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- PDB-3zrt: Crystal structure of human PSD-95 PDZ1-2 -

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Basic information

Entry
Database: PDB / ID: 3zrt
TitleCrystal structure of human PSD-95 PDZ1-2
ComponentsDISKS LARGE HOMOLOG 4
KeywordsSIGNALING PROTEIN
Function / homology
Function and homology information


LGI-ADAM interactions / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / neuroligin family protein binding / NrCAM interactions / synaptic vesicle maturation / positive regulation of neuron projection arborization / regulation of grooming behavior / receptor localization to synapse / vocalization behavior ...LGI-ADAM interactions / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / neuroligin family protein binding / NrCAM interactions / synaptic vesicle maturation / positive regulation of neuron projection arborization / regulation of grooming behavior / receptor localization to synapse / vocalization behavior / cerebellar mossy fiber / neuron spine / protein localization to synapse / Synaptic adhesion-like molecules / establishment or maintenance of epithelial cell apical/basal polarity / AMPA glutamate receptor clustering / cellular response to potassium ion / dendritic spine morphogenesis / Trafficking of AMPA receptors / negative regulation of receptor internalization / juxtaparanode region of axon / acetylcholine receptor binding / neuron projection terminus / RHO GTPases activate CIT / Assembly and cell surface presentation of NMDA receptors / NMDA selective glutamate receptor signaling pathway / Neurexins and neuroligins / Activation of Ca-permeable Kainate Receptor / neurotransmitter receptor localization to postsynaptic specialization membrane / cortical cytoskeleton / Negative regulation of NMDA receptor-mediated neuronal transmission / social behavior / Unblocking of NMDA receptors, glutamate binding and activation / locomotory exploration behavior / AMPA glutamate receptor complex / Signaling by ERBB4 / neuromuscular process controlling balance / Long-term potentiation / excitatory synapse / positive regulation of excitatory postsynaptic potential / positive regulation of synaptic transmission / D1 dopamine receptor binding / regulation of postsynaptic membrane neurotransmitter receptor levels / ionotropic glutamate receptor binding / dendrite cytoplasm / Ras activation upon Ca2+ influx through NMDA receptor / learning / PDZ domain binding / adherens junction / establishment of protein localization / regulation of long-term neuronal synaptic plasticity / synaptic membrane / postsynaptic density membrane / neuromuscular junction / cell-cell adhesion / kinase binding / endocytic vesicle membrane / cell junction / synaptic vesicle / nervous system development / positive regulation of cytosolic calcium ion concentration / RAF/MAP kinase cascade / protein-containing complex assembly / scaffold protein binding / protein phosphatase binding / chemical synaptic transmission / dendritic spine / postsynaptic membrane / neuron projection / postsynaptic density / synapse / protein-containing complex binding / protein kinase binding / glutamatergic synapse / endoplasmic reticulum / signal transduction / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Rhinovirus 14, subunit 4 - #60 / Rhinovirus 14, subunit 4 / Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site ...Rhinovirus 14, subunit 4 - #60 / Rhinovirus 14, subunit 4 / Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. / Guanylate kinase-like domain / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / Other non-globular / PDZ domain / Pdz3 Domain / PDZ domain / SH3 domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Special / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Disks large homolog 4
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.398 Å
AuthorsSorensen, P.L. / Kastrup, J.S. / Gajhede, M.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2012
Title: A High-Affinity, Dimeric Inhibitor of Psd-95 Bivalently Interacts with Pdz1-2 and Protects Against Ischemic Brain Damage.
Authors: Bach, A. / Clausen, B.H. / Moller, M. / Vestergaard, B. / Chi, C.N. / Round, A. / Sorensen, P.L. / Nissen, K.B. / Kastrup, J.S. / Gajhede, M. / Jemth, P. / Kristensen, A.S. / Lundstrom, P. / ...Authors: Bach, A. / Clausen, B.H. / Moller, M. / Vestergaard, B. / Chi, C.N. / Round, A. / Sorensen, P.L. / Nissen, K.B. / Kastrup, J.S. / Gajhede, M. / Jemth, P. / Kristensen, A.S. / Lundstrom, P. / Lambertsen, K.L. / Stromgaard, K.
History
DepositionJun 19, 2011Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 21, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop
Item: _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list
Revision 1.2Dec 20, 2023Group: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DISKS LARGE HOMOLOG 4
B: DISKS LARGE HOMOLOG 4
C: DISKS LARGE HOMOLOG 4
D: DISKS LARGE HOMOLOG 4


