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- PDB-4md8: Crystal Structure of full-length symmetric CK2 holoenzyme with mu... -

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Basic information

Entry
Database: PDB / ID: 4md8
TitleCrystal Structure of full-length symmetric CK2 holoenzyme with mutated alpha subunit (F121E)
Components
  • Casein kinase II subunit alpha
  • Casein kinase II subunit beta
KeywordsTRANSFERASE / protein serine/threonine kinase
Function / homology
Function and homology information


regulation of DNA binding / adiponectin-activated signaling pathway / positive regulation of activin receptor signaling pathway / UTP-C complex / endothelial tube morphogenesis / negative regulation of viral life cycle / regulation of transcription by RNA polymerase III / protein kinase regulator activity / regulation of chromosome separation / positive regulation of aggrephagy ...regulation of DNA binding / adiponectin-activated signaling pathway / positive regulation of activin receptor signaling pathway / UTP-C complex / endothelial tube morphogenesis / negative regulation of viral life cycle / regulation of transcription by RNA polymerase III / protein kinase regulator activity / regulation of chromosome separation / positive regulation of aggrephagy / WNT mediated activation of DVL / Condensation of Prometaphase Chromosomes / protein kinase CK2 complex / symbiont-mediated disruption of host cell PML body / Receptor Mediated Mitophagy / Sin3-type complex / Synthesis of PC / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Maturation of hRSV A proteins / positive regulation of SMAD protein signal transduction / negative regulation of apoptotic signaling pathway / negative regulation of blood vessel endothelial cell migration / positive regulation of Wnt signaling pathway / negative regulation of double-strand break repair via homologous recombination / chaperone-mediated protein folding / negative regulation of ubiquitin-dependent protein catabolic process / Signal transduction by L1 / peptidyl-threonine phosphorylation / Hsp90 protein binding / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / PML body / Wnt signaling pathway / Regulation of PTEN stability and activity / positive regulation of protein catabolic process / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / KEAP1-NFE2L2 pathway / double-strand break repair / rhythmic process / protein-macromolecule adaptor activity / kinase activity / positive regulation of cell growth / protein-containing complex assembly / peptidyl-serine phosphorylation / secretory granule lumen / RNA polymerase II-specific DNA-binding transcription factor binding / Regulation of TP53 Activity through Phosphorylation / ficolin-1-rich granule lumen / protein stabilization / negative regulation of translation / non-specific serine/threonine protein kinase / regulation of cell cycle / cell cycle / negative regulation of cell population proliferation / protein domain specific binding / protein phosphorylation / protein serine kinase activity / signaling receptor binding / protein serine/threonine kinase activity / apoptotic process / DNA damage response / chromatin binding / positive regulation of cell population proliferation / Neutrophil degranulation / chromatin / signal transduction / extracellular exosome / extracellular region / nucleoplasm / ATP binding / identical protein binding / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
protein kinase ck2 holoenzyme, chain C, domain 1 / protein kinase ck2 holoenzyme, chain C, domain 1 / Casein kinase II, regulatory subunit / Casein kinase II, regulatory subunit, N-terminal / Casein kinase II subunit beta-like / Casein kinase II regulatory subunit / Casein kinase II regulatory subunit signature. / Casein kinase II regulatory subunit / N-terminal domain of TfIIb - #20 / Casein Kinase 2, subunit alpha ...protein kinase ck2 holoenzyme, chain C, domain 1 / protein kinase ck2 holoenzyme, chain C, domain 1 / Casein kinase II, regulatory subunit / Casein kinase II, regulatory subunit, N-terminal / Casein kinase II subunit beta-like / Casein kinase II regulatory subunit / Casein kinase II regulatory subunit signature. / Casein kinase II regulatory subunit / N-terminal domain of TfIIb - #20 / Casein Kinase 2, subunit alpha / N-terminal domain of TfIIb / Single Sheet / 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 Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Casein kinase II subunit beta / Casein kinase II subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.3 Å
AuthorsLolli, G. / Ranchio, A. / Battistutta, R.
CitationJournal: Acs Chem.Biol. / Year: 2014
Title: Active Form of the Protein Kinase CK2 alpha 2 beta 2 Holoenzyme Is a Strong Complex with Symmetric Architecture.
Authors: Lolli, G. / Ranchio, A. / Battistutta, R.
History
DepositionAug 22, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 20, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 5, 2014Group: Database references
Revision 1.2Sep 20, 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 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Casein kinase II subunit beta
B: Casein kinase II subunit beta
C: Casein kinase II subunit beta
D: Casein kinase II subunit beta
E: Casein kinase II subunit alpha
F: Casein kinase II subunit alpha
G: Casein kinase II subunit alpha
H: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)280,90112
Polymers280,6408
Non-polymers2624
Water00
1
A: Casein kinase II subunit beta
B: Casein kinase II subunit beta
E: Casein kinase II subunit alpha
F: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)140,4516
Polymers140,3204
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7870 Å2
ΔGint-67 kcal/mol
Surface area47950 Å2
MethodPISA
2
C: Casein kinase II subunit beta
D: Casein kinase II subunit beta
G: Casein kinase II subunit alpha
H: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)140,4516
Polymers140,3204
Non-polymers1312
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7710 Å2
ΔGint-65 kcal/mol
Surface area48000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)141.518, 57.625, 185.685
Angle α, β, γ (deg.)90.000, 102.600, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
12E
22F
32G
42H

