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- PDB-7la9: Crystal structure of the first bromodomain (BD1) of human BRD4 (B... -

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Basic information

Entry
Database: PDB / ID: 7la9
TitleCrystal structure of the first bromodomain (BD1) of human BRD4 (BRD4-1) in complex with bivalent inhibitor NC-III-49-1
ComponentsBromodomain-containing protein 4
KeywordsTRANSCRIPTION/TRANSCRIPTION INHIBITOR / BET / ERK5 / dual BRD-kinase inhibitor / TRANSCRIPTION-TRANSCRIPTION INHIBITOR complex
Function / homology
Function and homology information


RNA polymerase II C-terminal domain binding / P-TEFb complex binding / negative regulation of DNA damage checkpoint / histone H4 reader activity / host-mediated suppression of viral transcription / positive regulation of G2/M transition of mitotic cell cycle / positive regulation of T-helper 17 cell lineage commitment / : / RNA polymerase II CTD heptapeptide repeat kinase activity / condensed nuclear chromosome ...RNA polymerase II C-terminal domain binding / P-TEFb complex binding / negative regulation of DNA damage checkpoint / histone H4 reader activity / host-mediated suppression of viral transcription / positive regulation of G2/M transition of mitotic cell cycle / positive regulation of T-helper 17 cell lineage commitment / : / RNA polymerase II CTD heptapeptide repeat kinase activity / condensed nuclear chromosome / transcription coregulator activity / positive regulation of transcription elongation by RNA polymerase II / p53 binding / chromosome / regulation of inflammatory response / histone binding / Potential therapeutics for SARS / transcription coactivator activity / positive regulation of canonical NF-kappaB signal transduction / transcription cis-regulatory region binding / chromatin remodeling / protein serine/threonine kinase activity / DNA damage response / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus
Similarity search - Function
Bromodomain protein 4, C-terminal / C-terminal domain of bromodomain protein 4 / Brdt, bromodomain, repeat I / Brdt, bromodomain, repeat II / NET domain superfamily / NET domain profile. / : / NET domain / Bromodomain extra-terminal - transcription regulation / Bromodomain, conserved site ...Bromodomain protein 4, C-terminal / C-terminal domain of bromodomain protein 4 / Brdt, bromodomain, repeat I / Brdt, bromodomain, repeat II / NET domain superfamily / NET domain profile. / : / NET domain / Bromodomain extra-terminal - transcription regulation / Bromodomain, conserved site / Bromodomain signature. / Bromodomain / bromo domain / Bromodomain / Bromodomain (BrD) profile. / Bromodomain-like superfamily
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Chem-XR7 / Bromodomain-containing protein 4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsKarim, M.R. / Schonbrunn, E.
CitationJournal: J.Med.Chem. / Year: 2022
Title: Bivalent BET Bromodomain Inhibitors Confer Increased Potency and Selectivity for BRDT via Protein Conformational Plasticity.
Authors: Guan, X. / Cheryala, N. / Karim, R.M. / Chan, A. / Berndt, N. / Qi, J. / Georg, G.I. / Schonbrunn, E.
History
DepositionJan 6, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 12, 2022Provider: repository / Type: Initial release
Revision 1.1Aug 3, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Aug 24, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Bromodomain-containing protein 4
B: Bromodomain-containing protein 4
C: Bromodomain-containing protein 4
D: Bromodomain-containing protein 4
E: Bromodomain-containing protein 4
F: Bromodomain-containing protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,19333
Polymers89,2876
Non-polymers3,90727
Water4,828268
1
A: Bromodomain-containing protein 4
D: Bromodomain-containing protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,32015
Polymers29,7622
Non-polymers1,55713
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Bromodomain-containing protein 4
