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- PDB-3i3j: Crystal Structure of the Bromodomain of Human EP300 -

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Basic information

Entry
Database: PDB / ID: 3i3j
TitleCrystal Structure of the Bromodomain of Human EP300
ComponentsHistone acetyltransferase p300
KeywordsTRANSFERASE / Structural Genomics Bromodomain / P300 / Consortium / SGC / Structural Genomics Consortium / Bromodomain / Cell cycle / Citrullination / Disease mutation / Host-virus interaction / Metal-binding / Methylation / Nucleus / Phosphoprotein / Transcription / Transcription regulation / Zinc-finger
Function / homology
Function and homology information


behavioral defense response / protein propionyltransferase activity / peptidyl-lysine propionylation / histone lactyltransferase activity / peptidyl-lysine crotonylation / peptidyl-lysine butyrylation / histone butyryltransferase activity / histone H3K122 acetyltransferase activity / swimming / peptide butyryltransferase activity ...behavioral defense response / protein propionyltransferase activity / peptidyl-lysine propionylation / histone lactyltransferase activity / peptidyl-lysine crotonylation / peptidyl-lysine butyrylation / histone butyryltransferase activity / histone H3K122 acetyltransferase activity / swimming / peptide butyryltransferase activity / histone H2B acetyltransferase activity / thigmotaxis / peptide 2-hydroxyisobutyryltransferase activity / histone crotonyltransferase activity / NOTCH2 intracellular domain regulates transcription / lysine N-acetyltransferase activity, acting on acetyl phosphate as donor / peptidyl-lysine acetylation / histone H3 acetyltransferase activity / histone H4 acetyltransferase activity / cellular response to L-leucine / internal peptidyl-lysine acetylation / NFE2L2 regulating ER-stress associated genes / peptide N-acetyltransferase activity / STAT3 nuclear events downstream of ALK signaling / acetylation-dependent protein binding / Activation of the TFAP2 (AP-2) family of transcription factors / NFE2L2 regulating inflammation associated genes / NGF-stimulated transcription / histone H3K27 acetyltransferase activity / histone H3K18 acetyltransferase activity / Polo-like kinase mediated events / N-terminal peptidyl-lysine acetylation / LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production / NFE2L2 regulates pentose phosphate pathway genes / regulation of androgen receptor signaling pathway / NFE2L2 regulating MDR associated enzymes / positive regulation by host of viral transcription / regulation of mitochondrion organization / face morphogenesis / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / NOTCH4 Intracellular Domain Regulates Transcription / Regulation of FOXO transcriptional activity by acetylation / Regulation of gene expression by Hypoxia-inducible Factor / Nuclear events mediated by NFE2L2 / Regulation of NFE2L2 gene expression / NOTCH3 Intracellular Domain Regulates Transcription / regulation of glycolytic process / TRAF6 mediated IRF7 activation / platelet formation / megakaryocyte development / peptide-lysine-N-acetyltransferase activity / nuclear androgen receptor binding / NFE2L2 regulating anti-oxidant/detoxification enzymes / regulation of tubulin deacetylation / macrophage derived foam cell differentiation / FOXO-mediated transcription of cell death genes / NFE2L2 regulating tumorigenic genes / internal protein amino acid acetylation / STAT family protein binding / acyltransferase activity / protein acetylation / fat cell differentiation / Formation of paraxial mesoderm / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of transforming growth factor beta receptor signaling pathway / PI5P Regulates TP53 Acetylation / Zygotic genome activation (ZGA) / acetyltransferase activity / stimulatory C-type lectin receptor signaling pathway / cellular response to nutrient levels / RUNX3 regulates p14-ARF / NF-kappaB binding / histone acetyltransferase complex / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / canonical NF-kappaB signal transduction / Attenuation phase / negative regulation of protein-containing complex assembly / negative regulation of gluconeogenesis / pre-mRNA intronic binding / somitogenesis / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / regulation of cellular response to heat / skeletal muscle tissue development / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / histone acetyltransferase activity / histone acetyltransferase / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / transcription initiation-coupled chromatin remodeling / Regulation of TP53 Activity through Acetylation / positive regulation of TORC1 signaling / RORA activates gene expression / CD209 (DC-SIGN) signaling / negative regulation of autophagy / B cell differentiation / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / SUMOylation of transcription cofactors / regulation of signal transduction by p53 class mediator / regulation of autophagy / transcription coregulator binding
Similarity search - Function
Nuclear receptor coactivator, CREB-bp-like, interlocking / Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamily / Creb binding / Zinc finger, TAZ-type / TAZ domain superfamily / TAZ zinc finger / Zinc finger TAZ-type profile. / TAZ zinc finger, present in p300 and CBP / Coactivator CBP, KIX domain / CREB-binding protein/p300, atypical RING domain ...Nuclear receptor coactivator, CREB-bp-like, interlocking / Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamily / Creb binding / Zinc finger, TAZ-type / TAZ domain superfamily / TAZ zinc finger / Zinc finger TAZ-type profile. / TAZ zinc finger, present in p300 and CBP / Coactivator CBP, KIX domain / CREB-binding protein/p300, atypical RING domain / CBP/p300-type histone acetyltransferase domain / CBP/p300, atypical RING domain superfamily / KIX domain / CREB-binding protein/p300, atypical RING domain / KIX domain profile. / CBP/p300-type histone acetyltransferase (HAT) domain profile. / Histone acetyltransferase Rtt109/CBP / Histone acetylation protein / Histone acetylation protein / Coactivator CBP, KIX domain superfamily / Zinc finger ZZ-type signature. / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Nuclear receptor coactivator, interlocking / Bromodomain-like / Histone Acetyltransferase; Chain A / Bromodomain, conserved site / Bromodomain signature. / Bromodomain / Bromodomain profile. / bromo domain / Bromodomain / Bromodomain-like superfamily / Zinc finger, RING/FYVE/PHD-type / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Histone acetyltransferase p300
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.33 Å
AuthorsFilippakopoulos, P. / Picaud, S. / Phillips, C. / Pike, A.C.W. / Muniz, J. / Roos, A. / Chaikuad, A. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. ...Filippakopoulos, P. / Picaud, S. / Phillips, C. / Pike, A.C.W. / Muniz, J. / Roos, A. / Chaikuad, A. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Weigelt, J. / Bountra, C. / Knapp, S. / Structural Genomics Consortium (SGC)
CitationJournal: Cell(Cambridge,Mass.) / Year: 2012
Title: Histone recognition and large-scale structural analysis of the human bromodomain family.
Authors: Filippakopoulos, P. / Picaud, S. / Mangos, M. / Keates, T. / Lambert, J.P. / Barsyte-Lovejoy, D. / Felletar, I. / Volkmer, R. / Muller, S. / Pawson, T. / Gingras, A.C. / Arrowsmith, C.H. / Knapp, S.
History
DepositionJun 30, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jul 28, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 14, 2012Group: Other
Revision 1.3Apr 11, 2012Group: Database references
Revision 1.4May 8, 2013Group: Other
Revision 1.5Nov 1, 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 / struct_ncs_dom_lim / 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 / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_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: Histone acetyltransferase p300
B: Histone acetyltransferase p300
C: Histone acetyltransferase p300
D: Histone acetyltransferase p300
E: Histone acetyltransferase p300
F: Histone acetyltransferase p300
G: Histone acetyltransferase p300
H: Histone acetyltransferase p300
I: Histone acetyltransferase p300
J: Histone acetyltransferase p300
K: Histone acetyltransferase p300
L: Histone acetyltransferase p300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)176,33318
Polymers175,85712
Non-polymers4756
Water4,990277
1
A: Histone acetyltransferase p300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,7963
Polymers14,6551
Non-polymers1422
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Histone acetyltransferase p300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,8924
Polymers14,6551
Non-polymers2383
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
9
I: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
10
J: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
11
K: Histone acetyltransferase p300