NCS domain segments:

Refine code: 2

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111TRPTRPPROPROAA9 - 589 - 58
211TRPTRPPROPROBB9 - 589 - 58
311TRPTRPPROPROCC9 - 589 - 58
411TRPTRPPROPRODD9 - 589 - 58
121ASNASNHISHISAA67 - 19367 - 193
221ASNASNHISHISBB67 - 19367 - 193
321ASNASNHISHISCC67 - 19367 - 193
421ASNASNHISHISDD67 - 19367 - 193
112PROPROARGARGEE4 - 474 - 47
212PROPROARGARGFF4 - 474 - 47
312PROPROARGARGGG4 - 474 - 47
412PROPROARGARGHH4 - 474 - 47
122TYRTYRASPASPEE50 - 10350 - 103
222TYRTYRASPASPFF50 - 10350 - 103
322TYRTYRASPASPGG50 - 10350 - 103
422TYRTYRASPASPHH50 - 10350 - 103
132ARGARGVALVALEE107 - 116107 - 116
232ARGARGVALVALFF107 - 116107 - 116
332ARGARGVALVALGG107 - 116107 - 116
432ARGARGVALVALHH107 - 116107 - 116
142LEULEULEULEUEE128 - 265128 - 265
242LEULEULEULEUFF128 - 265128 - 265
342LEULEULEULEUGG128 - 265128 - 265
442LEULEULEULEUHH128 - 265128 - 265
152LEULEUASPASPEE273 - 330273 - 330
252LEULEUASPASPFF273 - 330273 - 330
352LEULEUASPASPGG273 - 330273 - 330
452LEULEUASPASPHH273 - 330273 - 330

NCS ensembles :
ID
1
2

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Components

#1: Protein
Casein kinase II subunit beta / CK2 subunit beta / CK II beta / Phosvitin / Protein G5a


Mass: 24969.412 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CSNK2B, CK2N, G5A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P67870
#2: Protein
Casein kinase II subunit alpha / CK2 subunit alpha / CK II alpha


Mass: 45190.496 Da / Num. of mol.: 4 / Mutation: F121E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CSNK2A1, CK2A1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21
References: UniProt: P68400, non-specific serine/threonine protein kinase
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn

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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: 2.63 Å3/Da / Density % sol: 53.28 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 6.5
Details: 20% PEG3350, 0.2 M ammonium citrate, pH 6.5, VAPOR DIFFUSION, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 29, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.3→181.213 Å / Num. all: 44221 / Num. obs: 44221 / % possible obs: 98.8 % / Redundancy: 6.5 % / Rsym value: 0.177 / Net I/σ(I): 10.9
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRsym value% possible all
3.3-3.486.20.5681.43898963140.56897.6
3.48-3.696.20.39323703759990.39398.3
3.69-3.946.20.2792.83563257030.27998.9
3.94-4.266.80.2023.93597953090.20299
4.26-4.676.60.1495.33254349260.14999.2
4.67-5.226.80.1375.73066445080.13799.4
5.22-6.026.90.1475.32719739540.14799.5
6.02-7.386.50.1276.22198233720.12799.4
7.38-10.446.80.05912.61780426370.05999.3
10.44-47.6456.30.04414.5943714990.04497.8

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALA3.3.20data scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACT3.11data extraction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 4DGL AND 4KWP

4dgl

4kwp


Resolution: 3.3→181.213 Å / Cor.coef. Fo:Fc: 0.883 / Cor.coef. Fo:Fc free: 0.848 / WRfactor Rfree: 0.218 / WRfactor Rwork: 0.1989 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8557 / SU B: 45.918 / SU ML: 0.347 / SU R Cruickshank DPI: 0.11 / SU Rfree: 0.1151 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.115 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.2487 2230 5 %RANDOM
Rwork0.2217 ---
obs0.2231 44213 98.24 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 164.28 Å2 / Biso mean: 64.6566 Å2 / Biso min: 20 Å2
Baniso -1Baniso -2Baniso -3
1--5.88 Å2-0 Å2-4.06 Å2
2---0.08 Å20 Å2
3---5.96 Å2
Refinement stepCycle: LAST / Resolution: 3.3→181.213 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17613 0 4 0 17617
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0218104
X-RAY DIFFRACTIONr_angle_refined_deg1.6121.94824500
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3352101
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.73723.443976
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.701153111
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.17815140
X-RAY DIFFRACTIONr_chiral_restr0.1090.22513
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02114116
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A746MEDIUM POSITIONAL0.080.5
12B746MEDIUM POSITIONAL0.070.5
13C746MEDIUM POSITIONAL0.060.5
14D746MEDIUM POSITIONAL0.060.5
11A708TIGHT THERMAL3.110.5
12B708TIGHT THERMAL3.650.5
13C708TIGHT THERMAL2.850.5
14D708TIGHT THERMAL5.260.5
11A746MEDIUM THERMAL3.752
12B746MEDIUM THERMAL4.582
13C746MEDIUM THERMAL3.752
14D746MEDIUM THERMAL6.22
21E1363MEDIUM POSITIONAL0.110.5
22F1363MEDIUM POSITIONAL0.140.5
23G1363MEDIUM POSITIONAL0.10.5
24H1363MEDIUM POSITIONAL0.120.5
21E1216TIGHT THERMAL4.470.5
22F1216TIGHT THERMAL3.040.5
23G1216TIGHT THERMAL3.160.5
24H1216TIGHT THERMAL3.180.5
21E1363MEDIUM THERMAL5.32
22F1363MEDIUM THERMAL4.442