Theoretical massNumber of molelcules
Total (without water)85,3894
Polymers85,3894
Non-polymers00
Water00
1
A: DISKS LARGE HOMOLOG 4
C: DISKS LARGE HOMOLOG 4


Theoretical massNumber of molelcules
Total (without water)42,6952
Polymers42,6952
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: DISKS LARGE HOMOLOG 4
D: DISKS LARGE HOMOLOG 4


Theoretical massNumber of molelcules
Total (without water)42,6952
Polymers42,6952
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)112.150, 112.150, 196.130
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
32
42
13
23
33
14
24
34
44
15
25
35
16
26
36
46
17
27
18
28
38
48
19
29
110
210
310
410

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ -7:3 )
211CHAIN B AND (RESSEQ -7:3 )
112CHAIN A AND (RESSEQ 4:9 )
212CHAIN B AND (RESSEQ 4:9 )
312CHAIN C AND (RESSEQ 4:9 )
412CHAIN D AND (RESSEQ 4:9 )
113CHAIN A AND (RESSEQ 10:57 )
213CHAIN B AND (RESSEQ 10:57 )
313CHAIN C AND (RESSEQ 10:57 )
114CHAIN A AND (RESSEQ 58:66 )
214CHAIN B AND (RESSEQ 58:66 )
314CHAIN C AND (RESSEQ 58:66 )
414CHAIN D AND (RESSEQ 58:66 )
115CHAIN A AND (RESSEQ 67:86 )
215CHAIN B AND (RESSEQ 67:86 )
315CHAIN C AND (RESSEQ 67:86 )
116CHAIN A AND (RESSEQ 88:92 )
216CHAIN B AND (RESSEQ 88:92 )
316CHAIN C AND (RESSEQ 88:92 )
416CHAIN D AND (RESSEQ 88:92 )
117CHAIN A AND (RESSEQ 93:99 )
217CHAIN B AND (RESSEQ 93:99 )
118CHAIN A AND (RESSEQ 100:178 )
218CHAIN B AND (RESSEQ 100:178 )
318CHAIN C AND (RESSEQ 100:178 )
418CHAIN D AND (RESSEQ 100:178 )
119CHAIN A AND (RESSEQ 179:179 )
219CHAIN B AND (RESSEQ 179:179 )
1110CHAIN A AND (RESSEQ 180:187 )
2110CHAIN B AND (RESSEQ 180:187 )
3110CHAIN C AND (RESSEQ 180:187 )
4110CHAIN D AND (RESSEQ 180:187 )