Theoretical massNumber of molelcules
Total (without water)14,6551
Polymers14,6551
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
12
L: Histone acetyltransferase p300
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,7512
Polymers14,6551
Non-polymers961
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)64.899, 86.186, 149.897
Angle α, β, γ (deg.)90.000, 96.980, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L

NCS domain segments:

Component-ID: 1 / Ens-ID: 1

Dom-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1LYSLYSLEULEUCHAIN A AND (RESSEQ 1048:1160 )AA1047 - 116010 - 123
2ILEILEGLYGLYCHAIN B AND (RESSEQ 1048:1160 )BB1048 - 116111 - 124
3LYSLYSLEULEUCHAIN C AND (RESSEQ 1048:1160 )CC1047 - 116010 - 123
4ILEILELEULEUCHAIN D AND (RESSEQ 1048:1160 )DD1048 - 116011 - 123
5LYSLYSGLYGLYCHAIN E AND (RESSEQ 1048:1160 )EE1047 - 116110 - 124
6PHEPHESERSERCHAIN F AND (RESSEQ 1048:1160 )FF1049 - 115912 - 122
7ILEILELEULEUCHAIN G AND (RESSEQ 1048:1160 )GG1048 - 116011 - 123
8ILEILELEULEUCHAIN H AND (RESSEQ 1048:1160 )HH1048 - 116011 - 123
9LYSLYSGLYGLYCHAIN I AND (RESSEQ 1048:1160 )II1047 - 116110 - 124
10ILEILELEULEUCHAIN J AND (RESSEQ 1048:1160 )JJ1048 - 116011 - 123
11LYSLYSLEULEUCHAIN K AND (RESSEQ 1048:1160 )KK1047 - 116010 - 123
12ILEILELEULEUCHAIN L AND (RESSEQ 1048:1160 )LL1048 - 116011 - 123