23G1363MEDIUM THERMAL3.962
24H1363MEDIUM THERMAL3.892
LS refinement shellResolution: 3.3→3.383 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.361 151 -
Rwork0.261 3020 -
all-3171 -
obs--94.71 %
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)
16.569-1.6419-0.40162.30110.95324.98440.07490.3877-0.1069-0.07470.0361-0.20110.23290.4491-0.1110.05070.06930.06310.15480.06840.162863.7991-3.170.8254
24.43110.1401-0.67581.1413-1.84373.0333-0.09540.7672-1.2481-0.2542-0.0694-0.02280.3787-0.00660.16490.26760.0302-0.05840.3033-0.20330.384861.5938-9.00610.2176
321.5229-4.17530.53240.91510.4753.2772-0.32420.48720.698-0.087-0.0947-0.0426-0.81950.01950.41890.2145-0.0218-0.13480.08790.10710.246648.16348.85838.332
45.81150.7591-0.78840.80850.09560.92040.07660.0388-0.03250.0274-0.12680.20220.0908-0.30160.05030.0219-0.0354-0.02380.1725-0.00020.169637.08-0.016517.2931
57.45531.3730.12561.4782.77416.81640.1658-0.18480.22620.0840.0106-0.1835-0.29440.4137-0.17640.3354-0.0969-0.16640.5890.03970.417643.77291.96690.5794
63.7914-1.7511.280410.01815.05089.1717-0.2973-0.09830.84060.94350.2239-0.5117-1.08821.0280.07340.5286-0.1538-0.00010.6890.02170.398741.61477.673491.0208
76.5001-1.1409-0.21141.59410.15492.95790.1128-0.4835-0.2191-0.0394-0.110.21880.1175-0.0856-0.00270.12780.115-0.08610.2979-0.02030.254325.7063-3.309978.8397
83.88813.1116-0.657811.097-2.04644.90420.12181.06490.4867-0.3747-0.13630.24730.19650.19360.01460.22570.2571-0.09310.72320.00870.2592-0.82486.031264.9642
97.8862-2.127-2.05193.5811-0.91385.60150.01830.8490.4062-0.54830.33660.40.1326-0.4105-0.3550.2268-0.191-0.29220.56840.03040.63743.6721-1.4565-0.9118
104.6284-0.97433.33176.21792.17254.7866-0.52830.92190.8094-0.4506-0.1044-0.6562-0.7115-0.30460.63270.1404-0.108-0.161.20240.0620.80136.64073.2573-0.8255
116.4250.8791-0.63920.479-0.31170.5797-0.18830.1174-0.4704-0.12520.1690.20370.1947-0.35470.01920.0723-0.1184-0.02320.2501-0.0420.440423.9235-5.062313.6432
126.30073.55162.12613.5342-3.442314.79260.5383-0.5141.15980.95150.06910.9487-1.6618-1.3625-0.60740.36560.15690.11610.2174-0.07350.496147.38911.447827.1386
139.3314-1.20932.56172.19492.04645.80190.1706-0.7033-0.37730.4611-0.03770.54910.0231-0.8823-0.13290.45380.00850.1710.5767-0.0060.6053-16.09172.575391.8916
142.0746-0.7785-3.25478.58550.61785.2241-0.4211-0.8588-0.59160.198-0.7104-0.44250.79371.27721.13150.40050.0484-0.04390.79080.04390.8786-13.6115-3.067892.8124
156.1895-1.4394-1.03011.5382-0.8551.78670.1588-0.11280.4024-0.01390.03680.0211-0.0911-0.065-0.19560.19130.1151-0.07920.3966-0.12420.36991.51736.297378.6531
162.09461.32810.70881.24852.397210.4289-0.31650.2581-0.7951-0.2385-0.15-0.30930.2336-0.94210.46640.38690.2532-0.04250.6538-0.21350.565427.4167-10.570863.6417
177.21132.3416-0.03771.8701-0.56580.6666-0.0368-0.2639-0.50710.1098-0.068-0.19610.23070.03640.10480.25190.0250.01320.21560.00120.187572.6573-0.066331.6637
183.99572.76710.15762.44820.96112.53330.1003-0.33470.1796-0.0738-0.13960.3543-0.1871-0.0870.03930.06540.016-0.07180.24130.08080.204674.83769.11234.0517
193.67992.1456-1.20452.0554-2.18984.26260.03940.285-0.2225-0.2531-0.0698-0.16540.20420.10520.03040.18720.12350.00380.2448-0.00580.183489.246417.282121.5562