F: Bromodomain-containing protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,8948
Polymers29,7622
Non-polymers1,1326
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Bromodomain-containing protein 4
E: Bromodomain-containing protein 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,97910
Polymers29,7622
Non-polymers1,2178
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)114.126, 114.126, 94.834
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 60 through 98 or resid 100...
21(chain B and (resid 60 through 98 or resid 100...
31(chain C and (resid 60 through 98 or resid 100...
41(chain D and (resid 60 through 98 or resid 100...
51(chain E and (resid 60 through 98 or resid 100...
61(chain F and (resid 60 through 98 or resid 100...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRTYRTYR(chain A and (resid 60 through 98 or resid 100...AA60 - 9817 - 55
12ILEILEILEILE(chain A and (resid 60 through 98 or resid 100...AA100 - 10157 - 58
13LYSLYSLYSLYS(chain A and (resid 60 through 98 or resid 100...AA10259
14THRTHRLEULEU(chain A and (resid 60 through 98 or resid 100...AA60 - 16417 - 121
15THRTHRLEULEU(chain A and (resid 60 through 98 or resid 100...AA60 - 16417 - 121
16THRTHRLEULEU(chain A and (resid 60 through 98 or resid 100...AA60 - 16417 - 121
17THRTHRLEULEU(chain A and (resid 60 through 98 or resid 100...AA60 - 16417 - 121
21THRTHRTYRTYR(chain B and (resid 60 through 98 or resid 100...BB60 - 9817 - 55
22ILEILEILEILE(chain B and (resid 60 through 98 or resid 100...BB100 - 10157 - 58
23LYSLYSLYSLYS(chain B and (resid 60 through 98 or resid 100...BB10259
24THRTHRLEULEU(chain B and (resid 60 through 98 or resid 100...BB60 - 16417 - 121
25THRTHRLEULEU(chain B and (resid 60 through 98 or resid 100...BB60 - 16417 - 121
26THRTHRLEULEU(chain B and (resid 60 through 98 or resid 100...BB60 - 16417 - 121
27THRTHRLEULEU(chain B and (resid 60 through 98 or resid 100...BB60 - 16417 - 121
31THRTHRTYRTYR(chain C and (resid 60 through 98 or resid 100...CC60 - 9817 - 55
32ILEILEILEILE(chain C and (resid 60 through 98 or resid 100...CC100 - 12657 - 83
33ASPASPASNASN(chain C and (resid 60 through 98 or resid 100...CC128 - 14085 - 97
34PROPROALAALA(chain C and (resid 60 through 98 or resid 100...CC142 - 15099 - 107
35ALAALALEULEU(chain C and (resid 60 through 98 or resid 100...CC152 - 164109 - 121
41THRTHRTYRTYR(chain D and (resid 60 through 98 or resid 100...DD60 - 9817 - 55
42ILEILEILEILE(chain D and (resid 60 through 98 or resid 100...DD100 - 10157 - 58
43LYSLYSLYSLYS(chain D and (resid 60 through 98 or resid 100...DD10259
44THRTHRLEULEU(chain D and (resid 60 through 98 or resid 100...DD60 - 16417 - 121
45THRTHRLEULEU(chain D and (resid 60 through 98 or resid 100...DD60 - 16417 - 121
46THRTHRLEULEU(chain D and (resid 60 through 98 or resid 100...DD60 - 16417 - 121
47THRTHRLEULEU(chain D and (resid 60 through 98 or resid 100...DD60 - 16417 - 121
51THRTHRTYRTYR(chain E and (resid 60 through 98 or resid 100...EE60 - 9817 - 55
52ILEILEILEILE(chain E and (resid 60 through 98 or resid 100...EE100 - 10157 - 58
53LYSLYSLYSLYS(chain E and (resid 60 through 98 or resid 100...EE10259
54THRTHRLEULEU(chain E and (resid 60 through 98 or resid 100...EE60 - 16417 - 121
55THRTHRLEULEU(chain E and (resid 60 through 98 or resid 100...EE60 - 16417 - 121
56THRTHRLEULEU(chain E and (resid 60 through 98 or resid 100...EE60 - 16417 - 121
57THRTHRLEULEU(chain E and (resid 60 through 98 or resid 100...EE60 - 16417 - 121
61THRTHRTYRTYR(chain F and (resid 60 through 98 or resid 100...FF60 - 9817 - 55
62ILEILEILEILE(chain F and (resid 60 through 98 or resid 100...FF100 - 10157 - 58
63LYSLYSLYSLYS(chain F and (resid 60 through 98 or resid 100...FF10259
64THRTHRLEULEU(chain F and (resid 60 through 98 or resid 100...FF60 - 16417 - 121
65THRTHRLEULEU(chain F and (resid 60 through 98 or resid 100...FF60 - 16417 - 121
66THRTHRLEULEU(chain F and (resid 60 through 98 or resid 100...FF60 - 16417 - 121
67THRTHRLEULEU(chain F and (resid 60 through 98 or resid 100...FF60 - 16417 - 121

