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

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Basic information

Entry
Database: PDB / ID: 3qhr
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 / 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 / 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 / Processing of DNA double-strand break ends / Orc1 removal from chromatin / cyclin A2-CDK1 complex / cell cycle G1/S phase transition / Regulation of TP53 Activity through Phosphorylation / cellular response to luteinizing hormone stimulus / Ub-specific processing proteases / cellular response to leptin stimulus / male pronucleus / female pronucleus / cellular response to cocaine / response to glucagon / positive regulation of DNA biosynthetic process / cyclin-dependent protein serine/threonine kinase regulator activity / cellular response to insulin-like growth factor stimulus / cyclin A1-CDK2 complex / cyclin E2-CDK2 complex / cyclin E1-CDK2 complex / cyclin A2-CDK2 complex / positive regulation of DNA-templated DNA replication initiation / G2 Phase / Y chromosome / cyclin-dependent protein kinase activity / 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 / Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) / centriole replication / Regulation of APC/C activators between G1/S and early anaphase / regulation of DNA replication / telomere maintenance in response to DNA damage / centrosome duplication / G0 and Early G1 / cochlea development / Telomere Extension By Telomerase / animal organ regeneration / Activation of the pre-replicative complex / cyclin-dependent kinase / cyclin-dependent protein serine/threonine kinase activity / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / Cajal body / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / 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 / cyclin-dependent protein kinase holoenzyme complex / condensed chromosome / regulation of G2/M transition of mitotic cell cycle / cellular response to platelet-derived growth factor stimulus / mitotic G1 DNA damage checkpoint signaling / cellular response to nitric oxide / post-translational protein modification / cyclin binding / regulation of mitotic cell cycle / positive regulation of DNA replication / meiotic cell cycle / male germ cell nucleus / cellular response to estradiol stimulus / G1/S transition of mitotic cell cycle / peptidyl-serine phosphorylation / potassium ion transport / DNA Damage/Telomere Stress Induced Senescence / CDK-mediated phosphorylation and removal of Cdc6 / Meiotic recombination / SCF(Skp2)-mediated degradation of p27/p21 / G2/M transition of mitotic cell cycle / Orc1 removal from chromatin / Transcriptional regulation of granulopoiesis / positive regulation of fibroblast proliferation / Cyclin D associated events in G1 / cellular senescence / Regulation of TP53 Degradation / nuclear envelope / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / regulation of gene expression / Senescence-Associated Secretory Phenotype (SASP) / cellular response to hypoxia / transcription regulator complex / Regulation of TP53 Activity through Phosphorylation / Ras protein signal transduction / chromosome, telomeric region
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-like / Cyclin, C-terminal domain / Cyclin_C ...Cyclin-A, N-terminal APC/C binding region / Cyclin-A N-terminal APC/C binding region / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Cyclin-like / Cyclin, C-terminal domain / Cyclin_C / Cyclin A; domain 1 / Cyclin, N-terminal / Cyclin, N-terminal domain / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like 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, 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 / 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: 2.17 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_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_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 16, 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: 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)134,96035
Polymers132,2098
Non-polymers2,75127
Water10,827601
1
A: Cell division protein kinase 2
B: Cyclin-A2
K: CDK2 substrate peptide: PKTPKKAKKL
L: CDK2 substrate peptide: PKTPKKAKKL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,61819
Polymers66,1054
Non-polymers1,51415
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9910 Å2
ΔGint-59 kcal/mol
Surface area23240 Å2
MethodPISA
2
C: Cell division protein kinase 2
D: Cyclin-A2
J: CDK2 substrate peptide: PKTPKKAKKL
M: CDK2 substrate peptide: PKTPKKAKKL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,34216
Polymers66,1054
Non-polymers1,23712
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9560 Å2
ΔGint-62 kcal/mol
Surface area23390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.690, 163.910, 73.280
Angle α, β, γ (deg.)90.00, 107.38, 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 -1:159 or resseq 160:296 )
211chain C
112chain B and (resseq 172:432 )
212chain D
113chain A and (resseq 297:297)
213chain C
114chain L and (resseq 5:7 )
214chain M

