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- PDB-4gyw: Crystal structure of human O-GlcNAc Transferase in complex with U... -

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Basic information

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


negative regulation of non-canonical inflammasome complex assembly / protein N-acetylglucosaminyltransferase complex / regulation of insulin receptor signaling pathway / protein O-GlcNAc transferase / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of Rac protein signal transduction / regulation of necroptotic process / protein O-linked glycosylation ...negative regulation of non-canonical inflammasome complex assembly / protein N-acetylglucosaminyltransferase complex / regulation of insulin receptor signaling pathway / protein O-GlcNAc transferase / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of Rac protein signal transduction / regulation of necroptotic process / protein O-linked glycosylation / negative regulation of stem cell population maintenance / regulation of gluconeogenesis / Phosphorylation and nuclear translocation of BMAL1 (ARNTL) and CLOCK / positive regulation of aggrephagy / regulation of chromosome separation / WNT mediated activation of DVL / Condensation of Prometaphase Chromosomes / regulation of glycolytic process / protein kinase CK2 complex / symbiont-mediated disruption of host cell PML body / RIPK1-mediated regulated necrosis / Phosphorylation and nuclear translocation of the CRY:PER:kinase complex / Regulation of CDH1 posttranslational processing and trafficking to plasma membrane / Receptor Mediated Mitophagy / Sin3-type complex / regulation of synapse assembly / Formation of WDR5-containing histone-modifying complexes / hemopoiesis / positive regulation of stem cell population maintenance / Synthesis of PC / negative regulation of apoptotic signaling pathway / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of proteolysis / negative regulation of signal transduction by p53 class mediator / Maturation of hRSV A proteins / phosphatidylinositol-3,4,5-trisphosphate binding / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / histone acetyltransferase complex / negative regulation of double-strand break repair via homologous recombination / positive regulation of Wnt signaling pathway / mitophagy / cell projection / response to nutrient / positive regulation of TORC1 signaling / negative regulation of protein ubiquitination / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of cell migration / negative regulation of transforming growth factor beta receptor signaling pathway / Signal transduction by L1 / positive regulation of translation / protein processing / cellular response to glucose stimulus / circadian regulation of gene expression / Wnt signaling pathway / response to insulin / Hsp90 protein binding / chromatin DNA binding / peptidyl-serine phosphorylation / PML body / Regulation of necroptotic cell death / mitochondrial membrane / SPOP-mediated proteasomal degradation of PD-L1(CD274) / Regulation of PTEN stability and activity / positive regulation of protein catabolic process / kinase activity / double-strand break repair / KEAP1-NFE2L2 pathway / rhythmic process / UCH proteinases / positive regulation of cell growth / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / positive regulation of cold-induced thermogenesis / HATs acetylate histones / protein folding / heterochromatin formation / chromatin organization / Regulation of TP53 Activity through Phosphorylation / regulation of cell cycle / non-specific serine/threonine protein kinase / protein stabilization / negative regulation of translation / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / positive regulation of cell population proliferation / regulation of transcription by RNA polymerase II / DNA damage response / positive regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / glutamatergic synapse / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA-templated transcription / nucleoplasm / ATP binding / identical protein binding / nucleus / plasma membrane
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 / Tetratricopeptide repeat / Casein Kinase 2, subunit alpha ...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 / Tetratricopeptide repeat / Casein Kinase 2, subunit alpha / 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
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: 1.7 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: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / 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_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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 1.3Nov 6, 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)166,28511
Polymers164,7464
Non-polymers1,5397
Water17,475970
1
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)83,0955
Polymers82,3732
Non-polymers7213
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1520 Å2
ΔGint-12 kcal/mol
Surface area28570 Å2
MethodPISA
2
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)83,1916
Polymers82,3732
Non-polymers8174
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1510 Å2
ΔGint-10 kcal/mol
Surface area29400 Å2
MethodPISA
3
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)166,18910
Polymers164,7464
Non-polymers1,4436
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7660 Å2
ΔGint-38 kcal/mol
Surface area52510 Å2
MethodPISA
4
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)166,38112
Polymers164,7464
Non-polymers1,6358
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7720 Å2
ΔGint-37 kcal/mol
Surface area54110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.000, 137.770, 153.566
Angle α, β, γ (deg.)90.00, 102.90, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11A-1673-

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: synthesized peptide / Source: (synth.) Homo sapiens (human)
References: UniProt: P68400, non-specific serine/threonine protein kinase
#5: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 975 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.: 970 / 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: 3.1 Å3/Da / Density % sol: 60.3 %
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: Apr 29, 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: 1.7→43.904 Å / Num. all: 206769 / Num. obs: 206769 / % possible obs: 94.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.2 %
Reflection shellResolution: 1.7→1.79 Å / % possible all: 87.1

