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- PDB-3qhw: Structure of a pCDK2/CyclinA transition-state mimic -

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Basic information

Entry
Database: PDB / ID: 3qhw
TitleStructure of a pCDK2/CyclinA transition-state mimic
Components
  • CDK2 substrate peptide: PKTPKKAKKL
  • Cell division protein kinase 2
  • Cyclin-A2
KeywordsTRANSFERASE/PROTEIN BINDING / kinase catalytic domain / protein kinase / Cyclin / Phosphorylated Thr-160 / Phosphorylated on Thr-160 / TRANSFERASE-PROTEIN BINDING complex
Function / homology
Function and homology information


G0 and Early G1 / Telomere Extension By Telomerase / Regulation of APC/C activators between G1/S and early anaphase / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / G2 Phase / p53-Dependent G1 DNA Damage Response / Cyclin A:Cdk2-associated events at S phase entry / Cyclin A/B1/B2 associated events during G2/M transition / DNA Damage/Telomere Stress Induced Senescence / Regulation of TP53 Degradation ...G0 and Early G1 / Telomere Extension By Telomerase / Regulation of APC/C activators between G1/S and early anaphase / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / G2 Phase / p53-Dependent G1 DNA Damage Response / Cyclin A:Cdk2-associated events at S phase entry / Cyclin A/B1/B2 associated events during G2/M transition / DNA Damage/Telomere Stress Induced Senescence / Regulation of TP53 Degradation / Processing of DNA double-strand break ends / Senescence-Associated Secretory Phenotype (SASP) / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / CDK-mediated phosphorylation and removal of Cdc6 / Orc1 removal from chromatin / cyclin A2-CDK1 complex / cell cycle G1/S phase transition / cellular response to luteinizing hormone stimulus / Regulation of TP53 Activity through Phosphorylation / mitotic cell cycle phase transition / Ub-specific processing proteases / cellular response to leptin stimulus / male pronucleus / female pronucleus / cellular response to cocaine / response to glucagon / cyclin-dependent protein serine/threonine kinase regulator activity / cellular response to insulin-like growth factor stimulus / positive regulation of DNA biosynthetic process / cochlea development / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cellular response to platelet-derived growth factor stimulus / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / G2 Phase / cyclin-dependent protein kinase activity / Y chromosome / Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes / positive regulation of heterochromatin formation / p53-Dependent G1 DNA Damage Response / X chromosome / PTK6 Regulates Cell Cycle / regulation of anaphase-promoting complex-dependent catabolic process / regulation of DNA replication / Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / centrosome duplication / Telomere Extension By Telomerase / G0 and Early G1 / Activation of the pre-replicative complex / cyclin-dependent protein kinase holoenzyme complex / cellular response to nitric oxide / Cajal body / cyclin-dependent kinase / animal organ regeneration / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Activation of ATR in response to replication stress / Cyclin E associated events during G1/S transition / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / condensed chromosome / mitotic G1 DNA damage checkpoint signaling / regulation of mitotic cell cycle / regulation of G2/M transition of mitotic cell cycle / cyclin binding / post-translational protein modification / meiotic cell cycle / positive regulation of DNA replication / male germ cell nucleus / response to organic substance / cellular response to estradiol stimulus / G1/S transition of mitotic cell cycle / potassium ion transport / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / SCF(Skp2)-mediated degradation of p27/p21 / Meiotic recombination / Orc1 removal from chromatin / Transcriptional regulation of granulopoiesis / Cyclin D associated events in G1 / G2/M transition of mitotic cell cycle / positive regulation of fibroblast proliferation / cellular senescence / Regulation of TP53 Degradation / nuclear envelope / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / cellular response to hypoxia / Senescence-Associated Secretory Phenotype (SASP) / regulation of gene expression / peptidyl-serine phosphorylation / Ras protein signal transduction / Regulation of TP53 Activity through Phosphorylation / transcription regulator complex / DNA replication
Similarity search - Function
Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin-like ...Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin, C-terminal domain / Cyclin_C / Cyclin-like / Cyclin A; domain 1 / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; 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
ADENOSINE-5'-DIPHOSPHATE / (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL / TRIFLUOROMAGNESATE / Cyclin-dependent kinase 2 / Cyclin-A2
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.91 Å
AuthorsYoung, M.A. / Jacobsen, D.M. / Bao, Z.Q.
CitationJournal: Structure / Year: 2011
Title: Briefly Bound to Activate: Transient Binding of a Second Catalytic Magnesium Activates the Structure and Dynamics of CDK2 Kinase for Catalysis.
Authors: Bao, Z.Q. / Jacobsen, D.M. / Young, M.A.
History
DepositionJan 26, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 25, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 3, 2024Group: 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 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cell division protein kinase 2
B: Cyclin-A2
C: Cell division protein kinase 2
D: Cyclin-A2
J: CDK2 substrate peptide: PKTPKKAKKL
K: CDK2 substrate peptide: PKTPKKAKKL
L: CDK2 substrate peptide: PKTPKKAKKL
M: CDK2 substrate peptide: PKTPKKAKKL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,70320
Polymers132,2098
Non-polymers1,49412
Water14,286793
1
A: Cell division protein kinase 2
B: Cyclin-A2
J: CDK2 substrate peptide: PKTPKKAKKL
L: CDK2 substrate peptide: PKTPKKAKKL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,85110
Polymers66,1054
Non-polymers7476
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7260 Å2
ΔGint-67 kcal/mol
Surface area23260 Å2
MethodPISA
2
C: Cell division protein kinase 2
D: Cyclin-A2
K: CDK2 substrate peptide: PKTPKKAKKL
M: CDK2 substrate peptide: PKTPKKAKKL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,85110
Polymers66,1054
Non-polymers7476
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7170 Å2
ΔGint-66 kcal/mol
Surface area23390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.025, 163.450, 73.390
Angle α, β, γ (deg.)90.00, 107.08, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq -1:296 ) and not (resseq 10:18)...
211chain C
112chain B and (resseq 172:432 )
212chain D
113chain J and (resseq -2:7) and not (resseq 0:1)
213chain K
114chain L and (resseq 4:7 )
214chain M