NCS ensembles :
ID
1
2
3
4

NCS oper:
IDCodeMatrixVector
1given(0.825892, 0.020226, 0.563465), (0.022007, -0.999751, 0.00363), (0.563398, 0.009402, -0.826132)11.5142, -51.020901, -34.902901
2given(0.826285, 0.033518, 0.562254), (0.03651, -0.999316, 0.005918), (0.562068, 0.015638, -0.826943)11.5048, -51.056801, -34.919102
3given(0.81491, 0.039063, 0.578269), (0.038742, -0.999166, 0.0129), (0.578291, 0.011891, -0.815744)11.7075, -50.9706, -34.955799
4given(0.821214, 0.00382, 0.570607), (0.030488, -0.998843, -0.037191), (0.569805, 0.047938, -0.820381)11.7508, -52.702099, -34.491199

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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 / Plasmid: pET28a / 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 / Plasmid: pET28a / 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 substrate sequence

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Non-polymers , 6 types, 628 molecules

#4: Chemical ChemComp-ADP / ADENOSINE-5'-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


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#8: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: C3H8O3
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 601 / Source method: isolated from a natural source / Formula: H2O

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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: 3.06 Å3/Da / Density % sol: 59.86 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 22% w/v Poly(acrylic acid sodium salt) 5100, 20mM MgCl2, 100mM HEPES pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 6, 2010
RadiationMonochromator: diamond laue / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.17→37.805 Å / Num. all: 83902 / Num. obs: 83902 / % possible obs: 100 % / Observed criterion σ(F): 1.5 / Observed criterion σ(I): 1.5 / Redundancy: 3.9 % / Rsym value: 0.132 / Net I/σ(I): 7.4
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsRsym valueDiffraction-ID% possible all
2.17-2.293.80.0120.51.2221100
2.29-2.433.80.0120.80.7661100
2.43-2.593.90.0121.30.4941100
2.59-2.83.90.0122.10.3021100
2.8-3.073.90.0123.60.1851100
3.07-3.433.90.0125.90.1111100
3.43-3.963.90.0126.90.0811100
3.96-4.853.90.0127.50.0741100
4.85-6.863.90.0128.90.0611100
6.86-37.8053.70.01213.50.042199

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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 STRUCTURE

