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- PDB-4gz3: Crystal structure of human O-GlcNAc Transferase with UDP and a th... -

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Basic information

Entry
Database: PDB / ID: 4gz3
TitleCrystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide
Components
  • Casein kinase II subunit alpha
  • UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Keywordstransferase/peptide / OGT / O-GlcNAc / GT-B / Glycosyltransferase / O-GlcNAcylation / transferase-peptide complex
Function / homology
Function and homology information


negative regulation of non-canonical inflammasome complex assembly / protein N-acetylglucosaminyltransferase complex / protein O-acetylglucosaminyltransferase activity / RNA polymerase II C-terminal domain S5 O-GlcNAc transferase activity / RNA polymerase II C-terminal domain S7 O-GlcNAc transferase activity / regulation of insulin receptor signaling pathway / protein O-GlcNAc transferase / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of Rac protein signal transduction ...negative regulation of non-canonical inflammasome complex assembly / protein N-acetylglucosaminyltransferase complex / protein O-acetylglucosaminyltransferase activity / RNA polymerase II C-terminal domain S5 O-GlcNAc transferase activity / RNA polymerase II C-terminal domain S7 O-GlcNAc transferase activity / regulation of insulin receptor signaling pathway / protein O-GlcNAc transferase / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of Rac protein signal transduction / regulation of necroptotic process / negative regulation of stem cell population maintenance / protein O-linked glycosylation / NSL complex / regulation of chromosome separation / positive regulation of aggrephagy / Condensation of Prometaphase Chromosomes / WNT mediated activation of DVL / protein kinase CK2 complex / symbiont-mediated disruption of host cell PML body / regulation of glycolytic process / RIPK1-mediated regulated necrosis / regulation of gluconeogenesis / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / Receptor Mediated Mitophagy / regulation of synapse assembly / Formation of WDR5-containing histone-modifying complexes / Synthesis of PC / Maturation of hRSV A proteins / Sin3-type complex / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / phosphatidylinositol-3,4,5-trisphosphate binding / hemopoiesis / positive regulation of proteolysis / negative regulation of apoptotic signaling pathway / histone acetyltransferase complex / positive regulation of Wnt signaling pathway / negative regulation of double-strand break repair via homologous recombination / positive regulation of lipid biosynthetic process / mitophagy / : / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of protein ubiquitination / positive regulation of TORC1 signaling / response to nutrient / negative regulation of cell migration / positive regulation of translation / Signal transduction by L1 / cell projection / response to insulin / Hsp90 protein binding / negative regulation of transforming growth factor beta receptor signaling pathway / circadian regulation of gene expression / mitochondrial membrane / cellular response to glucose stimulus / protein processing / PML body / chromatin DNA binding / Regulation of necroptotic cell death / Wnt signaling pathway / Regulation of PTEN stability and activity / positive regulation of protein catabolic process / kinase activity / UCH proteinases / KEAP1-NFE2L2 pathway / rhythmic process / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / double-strand break repair / chromatin organization / HATs acetylate histones / positive regulation of cold-induced thermogenesis / positive regulation of cell growth / Regulation of TP53 Activity through Phosphorylation / 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 / regulation of cell cycle / negative regulation of translation / protein stabilization / protein phosphorylation / protein serine kinase activity
Similarity search - Function
Signal recognition particle alu RNA binding heterodimer, srp9/1 - #150 / UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110kDa subunit / Rossmann fold - #11380 / O-GlcNAc transferase, C-terminal / Glycosyl transferase family 41 / Signal recognition particle alu RNA binding heterodimer, srp9/1 / TPR repeat / Tetratricopeptide repeat / Casein Kinase 2, subunit alpha / Tetratricopeptide repeat ...Signal recognition particle alu RNA binding heterodimer, srp9/1 - #150 / UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110kDa subunit / Rossmann fold - #11380 / O-GlcNAc transferase, C-terminal / Glycosyl transferase family 41 / Signal recognition particle alu RNA binding heterodimer, srp9/1 / TPR repeat / Tetratricopeptide repeat / Casein Kinase 2, subunit alpha / Tetratricopeptide repeat / Tetratricopeptide repeat domain / Tetratricopeptide repeat / Glycogen Phosphorylase B; / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / 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 / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
2-acetamido-2-deoxy-5-thio-beta-D-glucopyranose / URIDINE-5'-DIPHOSPHATE / UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit / Casein kinase II subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsLazarus, M.B. / Jiang, J. / Gloster, T.M. / Zandberg, W.F. / Vocadlo, D.J. / Walker, S.
CitationJournal: Nat.Chem.Biol. / Year: 2012
Title: Structural snapshots of the reaction coordinate for O-GlcNAc transferase.
Authors: Lazarus, M.B. / Jiang, J. / Gloster, T.M. / Zandberg, W.F. / Whitworth, G.E. / Vocadlo, D.J. / Walker, S.
History
DepositionSep 5, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 31, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 12, 2012Group: Database references
Revision 1.2Jul 29, 2020Group: Database references / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_entity_nonpoly / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Oct 16, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: Casein kinase II subunit alpha
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)166,31711
Polymers164,7464
Non-polymers1,5717
Water15,061836
1
A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,2076
Polymers82,3732
Non-polymers8344
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1510 Å2
ΔGint-13 kcal/mol
Surface area29160 Å2
MethodPISA
2
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)83,1115
Polymers82,3732
Non-polymers7373
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1540 Å2
ΔGint-13 kcal/mol
Surface area28420 Å2
MethodPISA
3
A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: Casein kinase II subunit alpha
hetero molecules

