0695-0.650.13731.09230.09720.13690.0688-0.0150.27490.07180.359628.761410.38986.3805
62.1178-0.1193-0.99145.8962-2.48573.55950.15790.4549-0.0153-0.8666-0.14240.26610.0944-0.2018-0.0660.23210.0225-0.03560.1237-0.03330.153520.151922.3783-9.0709
72.51070.5613-0.14474.021-2.4044.01950.0193-0.2729-0.2680.06570.07190.11930.3201-0.2859-0.07670.05160.0044-0.00890.09420.01790.138611.397114.32738.7679
84.74150.6025-2.83062.2841-0.92922.64740.1023-0.01890.3288-0.0112-0.0391-0.1808-0.13250.1125-0.07120.08570.0081-0.02720.06350.00960.12720.627522.9464.3207
94.0648-0.451.01275.80431.06095.7435-0.0954-0.90580.18730.84970.11810.5639-0.36360.17060.07480.2210.01080.06640.2782-0.04540.20580.336430.277514.7224
101.2945-0.1369-1.02761.7227-0.80581.67590.0728-0.0018-0.3920.1962-0.198-0.00330.4784-0.55060.05580.344-0.1839-0.01430.3447-0.00630.2251-9.4598-21.892826.5914
119.08133.2723-0.15766.1230.91626.02620.1851-0.07051.59631.26990.05461.2262-1.0198-0.8411-0.26250.48390.17950.0920.5323-0.03010.395-8.56140.794136.6444
121.21010.29060.3382.579-1.12892.90470.0071-0.24990.02260.2033-0.07650.10780.2412-0.40730.01360.1884-0.04830.01390.2233-0.03880.1012-5.4752-11.936130.3192
138.82586.52163.1198.45741.28154.2923-0.13290.324-0.0805-0.2506-0.0696-0.3863-0.01850.38960.16330.18930.00520.04790.15230.02840.13966.3387-6.622917.083
144.74280.6110.89712.11240.57793.23620.01470.2547-0.0942-0.2835-0.2705-0.71750.50320.74960.00080.2850.07440.04320.20860.0250.17019.3965-13.613726.3165
151.70270.05870.76791.9801-0.07852.3073-0.0045-0.25710.02510.1892-0.0231-0.0430.204-0.22220.01320.1918-0.0368-0.00450.1777-0.02480.0809-1.9747-12.759329.1766
162.15591.216-2.86015.3165-2.06233.8586-0.11670.12380.46150.21260.3730.9627-0.0328-1.0353-0.20140.25220.07030.06350.44510.01230.335-15.84484.062226.5948
171.42470.6743-1.31312.0368-0.46556.72350.01080.4282-0.0478-0.09730.22990.30990.3995-0.4577-0.18730.1083-0.0363-0.01740.2975-0.0380.196-34.7985-16.6001-3.2406
181.0462-0.48760.03062.9773-0.45661.17910.23110.05950.7390.0435-0.10930.0152-0.2234-0.0911-0.06880.1380.03310.01250.1010.0030.2154-22.77460.8784-3.2141
193.95180.1311-0.95172.7817-0.16461.9434-0.2352-0.42240.1480.39120.20610.316-0.0507-0.2897-0.10160.12330.04550.04220.17920.00280.0786-30.1087-11.16497.7003
201.62870.3837-0.391.82970.25822.1997-0.04850.3623-0.1029-0.29270.0662-0.0090.19050.06650.01280.09770.0195-0.01070.1365-0.03150.0842-20.3363-15.6694-12.0013
213.0220.6861-0.9372.3792-1.04984.2108-0.0185-0.0534-0.250.0447-0.1578-0.63390.04450.62880.05970.09250.0104-0.00330.1430.00140.2074-9.124-14.0908-1.4483
221.02750.54970.15130.44130.65152.47120.14040.1577-0.4827-0.276-0.2094-0.0610.78040.022-0.00140.26880.0719-0.04970.0802-0.09870.2184-17.6858-24.6389-5.929