NCS oper:
IDCodeMatrixVector
1given(-0.980081, 0.129679, 0.150415), (0.123979, 0.991185, -0.046713), (-0.155147, -0.027134, -0.987519)42.9604, 46.304199, 253.539001
2given(-0.764309, -0.530118, -0.36716), (-0.532586, 0.197922, 0.822909), (-0.36357, 0.824501, -0.433607)72.943901, -104.607002, 198.871994
3given(-0.780579, -0.609981, -0.136454), (-0.321541, 0.204653, 0.924515), (-0.536011, 0.765533, -0.355882)57.3008, -65.9375, 194.514008
4given(0.600789, 0.635302, 0.485226), (-0.562719, -0.095036, 0.821167), (0.567803, -0.766394, 0.3004)-89.964302, -71.3909, 104.362999
5given(-0.641772, 0.61612, -0.456645), (0.446166, -0.184338, -0.87576), (-0.62375, -0.765778, -0.156589)86.882599, 51.337601, 171.279999
6given(-0.345271, -0.14867, -0.926653), (0.047014, -0.988873, 0.141136), (-0.937325, 0.005165, 0.348418)141.188995, 16.1229, 131.367004
7given(0.457678, -0.105365, 0.882853), (-0.029458, -0.994205, -0.103383), (0.88863, 0.021309, -0.45813)-83.514099, 0.987995, 133.462006
8given(0.404766, 0.045177, 0.913304), (0.143185, -0.98959, -0.014508), (0.90314, 0.136643, -0.407021)-113.355003, -7.14379, 175.511993
9given(0.954963, 0.104089, -0.27787), (-0.089026, 0.993819, 0.066323), (0.283056, -0.038598, 0.958326)-5.15837, 2.35306, 39.327301
10given(-0.68918, 0.457658, -0.561765), (0.56164, -0.152442, -0.813217), (-0.457812, -0.875962, -0.151979)101.046997, 96.949997, 156.871994
11given(0.743222, -0.622544, 0.245071), (0.403693, 0.125176, -0.906291), (0.533529, 0.772509, 0.344351)-21.374001, 81.612701, 43.301399

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Components

#1: Protein
Histone acetyltransferase p300 / p300 HAT / E1A-associated protein p300


Mass: 14654.789 Da / Num. of mol.: 12 / Fragment: UNP RESIDUES 1040-1161
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EP300, P300 / Plasmid: pNIC28-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3 / References: UniProt: Q09472, histone acetyltransferase
#2: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#3: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 277 / 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: 2.37 Å3/Da / Density % sol: 48.02 % / Mosaicity: 0.37 °
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 30w/v PEG 3350, 0.2M ammonium_sulfate, 5.5pH Bis-Tris, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 27, 2009
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.33→37.58 Å / Num. all: 69928 / Num. obs: 69648 / % possible obs: 99.6 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.117 / Rsym value: 0.117 / Net I/σ(I): 10.3
Reflection shellResolution: 2.33→2.46 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 2 / Num. unique all: 10054 / Rsym value: 0.82 / % possible all: 99.2

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Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 43.87 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å32.3 Å
Translation2.5 Å32.3 Å

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Processing

Software
NameVersionClassificationNB
SCALA3.3.9data scaling
PHASER2.1.4phasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
CrystalCleardata collection
MOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3DWY, 2NXB, 2OO1, 2OSS, 2OUO, 2RFJ, 3DAI, 3D7C

3dwy

2nxb

2oo1

2oss

2ouo

2rfj

3dai

3d7c


Resolution: 2.33→32.302 Å / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.731 / SU ML: 2.1 / σ(F): 0.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.275 1842 2.86 %
Rwork0.229 --
all0.231 70225 -
obs0.231 64495 91.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 51.901 Å2 / ksol: 0.345 e/Å3
Displacement parametersBiso max: 182.53 Å2 / Biso mean: 58.678 Å2 / Biso min: 7.4 Å2
Baniso -1Baniso -2Baniso -3
1-9.412 Å2-0 Å212.514 Å2
2---11.194 Å2-0 Å2
3---1.782 Å2
Refinement stepCycle: LAST / Resolution: 2.33→32.302 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11074 0 26 277 11377
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00711442
X-RAY DIFFRACTIONf_angle_d0.99715603
X-RAY DIFFRACTIONf_chiral_restr0.0821671
X-RAY DIFFRACTIONf_plane_restr0.0042006
X-RAY DIFFRACTIONf_dihedral_angle_d16.6184187
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A905X-RAY DIFFRACTIONPOSITIONAL0.062
12B905X-RAY DIFFRACTIONPOSITIONAL0.062
13C920X-RAY DIFFRACTIONPOSITIONAL0.073
14D913X-RAY DIFFRACTIONPOSITIONAL0.073
15E919X-RAY DIFFRACTIONPOSITIONAL0.067
16F871X-RAY DIFFRACTIONPOSITIONAL0.062
17G916X-RAY DIFFRACTIONPOSITIONAL0.069
18H898X-RAY DIFFRACTIONPOSITIONAL0.067
19I911X-RAY DIFFRACTIONPOSITIONAL0.078
110J911X-RAY DIFFRACTIONPOSITIONAL0.065
111K898X-RAY DIFFRACTIONPOSITIONAL0.059
112L894X-RAY DIFFRACTIONPOSITIONAL0.066
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 13

