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- PDB-5lw1: Crystal structure of DARPin-DARPin rigid fusion, variant DD_232_1... -

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Basic information

Entry
Database: PDB / ID: 5lw1
TitleCrystal structure of DARPin-DARPin rigid fusion, variant DD_232_11_D12 in complex JNK1a1 and JIP1 peptide
Components
  • C-Jun-amino-terminal kinase-interacting protein 1
  • DD_232_11_D12
  • Mitogen-activated protein kinase 8
  • Pepstatin
KeywordsDE NOVO PROTEIN / X-ray crystallography / designed ankyrin repeat proteins / protein design / protein engineering / rigid domain fusions / transferase
Function / homology
Function and homology information


dentate gyrus mossy fiber / JUN phosphorylation / positive regulation of cell killing / regulation of CD8-positive, alpha-beta T cell proliferation / basal dendrite / Activation of BMF and translocation to mitochondria / Interleukin-38 signaling / negative regulation of JUN kinase activity / positive regulation of establishment of protein localization to mitochondrion / JUN kinase activity ...dentate gyrus mossy fiber / JUN phosphorylation / positive regulation of cell killing / regulation of CD8-positive, alpha-beta T cell proliferation / basal dendrite / Activation of BMF and translocation to mitochondria / Interleukin-38 signaling / negative regulation of JUN kinase activity / positive regulation of establishment of protein localization to mitochondrion / JUN kinase activity / Activation of BIM and translocation to mitochondria / WNT5:FZD7-mediated leishmania damping / MAP-kinase scaffold activity / JUN kinase binding / positive regulation of cyclase activity / mitogen-activated protein kinase kinase binding / mitogen-activated protein kinase kinase kinase binding / regulation of JNK cascade / histone deacetylase regulator activity / NRAGE signals death through JNK / Activation of the AP-1 family of transcription factors / positive regulation of NLRP3 inflammasome complex assembly / Fc-epsilon receptor signaling pathway / negative regulation of intrinsic apoptotic signaling pathway / dendritic growth cone / protein kinase inhibitor activity / positive regulation of protein metabolic process / peptidyl-threonine phosphorylation / mitogen-activated protein kinase / kinesin binding / regulation of macroautophagy / response to mechanical stimulus / axonal growth cone / stress-activated MAPK cascade / response to UV / negative regulation of protein binding / energy homeostasis / vesicle-mediated transport / JNK cascade / protein serine/threonine kinase binding / NRIF signals cell death from the nucleus / cellular response to amino acid starvation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / cellular response to reactive oxygen species / positive regulation of JNK cascade / FCERI mediated MAPK activation / cellular response to mechanical stimulus / regulation of circadian rhythm / peptidyl-serine phosphorylation / mitochondrial membrane / histone deacetylase binding / cellular senescence / Signaling by ALK fusions and activated point mutants / rhythmic process / MAPK cascade / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / regulation of protein localization / cellular response to lipopolysaccharide / response to oxidative stress / cellular response to oxidative stress / protein phosphatase binding / Oxidative Stress Induced Senescence / protein phosphorylation / positive regulation of apoptotic process / axon / protein serine kinase activity / neuronal cell body / protein serine/threonine kinase activity / synapse / positive regulation of gene expression / regulation of DNA-templated transcription / endoplasmic reticulum membrane / negative regulation of apoptotic process / perinuclear region of cytoplasm / enzyme binding / nucleoplasm / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
JIP1, SH3 domain / : / Mitogen-activated protein (MAP) kinase, JNK / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / Variant SH3 domain / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. ...JIP1, SH3 domain / : / Mitogen-activated protein (MAP) kinase, JNK / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / Variant SH3 domain / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. / : / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / PH-like domain superfamily / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Pepstatin / ADENOSINE / Mitogen-activated protein kinase 8 / C-Jun-amino-terminal kinase-interacting protein 1
Similarity search - Component
Biological speciessynthetic construct (others)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsWu, Y. / Batyuk, A. / Mittl, P.R. / Honegger, A. / Plueckthun, A.
Funding support Switzerland, 2items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_166676 Switzerland
European Research CouncilNEXTBINDERS
CitationJournal: J.Mol.Biol. / Year: 2018
Title: Structural Basis for the Selective Inhibition of c-Jun N-Terminal Kinase 1 Determined by Rigid DARPin-DARPin Fusions.
Authors: Wu, Y. / Honegger, A. / Batyuk, A. / Mittl, P.R.E. / Pluckthun, A.
History
DepositionSep 15, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 13, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 13, 2018Group: Data collection / Structure summary / Category: pdbx_molecule_features
Revision 1.2Jul 10, 2019Group: Data collection / Database references
Category: citation / citation_author ...citation / citation_author / pdbx_database_proc / pdbx_seq_map_depositor_info
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _pdbx_seq_map_depositor_info.one_letter_code / _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.3Jan 1, 2020Group: Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_assembly_gen ...pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / struct_site / struct_site_gen
Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly_gen.asym_id_list
Revision 1.4Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.5Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DD_232_11_D12
B: Mitogen-activated protein kinase 8
C: C-Jun-amino-terminal kinase-interacting protein 1
D: DD_232_11_D12
E: Mitogen-activated protein kinase 8
F: C-Jun-amino-terminal kinase-interacting protein 1
G: DD_232_11_D12
H: Mitogen-activated protein kinase 8
I: C-Jun-amino-terminal kinase-interacting protein 1
L: Pepstatin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)243,04137
Polymers239,93410
Non-polymers3,10727
Water00
1
A: DD_232_11_D12
B: Mitogen-activated protein kinase 8
C: C-Jun-amino-terminal kinase-interacting protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,68911
Polymers79,7493
Non-polymers9408
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4910 Å2
ΔGint-102 kcal/mol
Surface area31120 Å2
MethodPISA
2
D: DD_232_11_D12
E: Mitogen-activated protein kinase 8
F: C-Jun-amino-terminal kinase-interacting protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)80,78512
Polymers79,7493
Non-polymers1,0369
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4740 Å2
ΔGint-99 kcal/mol
Surface area30620 Å2
MethodPISA
3
G: DD_232_11_D12
H: Mitogen-activated protein kinase 8
I: C-Jun-amino-terminal kinase-interacting protein 1
L: Pepstatin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,56714
Polymers80,4354
Non-polymers1,13210
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5790 Å2
ΔGint-124 kcal/mol
Surface area30780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)219.990, 141.760, 119.850
Angle α, β, γ (deg.)90.00, 97.83, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 2 types, 6 molecules ADGBEH

