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- PDB-4fr4: Crystal structure of human serine/threonine-protein kinase 32A (YANK1) -

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Basic information

Entry
Database: PDB / ID: 4fr4
TitleCrystal structure of human serine/threonine-protein kinase 32A (YANK1)
ComponentsSerine/threonine-protein kinase 32A
KeywordsTRANSFERASE / Structural Genomics / Structural Genomics Consortium / SGC
Function / homology
Function and homology information


eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity ...eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / non-specific serine/threonine protein kinase / intracellular signal transduction / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / metal ion binding / plasma membrane
Similarity search - Function
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, ATP binding site / Protein kinases ATP-binding region signature. ...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, ATP binding site / Protein kinases ATP-binding region signature. / 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
STAUROSPORINE / Serine/threonine-protein kinase 32A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.29 Å
AuthorsChaikuad, A. / Elkins, J.M. / Krojer, T. / Mahajan, P. / Goubin, S. / Szklarz, M. / Tumber, A. / Wang, J. / Savitsky, P. / Shrestha, B. ...Chaikuad, A. / Elkins, J.M. / Krojer, T. / Mahajan, P. / Goubin, S. / Szklarz, M. / Tumber, A. / Wang, J. / Savitsky, P. / Shrestha, B. / Daga, N. / Picaud, S. / Fedorov, O. / Allerston, C.K. / Latwiel, S.V.A. / Vollmar, M. / Canning, P. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Knapp, S. / Structural Genomics Consortium (SGC)
CitationJournal: To be Published
Title: Crystal structure of human serine/threonine-protein kinase 32A (YANK1)
Authors: Chaikuad, A. / Elkins, J.M. / Krojer, T. / Mahajan, P. / Goubin, S. / Szklarz, M. / Tumber, A. / Wang, J. / Savitsky, P. / Shrestha, B. / Daga, N. / Picaud, S. / Fedorov, O. / Allerston, C.K. ...Authors: Chaikuad, A. / Elkins, J.M. / Krojer, T. / Mahajan, P. / Goubin, S. / Szklarz, M. / Tumber, A. / Wang, J. / Savitsky, P. / Shrestha, B. / Daga, N. / Picaud, S. / Fedorov, O. / Allerston, C.K. / Latwiel, S.V.A. / Vollmar, M. / Canning, P. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Knapp, S. / Structural Genomics Consortium (SGC)
History
DepositionJun 26, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 18, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 13, 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
Revision 1.2Nov 27, 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: Serine/threonine-protein kinase 32A
B: Serine/threonine-protein kinase 32A
C: Serine/threonine-protein kinase 32A
D: Serine/threonine-protein kinase 32A
E: Serine/threonine-protein kinase 32A
F: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)274,28520
Polymers270,9896
Non-polymers3,29614
Water18,0691003
1
A: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,6933
Polymers45,1651
Non-polymers5292
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,7554
Polymers45,1651
Non-polymers5913
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,8185
Polymers45,1651
Non-polymers6534
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,6312
Polymers45,1651
Non-polymers4671
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,6933
Polymers45,1651
Non-polymers5292
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: Serine/threonine-protein kinase 32A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,6933
Polymers45,1651
Non-polymers5292
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)154.110, 154.110, 112.110
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
12A
22B
32C
42D
52E
62F
13A
23B
33C
14D
24E
34F
15A
25E
16B
26C
17D
27F
18A
28B
38C
48D
58E
68F