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.33-2.3930.3751160.3093903401975
2.393-2.4640.2971230.2984273439682
2.464-2.5430.381270.34420454784
2.543-2.6340.381300.2744497462786
2.634-2.7390.3221370.2614631476889
2.739-2.8640.3231430.2574798494192
2.864-3.0150.281450.2474924506994
3.015-3.2040.2861480.2465026517496
3.204-3.4510.2871530.2335125527898
3.451-3.7970.2861510.215191534299
3.797-4.3460.2221560.1885245540199
4.346-5.4710.221540.18452605414100
5.471-32.3050.2121590.195360551999
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)
12.1348-1.709-0.19551.5378-0.80380.727-0.263-0.2499-0.0768-0.3393-0.4818-0.92290.30670.280.50010.53250.1720.49390.54570.27340.783837.51682.9616139.5481
22.1121-0.95170.13111.0263-0.3291.6056-0.35780.0564-0.09440.1681-0.0657-0.08630.01750.16370.25520.1564-0.01760.01130.17590.04190.168126.86567.4097145.4885
31.02390.37620.27610.3692-0.03520.2840.07790.0415-0.1052-0.0345-0.40360.1123-0.42090.51410.01080.0717-0.06720.02250.1413-0.05180.115913.624411.6177143.5344
4-1.56234.95630.23870.89670.46110.0558-0.05971.1030.4635-0.13220.66230.86820.17220.1173-0.36590.31040.0149-0.05060.52880.05010.52273.76799.8325129.574
5-0.065-0.09550.08290.9234-1.33462.3266-0.07790.3241-0.18320.02710.38370.08920.3372-0.671-0.14270.1031-0.1271-0.08590.36680.1240.040613.682413.2153127.9252
61.8149-0.526-0.42842.70053.54553.45460.512-0.0252-0.2547-0.39520.0646-0.3693-0.53510.0596-0.460.13090.02290.06420.0719-0.03650.203424.47532.7541136.8922
7-1.44230.19470.70172.0892.10291.0589-0.6163-0.0326-0.3677-0.174-0.5167-0.34060.09930.52710.31750.13320.75620.507-2.1216-0.9316-0.153132.28074.9107133.1474
81.9968-0.2526-0.95112.3073-0.81221.52210.15410.13010.4699-0.19640.0629-0.36810.189-0.074-0.11270.1394-0.01520.06940.06480.02930.130423.201616.3631133.9805
96.3854.4954-0.92942.2427-0.64180.75141.2121-0.31071.54521.2293-0.57621.0611-0.41550.2504-0.4290.17240.08690.159600.03140.323514.538422.2395141.1185
101.7786-0.97630.83721.59480.34172.6060.6696-0.27010.5308-0.1434-0.023-0.081-0.4139-0.2426-0.13550.5343-0.1629-0.01930.0885-0.08460.067929.96118.5415146.5241
115.70562.5262-0.77440.8931-1.06280.0120.3051.58810.19620.28760.1988-0.06080.1624-0.0773-0.29420.3024-0.062-0.13130.69960.30820.557537.797213.8727144.3474
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970.7125-0.0305-0.13191.8093-0.4453-3.94740.0649-0.23930.0297-0.4947-0.063-0.0431-0.18390.2225-0.13090.4355-0.16520.0160.4903-0.05220.324835.9578-18.2349150.9142
980.84651.0403-1.0830.1267-0.21880.37230.119-0.59150.113-0.118-0.1636-0.26720.05870.30780.06290.20450.08470.14690.46030.38340.469265.97612.269887.9564
995.0742-3.1428-3.3182.64963.10894.1040.5871-0.3295-0.5394-0.6613-0.17620.2639-0.74260.2057-0.36940.4382-0.09390.01480.28080.19440.425353.00016.510197.728
1000.2726-0.7302-1.021-0.978-0.02986.40920.49560.04840.0913-0.1345-0.1527-0.5046-0.419-0.1303-0.22550.3019-0.09770.11010.0945-0.01120.231845.39318.67995.5416
1011.3437-0.18551.9512.1388-0.61331.60210.04160.2698-0.2524-0.6873-0.35620.01480.14790.30960.16560.48180.09160.01780.3259-0.02190.238537.76313.664885.4836
1022.8733-0.9014-0.69781.62790.79930.81830.56820.195-0.4221-0.9874-0.5246-0.03730.0144-0.08670.00510.55830.03090.07940.1023-0.04090.198539.60139.895180.1547