NCS ensembles :
ID
1
2
3
4

NCS oper:
IDCodeMatrixVector
1given(0.830725, 0.014354, 0.556498), (0.014899, -0.999883, 0.003551), (0.556484, 0.005342, -0.830841)26.943399, -111.115997, -85.304398
2given(0.830817, 0.02069, 0.556161), (0.022324, -0.999743, 0.003843), (0.556098, 0.009222, -0.831066)27.100599, -110.924004, -85.2006
3given(0.829614, -0.007753, 0.558283), (-0.008594, -0.999962, -0.001117), (0.558271, -0.003871, -0.82965)26.369499, -111.711998, -85.396301
4given(0.824094, 0.019955, 0.566102), (0.026147, -0.999654, -0.002826), (0.565849, 0.017131, -0.824331)27.909599, -111.321999, -84.241302

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Cell division protein kinase 2 / / p33 protein kinase


Mass: 33981.312 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDK2 / Production host: Escherichia coli (E. coli) / References: UniProt: P24941, cyclin-dependent kinase
#2: Protein Cyclin-A2 / Cyclin-A


Mass: 29836.354 Da / Num. of mol.: 2 / Fragment: UNP Residues 163-422
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ccna2, Ccna, Cyca / Production host: Escherichia coli (E. coli) / References: UniProt: P51943

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Protein/peptide , 1 types, 4 molecules JKLM

#3: Protein/peptide
CDK2 substrate peptide: PKTPKKAKKL


Mass: 1143.483 Da / Num. of mol.: 4 / Source method: obtained synthetically / Details: optimal CDK2 kinase substrate

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Non-polymers , 6 types, 805 molecules

#4: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-MGF / TRIFLUOROMAGNESATE


Mass: 81.300 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: F3Mg
#7: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-DTU / (2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL / Dithioerythritol


Mass: 154.251 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O2S2
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 793 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.08 Å3/Da / Density % sol: 60.07 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.25
Details: 22% w/v Poly(acrylic acid sodium salt) 5100, 20mM MgCl2, 100mM HEPES pH 8.25, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 23, 2010
RadiationMonochromator: Kohzu / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionRedundancy: 7.6 % / Av σ(I) over netI: 4.1 / Number: 935489 / Rsym value: 0.14 / D res high: 1.908 Å / D res low: 39.74 Å / Num. obs: 123388 / % possible obs: 100
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsRsym valueRedundancy
6.0439.7399.610.0560.0567.5
4.276.0410010.0670.0677.7
3.494.2710010.0730.0737.7
3.023.4910010.1040.1047.6
2.73.0210010.1630.1637.6
2.472.710010.2620.2627.6
2.282.4710010.4040.4047.6
2.142.2810010.620.627.6
2.012.1410010.9250.9257.5
1.912.0110011.4131.4137.5
ReflectionResolution: 1.908→39.74 Å / Num. all: 123388 / Num. obs: 123388 / % possible obs: 100 % / Observed criterion σ(F): 1.5 / Observed criterion σ(I): 1.5 / Redundancy: 7.6 % / Rsym value: 0.14 / Net I/σ(I): 8.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsRsym valueDiffraction-ID% possible all
1.908-2.017.50.0140.51.4131100
2.01-2.147.50.0140.80.9251100
2.14-2.287.60.0141.10.621100
2.28-2.477.60.0141.80.4041100
2.47-2.77.60.0142.70.2621100
2.7-3.027.60.0144.30.1631100
3.02-3.497.60.0146.30.1041100
3.49-4.277.70.0148.30.0731100
4.27-6.047.70.0148.70.0671100
6.04-39.7267.50.0148.80.056199.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
MOSFLMdata reduction
SCALA3.3.16data scaling
PHASERphasing
PHENIX1.7.1_743refinement
PDB_EXTRACT3.1data extraction
MAR345dtbdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: UNPUBLISHED MODEL