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLUGLUILEILE3AA14 - 258 - 19
211GLUGLUILEILE3BB14 - 258 - 19
311GLUGLUILEILE3CC14 - 258 - 19
411GLUGLUILEILE3DD14 - 258 - 19
511GLUGLUILEILE3EE14 - 258 - 19
611GLUGLUILEILE3FF14 - 258 - 19
121LEULEUALAALA6AA26 - 2820 - 22
221LEULEUALAALA6BB26 - 2820 - 22
321LEULEUALAALA6CC26 - 2820 - 22
421LEULEUALAALA6DD26 - 2820 - 22
521LEULEUALAALA6EE26 - 2820 - 22
621LEULEUALAALA6FF26 - 2820 - 22
131ILEILEMETMET3AA29 - 5123 - 45
231ILEILEMETMET3BB29 - 5123 - 45
331ILEILEMETMET3CC29 - 5123 - 45
431ILEILEMETMET3DD29 - 5123 - 45
531ILEILEMETMET3EE29 - 5123 - 45
631ILEILEMETMET3FF29 - 5123 - 45
141ASNASNVALVAL3AA55 - 6549 - 59
241ASNASNVALVAL3BB55 - 6549 - 59
341ASNASNVALVAL3CC55 - 6549 - 59
441ASNASNVALVAL3DD55 - 6549 - 59
541ASNASNVALVAL3EE55 - 6549 - 59
641ASNASNVALVAL3FF55 - 6549 - 59
151ASNASNMETMET3AA67 - 7561 - 69
251ASNASNMETMET3BB67 - 7561 - 69
351ASNASNMETMET3CC67 - 7561 - 69
451ASNASNMETMET3DD67 - 7561 - 69
551ASNASNMETMET3EE67 - 7561 - 69
651ASNASNMETMET3FF67 - 7561 - 69
161GLYGLYPHEPHE2AA77 - 16571 - 159
261GLYGLYPHEPHE2BB77 - 16571 - 159
361GLYGLYPHEPHE2CC77 - 16571 - 159
461GLYGLYPHEPHE2DD77 - 16571 - 159
561GLYGLYPHEPHE2EE77 - 16571 - 159
661GLYGLYPHEPHE2FF77 - 16571 - 159
112ILEILETRPTRP2AA167 - 206161 - 200
212ILEILETRPTRP2BB167 - 206161 - 200
312ILEILETRPTRP2CC167 - 206161 - 200
412ILEILETRPTRP2DD167 - 206161 - 200
512ILEILETRPTRP2EE167 - 206161 - 200
612ILEILETRPTRP2FF167 - 206161 - 200
113TRPTRPLEULEU2AA207 - 305201 - 299
213TRPTRPLEULEU2BB207 - 305201 - 299
313TRPTRPLEULEU2CC207 - 305201 - 299
123CYSCYSLYSLYS4AA307 - 321301 - 315
223CYSCYSLYSLYS4BB307 - 321301 - 315
323CYSCYSLYSLYS4CC307 - 321301 - 315
114TRPTRPLYSLYS2DD207 - 321201 - 315
214TRPTRPLYSLYS2EE207 - 321201 - 315
314TRPTRPLYSLYS2FF207 - 321201 - 315
115LYSLYSVALVAL2AA339 - 355333 - 349
215LYSLYSVALVAL2EE339 - 355333 - 349
116LYSLYSVALVAL2BB339 - 355333 - 349
216LYSLYSVALVAL2CC339 - 355333 - 349
117ASPASPVALVAL2DD336 - 355330 - 349
217ASPASPVALVAL2FF336 - 355330 - 349
118GLNGLNPHEPHE2AA356 - 371350 - 365
218GLNGLNPHEPHE2BB356 - 371350 - 365
318GLNGLNPHEPHE2CC356 - 371350 - 365
418GLNGLNPHEPHE2DD356 - 371350 - 365
518GLNGLNPHEPHE2EE356 - 371350 - 365
618GLNGLNPHEPHE2FF356 - 371350 - 365

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

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.553822, 0.832274, 0.024518), (0.832459, -0.55407, 0.004288), (0.017153, 0.018036, -0.99969)-225.22955, 321.24414, -101.26797
3given(-0.478496, 0.877888, -0.018855), (-0.878071, -0.478516, 0.003688), (-0.005785, 0.01832, 0.999815)-239.15379, 218.81169, -78.3996
4given(-0.994528, 0.103675, 0.01286), (0.103688, 0.99461, 0.00035), (-0.012754, 0.001682, -0.999917)-98.70463, -36.47165, -135.70724
5given(0.422091, -0.90587, 0.035199), (-0.906388, -0.422437, -0.002677), (0.017294, -0.030774, -0.999377)158.27574, 253.5542, -165.21646
6given(-0.487039, -0.873325, -0.009849), (0.873281, -0.487123, 0.009609), (-0.013189, -0.003921, 0.999905)75.92924, 316.78668, -37.44228
DetailsTHE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS UNKNOWN.