1032.97812.5262-1.3018-0.7356-0.44120.6955-0.2003-0.0462-0.8651-0.1281-0.0175-0.147-0.25050.07970.17830.49120.10750.18610.28020.20840.399554.22020.696185.9952
1046.30520.2517-2.72618.5806-4.04347.8831-1.0539-0.0309-0.50351.086-0.23950.7210.91750.87040.91710.58280.09210.4480.29380.19330.52161.57771.768380.0202
1050.04380.8163-0.15820.5612-0.82842.1688-0.0486-0.01550.18790.051-0.2347-0.0214-0.56550.4353-0.07340.6496-0.01040.18510.27840.14940.293657.301611.001383.1135
1060.28970.35580.39961.14610.55550.71030.31650.10890.21510.1684-0.4190.14590.0575-0.1560.06710.65420.12490.03820.1697-0.03290.239142.441117.695387.9579
1077.31852.00511.05010.9952.05873.49280.1195-0.34510.942-0.4135-0.44250.1941-1.2175-0.02160.11060.6691-0.0883-0.01370.16160.02740.249250.481117.244394.0204
1080.18390.09270.24860.4672-0.78460.336-0.0583-0.1435-0.03080.2628-0.3322-0.2878-0.29950.14460.11180.5972-0.3081-0.16710.64870.3820.418266.402213.42891.9785
1093.5073-1.9544-1.38112.11950.76931.1793-0.01260.34850.35990.12630.1811-0.08490.03820.0951-0.1960.90370.30950.11521.09920.22221.0847-1.44741.7462113.85
1102.3662-0.75392.75811.0564-2.23344.4310.1817-0.7146-0.0497-0.70030.14560.09940.9394-0.8101-0.36370.2782-0.2049-0.11550.40840.11690.126111.2943-13.0142117.8659
1113.5204-0.3936-2.67690.69350.29873.1465-0.9826-0.3693-0.28560.30520.58970.0750.74940.47370.35050.27780.04370.06190.13720.010.105628.6684-7.1857128.334
112-0.0563-0.7262-0.52220.417-0.17932.7053-0.17880.29430.2342-0.36380.2592-0.3082-0.759-0.2034-0.03470.3309-0.02330.09820.2230.01370.276523.2338-2.4301121.4017
1135.7362-1.83281.66444.0081-1.63322.0034-0.4023-1.0325-0.260.2910.70220.2384-1.3701-1.1806-0.35120.44310.1616-0.05090.67010.09050.1947.3166-0.6886122.7831
1144.78395.033-0.93255.9511-0.5691-1.146-0.7633-0.38420.4123-0.8056-0.51970.0973-0.2777-1.10111.02410.44590.2473-0.08010.725-0.22160.35817.9042.864113.3297
1155.1817-2.14410.07361.00480.18181.17620.82260.29630.2288-0.3173-0.3863-0.1645-0.2201-0.3648-0.41690.37870.02120.05880.26170.02420.196719.8772-4.4218112.6424
1165.73744.6029-0.03913.7091-2.3601-1.385-0.2145-0.8255-0.7375-1.1383-0.3321-1.06620.1854-0.01140.49080.36180.08870.23620.23790.02490.252933.4798-11.3957113.6474
1175.3036-0.1456-0.96572.1827-1.10420.59271.133-0.56710.3043-0.4544-0.7730.03180.51160.278-0.37470.571-0.06490.09380.2788-0.03270.223.3207-15.3234111.706
1183.9028-0.95440.13-0.12031.25541.37010.23771.0421-0.0737-0.34870.0020.13880.39920.2902-0.20840.6549-0.0783-0.24060.63160.0770.549511.2514-10.996105.9037
119-0.40760.25310.56790.39770.44410.2152-0.0764-0.27910.0256-0.04980.00480.0904-0.0848-0.52740.07210.6591-0.0788-0.24721.05360.19120.72452.8489-5.8928105.3491
1201.8956-0.3711.44780.2268-0.65644.190.59230.021-0.3447-0.04270.29690.36290.0738-0.2594-0.82810.69750.12340.10930.82920.22051.233763.402827.7474118.7454
1211.49170.0255-0.1031-3.6097-1.07920.3371-0.0435-0.02560.7242-0.16130.1399-0.4206-0.4778-0.0633-0.18560.76570.01930.18630.35340.00060.626660.607739.4863114.5672
1222.9082-2.81866.03213.67870.52779.57560.2507-0.09870.411-1.7497-0.198-1.0163-0.326-0.5119-0.24680.9893-0.02740.42110.14290.0470.310555.103349.5243107.4005