Resolution: 2.17→37.805 Å / Occupancy max: 1 / Occupancy min: 0 / SU ML: 0.7 / σ(F): 0 / Phase error: 22.85 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2098 4192 5 %
Rwork0.1789 --
obs0.1805 83847 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 57.53 Å2 / ksol: 0.371 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-6.7517 Å20 Å28.2384 Å2
2---4.3177 Å2-0 Å2
3----2.434 Å2
Refinement stepCycle: LAST / Resolution: 2.17→37.805 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9306 0 170 601 10077
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0119685
X-RAY DIFFRACTIONf_angle_d1.21613115
X-RAY DIFFRACTIONf_dihedral_angle_d14.8533644
X-RAY DIFFRACTIONf_chiral_restr0.0821474
X-RAY DIFFRACTIONf_plane_restr0.0061624
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2396X-RAY DIFFRACTIONPOSITIONAL
12C2396X-RAY DIFFRACTIONPOSITIONAL0.228
21B2099X-RAY DIFFRACTIONPOSITIONAL
22D2099X-RAY DIFFRACTIONPOSITIONAL0.42
31A27X-RAY DIFFRACTIONPOSITIONAL
32C27X-RAY DIFFRACTIONPOSITIONAL0.021
41L26X-RAY DIFFRACTIONPOSITIONAL
42M26X-RAY DIFFRACTIONPOSITIONAL0.127
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.17-2.19470.32271400.32572667X-RAY DIFFRACTION100
2.1947-2.22050.34671250.30942679X-RAY DIFFRACTION100
2.2205-2.24760.35591320.31072615X-RAY DIFFRACTION100
2.2476-2.2760.30611360.29862696X-RAY DIFFRACTION100
2.276-2.3060.28981320.28332671X-RAY DIFFRACTION100
2.306-2.33750.31631510.27562587X-RAY DIFFRACTION100
2.3375-2.37090.29321300.25672698X-RAY DIFFRACTION100
2.3709-2.40630.31061280.24432608X-RAY DIFFRACTION100
2.4063-2.44390.28821610.23582666X-RAY DIFFRACTION100
2.4439-2.4840.27241310.23122605X-RAY DIFFRACTION100
2.484-2.52680.26641080.21862754X-RAY DIFFRACTION100
2.5268-2.57270.27171400.21012597X-RAY DIFFRACTION100
2.5727-2.62220.2391620.20892648X-RAY DIFFRACTION100
2.6222-2.67570.24671420.2062630X-RAY DIFFRACTION100
2.6757-2.73390.26551330.1932656X-RAY DIFFRACTION100
2.7339-2.79740.21891290.17542649X-RAY DIFFRACTION100
2.7974-2.86740.23631350.17452651X-RAY DIFFRACTION100
2.8674-2.94490.22961560.16512696X-RAY DIFFRACTION100
2.9449-3.03150.19221540.16182602X-RAY DIFFRACTION100
3.0315-3.12930.18971440.1642650X-RAY DIFFRACTION100
3.1293-3.24110.18241430.15952650X-RAY DIFFRACTION100
3.2411-3.37080.18541500.14762652X-RAY DIFFRACTION100
3.3708-3.52410.16731560.14752643X-RAY DIFFRACTION100
3.5241-3.70970.17371350.14292667X-RAY DIFFRACTION100
3.7097-3.94190.17391280.14252670X-RAY DIFFRACTION100
3.9419-4.24590.17481430.14062645X-RAY DIFFRACTION100
4.2459-4.67250.17591420.13772667X-RAY DIFFRACTION100
4.6725-5.3470.15531380.14132669X-RAY DIFFRACTION100
5.347-6.73050.2041420.19952681X-RAY DIFFRACTION100
6.7305-37.81040.20521460.18692686X-RAY DIFFRACTION99
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)
15.66970.1862-1.47566.7122-2.69343.59580.51060.0323-0.335-0.1311-0.05661.37510.7201-0.6706-0.41770.7689-0.0612-0.19580.28940.03940.47216.1957-32.9255-34.0419
20.48331.8233-1.54679.4802-6.59444.81280.02520.19440.3869-0.78390.59460.91290.7189-0.8938-0.51990.4843-0.1246-0.04590.3132-0.03480.25327.8493-40.6671-22.3775
34.0041-1.5368-1.65583.55380.78575.84560.17880.39030.0882-0.6512-0.08260.1025-0.504-0.4652-0.00720.5481-0.0068-0.01120.14180.01760.110315.9258-39.7945-33.1791
44.4680.0501-0.79883.89330.72994.29060.0968-0.0266-0.0737-0.17930.0028-0.0122-0.14220.1626-0.0610.3022-0.02170.02370.1011-0.03980.128424.0409-48.0296-28.9107
53.13051.5714-0.02815.61470.26522.713-0.02510.081-0.1742-0.27030.0614-0.070.17540.1734-0.04420.35620.0350.04040.1904-0.06440.179626.2405-63.0687-33.347
61.8284-0.2799-0.06174.05273.79753.5852-0.05641.0242-0.7515-0.8607-0.4614-0.1767-0.28680.17190.29820.3438-0.01850.08870.3423-0.09040.316531.8136-44.449-12.2184
73.6641-1.7253-1.32583.9454.87326.1083-0.231-0.37150.0280.52150.2930.13710.07070.3756-0.10730.27990.08710.01750.23890.04110.17213.0929-42.30133.6488