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Processing

Software
NameVersionClassification
CBASSdata collection
PHENIX(phenix.refine: 1.7_650)model building
PHENIX(phenix.refine: 1.7_650)refinement
iMOSFLMdata reduction
SCALAdata scaling
PHENIX1.7_650phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→43.904 Å / SU ML: 0.2 / σ(F): 0 / Phase error: 20.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.205 10329 5 %RANDOM
Rwork0.1872 ---
all0.1881 217098 --
obs0.1881 206769 94.15 %-
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 44.181 Å2 / ksol: 0.407 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-1.4153 Å20 Å22.1771 Å2
2---1.9612 Å2-0 Å2
3---0.5459 Å2
Refinement stepCycle: LAST / Resolution: 1.7→43.904 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11018 0 93 970 12081
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00511462
X-RAY DIFFRACTIONf_angle_d0.97215576
X-RAY DIFFRACTIONf_dihedral_angle_d13.2244315
X-RAY DIFFRACTIONf_chiral_restr0.0661718
X-RAY DIFFRACTIONf_plane_restr0.0052017
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.71930.31453000.30835791X-RAY DIFFRACTION83
1.7193-1.73950.3093090.29676054X-RAY DIFFRACTION87
1.7395-1.76080.29563050.27646168X-RAY DIFFRACTION89
1.7608-1.7830.29923580.25926132X-RAY DIFFRACTION89
1.783-1.80650.30513130.23556206X-RAY DIFFRACTION89
1.8065-1.83130.23053150.2156155X-RAY DIFFRACTION89
1.8313-1.85740.25653250.23016201X-RAY DIFFRACTION89
1.8574-1.88510.23472970.2216241X-RAY DIFFRACTION90
1.8851-1.91460.26143310.19416345X-RAY DIFFRACTION91
1.9146-1.9460.21593700.18166347X-RAY DIFFRACTION92
1.946-1.97950.21833290.18036481X-RAY DIFFRACTION93
1.9795-2.01550.20023420.17126440X-RAY DIFFRACTION93
2.0155-2.05430.20043600.17496591X-RAY DIFFRACTION95
2.0543-2.09620.19173180.18176656X-RAY DIFFRACTION95
2.0962-2.14180.24083430.2146574X-RAY DIFFRACTION95
2.1418-2.19160.20753440.20096713X-RAY DIFFRACTION96
2.1916-2.24650.19933620.17926825X-RAY DIFFRACTION98
2.2465-2.30720.21173900.17946813X-RAY DIFFRACTION99
2.3072-2.37510.20233430.17796938X-RAY DIFFRACTION99
2.3751-2.45170.21653890.18976829X-RAY DIFFRACTION100
2.4517-2.53930.2083780.18696956X-RAY DIFFRACTION100
2.5393-2.6410.223640.18856940X-RAY DIFFRACTION100
2.641-2.76120.21623340.19536943X-RAY DIFFRACTION100
2.7612-2.90670.21813490.19576983X-RAY DIFFRACTION100
2.9067-3.08880.19553860.18436874X-RAY DIFFRACTION99
3.0888-3.32720.19363600.18126938X-RAY DIFFRACTION99
3.3272-3.66190.16653960.1636844X-RAY DIFFRACTION99
3.6619-4.19140.15573470.14996779X-RAY DIFFRACTION97
4.1914-5.27930.16673380.15586576X-RAY DIFFRACTION94
5.2793-43.91830.23443340.22626107X-RAY DIFFRACTION86
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)
10.0146-0.01740.01390.0219-0.0140.0120.0202-0.0216-0.0292-0.0640.05940.0954-0.0133-0.10340.02020.30320.0135-0.25690.43450.32330.3975-13.042935.5775-36.5121
20.2876-0.01410.15860.4047-0.15250.17290.03780.20180.0586-0.11790.06490.1652-0.0484-0.0046-0.03080.11830.0291-0.00670.24420.01790.1455-2.577735.8779-22.9261
30.02490.0488-0.03870.0653-0.02620.07070.09250.05850.1698-0.0015-0.01280.0005-0.0708-0.0232-0.02370.13730.05110.08070.11970.05490.1592-11.907947.7776-3.7658
40.1498-0.02070.05480.3289-0.21370.29610.0410.0770.0731-0.13870.10080.1003-0.001-0.126-0.04970.22080.0412-0.01360.19240.06740.192-28.402942.2977-6.5668
50.2411-0.01850.01340.4762-0.14010.19030.04640.09680.0141-0.2485-0.01460.07960.0653-0.03160.01030.19410.0391-0.04810.1328-0.00110.1016-25.862916.409-3.4643