A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)166,41312
Polymers164,7464
Non-polymers1,6678
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7750 Å2
ΔGint-42 kcal/mol
Surface area53600 Å2
MethodPISA
4
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: Casein kinase II subunit alpha
hetero molecules

C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: Casein kinase II subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)166,22110
Polymers164,7464
Non-polymers1,4756
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7770 Å2
ΔGint-43 kcal/mol
Surface area52150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.770, 137.620, 153.016
Angle α, β, γ (deg.)90.00, 102.82, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11A-1606-

HOH

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Components

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Protein / Protein/peptide / Sugars , 3 types, 6 molecules ACBD

#1: Protein UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit / O-GlcNAc transferase subunit p110 / O-linked N-acetylglucosamine transferase 110 kDa subunit / OGT


Mass: 80974.508 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: OGT / Production host: Escherichia coli (E. coli) / References: UniProt: O15294, protein O-GlcNAc transferase
#2: Protein/peptide Casein kinase II subunit alpha / CK II alpha


Mass: 1398.562 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: synthetic peptide / Source: (synth.) Homo sapiens (human)
References: UniProt: P68400, non-specific serine/threonine protein kinase
#5: Sugar ChemComp-0YT / 2-acetamido-2-deoxy-5-thio-beta-D-glucopyranose / 2-(acetylamino)-2-deoxy-5-thio-beta-D-glucopyranose / 2-acetamido-2-deoxy-5-thio-beta-D-glucose / 2-acetamido-2-deoxy-5-thio-D-glucose / 2-acetamido-2-deoxy-5-thio-glucose


Type: D-saccharide, beta linking / Mass: 237.273 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C8H15NO5S

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Non-polymers , 3 types, 841 molecules

#3: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 836 / 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: 3.08 Å3/Da / Density % sol: 60.03 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 1.6M Lithium Sulfate, 0.1M Bis Tris Propane pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 19, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.075 Å / Relative weight: 1
ReflectionResolution: 1.9→49.87 Å / Num. all: 154828 / Num. obs: 154828 / % possible obs: 99.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2
Reflection shellResolution: 1.9→2 Å / % possible all: 99