1230.2291-1.08820.23750.2820.1382.58410.65210.16250.0532-0.4692-0.0767-0.0126-0.25940.0672-0.35581.04610.22980.19780.23250.03030.26248.454245.5038105.8231
1242.7367-0.75845.63295.6083-2.22045.0605-0.2215-0.7853-0.0286-1.55360.521-0.0255-2.0334-1.9838-0.31330.84840.56020.2520.4960.13530.088137.270641.2516100.8964
1252.12032.47991.50033.33682.06876.04-0.5071-0.3267-0.7259-1.81160.4513-0.6893-0.8061-0.58460.25010.98970.12120.29830.19580.08270.225644.413734.711100.607
1260.6013-1.8507-0.90231.5522.24281.61380.3552-0.20750.3151-0.03080.0787-0.2757-0.6456-0.2128-0.35020.47860.05170.20540.30310.1140.328852.530134.2844114.9783
1273.1264-1.939-0.30672.27340.9067-0.02760.2772-0.30820.1137-0.38540.0859-0.8804-0.21030.086-0.07910.37020.05820.38170.4170.2720.659457.887327.6418111.7444
1280.63910.995-0.17531.298-0.11840.41350.22930.0551-0.2029-1.3897-0.1856-0.9609-0.32350.0508-0.03531.07650.00050.63220.21130.04230.569653.545335.94198.9763
1290.34420.97671.17323.51734.31384.3132-0.49340.0629-0.4669-2.45030.3921-0.8394-2.3448-0.0483-0.36211.3748-0.18220.65080.18330.03330.403656.215845.013997.42
1300.27680.6275-0.9426-0.0617-0.47970.98050.2949-0.11360.363-0.13820.3577-0.2817-0.0737-0.2004-0.45950.9732-0.23480.42991.167-0.13491.591570.388634.1203109.5135
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1048:1054)A1048 - 1054
2X-RAY DIFFRACTION2(CHAIN A AND RESID 1055:1065)A1055 - 1065
3X-RAY DIFFRACTION3(CHAIN A AND RESID 1066:1079)A1066 - 1079
4X-RAY DIFFRACTION4(CHAIN A AND RESID 1080:1086)A1080 - 1086
5X-RAY DIFFRACTION5(CHAIN A AND RESID 1087:1100)A1087 - 1100
6X-RAY DIFFRACTION6(CHAIN A AND RESID 1101:1108)A1101 - 1108
7X-RAY DIFFRACTION7(CHAIN A AND RESID 1109:1113)A1109 - 1113
8X-RAY DIFFRACTION8(CHAIN A AND RESID 1114:1131)A1114 - 1131
9X-RAY DIFFRACTION9(CHAIN A AND RESID 1132:1149)A1132 - 1149
10X-RAY DIFFRACTION10(CHAIN A AND RESID 1150:1155)A1150 - 1155
11X-RAY DIFFRACTION11(CHAIN A AND RESID 1156:1160)A1156 - 1160
12X-RAY DIFFRACTION12(CHAIN B AND RESID 1048:1054)B1048 - 1054
13X-RAY DIFFRACTION13(CHAIN B AND RESID 1055:1067)B1055 - 1067
14X-RAY DIFFRACTION14(CHAIN B AND RESID 1068:1083)B1068 - 1083
15X-RAY DIFFRACTION15(CHAIN B AND RESID 1084:1094)B1084 - 1094
16X-RAY DIFFRACTION16(CHAIN B AND RESID 1095:1109)B1095 - 1109
17X-RAY DIFFRACTION17(CHAIN B AND RESID 1110:1117)B1110 - 1117
18X-RAY DIFFRACTION18(CHAIN B AND RESID 1118:1128)B1118 - 1128
19X-RAY DIFFRACTION19(CHAIN B AND RESID 1129:1139)B1129 - 1139
20X-RAY DIFFRACTION20(CHAIN B AND RESID 1140:1145)B1140 - 1145
21X-RAY DIFFRACTION21(CHAIN B AND RESID 1146:1154)B1146 - 1154
22X-RAY DIFFRACTION22(CHAIN B AND RESID 1155:1161)B1155 - 1161
23X-RAY DIFFRACTION23(CHAIN C AND RESID 1047:1055)C1047 - 1055
24X-RAY DIFFRACTION24(CHAIN C AND RESID 1056:1067)C1056 - 1067
25X-RAY DIFFRACTION25(CHAIN C AND RESID 1068:1079)C1068 - 1079
26X-RAY DIFFRACTION26(CHAIN C AND RESID 1080:1091)C1080 - 1091
27X-RAY DIFFRACTION27(CHAIN C AND RESID 1092:1101)C1092 - 1101
28X-RAY DIFFRACTION28(CHAIN C AND RESID 1102:1109)C1102 - 1109
29X-RAY DIFFRACTION29(CHAIN C AND RESID 1110:1115)C1110 - 1115
30X-RAY DIFFRACTION30(CHAIN C AND RESID 1116:1136)C1116 - 1136
31X-RAY DIFFRACTION31(CHAIN C AND RESID 1137:1145)C1137 - 1145