60.1175-0.1693-0.05930.28750.12950.1052-0.0048-0.03230.01280.1470.00920.03650.0126-0.0081-0.00150.22410.00580.02780.1149-0.00450.1384-19.429723.385638.7429
70.3238-0.0053-0.11250.26470.03490.0622-0.0216-0.2346-0.01140.20260.05080.1460.0282-0.00350.0060.18750.0170.04960.15250.00810.1123-18.841117.759138.934
80.0022-0.00380.00030.007-0.0010.00210.015-0.13280.0520.130.0098-0.00960.1299-0.0789-0.00970.4204-0.03680.00940.4463-0.14130.1973-11.34120.977345.8929
90.26130.0212-0.09030.26450.00940.18530.0499-0.04730.09270.05430.0132-0.0189-0.05160.0077-0.00430.09770.00980.02450.0876-0.02240.1048-15.196333.056224.3721
100.05530.0248-0.0430.10020.01090.11860.0513-0.00530.04020.0267-0.02070.1466-0.0297-0.06110.02090.08970.0190.02140.1049-0.01150.1461-32.690227.91820.7683
110.058-0.03680.04010.0194-0.01870.0209-0.02740.0557-0.0151-0.08850.04040.15950.004-0.1083-0.00990.1574-0.0146-0.29050.19330.00410.2071-41.150212.7835-3.318
120.06620.00170.04190.00160.00190.02790.049-0.03840.0069-0.0035-0.0124-0.0706-0.01090.057-0.01290.1109-0.00260.00240.1615-0.01410.1818-8.356527.784711.4055
130.01340.00950.00830.0060.00540.0050.03310.03070.017-0.0277-0.011-0.01620.0011-0.0139-0.0080.18050.0370.01690.23390.0470.1378-17.450232.1735-4.1756
140.0171-0.02260.02290.0323-0.03180.0337-0.0119-0.0145-0.0110.0167-0.0123-0.0585-0.02390.16090.01760.87660.0338-0.12931.2421-0.11381.026337.6917-22.10031.0601
150.13390.091-0.04970.2665-0.06650.11430.0613-0.23920.00760.1115-0.2725-0.1867-0.14450.52380.01520.1625-0.04750.01860.37960.09320.156621.1696-25.12880.2554
160.06640.0102-0.12310.0387-0.00850.2104-0.0345-0.0036-0.0346-0.0310.0045-0.01580.13430.07160.01520.1610.05230.05660.15940.03780.10397.9658-36.38877.7101
170.2071-0.14220.13480.1249-0.03360.1453-0.1126-0.0266-0.01020.08610.0169-0.07660.12310.07520.01640.16360.0558-0.00040.14220.04060.16216.2059-32.640525.4891
180.1338-0.0285-0.05520.49320.00510.3298-0.0071-0.02990.01450.0443-0.0137-0.22480.00660.11520.04320.09710.0011-0.02610.12940.03080.18916.3444-5.180324.985
190.02010.0096-0.03010.1838-0.03930.0950.0101-0.0324-0.02510.05310.00320.06430.0351-0.0750.00080.1533-0.00980.05030.13280.00510.2322-36.2233-13.394224.5259
200.14020.1234-0.21020.3135-0.05940.4670.0215-0.00080.08330.11710.00150.1197-0.0339-0.2049-0.02640.12330.00260.03290.15950.02230.1838-36.3184-5.237722.8935
210.0499-0.09540.03730.1866-0.06810.0282-0.0550.05590.07990.00910.06040.16650.0558-0.24470.00840.1871-0.03390.01620.314-0.00510.3565-42.03-9.135719.9001
220.1685-0.0693-0.00740.26710.02740.2567-0.04220.0075-0.042-0.0086-0.00370.07010.0829-0.0431-0.04350.0939-0.0160.02240.08730.01380.1045-23.0386-21.788917.6068
230.0619-0.0007-0.02620.06660.01810.0155-0.0291-0.05310.00430.1331-0.0089-0.0102-0.02510.05160.01810.1340.00130.0140.10560.03010.0909-12.1463-18.402132.6911
240.1668-0.0432-0.01690.2910.02120.1106-0.1331-0.21360.14340.47840.07160.0165-0.0025-0.0167-0.02930.1413-0.01840.00010.0920.03770.0307-10.2985-10.987637.5303
250.0717-0.0397-0.04030.04210.0140.0694-0.0130.0522-0.0061-0.0324-0.0519-0.0180.0118-0.0470.01160.1575-0.0130.01680.16010.01760.1345-10.5786-16.64499.4018
260.0233-0.004-0.00230.0210.03240.0857-0.02360.0038-0.0105-0.0321-0.0281-0.01940.01370.01880.01060.18780.0350.02310.1970.00830.18766.0175-20.979316.5844
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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