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10

NCS oper:
IDCodeMatrixVector
1given(0.878148, 0.478117, 0.016137), (0.478046, -0.878296, 0.008278), (0.018131, 0.000445, -0.999836)-6.83139, 26.5973, 19.8615
2given(0.878148, 0.478117, 0.016137), (0.478046, -0.878296, 0.008278), (0.018131, 0.000445, -0.999836)-6.83139, 26.5973, 19.8615
3given(-0.513938, -0.686193, 0.514788), (-0.751825, 0.071339, -0.655492), (0.41307, -0.723913, -0.552561)-61.815, -11.3248, 46.1599
4given(-0.663541, 0.568581, -0.486239), (-0.72147, -0.314325, 0.616993), (0.197973, 0.760207, 0.618782)-65.4018, -22.5045, 22.1794
5given(0.888485, 0.458901, -0.002092), (0.458886, -0.88848, -0.005197), (-0.004244, 0.003658, -0.999984)-6.51625, 26.1868, 19.6697
6given(-0.437725, -0.739458, 0.511467), (-0.785329, 0.03746, -0.617944), (0.437784, -0.67216, -0.597115)-59.0497, -14.5356, 49.8447
7given(0.891557, 0.452828, 0.008548), (0.452651, -0.891528, 0.016904), (0.015276, -0.011202, -0.999821)-6.44304, 26.3939, 19.8307
8given(-0.527988, -0.662466, 0.531383), (-0.745032, 0.060991, -0.664235), (0.407623, -0.746605, -0.525761)-62.5621, -11.0456, 44.9251
9given(-0.676752, 0.58235, -0.450418), (-0.712288, -0.363225, 0.600595), (0.186153, 0.72728, 0.660613)-67.5719, -20.6265, 22.1949
10given(0.88002, 0.474751, 0.0133), (0.474447, -0.880038, 0.02079), (0.021574, -0.011986, -0.999695)-6.64562, 26.46, 19.9407
11given(-0.530087, -0.677758, 0.50956), (-0.737147, 0.071337, -0.671957), (0.419074, -0.731816, -0.537422)-62.4819, -10.5939, 45.8882
12given(0.888876, 0.457748, -0.019138), (0.456291, -0.888258, -0.05289), (-0.04121, 0.03828, -0.998417)-6.40826, 26.3994, 18.8313
13given(-0.519313, -0.6834, 0.513107), (-0.72424, 0.033226, -0.688747), (0.453641, -0.729288, -0.5122)-62.0343, -9.64369, 47.3374
14given(-0.696348, 0.604936, -0.386202), (-0.694786, -0.433295, 0.574045), (0.179921, 0.668063, 0.722025)-67.8071, -18.9254, 22.4473
15given(0.87939, 0.475936, -0.012566), (0.476073, -0.879321, 0.012195), (-0.005246, -0.016706, -0.999847)-6.79841, 26.4852, 19.7844
16given(-0.533114, -0.678428, 0.505495), (-0.706477, 0.028243, -0.707172), (0.465489, -0.734124, -0.49435)-62.5783, -8.0902, 47.7177
17given(-0.660206, 0.596066, -0.456984), (-0.732926, -0.378295, 0.565432), (0.16416, 0.708236, 0.686624)-66.4658, -21.6446, 21.0095
18given(0.879072, 0.476685, 0.002073), (0.476572, -0.878943, 0.01839), (0.010588, -0.015178, -0.999829)-6.70362, 26.5083, 19.8291
19given(-0.527852, -0.665354, 0.527899), (-0.747427, 0.068691, -0.660783), (0.403393, -0.743361, -0.533562)-62.4399, -11.1566, 44.9243
20given(-0.665914, 0.575722, -0.474451), (-0.721833, -0.336573, 0.604712), (0.188458, 0.74516, 0.639703)-66.008, -22.0293, 21.9513
21given(0.89639, 0.442406, 0.027609), (0.442401, -0.896793, 0.006606), (0.027682, 0.006293, -0.999597)-5.78042, 26.022, 19.8424
22given(-0.583085, -0.55817, 0.590304), (-0.750745, 0.092519, -0.654081), (0.310474, -0.824552, -0.47299)-64.3678, -11.1633, 38.0664
23given(-0.729671, 0.476449, -0.490486), (-0.663912, -0.321896, 0.674985), (0.16371, 0.818156, 0.551198)-67.1497, -19.3767, 18.943
24given(0.877441, 0.479642, -0.006334), (0.479573, -0.877445, -0.009969), (-0.01034, 0.005709, -0.99993)-6.89592, 26.6827, 19.2049
25given(0.88505, 0.465022, 0.021008), (0.465222, -0.885176, -0.005643), (0.015971, 0.014768, -0.999763)-6.55451, 26.4844, 19.6421
26given(-0.337578, -0.76012, 0.55521), (-0.834373, -0.031402, -0.550305), (0.435733, -0.649024, -0.623623)-58.3193, -17.0808, 50.0395
27given(-0.63193, 0.522624, -0.572301), (-0.771007, -0.348825, 0.532794), (0.078818, 0.777937, 0.62338)-64.857, -23.8943, 17.8998