32X-RAY DIFFRACTION32(CHAIN C AND RESID 1146:1155)C1146 - 1155
33X-RAY DIFFRACTION33(CHAIN C AND RESID 1156:1160)C1156 - 1160
34X-RAY DIFFRACTION34(CHAIN D AND RESID 1048:1054)D1048 - 1054
35X-RAY DIFFRACTION35(CHAIN D AND RESID 1055:1061)D1055 - 1061
36X-RAY DIFFRACTION36(CHAIN D AND RESID 1062:1082)D1062 - 1082
37X-RAY DIFFRACTION37(CHAIN D AND RESID 1083:1100)D1083 - 1100
38X-RAY DIFFRACTION38(CHAIN D AND RESID 1101:1107)D1101 - 1107
39X-RAY DIFFRACTION39(CHAIN D AND RESID 1108:1115)D1108 - 1115
40X-RAY DIFFRACTION40(CHAIN D AND RESID 1116:1130)D1116 - 1130
41X-RAY DIFFRACTION41(CHAIN D AND RESID 1131:1137)D1131 - 1137
42X-RAY DIFFRACTION42(CHAIN D AND RESID 1138:1149)D1138 - 1149
43X-RAY DIFFRACTION43(CHAIN D AND RESID 1150:1155)D1150 - 1155
44X-RAY DIFFRACTION44(CHAIN D AND RESID 1156:1160)D1156 - 1160
45X-RAY DIFFRACTION45(CHAIN E AND RESID 1047:1056)E1047 - 1056
46X-RAY DIFFRACTION46(CHAIN E AND RESID 1072:1076)E1072 - 1076
47X-RAY DIFFRACTION47(CHAIN E AND RESID 1077:1083)E1077 - 1083
48X-RAY DIFFRACTION48(CHAIN E AND RESID 1084:1090)E1084 - 1090
49X-RAY DIFFRACTION49(CHAIN E AND RESID 1091:1100)E1091 - 1100
50X-RAY DIFFRACTION50(CHAIN E AND RESID 1101:1115)E1101 - 1115
51X-RAY DIFFRACTION51(CHAIN E AND RESID 1116:1142)E1116 - 1142
52X-RAY DIFFRACTION52(CHAIN E AND RESID 1143:1150)E1143 - 1150
53X-RAY DIFFRACTION53(CHAIN E AND RESID 1151:1155)E1151 - 1155
54X-RAY DIFFRACTION54(CHAIN E AND RESID 1156:1161)E1156 - 1161
55X-RAY DIFFRACTION55(CHAIN F AND RESID 1049:1053)F1049 - 1053
56X-RAY DIFFRACTION56(CHAIN F AND RESID 1054:1061)F1054 - 1061
57X-RAY DIFFRACTION57(CHAIN F AND RESID 1072:1083)F1072 - 1083
58X-RAY DIFFRACTION58(CHAIN F AND RESID 1084:1094)F1084 - 1094
59X-RAY DIFFRACTION59(CHAIN F AND RESID 1095:1106)F1095 - 1106
60X-RAY DIFFRACTION60(CHAIN F AND RESID 1107:1117)F1107 - 1117
61X-RAY DIFFRACTION61(CHAIN F AND RESID 1118:1122)F1118 - 1122
62X-RAY DIFFRACTION62(CHAIN F AND RESID 1123:1131)F1123 - 1131
63X-RAY DIFFRACTION63(CHAIN F AND RESID 1132:1147)F1132 - 1147
64X-RAY DIFFRACTION64(CHAIN F AND RESID 1148:1159)F1148 - 1159
65X-RAY DIFFRACTION65(CHAIN G AND RESID 1048:1054)G1048 - 1054
66X-RAY DIFFRACTION66(CHAIN G AND RESID 1055:1060)G1055 - 1060
67X-RAY DIFFRACTION67(CHAIN G AND RESID 1061:1067)G1061 - 1067
68X-RAY DIFFRACTION68(CHAIN G AND RESID 1068:1081)G1068 - 1081
69X-RAY DIFFRACTION69(CHAIN G AND RESID 1082:1087)G1082 - 1087
70X-RAY DIFFRACTION70(CHAIN G AND RESID 1088:1109)G1088 - 1109
71X-RAY DIFFRACTION71(CHAIN G AND RESID 1110:1117)G1110 - 1117
72X-RAY DIFFRACTION72(CHAIN G AND RESID 1118:1138)G1118 - 1138
73X-RAY DIFFRACTION73(CHAIN G AND RESID 1139:1148)G1139 - 1148
74X-RAY DIFFRACTION74(CHAIN G AND RESID 1149:1153)G1149 - 1153
75X-RAY DIFFRACTION75(CHAIN G AND RESID 1154:1160)G1154 - 1160
76X-RAY DIFFRACTION76(CHAIN H AND RESID 1048:1054)H1048 - 1054
77X-RAY DIFFRACTION77(CHAIN H AND RESID 1055:1076)H1055 - 1076
78X-RAY DIFFRACTION78(CHAIN H AND RESID 1077:1085)H1077 - 1085
79X-RAY DIFFRACTION79(CHAIN H AND RESID 1086:1093)H1086 - 1093
80X-RAY DIFFRACTION80(CHAIN H AND RESID 1094:1114)H1094 - 1114
81X-RAY DIFFRACTION81(CHAIN H AND RESID 1115:1120)H1115 - 1120