233.8266-1.9439-2.23573.8472.25823.09970.0538-0.39930.08580.37520.0515-0.0335-0.6662-0.2837-0.14060.24590.09910.01240.1701-0.01470.0551-25.5858-12.31779.7129
244.14160.4485-1.71022.7328-0.09025.03590.03710.33950.0923-0.20280.0197-0.2252-0.26270.268-0.04190.07510.01270.00370.0761-0.00950.109-15.5192-7.3643-9.4373
253.80320.97-1.30990.8558-0.86563.2085-0.04440.1315-0.1364-0.0230.00230.08550.1456-0.29370.04220.07520.0023-0.00480.0786-0.04090.0937-27.9057-15.2253-2.6451
262.8346-0.2698-0.97482.18150.31870.35350.45781.36040.9575-0.5665-0.02780.2706-0.2643-0.5118-0.18730.28980.13120.03570.31530.20480.3703-21.41116.1123-12.1621
274.1133-0.309-1.50251.51791.1862.5650.44850.06470.5929-0.2195-0.1428-0.1835-0.5870.2987-0.25330.3647-0.04850.08970.26780.02140.210413.95671.3575-31.7568
283.2335-0.0908-0.45491.77870.242.75760.1915-0.13730.073-0.0073-0.138-0.0498-0.04120.1799-0.04440.1337-0.0339-0.00680.2487-0.00220.075813.121-9.7542-28.3986
292.6431-1.7512-0.16942.50930.26740.95360.53520.03460.7239-0.2633-0.2158-0.1226-0.71040.3854-0.24890.4273-0.05370.14130.2148-0.0140.24358.64436.5089-28.186
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1CHAIN A AND (RESID 96:109 )A0
2X-RAY DIFFRACTION2CHAIN A AND (RESID 110:140 )A0
3X-RAY DIFFRACTION3CHAIN A AND (RESID 141:194 )A0
4X-RAY DIFFRACTION4CHAIN A AND (RESID 195:203 )A0
5X-RAY DIFFRACTION5CHAIN A AND (RESID 204:213 )A0
6X-RAY DIFFRACTION6CHAIN A AND (RESID 214:229 )A0
7X-RAY DIFFRACTION7CHAIN A AND (RESID 230:250 )A0
8X-RAY DIFFRACTION8CHAIN A AND (RESID 251:277 )A0
9X-RAY DIFFRACTION9CHAIN A AND (RESID 278:292 )A0
10X-RAY DIFFRACTION10CHAIN B AND (RESID 94:112 )B0
11X-RAY DIFFRACTION11CHAIN B AND (RESID 113:123 )B0
12X-RAY DIFFRACTION12CHAIN B AND (RESID 124:168 )B0
13X-RAY DIFFRACTION13CHAIN B AND (RESID 169:181 )B0
14X-RAY DIFFRACTION14CHAIN B AND (RESID 182:213 )B0
15X-RAY DIFFRACTION15CHAIN B AND (RESID 214:277 )B0
16X-RAY DIFFRACTION16CHAIN B AND (RESID 278:290 )B0
17X-RAY DIFFRACTION17CHAIN C AND (RESID 96:109 )C0
18X-RAY DIFFRACTION18CHAIN C AND (RESID 110:140 )C0
19X-RAY DIFFRACTION19CHAIN C AND (RESID 141:155 )C0
20X-RAY DIFFRACTION20CHAIN C AND (RESID 156:176 )C0
21X-RAY DIFFRACTION21CHAIN C AND (RESID 177:203 )C0
22X-RAY DIFFRACTION22CHAIN C AND (RESID 204:213 )C0
23X-RAY DIFFRACTION23CHAIN C AND (RESID 214:229 )C0
24X-RAY DIFFRACTION24CHAIN C AND (RESID 230:250 )C0
25X-RAY DIFFRACTION25CHAIN C AND (RESID 251:274 )C0
26X-RAY DIFFRACTION26CHAIN C AND (RESID 275:288 )C0
27X-RAY DIFFRACTION27CHAIN D AND (RESID 95:140 )D0
28X-RAY DIFFRACTION28CHAIN D AND (RESID 141:263 )D0
29X-RAY DIFFRACTION29CHAIN D AND (RESID 264:290 )D0

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