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Components

#1: Protein
DISKS LARGE HOMOLOG 4 / POSTSYNAPTIC DENSITY PROTEIN 95 / PSD-95 / SYNAPSE-ASSOCIATED PROTEIN 90 / SAP-90 / SAP90


Mass: 21347.328 Da / Num. of mol.: 4 / Fragment: PDZ1-2, REISDUES 61-249
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P78352

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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: 2.5 Å3/Da / Density % sol: 51 % / Description: NONE
Crystal growpH: 4.5
Details: 0.1 M SODIUM ACETATE TRIHYDRATE PH 6.0, 2.0 M SODIUM FORMATE AND 5 % PEG 4000 (DROP SIZE: 1 UL SAMPLE AND 1UL RESERVOIR SOLUTION)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 1.03
DetectorType: MARRESEARCH / Detector: CCD / Date: Oct 3, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 3.4→50 Å / Num. obs: 16900 / % possible obs: 95 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Biso Wilson estimate: 49.14 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 4.3
Reflection shellResolution: 3.4→3.58 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 1.6 / % possible all: 97

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2I1N

2i1n


Resolution: 3.398→48.679 Å / SU ML: 0.62 / σ(F): 1.35 / Phase error: 23.21 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2638 861 5.1 %
Rwork0.2192 --
obs0.2214 16881 94.23 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 20.003 Å2 / ksol: 0.325 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-3.9291 Å20 Å20 Å2
2--3.9291 Å20 Å2
3----9.5579 Å2
Refinement stepCycle: LAST / Resolution: 3.398→48.679 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5311 0 0 0 5311
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0075398
X-RAY DIFFRACTIONf_angle_d0.9857284
X-RAY DIFFRACTIONf_dihedral_angle_d16.2861996
X-RAY DIFFRACTIONf_chiral_restr0.056825
X-RAY DIFFRACTIONf_plane_restr0.006954
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A94X-RAY DIFFRACTIONPOSITIONAL
12B94X-RAY DIFFRACTIONPOSITIONAL0.032
21A54X-RAY DIFFRACTIONPOSITIONAL
22B54X-RAY DIFFRACTIONPOSITIONAL0.031
23C54X-RAY DIFFRACTIONPOSITIONAL0.038
24D54X-RAY DIFFRACTIONPOSITIONAL0.029
31A344X-RAY DIFFRACTIONPOSITIONAL
32B344X-RAY DIFFRACTIONPOSITIONAL0.031
33C344X-RAY DIFFRACTIONPOSITIONAL0.032
41A72X-RAY DIFFRACTIONPOSITIONAL
42B72X-RAY DIFFRACTIONPOSITIONAL0.034
43C72X-RAY DIFFRACTIONPOSITIONAL0.029
44D72X-RAY DIFFRACTIONPOSITIONAL0.037
51A144X-RAY DIFFRACTIONPOSITIONAL
52B144X-RAY DIFFRACTIONPOSITIONAL0.03
53C144X-RAY DIFFRACTIONPOSITIONAL0.033
61A46X-RAY DIFFRACTIONPOSITIONAL
62B46X-RAY DIFFRACTIONPOSITIONAL0.036