#1: Protein DD_232_11_D12


Mass: 35248.953 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli K-12 (bacteria) / Variant (production host): XL1-Blue
#2: Protein Mitogen-activated protein kinase 8 / MAPK 8 / JNK-46 / Stress-activated protein kinase 1c / SAPK1c / Stress-activated protein kinase ...MAPK 8 / JNK-46 / Stress-activated protein kinase 1c / SAPK1c / Stress-activated protein kinase JNK1 / c-Jun N-terminal kinase 1


Mass: 43154.875 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C / Production host: Escherichia coli K-12 (bacteria) / Variant (production host): XL1-Blue
References: UniProt: P45983, mitogen-activated protein kinase

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Protein/peptide , 2 types, 4 molecules CFIL

#3: Protein/peptide C-Jun-amino-terminal kinase-interacting protein 1 / JNK-interacting protein 1 / Islet-brain 1 / IB-1 / JNK MAP kinase scaffold protein 1 / Mitogen- ...JNK-interacting protein 1 / Islet-brain 1 / IB-1 / JNK MAP kinase scaffold protein 1 / Mitogen-activated protein kinase 8-interacting protein 1


Mass: 1345.612 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9UQF2
#4: Protein/peptide Pepstatin


Type: Oligopeptide / Class: Enzyme inhibitor / Mass: 685.891 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: Pepstatin

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Non-polymers , 2 types, 27 molecules

#5: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-ADN / ADENOSINE


Mass: 267.241 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H13N5O4

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Details

Has protein modificationY

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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: 3.86 Å3/Da / Density % sol: 68.12 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: Lithium Sulfate 1.8 M Tris 0.1 M Additives (0.002% w/v) Adenosine, Pepstatin A Epinephrine Sodium phenyl phosphate dibasic dehydrate Inosine 5-triphosphate trisodium salt pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 5, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→49.383 Å / Num. obs: 58948 / % possible obs: 97.94 % / Redundancy: 7 % / CC1/2: 0.998 / Rmerge(I) obs: 0.1345 / Rpim(I) all: 0.05445 / Net I/σ(I): 11.27
Reflection shellResolution: 3.2→3.314 Å / Redundancy: 7.2 % / Rmerge(I) obs: 1.842 / Mean I/σ(I) obs: 1.13 / Num. unique obs: 5875 / CC1/2: 0.42 / Rpim(I) all: 0.7352 / % possible all: 98.46