82X-RAY DIFFRACTION82(CHAIN H AND RESID 1121:1128)H1121 - 1128
83X-RAY DIFFRACTION83(CHAIN H AND RESID 1129:1135)H1129 - 1135
84X-RAY DIFFRACTION84(CHAIN H AND RESID 1136:1150)H1136 - 1150
85X-RAY DIFFRACTION85(CHAIN H AND RESID 1151:1155)H1151 - 1155
86X-RAY DIFFRACTION86(CHAIN H AND RESID 1156:1160)H1156 - 1160
87X-RAY DIFFRACTION87(CHAIN I AND RESID 1047:1054)I1047 - 1054
88X-RAY DIFFRACTION88(CHAIN I AND RESID 1055:1065)I1055 - 1065
89X-RAY DIFFRACTION89(CHAIN I AND RESID 1066:1076)I1066 - 1076
90X-RAY DIFFRACTION90(CHAIN I AND RESID 1077:1093)I1077 - 1093
91X-RAY DIFFRACTION91(CHAIN I AND RESID 1094:1107)I1094 - 1107
92X-RAY DIFFRACTION92(CHAIN I AND RESID 1108:1116)I1108 - 1116
93X-RAY DIFFRACTION93(CHAIN I AND RESID 1117:1131)I1117 - 1131
94X-RAY DIFFRACTION94(CHAIN I AND RESID 1132:1138)I1132 - 1138
95X-RAY DIFFRACTION95(CHAIN I AND RESID 1139:1149)I1139 - 1149
96X-RAY DIFFRACTION96(CHAIN I AND RESID 1150:1155)I1150 - 1155
97X-RAY DIFFRACTION97(CHAIN I AND RESID 1156:1161)I1156 - 1161
98X-RAY DIFFRACTION98(CHAIN J AND RESID 1048:1061)J1048 - 1061
99X-RAY DIFFRACTION99(CHAIN J AND RESID 1062:1069)J1062 - 1069
100X-RAY DIFFRACTION100(CHAIN J AND RESID 1070:1076)J1070 - 1076
101X-RAY DIFFRACTION101(CHAIN J AND RESID 1077:1083)J1077 - 1083
102X-RAY DIFFRACTION102(CHAIN J AND RESID 1084:1098)J1084 - 1098
103X-RAY DIFFRACTION103(CHAIN J AND RESID 1099:1107)J1099 - 1107
104X-RAY DIFFRACTION104(CHAIN J AND RESID 1108:1113)J1108 - 1113
105X-RAY DIFFRACTION105(CHAIN J AND RESID 1114:1124)J1114 - 1124
106X-RAY DIFFRACTION106(CHAIN J AND RESID 1125:1138)J1125 - 1138
107X-RAY DIFFRACTION107(CHAIN J AND RESID 1139:1150)J1139 - 1150
108X-RAY DIFFRACTION108(CHAIN J AND RESID 1151:1160)J1151 - 1160
109X-RAY DIFFRACTION109(CHAIN K AND RESID 1047:1053)K1047 - 1053
110X-RAY DIFFRACTION110(CHAIN K AND RESID 1054:1076)K1054 - 1076
111X-RAY DIFFRACTION111(CHAIN K AND RESID 1077:1087)K1077 - 1087
112X-RAY DIFFRACTION112(CHAIN K AND RESID 1088:1103)K1088 - 1103
113X-RAY DIFFRACTION113(CHAIN K AND RESID 1104:1110)K1104 - 1110
114X-RAY DIFFRACTION114(CHAIN K AND RESID 1111:1116)K1111 - 1116
115X-RAY DIFFRACTION115(CHAIN K AND RESID 1117:1130)K1117 - 1130
116X-RAY DIFFRACTION116(CHAIN K AND RESID 1131:1136)K1131 - 1136
117X-RAY DIFFRACTION117(CHAIN K AND RESID 1137:1148)K1137 - 1148
118X-RAY DIFFRACTION118(CHAIN K AND RESID 1149:1154)K1149 - 1154
119X-RAY DIFFRACTION119(CHAIN K AND RESID 1155:1160)K1155 - 1160
120X-RAY DIFFRACTION120(CHAIN L AND RESID 1048:1054)L1048 - 1054
121X-RAY DIFFRACTION121(CHAIN L AND RESID 1055:1065)L1055 - 1065
122X-RAY DIFFRACTION122(CHAIN L AND RESID 1066:1072)L1066 - 1072
123X-RAY DIFFRACTION123(CHAIN L AND RESID 1073:1077)L1073 - 1077
124X-RAY DIFFRACTION124(CHAIN L AND RESID 1078:1087)L1078 - 1087
125X-RAY DIFFRACTION125(CHAIN L AND RESID 1088:1101)L1088 - 1101
126X-RAY DIFFRACTION126(CHAIN L AND RESID 1102:1107)L1102 - 1107
127X-RAY DIFFRACTION127(CHAIN L AND RESID 1108:1117)L1108 - 1117
128X-RAY DIFFRACTION128(CHAIN L AND RESID 1118:1131)L1118 - 1131
129X-RAY DIFFRACTION129(CHAIN L AND RESID 1132:1153)L1132 - 1153
130X-RAY DIFFRACTION130(CHAIN L AND RESID 1154:1160)L1154 - 1160

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