Resolution: 1.91→39.726 Å / Occupancy max: 1 / Occupancy min: 0.48 / SU ML: 0.66 / σ(F): 0 / Phase error: 24.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2187 2401 1.95 %
Rwork0.188 --
obs0.1886 123234 99.82 %
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 61.71 Å2 / ksol: 0.38 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-9.9122 Å20 Å28.0538 Å2
2---6.7353 Å2-0 Å2
3----3.1769 Å2
Refinement stepCycle: LAST / Resolution: 1.91→39.726 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9210 0 84 793 10087
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.019587
X-RAY DIFFRACTIONf_angle_d1.26613016
X-RAY DIFFRACTIONf_dihedral_angle_d13.9233594
X-RAY DIFFRACTIONf_chiral_restr0.0911475
X-RAY DIFFRACTIONf_plane_restr0.0071624
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2282X-RAY DIFFRACTIONPOSITIONAL
12C2282X-RAY DIFFRACTIONPOSITIONAL0.072
21B2099X-RAY DIFFRACTIONPOSITIONAL
22D2099X-RAY DIFFRACTIONPOSITIONAL0.154
31J65X-RAY DIFFRACTIONPOSITIONAL
32K65X-RAY DIFFRACTIONPOSITIONAL0.552
41L31X-RAY DIFFRACTIONPOSITIONAL
42M31X-RAY DIFFRACTIONPOSITIONAL0.035
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.91-1.9490.41151600.37556893X-RAY DIFFRACTION97
1.949-1.99140.34851240.33617122X-RAY DIFFRACTION100
1.9914-2.03770.32021380.30337126X-RAY DIFFRACTION100
2.0377-2.08870.31491330.26397120X-RAY DIFFRACTION100
2.0887-2.14510.27251430.23987089X-RAY DIFFRACTION100
2.1451-2.20820.26371440.2247071X-RAY DIFFRACTION100
2.2082-2.27950.24961480.20837129X-RAY DIFFRACTION100
2.2795-2.3610.26221320.19817115X-RAY DIFFRACTION100
2.361-2.45550.2231450.19097082X-RAY DIFFRACTION100
2.4555-2.56720.20911440.17957079X-RAY DIFFRACTION100
2.5672-2.70260.21291370.16927151X-RAY DIFFRACTION100
2.7026-2.87180.18931410.15357106X-RAY DIFFRACTION100
2.8718-3.09350.20691440.16167134X-RAY DIFFRACTION100
3.0935-3.40460.22481410.16747121X-RAY DIFFRACTION100
3.4046-3.89690.19991410.16837136X-RAY DIFFRACTION100
3.8969-4.90830.1581430.14957154X-RAY DIFFRACTION100
4.9083-39.73410.21041430.19667205X-RAY DIFFRACTION100
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)
11.3836-0.62870.31885.5355-3.63962.40440.1951-0.208-0.31330.95150.2880.92991.0157-0.377-0.38270.8169-0.024-0.24180.25120.03120.4758-19.4139-66.1019-68.8677
25.3469-0.698-3.0053.91880.96538.476-0.25940.119-0.0182-0.97040.26630.21260.6456-0.9257-0.11370.3987-0.0315-0.11910.31760.00260.2323-16.7385-61.1983-66.2717
33.59372.612-5.09692.0021-4.09572.00150.23981.364-0.1228-1.60680.03562.05650.157-2.3992-0.10960.5166-0.0658-0.19750.6797-0.08140.4896-24.2988-74.7124-52.624
42.5982-0.3805-1.05852.32520.46634.18590.04680.120.0386-0.326-0.03360.068-0.1514-0.106-0.01370.2788-0.0313-0.0210.1229-0.0020.1419-4.6866-74.5648-64.9151
52.59251.2706-0.00894.344-0.02191.91640.00140.0671-0.1655-0.27650.0318-0.07920.09690.1339-0.04440.30650.0090.02630.1665-0.03040.15911.2856-93.2084-68.6506
61.2904-1.7818-1.47235.8193.50413.2524-0.15210.6709-0.4848-0.3726-0.0361-0.19720.35320.4002-0.03150.22270.00740.04080.2804-0.06640.22727.3609-75.2093-47.7656
72.3303-0.2377-0.98063.59610.36022.9016-0.125-0.0286-0.08350.18880.08140.20310.0931-0.01020.03220.1280.0172-0.00380.11460.01840.1463-15.832-71.8321-36.8843