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1SVX chain A and 1UKH

1svx

1ukh


Resolution: 3.2→49.383 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.73 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2124 2944 5 %
Rwork0.1753 --
obs0.1771 58926 97.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.2→49.383 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16102 0 177 0 16279
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00216587
X-RAY DIFFRACTIONf_angle_d0.49422485
X-RAY DIFFRACTIONf_dihedral_angle_d10.5399907
X-RAY DIFFRACTIONf_chiral_restr0.0412544
X-RAY DIFFRACTIONf_plane_restr0.0042870
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.2-3.25250.43511550.38182636X-RAY DIFFRACTION99
3.2525-3.30860.37811530.35252648X-RAY DIFFRACTION98
3.3086-3.36870.36071400.32022654X-RAY DIFFRACTION98
3.3687-3.43350.38161430.3012693X-RAY DIFFRACTION98
3.4335-3.50360.33071250.29312628X-RAY DIFFRACTION98
3.5036-3.57970.33931400.27542558X-RAY DIFFRACTION94
3.5797-3.6630.24331600.23322655X-RAY DIFFRACTION99
3.663-3.75450.22551290.20742710X-RAY DIFFRACTION99
3.7545-3.8560.25851690.19872669X-RAY DIFFRACTION99
3.856-3.96940.23011220.18862696X-RAY DIFFRACTION99
3.9694-4.09750.22561280.18212679X-RAY DIFFRACTION99
4.0975-4.24390.21661350.16742674X-RAY DIFFRACTION99
4.2439-4.41370.18851510.14982699X-RAY DIFFRACTION99
4.4137-4.61440.16281510.14242623X-RAY DIFFRACTION97
4.6144-4.85750.16371230.12932586X-RAY DIFFRACTION95
4.8575-5.16160.16851390.13632701X-RAY DIFFRACTION99
5.1616-5.55960.18361350.14242718X-RAY DIFFRACTION99
5.5596-6.11810.20661230.16142721X-RAY DIFFRACTION99
6.1181-7.00130.19971580.16452604X-RAY DIFFRACTION96
7.0013-8.81270.16541300.14172734X-RAY DIFFRACTION99
8.8127-49.38880.18421350.15342696X-RAY DIFFRACTION96
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)
10.95590.26361.95210.08870.64474.0455-0.5381-1.94981.09461.04880.22820.0884-0.0714-0.16930.51420.8853-0.02820.23170.8101-0.27341.2104204.2697.240230.216
27.3003-0.237-2.45062.80750.42154.5457-0.1482-0.60760.08820.2702-0.14030.03230.4890.06620.25510.6201-0.0567-0.09280.8772-0.15460.6406224.7486-2.963127.9972
33.48250.79681.16342.93063.45564.0864-0.21110.23240.2887-0.25220.2423-0.9179-0.41890.5536-0.20550.6485-0.0925-0.02390.98640.01820.8519243.6012-9.048512.9426
44.56250.65722.38724.02020.12298.629-0.04740.2313-0.22480.02640.25020.11980.30130.2419-0.26210.53390.02090.12630.68-0.01810.885230.8307-25.1994-6.4433
52.4638-0.7881-3.89667.2216-2.7888.7922-0.7287-0.5643-0.06820.1451-0.0411-1.41360.23711.56380.58151.0614-0.2624-0.28771.46860.14631.3406278.253511.692635.9807
66.436-0.18880.7226.29292.20955.4146-0.2264-0.3002-0.3377-0.10830.103-0.5868-0.31110.91270.24460.695-0.2223-0.1111.13870.25030.7467270.22214.882632.4744
74.9886-3.3966-0.6896.4179-0.721.881-0.1441-0.17240.33330.3714-0.0153-0.6986-0.47510.60660.16130.7639-0.2199-0.1010.86470.01090.6096262.055620.83126.0678
83.4571-0.7268-0.62222.724-1.81182.55330.1303-0.0072-0.142-0.2457-0.38060.1628-0.08270.14210.16940.9334-0.1316-0.09320.78120.00120.5866253.602518.278328.5055