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Processing

Software
NameVersionClassification
CBASSdata collection
PHENIX(phenix.refine: 1.7.2_869)model building
PHENIX(phenix.refine: 1.7.2_869)refinement
iMOSFLMdata reduction
SCALAdata scaling
PHENIX1.7.2_869phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→48.154 Å / SU ML: 0.58 / σ(F): 0 / Phase error: 24.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2496 7781 5.03 %RANDOM
Rwork0.2262 ---
all0.2274 154706 --
obs0.2274 154706 98.93 %-
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.196 Å2 / ksol: 0.4 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-0.5463 Å2-0 Å24.3117 Å2
2---0.3929 Å20 Å2
3----0.1534 Å2
Refinement stepCycle: LAST / Resolution: 1.9→48.154 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11018 0 93 836 11947
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00511448
X-RAY DIFFRACTIONf_angle_d0.91515554
X-RAY DIFFRACTIONf_dihedral_angle_d13.0554291
X-RAY DIFFRACTIONf_chiral_restr0.0631716
X-RAY DIFFRACTIONf_plane_restr0.0042013
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.92160.34872510.30094842X-RAY DIFFRACTION99
1.9216-1.94420.35282920.29024859X-RAY DIFFRACTION99
1.9442-1.96790.28712460.26184868X-RAY DIFFRACTION99
1.9679-1.99280.26952560.24184926X-RAY DIFFRACTION99
1.9928-2.0190.2582870.22594878X-RAY DIFFRACTION99
2.019-2.04670.27462510.22484876X-RAY DIFFRACTION99
2.0467-2.07590.25812360.22124872X-RAY DIFFRACTION99
2.0759-2.10690.25862340.21724936X-RAY DIFFRACTION99
2.1069-2.13990.28622630.25464896X-RAY DIFFRACTION99
2.1399-2.17490.30522480.28174907X-RAY DIFFRACTION99
2.1749-2.21240.23732620.22294898X-RAY DIFFRACTION99
2.2124-2.25270.24192670.22294884X-RAY DIFFRACTION99
2.2527-2.2960.26172810.22484862X-RAY DIFFRACTION99
2.296-2.34290.27392370.22424916X-RAY DIFFRACTION99
2.3429-2.39380.26082650.23044874X-RAY DIFFRACTION99
2.3938-2.44950.27182720.23554857X-RAY DIFFRACTION99
2.4495-2.51070.28072760.24094895X-RAY DIFFRACTION99
2.5107-2.57860.23862590.22654910X-RAY DIFFRACTION99
2.5786-2.65450.28032450.23424905X-RAY DIFFRACTION99
2.6545-2.74020.27622250.23454954X-RAY DIFFRACTION99
2.7402-2.83810.27052290.23684893X-RAY DIFFRACTION99
2.8381-2.95170.24762840.22414908X-RAY DIFFRACTION99
2.9517-3.0860.2252750.21574931X-RAY DIFFRACTION100
3.086-3.24870.25382450.22394942X-RAY DIFFRACTION100
3.2487-3.45220.2222890.20524934X-RAY DIFFRACTION100
3.4522-3.71860.22522680.20514898X-RAY DIFFRACTION99
3.7186-4.09270.19732440.19484923X-RAY DIFFRACTION98
4.0927-4.68450.22182690.19224746X-RAY DIFFRACTION96
4.6845-5.90030.22752560.22284987X-RAY DIFFRACTION100
5.9003-48.1690.28392690.27974948X-RAY DIFFRACTION98
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)
13.3603-2.52592.67413.9361-1.02143.738-0.07040.01560.2325-0.33140.18850.407-0.3108-0.30450.29180.430.0148-0.25810.61610.33420.5865-13.08335.5304-36.4377