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Components

#1: Protein
Serine/threonine-protein kinase 32A / YANK1


Mass: 45164.801 Da / Num. of mol.: 6 / Fragment: UNP residues 9-390
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: STK32A / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm)
References: UniProt: Q8WU08, non-specific serine/threonine protein kinase
#2: Chemical
ChemComp-STU / STAUROSPORINE


Mass: 466.531 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C28H26N4O3 / Comment: anticancer, antifungal, antibiotic, alkaloid*YM
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1003 / Source method: isolated from a natural source / Formula: H2O
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: 2.84 Å3/Da / Density % sol: 56.63 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.8
Details: 20% PEG 3350, 0.2M sodium acetate, 10% ethylene glycol, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9173 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jun 1, 2011 / Details: Kirkpatrick Baez bimorph mirror pair
RadiationMonochromator: Si (111) double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9173 Å / Relative weight: 1
ReflectionResolution: 2.29→51.68 Å / Num. all: 128341 / Num. obs: 128336 / % possible obs: 95.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 35.7 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 9.3
Reflection shellResolution: 2.29→2.41 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.638 / Mean I/σ(I) obs: 2 / Num. unique all: 19231 / % possible all: 97.8

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Processing

Software
NameVersionClassification
GDAdata collection
PHASERphasing
REFMAC5.6.0117refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3A8X, 3L9N and 3G51