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Components

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein
Bromodomain-containing protein 4 / Protein HUNK1


Mass: 14881.105 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BRD4, HUNK1 / Production host: Escherichia coli (E. coli) / References: UniProt: O60885

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Non-polymers , 6 types, 295 molecules

#2: Chemical ChemComp-XR7 / N,N'-(oxybis{(ethane-2,1-diyl)oxyethane-2,1-diyloxy[3-(2-methyl-1-oxo-1,2-dihydroisoquinolin-4-yl)-4,1-phenylene]})di(ethane-1-sulfonamide)


Mass: 875.018 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C44H50N4O11S2 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C4H10O3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 268 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 3.94 Å3/Da / Density % sol: 68.75 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.01 M Iron(III) chloride hexahydrate, 0.1 M Sodium citrate tribasic dihydrate (pH 5.6), 10% v/v Jeffamine M-600

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5417 Å
DetectorType: RIGAKU SATURN 944+ / Detector: CCD / Date: Sep 8, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5417 Å / Relative weight: 1
ReflectionResolution: 2.2→98.84 Å / Num. obs: 139185 / % possible obs: 100 % / Redundancy: 5.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.059 / Rpim(I) all: 0.028 / Rrim(I) all: 0.065 / Net I/σ(I): 18.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.2-2.255.52.6492520745500.4351.2482.930.7100
10.55-98.8450.024304560410.0110.02757.996.2

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Processing

Software
NameVersionClassification
PHENIX1.18.2-3874_3874refinement
Aimless0.7.4data scaling
PDB_EXTRACT3.27data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7K6H

7k6h


Resolution: 2.2→37.36 Å / SU ML: 0.3 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 27.57 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2077 4004 2.88 %
Rwork0.1846 135181 -
obs0.1853 139185 99.26 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 128.87 Å2 / Biso mean: 62.8059 Å2 / Biso min: 40.47 Å2
Refinement stepCycle: final / Resolution: 2.2→37.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5313 0 255 268 5836
Biso mean--65.62 59.11 -
Num. residues----630
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0095697
X-RAY DIFFRACTIONf_angle_d1.0417710
X-RAY DIFFRACTIONf_chiral_restr0.056801
X-RAY DIFFRACTIONf_plane_restr0.007942
X-RAY DIFFRACTIONf_dihedral_angle_d10.569746
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1740X-RAY DIFFRACTION6.103TORSIONAL
12B1740X-RAY DIFFRACTION6.103TORSIONAL
13C1740X-RAY DIFFRACTION6.103TORSIONAL
14D1740X-RAY DIFFRACTION6.103TORSIONAL
15E1740X-RAY DIFFRACTION6.103TORSIONAL
16F1740X-RAY DIFFRACTION6.103TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 29