203.2435-0.7335-0.57724.2182-0.83355.54920.3244-0.18510.14460.193-0.203-0.442-0.68950.5737-0.12150.1223-0.1109-0.02720.27180.01830.202891.167623.772530.1865
215.4218-0.5739-1.36590.21610.1040.4655-0.50810.968-1.8020.2290.20670.43530.3991-0.3640.30131.10770.10970.030.76340.0611.2198-47.059-0.368258.931
223.8096-0.86110.59050.71480.6291.31840.14840.206-0.1918-0.0350.0414-0.1767-0.03270.3332-0.18980.50760.198-0.1590.7173-0.06130.5523-20.2253.221660.8909
232.4815-0.318-1.07235.35010.93023.78090.2466-0.21270.05290.51320.1609-0.13310.1380.329-0.40750.14280.0934-0.11910.58170.03740.3318-36.226916.197861.6823
242.87210.7177-1.30943.3149-1.01336.26070.29550.10570.33210.18670.13130.433-0.565-0.441-0.42680.13750.1713-0.02110.61020.02430.5189-45.30424.903660.0885
257.23071.4832-0.23662.0085-0.52060.4360.1151-0.34961.3921-0.0203-0.09460.2594-0.3765-0.0939-0.02050.50580.09510.02190.5097-0.0950.889-13.68055.084629.2547
265.6412.1344-2.46980.8244-1.05924.71950.0966-0.17990.25790.0087-0.02640.01350.43350.1224-0.07020.1864-0.0220.04680.4203-0.09910.6785-0.9114-2.411430.2491
274.99540.4110.36084.73550.0282.66630.26410.17250.1837-0.1605-0.1792-0.05070.18890.05-0.08490.034-0.0082-0.00020.4283-0.06220.4655-18.0142-13.758227.6246
283.285-0.41640.45594.4799-1.00774.2960.3629-0.1726-0.22910.1021-0.20840.11850.5675-0.3321-0.15450.1256-0.10670.01380.4976-0.04930.5993-24.5459-22.010431.2821
297.47130.8919-1.17881.51051.40431.90640.4971.38321.6310.1257-0.14490.0722-0.0668-0.447-0.35210.98330.09230.11381.12510.47340.672972.87840.374354.6078
303.3505-1.3277-0.15890.9414-0.77491.8540.0762-0.0452-0.08680.0908-0.06040.0992-0.11790.0201-0.01580.41220.1359-0.01720.5734-0.05620.385446.897-3.315659.1628
313.8477-1.59731.35073.544-0.83743.13830.2214-0.3003-0.1094-0.3972-0.36630.11540.1555-0.16130.14480.36380.28250.04690.53030.03070.17359.642-12.042357.0988
322.8794-0.6956-0.41223.6321-0.7763.50720.1694-0.1038-0.2009-0.0337-0.3201-0.41180.43290.43590.15070.37370.2730.09670.64220.06660.383269.8577-22.546362.943
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 59
2X-RAY DIFFRACTION2A63 - 89
3X-RAY DIFFRACTION3A90 - 111
4X-RAY DIFFRACTION4A112 - 207
5X-RAY DIFFRACTION5C6 - 58
6X-RAY DIFFRACTION6C64 - 89
7X-RAY DIFFRACTION7C90 - 179
8X-RAY DIFFRACTION8C180 - 207
9X-RAY DIFFRACTION9B7 - 59
10X-RAY DIFFRACTION10B66 - 89
11X-RAY DIFFRACTION11B90 - 189
12X-RAY DIFFRACTION12B190 - 207
13X-RAY DIFFRACTION13D7 - 59
14X-RAY DIFFRACTION14D66 - 87
15X-RAY DIFFRACTION15D88 - 180
16X-RAY DIFFRACTION16D190 - 207
17X-RAY DIFFRACTION17E2 - 74
18X-RAY DIFFRACTION18E75 - 188
19X-RAY DIFFRACTION19E189 - 260
20X-RAY DIFFRACTION20E261 - 333
21X-RAY DIFFRACTION21G2 - 24
22X-RAY DIFFRACTION22G25 - 129
23X-RAY DIFFRACTION23G130 - 249
24X-RAY DIFFRACTION24G250 - 333
25X-RAY DIFFRACTION25F2 - 44
26X-RAY DIFFRACTION26F45 - 129
27X-RAY DIFFRACTION27F130 - 260
28X-RAY DIFFRACTION28F261 - 333
29X-RAY DIFFRACTION29H3 - 24
30X-RAY DIFFRACTION30H25 - 131
31X-RAY DIFFRACTION31H132 - 197
32X-RAY DIFFRACTION32H198 - 333

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