3a8x

3l9n

3g51


Resolution: 2.29→50.44 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.929 / SU B: 14.251 / SU ML: 0.179 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 2 / ESU R: 0.296 / ESU R Free: 0.224 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24449 6421 5 %RANDOM
Rwork0.20436 ---
obs0.20636 121915 95.73 %-
all-128336 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 37.803 Å2
Baniso -1Baniso -2Baniso -3
1-1.95 Å20.97 Å20 Å2
2--1.95 Å20 Å2
3----2.92 Å2
Refine analyzeLuzzati coordinate error obs: 0.32 Å
Refinement stepCycle: LAST / Resolution: 2.29→50.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16848 0 242 1003 18093
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0217740
X-RAY DIFFRACTIONr_bond_other_d0.0020.0212046
X-RAY DIFFRACTIONr_angle_refined_deg1.4881.9624079
X-RAY DIFFRACTIONr_angle_other_deg0.7763.00129318
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.93352136
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.54524.539901
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.797153108
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.0881599
X-RAY DIFFRACTIONr_chiral_restr0.0820.22576
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0219629
X-RAY DIFFRACTIONr_gen_planes_other0.0030.023696
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A713MEDIUM POSITIONAL0.050.5
1B713MEDIUM POSITIONAL0.050.5
1C713MEDIUM POSITIONAL0.040.5
1D713MEDIUM POSITIONAL0.040.5
1E713MEDIUM POSITIONAL0.050.5
1F713MEDIUM POSITIONAL0.050.5
1A463LOOSE POSITIONAL0.045
1B463LOOSE POSITIONAL0.055
1C463LOOSE POSITIONAL0.045
1D463LOOSE POSITIONAL0.045
1E463LOOSE POSITIONAL0.045
1F463LOOSE POSITIONAL0.055
1A844TIGHT THERMAL2.80.5
1B844TIGHT THERMAL2.490.5
1C844TIGHT THERMAL2.360.5
1D844TIGHT THERMAL2.540.5
1E844TIGHT THERMAL3.170.5
1F844TIGHT THERMAL3.250.5
1A713MEDIUM THERMAL2.972
1B713MEDIUM THERMAL2.322
1C713MEDIUM THERMAL2.232
1D713MEDIUM THERMAL2.252
1E713MEDIUM THERMAL2.872
1F713MEDIUM THERMAL2.672
1A463LOOSE THERMAL3.3310
1B463LOOSE THERMAL3.1710
1C463LOOSE THERMAL3.1510
1D463LOOSE THERMAL3.5110
1E463LOOSE THERMAL4.1510
1F463LOOSE THERMAL3.7310
2A259MEDIUM POSITIONAL0.040.5
2B259MEDIUM POSITIONAL0.040.5
2C259MEDIUM POSITIONAL0.030.5
2D259MEDIUM POSITIONAL0.030.5
2E259MEDIUM POSITIONAL0.030.5
2F259MEDIUM POSITIONAL0.040.5
2A234TIGHT THERMAL1.880.5
2B234TIGHT THERMAL2.850.5
2C234TIGHT THERMAL4.420.5
2D234TIGHT THERMAL3.970.5
2E234TIGHT THERMAL20.5
2F234TIGHT THERMAL3.680.5
2A259MEDIUM THERMAL1.862
2B259MEDIUM THERMAL2.852
2C259MEDIUM THERMAL3.922
2D259MEDIUM THERMAL3.482
2E259MEDIUM THERMAL2.652
2F259MEDIUM THERMAL2.852
3A996MEDIUM POSITIONAL0.250.5
3B996MEDIUM POSITIONAL0.190.5
3C996MEDIUM POSITIONAL0.180.5
3A585TIGHT THERMAL1.410.5
3B585TIGHT THERMAL1.610.5
3C585TIGHT THERMAL1.740.5
3A996MEDIUM THERMAL2.432
3B996MEDIUM THERMAL1.962
3C996MEDIUM THERMAL2.372
4D818MEDIUM POSITIONAL0.030.5
4E818MEDIUM POSITIONAL0.030.5
4F818MEDIUM POSITIONAL0.030.5
4D668TIGHT THERMAL3.680.5
4E668TIGHT THERMAL2.720.5
4F668TIGHT THERMAL5.430.5
4D818MEDIUM THERMAL3.662
4E818MEDIUM THERMAL2.972
4F818MEDIUM THERMAL4.382
5A94MEDIUM POSITIONAL0.080.5
5A100TIGHT THERMAL1.590.5
5A94MEDIUM THERMAL2.652
6B101MEDIUM POSITIONAL0.040.5
6B102TIGHT THERMAL1.470.5
6B101MEDIUM THERMAL1.822
7D112MEDIUM POSITIONAL0.030.5
7D118TIGHT THERMAL1.820.5
7D112MEDIUM THERMAL3.142
8A146MEDIUM POSITIONAL0.040.5
8B146MEDIUM POSITIONAL0.040.5
8C146MEDIUM POSITIONAL0.040.5
8D146MEDIUM POSITIONAL0.030.5
8E146MEDIUM POSITIONAL0.040.5
8F146MEDIUM POSITIONAL0.080.5
8A94TIGHT THERMAL1.880.5
8B94TIGHT THERMAL2.10.5
8C94TIGHT THERMAL1.840.5
8D94TIGHT THERMAL3.140.5
8E94TIGHT THERMAL2.760.5
8F94TIGHT THERMAL2.330.5
8A146MEDIUM THERMAL3.092
8B146MEDIUM THERMAL2.142
8C146MEDIUM THERMAL2.032
8D146MEDIUM THERMAL3.342
8E146MEDIUM THERMAL4.832
8F146MEDIUM THERMAL3.422
LS refinement shellResolution: 2.29→2.349 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.318 473 -
Rwork0.309 9265 -
obs--98.01 %
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)
12.488-0.6529-1.07041.5031.24465.2619-0.08590.13310.1138-0.2350.16720.19330.1976-0.091-0.08140.1388-0.0520.00950.1128-0.00930.2126-69.6937164.8551-81.9262
21.5960.6547-0.35762.0782-0.14472.1657-0.11080.0210.1162-0.06350.127-0.1264-0.17010.2296-0.01630.0276-0.0152-0.00710.1021-0.01280.0274-53.7427182.8989-76.3823