63C46X-RAY DIFFRACTIONPOSITIONAL0.057
64D46X-RAY DIFFRACTIONPOSITIONAL0.047
71A57X-RAY DIFFRACTIONPOSITIONAL
72B57X-RAY DIFFRACTIONPOSITIONAL0.036
81A579X-RAY DIFFRACTIONPOSITIONAL
82B579X-RAY DIFFRACTIONPOSITIONAL0.041
83C579X-RAY DIFFRACTIONPOSITIONAL0.051
84D579X-RAY DIFFRACTIONPOSITIONAL0.046
91A8X-RAY DIFFRACTIONPOSITIONAL
92B8X-RAY DIFFRACTIONPOSITIONAL0.023
101A64X-RAY DIFFRACTIONPOSITIONAL
102B64X-RAY DIFFRACTIONPOSITIONAL0.04
103C64X-RAY DIFFRACTIONPOSITIONAL0.045
104D64X-RAY DIFFRACTIONPOSITIONAL0.047
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.398-3.61080.31471370.27082653X-RAY DIFFRACTION95
3.6108-3.88950.27441620.23412622X-RAY DIFFRACTION95
3.8895-4.28070.26991570.20442636X-RAY DIFFRACTION95
4.2807-4.89970.22831400.17772654X-RAY DIFFRACTION94
4.8997-6.17110.2431290.20292686X-RAY DIFFRACTION94
6.1711-48.68360.25871360.23372769X-RAY DIFFRACTION91
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)
10.6281-0.48470.38952.15021.3569-0.745-0.04540.69230.08150.0820.34430.02580.6898-0.5039-0.09490.34190.08210.06530.52940.01390.2667-30.191912.564818.6235
21.34980.38880.4271.5747-0.926-0.8586-0.4055-0.54470.1983-1.03910.1377-0.11580.2514-0.22350.2840.36210.10.13910.2027-0.02750.3021-27.27141.16530.6359
30.0277-0.00030.00380.1073-0.0240.1014-0.1317-0.21970.21980.03320.36390.13630.23580.0740.04940.35390.07910.11380.21980.07270.1636-17.15016.279528.2277
4-0.00440.032-0.05350.0836-0.11580.12050.0653-0.1073-0.0427-0.1569-0.0496-0.14-0.0399-0.05480.11340.2679-0.04750.04530.22340.25010.2542-18.708812.7224-8.9046
50.93320.2388-0.80710.14410.090.40970.252-0.7136-0.0915-0.16340.12390.092-0.2990.1298-0.06680.17380.0520.04230.27930.06090.4405-43.6045-16.527521.306
60.4882-0.4658-1.19321.09980.3522-1.8623-0.08980.4380.35890.2197-0.2054-0.0357-0.0278-0.11650.19770.9739-0.2471-0.25661.13210.27810.6637-51.573823.0891-2.0249
7-0.44080.5481-0.35290.66920.32290.2532-0.0036-0.0379-0.0142-0.19050.186-0.2984-0.06420.2045-0.07710.0835-0.05050.06340.1497-0.14840.2944-11.211415.540221.819
80.3272-0.40050.1172-0.55090.19861.4298-0.225-0.11730.194-0.0308-0.1731-0.3373-0.94860.1268-0.60080.144-0.13680.15710.134-0.08850.265-9.17967.3976-2.2696
91.3790.3426-0.17541.3424-0.46980.56390.3249-0.47880.2410.613-0.26750.5485-0.1345-0.2619-0.28860.2351-0.11310.15330.33690.04550.3919-56.3023-15.148521.6987
100.42730.22070.40110.51121.08340.94010.1977-0.505-0.10730.13450.2137-0.21750.2199-0.1715-0.13850.3304-0.10770.05520.1123-0.02860.1344-20.673916.323329.7174
110.28240.1865-0.09620.233-0.24991.08820.35330.27060.4314-0.52470.27060.2965-0.71090.1108-0.23630.4478-0.20240.1548-0.01930.1791-0.02-16.97912.1032-10.1386