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.230.43411140.39314076419088
2.23-2.250.4091460.35194562470896
2.25-2.280.34541450.31634706485199
2.28-2.310.29821390.31954602474199
2.31-2.340.29371320.301846794811100
2.34-2.380.37921520.281147714923100
2.38-2.410.30691280.27546404768100
2.41-2.450.31971320.280746534785100
2.45-2.490.27051520.27247554907100
2.49-2.530.33491240.237747114835100
2.53-2.580.26031400.229246654805100
2.58-2.630.28291320.220346044736100
2.63-2.680.26571400.218247644904100
2.68-2.740.25621400.211147444884100
2.74-2.80.27121320.207246464778100
2.8-2.870.25981400.221247344874100
2.87-2.950.26981360.215746824818100
2.95-3.040.19291440.214146884832100
3.04-3.140.28961400.206546504790100
3.14-3.250.23071560.206347224878100
3.25-3.380.20241280.177947364864100
3.38-3.530.20931480.17546774825100
3.53-3.720.24351320.1746964828100
3.72-3.950.1751360.161846734809100
3.95-4.250.16961360.153647024838100
4.26-4.680.13141360.133446774813100
4.68-5.360.15851360.149347354871100
5.36-6.740.16571400.15947004840100
6.75-37.360.15181480.14854531467997
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)
18.4768-0.16460.51874.7443.98513.3918-0.11010.1960.9138-0.7631-0.06890.1779-0.9030.04010.31190.64-0.0172-0.05480.3830.01670.57483.702757.9393-10.5333
23.8484-0.3441-1.34589.6103-0.04253.8969-0.1318-0.0533-0.1707-0.03540.00520.41430.1864-0.47590.12370.4355-0.0216-0.04040.41160.08340.3782-6.214439.3779-8.4015
38.04523.35390.67234.52640.05050.4968-0.16270.45050.2048-0.5310.27420.0534-0.0447-0.1374-0.09590.5422-0.005-0.03710.43920.03530.3175-1.846144.1714-18.2416
45.69631.38282.24487.342.27044.2902-0.206-0.08220.3155-0.54760.16990.6847-0.2388-0.39040.01750.45420.0587-0.03330.49780.11170.3979-13.482948.512-11.0624
56.42274.41653.34157.13812.08857.39120.66460.9009-0.9003-0.8594-0.42550.14530.56570.5047-0.22210.6980.1404-0.07340.5206-0.0150.6197-17.384349.5594-39.5869
63.4424-1.6645-3.29345.79173.974.84190.14860.0752-0.5744-0.0552-0.06260.36730.1392-0.5356-0.13290.55140.0186-0.14070.52060.11770.6379-28.073951.8365-26.0178
74.5665-2.1767-4.58792.49971.68214.770.5593-1.87840.70331.16820.35940.0351-0.52350.8883-0.96230.7347-0.0001-0.0370.8709-0.04680.6572-28.380865.708-11.5569
82.3545-0.5302-2.23171.0475-1.82347.46030.14330.01690.0746-0.05530.0456-0.2934-0.13450.2907-0.16550.53160.019-0.08990.46930.05250.5918-18.670961.8607-27.9182
90.9367-0.3145-0.52181.8114-1.73312.37380.0642-0.043-0.109-0.090.0272-0.07110.21090.0848-0.10030.55830.0061-0.1010.54340.08630.628-15.907855.345-22.7787
103.2839-1.33010.08093.72830.16564.5727-0.0988-0.1919-0.53920.1420.09090.16290.6539-0.0152-0.01220.5266-0.0216-0.12970.40560.12060.5976-20.682746.3604-20.3644
116.5193-0.29273.94837.8875-1.67389.3068-0.2811-0.3215-0.4661.42180.4563-0.53620.68090.4608-0.18550.64050.1479-0.06130.5149-0.04840.586722.80816.8878-0.8968
125.6156-2.54171.04637.0895-4.77125.20780.08580.4190.1426-0.25020.0845-0.362-0.29780.3587-0.24530.5603-0.00250.04510.5112-0.16390.511423.181919.178-18.2122
130.6445-0.3451-1.14552.05330.89575.5721-0.02260.0137-0.2031-0.01330.1602-0.03410.16970.0305-0.11030.48440.01960.00990.5238-0.11310.583414.714911.8297-14.5834
143.1383-1.1630.10113.62970.57692.7680.01520.0463-0.2086-0.28790.0958-0.38140.25320.3643-0.06370.45320.02970.04650.522-0.17350.635127.25258.1779-20.1217
158.4464-0.4884-0.91112.50332.10636.0329-0.181-0.1555-1.08210.2994-0.2879-0.14541.20580.3660.47090.70610.01140.06610.42020.03870.60233.70027.96771.6611
163.3858-0.06761.02167.27460.23653.5804-0.092-0.20410.23970.10160.03860.2241-0.4006-0.35120.06340.45950.02550.03130.45630.07790.4129-6.055527.56653.06