95.3262.31830.22885.54340.28632.10670.2029-0.41010.05020.0595-0.21810.2905-0.2839-0.42780.04820.79780.055-0.04450.7273-0.04080.6175234.929818.223827.5132
105.15232.2661-0.93226.6451-1.12616.4240.2547-0.30271.10120.2442-0.28071.022-1.51740.16410.04881.1530.0461-0.10480.6623-0.0680.9521240.228936.073327.125
111.8718-1.81280.30797.1283-0.77013.84070.4190.41840.14-0.768-0.64120.092-0.30010.68530.2750.6168-0.13940.0340.86330.06010.684262.510315.604114.8143
123.6188-1.74242.78664.4208-5.79647.6314-0.46720.30632.03190.5002-0.9695-0.1971-2.83921.97971.80841.1527-0.4446-0.13591.1382-0.13130.8659259.012240.207633.6161
134.541-0.82512.3154.746-1.8155.90660.1232-0.2116-0.080.13690.2770.3187-0.30720.0088-0.41341.03880.11440.09690.79040.08610.6117281.3107-26.988849.6597
144.2763-2.7376-1.41792.89070.16320.92480.58890.6012-0.1906-1.3576-0.5124-0.06850.3614-0.1234-0.07131.54830.1324-0.06990.91130.04810.8469268.2551-12.689132.0444
152.4885-0.8949-1.30237.40121.85855.1691-0.0187-0.3325-0.04860.4936-0.04920.17930.23710.23950.00540.8038-0.0804-0.14020.87350.10160.5927251.7874.934347.3345
168.0999-2.47142.22366.2063-4.98588.49180.23350.4653-0.20040.30510.4780.4937-1.98770.0488-0.88291.65780.18530.10670.7136-0.14651.06289.6862-29.9317-6.7884
176.4783-3.15790.91155.31780.32337.36090.86260.0217-0.59810.2184-0.4207-0.1723-1.84780.1073-0.43881.62920.15040.0260.6511-0.0960.8421292.9514-26.08221.0384
183.67-1.1931.76385.2591-1.75082.44240.2355-0.34040.2753-1.96710.0160.7885-2.22320.0645-0.12242.35510.16840.25440.8982-0.2560.8112292.8877-14.82617.2676
195.6291-1.47122.01274.0809-0.52127.3166-0.03370.2420.085-1.04070.19910.5589-1.705-0.494-0.13641.78670.21510.03210.6726-0.1380.9391287.9113-22.4537-0.1558
206.3293-2.40140.54096.0232.18037.77350.28860.0679-0.3293-1.00340.0384-0.9337-0.71981.459-0.25651.4987-0.42890.22471.0439-0.18481.0141308.4224-20.231415.8247
213.7054-3.995-5.1146.24984.0999.13310.9202-0.74440.3251-0.2136-0.20110.6743-1.1937-0.3828-1.04141.3495-0.05670.13821.042-0.00881.1505292.7835-19.398817.3845
222.74421.72980.12932.34031.2658.87640.0798-0.333-0.23810.07110.2011-0.1719-0.76730.94-0.27110.906-0.07180.04441.0254-0.12180.9022300.3209-24.36929.4732
238.15540.4217-2.34885.13270.9557.20010.5777-0.71090.04780.6286-0.0537-0.233-0.93421.2044-0.48611.2721-0.13620.00321.1839-0.21820.603297.205-19.010444.4692
242.5187-2.2377-0.9664.94340.06072.2960.1653-0.62380.0899-0.17890.0909-0.7506-0.90721.2176-0.25391.2261-0.52280.01791.5911-0.35351.3165316.4456-17.738128.7815
257.1622-0.74522.6512.55951.72655.003-0.2171-0.66521.0411-0.625-0.23340.2089-2.2705-0.1560.41592.11760.16340.02651.05090.00011.1236291.3342-8.95339.495
265.23795.62-5.56756.2711-5.69416.2596-0.7259-1.305-0.8225-3.50471.2022-3.3113-0.44732.0012-0.69481.4-0.30920.34551.6866-0.19411.2976319.6066-22.68549.1081
272.83351.69693.07193.14292.34856.11490.0902-0.1617-0.1669-0.20620.2248-0.09050.4529-0.0919-0.39750.8650.1876-0.01150.87550.05541.4305259.2815-43.5705-2.7402
288.5078-1.0628-1.2055.43360.85634.99180.1003-0.2605-0.29370.04620.1225-0.23010.27580.3369-0.24340.690.1069-0.06970.6885-0.12470.8584288.5765-43.20519.5477