21.56940.60350.63123.41510.55723.67170.04090.4774-0.0262-0.39680.06840.2165-0.0963-0.1553-0.11250.14090.0557-0.01030.3629-0.00440.211-2.622735.8219-22.923
32.69070.5511-3.03570.4311-0.48244.40780.14520.06670.3013-0.02920.01070.0215-0.0901-0.0019-0.12720.19030.0480.06450.15420.05290.1933-11.830547.7037-3.7111
44.30740.66861.77174.0657-0.11541.94110.04470.28910.0718-0.49760.09260.2465-0.0427-0.1559-0.13690.27670.076-0.01470.19150.0510.145-28.086542.3473-6.4877
50.8582-0.12030.03211.5207-0.25931.28480.07690.23260.0073-0.51-0.04820.13520.1303-0.0805-0.01990.25560.0473-0.05850.1474-0.00580.0932-25.687916.335-3.5037
68.4915-1.4402-2.142.7121-2.74385.4797-0.1667-1.0250.89641.1892-0.41530.2919-0.5828-0.16220.2340.32590.03290.02650.1845-0.04480.1943-19.36923.295738.5321
70.7916-0.2059-0.6011.6993-0.80861.0471-0.1104-0.338-0.1670.74430.16320.4695-0.0115-0.103-0.02490.31420.02580.07750.24650.03240.1836-18.841417.692938.788
83.72090.94424.55660.66950.8415.8092-0.33-0.28730.46760.26180.3734-0.4397-0.61570.35630.09090.5945-0.1844-0.02970.6004-0.27460.2739-11.251420.901945.8431
90.979-0.6443-0.02391.836-0.34080.81190.0186-0.14020.16820.1930.045-0.1198-0.13920.0112-0.03760.0934-0.00810.02050.1124-0.0260.1104-15.105932.985424.337
100.4046-0.3562-0.13151.35790.57391.45230.0652-0.03460.10680.0656-0.02570.2765-0.0596-0.1675-0.03290.07460.01670.02180.128-0.01450.1756-32.558927.847620.6564
111.9438-1.06891.56340.6358-0.69181.6036-0.05660.2935-0.0662-0.49350.06691.0020.0024-0.722-0.1420.1484-0.0402-0.42360.3194-0.04380.2004-40.980712.7551-3.3595
127.2295-0.80625.70990.4389-0.74054.56730.18510.33110.10490.079-0.1385-0.09520.15940.4709-0.07890.15160.01450.02880.2172-0.02260.2023-8.252327.722611.3862
136.4776-2.683.85454.6815-4.63174.87610.13440.97240.7054-0.5578-0.4611-0.8745-0.58120.87290.36760.35230.01110.08260.29360.06760.2712-17.19332.0677-4.2427
144.9594-0.7301-0.68872.5283-1.40051.4755-0.39590.0799-0.02930.29920.1961-0.8122-0.16340.30390.22390.46620.1519-0.15991.3663-0.19880.920237.6539-21.79441.1276
153.7307-0.1313-0.99514.0988-0.00331.73450.0407-0.4271-0.05050.1461-0.1583-0.4629-0.23630.9350.05270.2217-0.0390.02170.49570.06320.170421.1009-24.74730.3376
161.95350.9823-2.12211.007-0.80725.4935-0.14830.0396-0.0835-0.07350.0742-0.03210.3110.04920.04830.1750.06130.04260.1560.03040.13948.0123-36.27267.6866
173.06310.16972.05152.11940.66463.0561-0.1087-0.0965-0.06390.23040.0057-0.36240.14610.19530.09880.16530.05640.02120.16750.06070.19726.1516-32.731925.3482
181.1416-0.1263-0.06711.3652-0.14731.0464-0.0053-0.06680.06470.064-0.0452-0.46120.00760.2510.01760.09220.0047-0.03690.14860.04380.26516.4357-5.190724.9553
196.0159-0.14660.50263.4572-0.6538.71290.1177-0.4172-0.51130.3348-0.11591.00380.6902-0.88010.0010.1874-0.00670.09350.23590.01180.3743-36.1125-13.370524.5421