83.12160.4952-0.37573.5603-1.21993.217-0.2034-0.3373-0.22490.18180.1361-0.30170.14380.28230.02990.18140.0727-0.03480.2305-0.00210.19156.337-80.5956-30.4887
94.0235-0.59620.38243.83041.56777.6252-0.2864-0.3393-0.70490.45450.2166-0.01540.24340.48940.0970.41760.09570.08210.28160.14920.2099-2.9902-87.2437-22.7798
102.32960.97260.87544.5329-2.97464.05150.21140.27360.3416-0.6286-0.1470.7412-0.1578-0.3343-0.04390.27840.0840.07520.20270.03040.532-28.536-43.3507-39.7479
113.8034-0.33160.67336.45152.19115.04450.37750.67220.13090.2035-0.10570.754-0.4608-0.3503-0.2970.19090.08860.0680.34130.05080.3423-25.2817-49.7506-40.54
127.435-3.0059-3.11492.0033-6.70362.0017-0.02270.12430.1836-0.51380.42192.7026-0.5103-2.5396-0.31740.62370.197-0.03370.63740.09440.7711-23.817-36.9576-55.5459
132.31380.09120.06582.98170.56664.07460.00360.0143-0.04210.0187-0.05260.17560.24230.00490.05440.20270.04970.03540.11190.02510.1616-14.3795-36.8911-34.4102
142.622-1.4210.17635.4513-1.15082.52780.0286-0.14410.27110.0891-0.0482-0.05850.06250.12690.01020.1525-0.01450.02790.1783-0.03130.1839-11.7811-18.2013-28.0451
153.27340.5732-1.0587.11485.6217.6746-0.0989-0.89380.58890.0162-0.22960.3287-0.4680.33960.13570.2770.09970.01580.3597-0.03730.20425.0244-36.1478-42.3559
167.5816-4.733-4.28979.60721.51463.37470.3267-0.2856-0.09810.00870.6592-0.85130.84421.3758-0.93820.43220.0560.10050.3628-0.05590.3364.4185-49.4201-62.5398
171.88240.31320.55632.36030.31143.229-0.09750.0292-0.013-0.38050.09960.0871-0.2351-0.0092-0.00040.35240.02030.01710.16520.01210.1805-8.7645-38.7099-63.9032
183.1904-0.091-0.00713.071-0.95034.8978-0.19510.03470.048-0.07980.1923-0.3507-0.4120.8458-0.00030.2734-0.05210.06530.3798-0.04670.207314.0819-30.1277-56.987
195.2671-0.9964-1.8783.10754.17557.4177-0.33990.06630.5262-0.50540.272-0.3889-0.87140.9208-0.10490.6733-0.21010.08850.44640.06380.258710.2438-23.7405-68.5332
204.8559-4.36831.43447.32711.92413.4652-0.3076-0.4022-0.48141.0002-0.58570.36360.1515-0.02640.86530.76260.00450.02490.52160.21350.6993-12.818-73.3585-68.7642
219.3912-5.294-2.5196.7032.31340.89040.410.62470.9832-1.0784-0.23180.0142-0.3504-0.1196-0.1811.1616-0.2062-0.07910.44920.13840.7008-23.2836-38.2197-35.7367
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 1:21)
2X-RAY DIFFRACTION2(chain A and resid 22:37)
3X-RAY DIFFRACTION3(chain A and resid 38:46)
4X-RAY DIFFRACTION4(chain A and resid 47:160)
5X-RAY DIFFRACTION5(chain A and resid 161:296)
6X-RAY DIFFRACTION6(chain B and resid 175:192)
7X-RAY DIFFRACTION7(chain B and resid 193:308)
8X-RAY DIFFRACTION8(chain B and resid 309:402)
9X-RAY DIFFRACTION9(chain B and resid 403:432)
10X-RAY DIFFRACTION10(chain C and resid 1:21)
11X-RAY DIFFRACTION11(chain C and resid 22:37)
12X-RAY DIFFRACTION12(chain C and resid 38:46)
13X-RAY DIFFRACTION13(chain C and resid 47:160)
14X-RAY DIFFRACTION14(chain C and resid 161:296)
15X-RAY DIFFRACTION15(chain D and resid 175:193)
16X-RAY DIFFRACTION16(chain D and resid 194:201)
17X-RAY DIFFRACTION17(chain D and resid 202:310)
18X-RAY DIFFRACTION18(chain D and resid 311:402)
19X-RAY DIFFRACTION19(chain D and resid 403:432)
20X-RAY DIFFRACTION20(chain A and resid 297)
21X-RAY DIFFRACTION21(chain C and resid 297)

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