12-0.39920.7209-0.71230.4194-0.09510.77260.19020.4607-0.12330.19070.13890.39180.0694-0.2718-0.14110.08820.0781-0.07390.2454-0.06240.2458-48.793-14.710512.0245
13-0.6964-1.5504-0.95030.8109-0.61390.1856-0.0587-0.3442-0.7969-0.19790.34120.58550.1-1.1493-0.1921-0.6527-0.2166-0.39261.8168-0.03010.3299-56.375819.00556.7116
14-0.3564-0.16550.0268-0.2266-1.03670.83360.6043-0.2410.5678-0.01050.01970.0406-0.1035-0.22870.0969-0.3212-0.4701-0.0270.0244-0.11880.3482-16.309222.715228.1548
150.5477-0.06140.49761.2483-0.64620.49920.5474-0.1653-0.5209-0.29770.0233-0.6853-0.1739-0.0507-0.0252-0.2043-0.11120.27970.0588-0.0180.2874-10.1736-1.3262-8.5512
160.54070.7423-0.62760.4252-0.73110.84960.23590.66260.6322-0.07110.44610.8567-0.195-0.6685-0.3527-0.4033-0.1010.0250.37810.18580.2171-56.3552-16.029610.8446
17-3.8655-0.9556-1.812-1.972-3.9471-1.01860.0669-0.42890.5599-0.21770.198-0.16780.5838-0.22140.05650.2210.04550.0710.3946-0.08440.2012-18.42028.919925.3333
18-1.5132-3.77641.20892.1792-3.6034-0.4572-0.67660.3851-0.73150.17190.42-0.51560.1054-0.37480.2970.4762-0.20160.18730.1549-0.00780.3305-18.69669.7785-5.9676
19-0.3399-0.3028-1.6715-1.7946-1.4443-2.4367-0.05611.26120.3961-0.7296-0.0109-0.10550.41640.1603-0.28860.1085-0.0067-0.51690.3879-0.0458-0.8607-46.1408-13.29220.4249
202.86932.2244-3.4688-9.0253-2.28151.1127-0.5675-1.50830.47530.72220.6834-0.2697-1.2394-0.7843-0.25921.25770.0847-0.3321.30180.1410.7179-53.343419.4629-1.5946
21-0.15130.1724-0.09480.42840.18620.0001-0.1892-0.19490.4565-0.0965-0.64450.37350.27760.0341-0.03590.1825-0.1706-0.1131-0.4989-0.8914-0.6281-17.4778-3.37212.8736
220.3380.1578-0.04190.0179-0.3883-0.005-0.38730.2637-0.53710.2059-0.24430.2236-0.3067-0.432-0.0528-0.04540.07920.20020.2485-0.05630.0261-23.60521.36256.62
230.1966-0.1108-0.0120.29530.07290.64720.0605-0.17180.12310.09090.0390.05350.18110.03910.30820.2052-0.040.01510.00870.0480.0369-31.4378-14.07179.8097
240.368-0.2681-0.28180.3637-0.00860.890.7629-0.93440.25520.2649-0.2868-0.2414-0.2222-0.51240.3489-0.30420.7367-0.1793-0.4740.29270.018-41.05924.18839.4598
250.6218-0.8359-0.25822.6530.52480.6674-0.1934-0.10570.14190.89380.5825-0.17240.2464-0.5210.04730.09370.0347-0.0678-0.0588-0.15220.0923-29.0945.596338.2925
261.04410.6529-1.0454.00581.01980.9315-0.13080.39550.138-0.91280.3495-0.4567-0.6741-0.3023-0.00910.3102-0.06650.01030.17730.03130.0794-29.32837.7317-18.9379
277.17451.99895.28341.99952.00067.6769-0.2347-0.08780.0733-0.139-0.32750.4407-0.3083-0.33190.51690.03650.0428-0.59520.31950.0049-0.0117-37.0569-22.0086-3.1914