84.1452-0.326-1.8115.0961.57164.5879-0.12230.11710.0060.05530.10050.37770.0076-0.11120.01550.18370.0082-0.01890.1310.04030.18936.1739-40.9062-4.9559
93.45070.579-0.27583.6882-1.20633.5972-0.2923-0.5733-0.22010.18840.2253-0.40770.17140.32590.0360.16520.1094-0.02320.27790.00320.197231.4271-50.03144.2507
106.3975-2.1071-0.46613.15750.21136.498-0.5168-1.2763-1.39680.45390.46920.16990.32630.63990.07520.44580.21320.14820.55840.20180.147421.7838-56.172512.9177
113.4902-1.61571.73092.5743-2.84653.36270.73210.68430.8315-0.4813-0.39271.0155-0.2858-0.356-0.31680.51690.13660.17050.29940.08770.7654-3.5066-18.1621-3.6282
123.0263.839-3.72058.4248-6.33575.08320.27050.63840.2524-0.43840.52690.888-0.0309-0.8105-0.6820.53190.16870.06460.35230.02830.29184.3187-10.2878-12.4113
133.01490.4408-0.22995.68022.91845.2249-0.2395-0.0631-0.03040.4565-0.10670.48050.8453-0.31630.38920.32080.00320.12390.14230.06090.24034.8557-11.1271.0979
144.2088-0.3766-0.09063.530.76564.8203-0.0073-0.03960.1720.0653-0.0086-0.00630.19890.3230.02540.30760.05430.05060.1279-0.01160.153613.7834-2.67342.1114
153.1992-1.8778-0.06376.2559-0.95443.03220.0814-0.24940.39760.2020.0321-0.09290.05880.2407-0.08850.1999-0.02440.04640.1986-0.06670.19512.764112.34886.9642
163.8961-3.6355-3.65463.47623.46893.449-0.2272-0.75050.50720.45880.02910.0196-0.29810.61920.10360.45180.1610.07170.5831-0.04490.272329.8478-5.6146-7.2512
173.36080.8462-1.19417.10933.39497.4947-0.20660.1193-0.193-0.65790.337-0.33560.1430.5854-0.11530.4449-0.01610.09130.2507-0.01740.178722.1396-10.4818-30.76
183.5529-0.19791.61023.63050.59626.7632-0.1293-0.1377-0.0581-0.36730.09130.2375-0.1255-0.17490.02950.38260.04620.03240.16380.00360.207310.3688-7.6406-26.9053
193.95010.12150.16393.3516-1.20895.8354-0.330.00230.0399-0.14040.3542-0.5241-0.40131.3735-0.04510.4348-0.07160.1050.6187-0.12570.300338.42980.1944-21.4655
204.52190.41210.033543.20887.6061-0.7540.56340.5734-0.73340.5775-0.2653-1.02141.2723-0.02660.7691-0.31760.2010.6711-0.01960.252734.996.5933-33.566
216.0714-0.06380.82545.33044.08053.233-0.1777-0.74230.0105-0.1209-0.21471.0087-1.446-0.67640.16991.38330.20590.16841.03210.03330.42572.19837.07-12.6573
224.5698-3.205-1.19267.85094.50932.7103-0.49660.5629-1.02950.1265-0.21630.92360.5066-0.70610.49921.0532-0.16640.23151.10340.05750.54236.1787-57.9457-22.9832
234.9347-2.84166.1321.6715-3.50197.6508-0.0266-0.04820.41160.9035-0.57571.60090.23350.19760.52841.03090.08310.15610.38880.17920.751611.9794-43.2213-33.7946
247.1974.5792-5.02455.0405-1.20765.38350.69690.90570.8578-2.5655-0.8025-0.456-0.6039-0.23760.13921.06290.10610.17820.51890.06180.66391.1935-7.7185-0.6903
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 1:27)
2X-RAY DIFFRACTION2(chain A and resid 28:56)
3X-RAY DIFFRACTION3(chain A and resid 57:99)
4X-RAY DIFFRACTION4(chain A and resid 100:160)
5X-RAY DIFFRACTION5(chain A and resid 161:296)
6X-RAY DIFFRACTION6(chain B and resid 175:193)
7X-RAY DIFFRACTION7(chain B and resid 194:236)
8X-RAY DIFFRACTION8(chain B and resid 237:308)
9X-RAY DIFFRACTION9(chain B and resid 309:399)
10X-RAY DIFFRACTION10(chain B and resid 400:432)
11X-RAY DIFFRACTION11(chain C and resid 1:27)
12X-RAY DIFFRACTION12(chain C and resid 28:56)
13X-RAY DIFFRACTION13(chain C and resid 57:99)
14X-RAY DIFFRACTION14(chain C and resid 100:160)
15X-RAY DIFFRACTION15(chain C and resid 161:296)
16X-RAY DIFFRACTION16(chain D and resid 175:193)
17X-RAY DIFFRACTION17(chain D and resid 194:254)
18X-RAY DIFFRACTION18(chain D and resid 255:307)
19X-RAY DIFFRACTION19(chain D and resid 308:401)
20X-RAY DIFFRACTION20(chain D and resid 402:432)
21X-RAY DIFFRACTION21(chain J and resid -2:7)
22X-RAY DIFFRACTION22(chain K and resid -2:7)
23X-RAY DIFFRACTION23(chain A and resid 297:297)
24X-RAY DIFFRACTION24(chain C and resid 297:297)

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