201.2896-1.2539-0.42312.8119-0.15540.8855-0.0564-0.07720.13990.49030.16960.4848-0.1763-0.435-0.08750.17470.03580.05090.24420.02380.2366-36.1494-5.22322.8465
219.02412.23665.83022.27190.97394.8917-0.49460.5631-0.3664-0.09580.2390.69180.4602-0.58040.17620.2774-0.02640.01910.369-0.06190.4041-41.8937-9.133119.8555
220.8984-0.54640.0482.1061-0.57211.0138-0.02480.0308-0.1156-0.09760.01960.24790.1449-0.1401-0.00730.1072-0.02740.01020.1208-0.0060.1046-22.9414-21.759717.5474
231.7704-0.5332-0.18812.5211-0.18720.7257-0.0784-0.2017-0.05920.25590.0285-0.01840.03280.0410.04580.1803-0.00350.0030.15390.03280.1172-12.0326-18.388832.6106
241.004-0.0706-0.24471.1319-0.11180.6931-0.0273-0.25780.0860.416-0.0332-0.07310.07870.04320.02360.190.0016-0.03120.14060.0280.0782-10.1718-10.995237.4503
255.6835-1.1755.61941.34-1.04715.58780.04840.66610.2145-0.0968-0.19420.072-0.06950.31790.13990.2233-0.00140.02070.25550.0270.1656-10.4618-16.58999.4186
262.5432-4.33670.30277.49480.39358.40560.23711.0026-0.542-0.9815-0.5502-0.43840.60810.63740.22350.2910.02480.10630.2468-0.01650.28346.1995-20.87916.4374
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 314:339 )A314 - 339
2X-RAY DIFFRACTION2( CHAIN A AND RESID 340:410 )A340 - 410
3X-RAY DIFFRACTION3( CHAIN A AND RESID 411:474 )A411 - 474
4X-RAY DIFFRACTION4( CHAIN A AND RESID 475:515 )A475 - 515
5X-RAY DIFFRACTION5( CHAIN A AND RESID 516:705 )A516 - 705
6X-RAY DIFFRACTION6( CHAIN A AND RESID 706:718 )A706 - 718
7X-RAY DIFFRACTION7( CHAIN A AND RESID 719:766 )A719 - 766
8X-RAY DIFFRACTION8( CHAIN A AND RESID 767:772 )A767 - 772
9X-RAY DIFFRACTION9( CHAIN A AND RESID 773:917 )A773 - 917
10X-RAY DIFFRACTION10( CHAIN A AND RESID 918:1004 )A918 - 1004
11X-RAY DIFFRACTION11( CHAIN A AND RESID 1005:1028 )A1005 - 1028
12X-RAY DIFFRACTION12( CHAIN B AND RESID 13:20 )B13 - 20
13X-RAY DIFFRACTION13( CHAIN B AND RESID 21:26 )B21 - 26
14X-RAY DIFFRACTION14( CHAIN C AND RESID 336:348 )C336 - 348
15X-RAY DIFFRACTION15( CHAIN C AND RESID 349:408 )C349 - 408
16X-RAY DIFFRACTION16( CHAIN C AND RESID 409:460 )C409 - 460
17X-RAY DIFFRACTION17( CHAIN C AND RESID 461:515 )C461 - 515
18X-RAY DIFFRACTION18( CHAIN C AND RESID 516:705 )C516 - 705
19X-RAY DIFFRACTION19( CHAIN C AND RESID 706:721 )C706 - 721
20X-RAY DIFFRACTION20( CHAIN C AND RESID 722:763 )C722 - 763
21X-RAY DIFFRACTION21( CHAIN C AND RESID 764:772 )C764 - 772
22X-RAY DIFFRACTION22( CHAIN C AND RESID 773:913 )C773 - 913
23X-RAY DIFFRACTION23( CHAIN C AND RESID 914:958 )C914 - 958
24X-RAY DIFFRACTION24( CHAIN C AND RESID 959:1028 )C959 - 1028
25X-RAY DIFFRACTION25( CHAIN D AND RESID 13:20 )D13 - 20
26X-RAY DIFFRACTION26( CHAIN D AND RESID 21:26 )D21 - 26

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