289.50031.9964-3.90152.00741.99957.2738-0.1131-0.1737-0.07930.15370.11450.0626-0.0849-0.4591-0.030.2008-0.12480.19720.76620.43291.0185-49.792428.346122.5455
292.90350.95921.8192.94542.14763.5045-0.88630.10520.3543-0.43970.90880.282-0.06330.03090.07840.98350.2269-0.34420.5264-0.04780.3232-24.864918.20746.9812
303.65031.88324.46479.73730.27515.4540.48360.5153-1.3119-1.35190.26440.3011-0.06040.1137-0.72771.07510.3030.170.5817-0.3180.5264-19.3961-1.9222-26.914
310.1387-0.10750.0584-0.0755-0.1980.7713-0.2462-0.1104-0.3957-0.4166-0.19730.19660.1535-0.0779-0.0584-0.2107-0.0321-0.14450.15260.0107-0.0044-27.2188-13.7292.891
32-0.61160.20121.04350.1598-0.37580.719-0.2854-0.19380.0454-0.103-0.30120.01750.0637-0.2453-0.2764-0.3492-0.00610.68330.13490.2297-0.5907-37.124725.656416.5002
330.2643-0.30490.7551.3568-1.1918-1.0271-0.4409-0.54940.02310.24170.4562-0.0710.3566-0.2571-0.06050.38590.01630.07510.19670.03740.0926-33.96986.976944.7697
341.3715-1.7353-0.08633.2981-2.1566-5.68660.0630.4506-0.2684-0.78951.12930.2198-0.1637-0.37650.00840.71190.0139-0.4840.3680.0057-0.2319-32.74094.2297-25.5025
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID -7:3
2X-RAY DIFFRACTION2CHAIN B AND RESID -7:3
3X-RAY DIFFRACTION3CHAIN A AND RESID 4:9
4X-RAY DIFFRACTION4CHAIN B AND RESID 4:9
5X-RAY DIFFRACTION5CHAIN C AND RESID 4:9
6X-RAY DIFFRACTION6CHAIN D AND RESID 4:9
7X-RAY DIFFRACTION7CHAIN A AND RESID 10:57
8X-RAY DIFFRACTION8CHAIN B AND RESID 10:57
9X-RAY DIFFRACTION9CHAIN C AND RESID 10:57
10X-RAY DIFFRACTION10CHAIN A AND RESID 58:66
11X-RAY DIFFRACTION11CHAIN B AND RESID 58:66
12X-RAY DIFFRACTION12CHAIN C AND RESID 58:66
13X-RAY DIFFRACTION13CHAIN D AND RESID 58:66
14X-RAY DIFFRACTION14CHAIN A AND RESID 67:86
15X-RAY DIFFRACTION15CHAIN B AND RESID 67:86
16X-RAY DIFFRACTION16CHAIN C AND RESID 67:86
17X-RAY DIFFRACTION17CHAIN A AND RESID 88:92
18X-RAY DIFFRACTION18CHAIN B AND RESID 88:92
19X-RAY DIFFRACTION19CHAIN C AND RESID 88:92
20X-RAY DIFFRACTION20CHAIN D AND RESID 88:92
21X-RAY DIFFRACTION21CHAIN A AND RESID 93:99
22X-RAY DIFFRACTION22CHAIN B AND RESID 93:99
23X-RAY DIFFRACTION23CHAIN A AND RESID 100:178
24X-RAY DIFFRACTION24CHAIN B AND RESID 100:178
25X-RAY DIFFRACTION25CHAIN C AND RESID 100:178
26X-RAY DIFFRACTION26CHAIN D AND RESID 100:178
27X-RAY DIFFRACTION27CHAIN A AND RESID 179
28X-RAY DIFFRACTION28CHAIN B AND RESID 179
29X-RAY DIFFRACTION29CHAIN C AND RESID 179
30X-RAY DIFFRACTION30CHAIN D AND RESID 179
31X-RAY DIFFRACTION31CHAIN A AND RESID 180:187
32X-RAY DIFFRACTION32CHAIN B AND RESID 180:187
33X-RAY DIFFRACTION33CHAIN C AND RESID 180:187
34X-RAY DIFFRACTION34CHAIN D AND RESID 180:187

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