36.359116.6536-2.684243.6938-7.0041.1479-1.18950.6132-1.2735-1.77561.1783-3.4760.405-0.28480.01131.0749-0.0158-0.19120.66220.07731.343-85.0496176.7384-88.1775
42.0622-0.05520.05063.59672.581810.6218-0.030.2488-0.05560.1685-0.00430.04181.1601-0.11770.03430.15710.00570.08840.15950.03250.3019-62.5892153.2771-84.3097
51.8028-0.3335-0.26823.1112.47746.227-0.0764-0.1631-0.28410.09170.17890.1540.1699-0.0211-0.10240.0496-0.01910.05260.1379-0.04650.2473-43.7665216.5087-16.2348
62.4883-0.16620.15731.14270.0331.93330.08440.0740.0291-0.0423-0.0752-0.1658-0.050.2861-0.00910.0467-0.02640.02220.1355-0.01020.032-19.6959219.9461-21.4631
715.6352-5.39133.21471.8729-1.12420.68740.3309-0.71720.8385-0.1601-0.0753-0.17150.0185-0.1639-0.25560.91210.02720.12650.8423-0.08131.5471-39.8542196.1322-10.5868
84.3096-0.436-2.81673.46321.469313.66570.15520.17710.01530.15620.01120.38910.1527-1.096-0.16640.08430.0196-0.03190.1274-0.05760.2902-50.6132228.2371-13.4476
91.70540.2152-0.97194.1641-2.10814.5509-0.06580.2439-0.2991-0.17290.079-0.12690.35880.0498-0.01320.09990.00010.08170.17390.01220.2492-33.5341174.3441-6.6393
102.5453-0.0428-0.02261.3304-0.10382.25230.03260.08190.0535-0.1095-0.02980.17110.0643-0.3762-0.00280.0324-0.0316-0.00520.1403-0.0050.0279-57.3888180.2833-1.5194
1112.76891.36741.21850.15480.14240.15310.4281-0.37150.68820.0178-0.2008-0.0075-0.05330.0738-0.22730.8787-0.22440.11830.5911-0.15161.1292-39.851154.8327-11.7564
123.42330.7791-4.86963.1932-1.965924.75820.0407-0.1870.0173-0.1078-0.1309-0.139-0.37430.85010.09020.013-0.0158-0.01240.13880.0690.2865-27.6256186.4265-8.2805
132.12270.7573-2.54081.6824-1.47887.0291-0.0553-0.11050.00970.20510.0225-0.24340.07890.23710.03280.14130.0210.0250.27510.05850.3065-8.6924203.3606-53.3557
142.0271-0.6422-0.52373.3843-0.27422.2073-0.06660.00570.04150.14690.07590.0741-0.2105-0.2775-0.00930.09460.01160.01710.25660.01280.0088-21.7854218.884-57.3616
150.34330.49830.04321.6632-0.22253.57170.030.0470.19620.06120.1316-0.0891-0.4179-0.2306-0.16160.26690.04780.03480.30230.03950.2886-21.8757228.9797-62.5679
161.6146-0.6594-0.14993.0735-4.677714.16240.01590.0125-0.2382-0.22550.17460.05680.8811-0.0138-0.19050.2562-0.11770.10350.2805-0.01680.3343-17.4737193.0344-51.197
174.5227-1.93823.30382.4274-0.50194.74-0.1903-0.41830.30150.28320.11880.1459-0.607-0.38080.07140.31510.0449-0.02140.1762-0.09030.3384-14.66241.9528-91.424
182.0591.0920.31262.88150.11112.4035-0.0193-0.2492-0.05950.2337-0.0185-0.04080.2053-0.33010.03780.072-0.034-0.00930.17750.00720.0094-20.9171221.9499-94.3981
191.8510.50560.14430.4976-0.03043.19920.0339-0.1269-0.05970.0630.03710.21920.1741-0.5362-0.0710.1326-0.12360.01550.29510.02960.1759-29.485216.8466-100.7689
204.48121.30065.76453.60033.632824.2619-0.21670.03870.0691-0.03330.0555-0.0452-0.38760.63320.16110.0262-0.0102-0.0510.11260.01810.2756-1.5066239.2175-89.3846
213.15050.8963.0190.93981.31056.5714-0.04790.25250.2675-0.14120.018-0.1509-0.3250.32050.02990.1963-0.0133-0.0720.11480.02480.2868-61.1131201.6192-44.2681
221.4179-0.67640.36142.16480.0922.41570.07550.0487-0.1574-0.0568-0.0434-0.00670.37350.2099-0.03210.1030.043-0.02990.0955-0.02010.0384-53.8281177.9433-38.9731
2310.6877-0.9669-7.06094.62144.85518.6031-0.3252-0.5835-0.20240.49480.1141-0.01360.71420.45570.21120.5886-0.026-0.07320.6716-0.08620.7681-42.3009201.1508-30.9035
243.0153-0.56663.5461.8309-0.871319.0102-0.1582-0.13360.050.08250.18640.1255-0.7008-0.725-0.02820.12710.0107-0.03620.1181-0.06370.2755-74.39200.0997-46.6696
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A14 - 66
2X-RAY DIFFRACTION2A67 - 308
3X-RAY DIFFRACTION3A309 - 322
4X-RAY DIFFRACTION4A333 - 373
5X-RAY DIFFRACTION5B14 - 66
6X-RAY DIFFRACTION6B67 - 306
7X-RAY DIFFRACTION7B307 - 321
8X-RAY DIFFRACTION8B332 - 373
9X-RAY DIFFRACTION9C14 - 66
10X-RAY DIFFRACTION10C67 - 305
11X-RAY DIFFRACTION11C306 - 321
12X-RAY DIFFRACTION12C338 - 373
13X-RAY DIFFRACTION13D14 - 66
14X-RAY DIFFRACTION14D67 - 224
15X-RAY DIFFRACTION15D225 - 321
16X-RAY DIFFRACTION16D336 - 373
17X-RAY DIFFRACTION17E14 - 65
18X-RAY DIFFRACTION18E66 - 226
19X-RAY DIFFRACTION19E227 - 321
20X-RAY DIFFRACTION20E339 - 372
21X-RAY DIFFRACTION21F14 - 66
22X-RAY DIFFRACTION22F67 - 299
23X-RAY DIFFRACTION23F300 - 321
24X-RAY DIFFRACTION24F336 - 373

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