291.877-0.8268-0.50083.73110.9933.62190.00360.26880.44820.2299-0.1232-0.1029-0.08790.02710.12430.5521-0.08950.06730.77940.11920.9293242.688-3.3725-16.615
301.3215-0.8143-0.88725.34310.67761.36930.3550.2179-0.20760.2882-0.1491-0.21120.1560.6849-0.07470.5669-0.04560.12091.00030.05370.9465246.9072-15.3359-19.6478
315.0295-1.46152.22654.2763-2.04484.75180.35470.5073-0.4764-0.581-0.0477-0.39880.53520.2611-0.18210.80240.15210.14360.8658-0.15830.9022251.4248-30.9695-27.915
321.8278-0.4147-0.54722.36521.71824.5882-0.05620.46530.5486-0.3158-0.0589-0.575-0.23860.73630.0690.67120.0840.14371.02620.14051.0448256.8726-11.2544-24.0553
334.06192.2832-0.79351.9382-0.37747.06860.46752.51681.5758-0.3309-0.67250.39021.012-0.78620.24530.8760.32150.25341.52610.27661.1303237.6082-7.5924-40.8526
340.1055-0.48090.68212.1949-3.11124.4078-0.03352.28220.0713-0.28040.1196-0.7471-0.20330.82120.44661.1031-0.37481.00331.4907-0.18142.1403264.6813-28.463-10.6279
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 23 )
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 134 )
3X-RAY DIFFRACTION3chain 'A' and (resid 135 through 181 )
4X-RAY DIFFRACTION4chain 'A' and (resid 182 through 325 )
5X-RAY DIFFRACTION5chain 'B' and (resid 8 through 29 )
6X-RAY DIFFRACTION6chain 'B' and (resid 30 through 63 )
7X-RAY DIFFRACTION7chain 'B' and (resid 64 through 144 )
8X-RAY DIFFRACTION8chain 'B' and (resid 145 through 191 )
9X-RAY DIFFRACTION9chain 'B' and (resid 192 through 270 )
10X-RAY DIFFRACTION10chain 'B' and (resid 271 through 321 )
11X-RAY DIFFRACTION11chain 'B' and (resid 322 through 362 )
12X-RAY DIFFRACTION12chain 'C' and (resid 154 through 162 )
13X-RAY DIFFRACTION13chain 'D' and (resid 13 through 134 )
14X-RAY DIFFRACTION14chain 'D' and (resid 135 through 181 )
15X-RAY DIFFRACTION15chain 'D' and (resid 182 through 325 )
16X-RAY DIFFRACTION16chain 'E' and (resid 8 through 29 )
17X-RAY DIFFRACTION17chain 'E' and (resid 30 through 63 )
18X-RAY DIFFRACTION18chain 'E' and (resid 64 through 92 )
19X-RAY DIFFRACTION19chain 'E' and (resid 93 through 114 )
20X-RAY DIFFRACTION20chain 'E' and (resid 115 through 164 )
21X-RAY DIFFRACTION21chain 'E' and (resid 165 through 182 )
22X-RAY DIFFRACTION22chain 'E' and (resid 183 through 241 )
23X-RAY DIFFRACTION23chain 'E' and (resid 242 through 270 )
24X-RAY DIFFRACTION24chain 'E' and (resid 271 through 321 )
25X-RAY DIFFRACTION25chain 'E' and (resid 322 through 362 )
26X-RAY DIFFRACTION26chain 'F' and (resid 154 through 162 )
27X-RAY DIFFRACTION27chain 'G' and (resid 13 through 181 )
28X-RAY DIFFRACTION28chain 'G' and (resid 182 through 326 )
29X-RAY DIFFRACTION29chain 'H' and (resid 8 through 145 )
30X-RAY DIFFRACTION30chain 'H' and (resid 146 through 191 )
31X-RAY DIFFRACTION31chain 'H' and (resid 192 through 290 )
32X-RAY DIFFRACTION32chain 'H' and (resid 291 through 362 )
33X-RAY DIFFRACTION33chain 'I' and (resid 154 through 163 )
34X-RAY DIFFRACTION34chain 'L' and (resid 2 through 5 )

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