174.9232-2.51960.87294.3019-0.09710.9104-0.19-0.3535-0.26430.530.25120.09270.1697-0.1522-0.06510.5259-0.00720.03580.41460.03640.3582-0.701319.11138.3736
185.3393-1.3673-2.56336.93792.23054.0942-0.11870.2966-0.20390.40130.07720.57750.1725-0.41940.05760.5092-0.06230.01750.5470.11060.4433-13.312717.21862.1054
198.09990.72182.43518.9411.46737.72240.46671.2761.2064-0.1819-0.0056-0.1629-0.645-0.1332-0.39610.79570.00660.11460.56420.11380.607215.579552.3215-24.6074
209.3729-4.72212.86763.9277-3.31223.85060.11711.2629-0.5545-1.4796-0.32180.39730.33210.2637-0.0440.7139-0.08820.10260.5378-0.05450.412918.104138.4907-28.6378
216.4706-3.9323.96283.2362-2.99643.06060.07040.3682-0.0099-0.04080.0365-1.44980.32550.63230.04120.6054-0.01670.07260.5497-0.17860.869730.530229.5792-18.9233
222.9775-2.8053-0.72986.40951.29362.01030.01780.09760.2727-0.38550.1714-1.034-0.31660.4992-0.14810.5749-0.13590.15410.6287-0.08490.708929.216543.8382-19.6436
234.4556-1.72581.29736.7457-1.96613.52450.51180.94990.1027-1.5015-0.399-0.80010.15190.4173-0.09070.9418-0.0940.29840.7445-0.0960.556427.674739.7131-33.1019
249.2775.07422.53264.5434-0.05367.00810.3006-0.12490.7360.98610.16860.9548-0.559-0.6507-0.45430.62930.14660.16660.76780.05010.6402-53.105978.5679-15.8974
256.0908-5.7036-1.03669.46194.53626.3115-0.0549-0.4015-0.74520.86340.06730.25030.59040.0036-0.01750.4514-0.04280.0050.57770.20620.533-41.500260.8903-17.3078
263.6489-3.26980.87637.231-1.3172.1796-0.0248-0.3354-0.72980.0330.260.87110.2627-0.5467-0.1770.4814-0.09160.00150.70210.17530.6931-52.589562.5173-20.8602
273.9173-1.3555-0.98047.31041.8873.1195-0.5367-0.9975-0.59451.52050.64230.47550.6239-0.1095-0.12970.74810.02440.0791.0210.28470.5593-48.312461.7487-7.4052
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 60 through 68 )A60 - 68
2X-RAY DIFFRACTION2chain 'A' and (resid 69 through 96 )A69 - 96
3X-RAY DIFFRACTION3chain 'A' and (resid 97 through 139 )A97 - 139
4X-RAY DIFFRACTION4chain 'A' and (resid 140 through 164 )A140 - 164
5X-RAY DIFFRACTION5chain 'B' and (resid 60 through 68 )B60 - 68
6X-RAY DIFFRACTION6chain 'B' and (resid 69 through 88 )B69 - 88
7X-RAY DIFFRACTION7chain 'B' and (resid 89 through 96 )B89 - 96
8X-RAY DIFFRACTION8chain 'B' and (resid 97 through 121 )B97 - 121
9X-RAY DIFFRACTION9chain 'B' and (resid 122 through 139 )B122 - 139
10X-RAY DIFFRACTION10chain 'B' and (resid 140 through 164 )B140 - 164
11X-RAY DIFFRACTION11chain 'C' and (resid 60 through 68 )C60 - 68
12X-RAY DIFFRACTION12chain 'C' and (resid 69 through 96 )C69 - 96
13X-RAY DIFFRACTION13chain 'C' and (resid 97 through 139 )C97 - 139
14X-RAY DIFFRACTION14chain 'C' and (resid 140 through 164 )C140 - 164
15X-RAY DIFFRACTION15chain 'D' and (resid 60 through 68 )D60 - 68
16X-RAY DIFFRACTION16chain 'D' and (resid 69 through 106 )D69 - 106
17X-RAY DIFFRACTION17chain 'D' and (resid 107 through 139 )D107 - 139
18X-RAY DIFFRACTION18chain 'D' and (resid 140 through 164 )D140 - 164
19X-RAY DIFFRACTION19chain 'E' and (resid 60 through 68 )E60 - 68
20X-RAY DIFFRACTION20chain 'E' and (resid 69 through 80 )E69 - 80
21X-RAY DIFFRACTION21chain 'E' and (resid 81 through 96 )E81 - 96
22X-RAY DIFFRACTION22chain 'E' and (resid 97 through 139 )E97 - 139
23X-RAY DIFFRACTION23chain 'E' and (resid 140 through 164 )E140 - 164
24X-RAY DIFFRACTION24chain 'F' and (resid 60 through 68 )F60 - 68
25X-RAY DIFFRACTION25chain 'F' and (resid 69 through 96 )F69 - 96
26X-RAY DIFFRACTION26chain 'F' and (resid 97 through 139 )F97 - 139
27X-RAY DIFFRACTION27chain 'F' and (resid 140 through 164 )F140 - 164

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