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- PDB-5hgv: Structure of an O-GlcNAc transferase point mutant, D554N in compl... -

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Basic information

Entry
Database: PDB / ID: 5hgv
TitleStructure of an O-GlcNAc transferase point mutant, D554N in complex with peptide
Components
  • TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
  • UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
KeywordsTRANSFERASE/PEPTIDE / Point mutant / Glycosyltransferase / OGT / TRANSFERASE-PEPTIDE complex
Function / homology
Function and homology information


protein N-acetylglucosaminyltransferase complex / protein O-GlcNAc transferase / regulation of insulin receptor signaling pathway / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of necroptotic process / regulation of Rac protein signal transduction / negative regulation of stem cell population maintenance / protein O-linked glycosylation ...protein N-acetylglucosaminyltransferase complex / protein O-GlcNAc transferase / regulation of insulin receptor signaling pathway / protein O-acetylglucosaminyltransferase activity / positive regulation of transcription from RNA polymerase II promoter by glucose / acetylglucosaminyltransferase activity / regulation of necroptotic process / regulation of Rac protein signal transduction / negative regulation of stem cell population maintenance / protein O-linked glycosylation / NSL complex / 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 / regulation of glycolytic process / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / RIPK1-mediated regulated necrosis / regulation of synapse assembly / regulation of gluconeogenesis / Receptor Mediated Mitophagy / Sin3-type complex / positive regulation of stem cell population maintenance / Formation of WDR5-containing histone-modifying complexes / Synthesis of PC / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Maturation of hRSV A proteins / phosphatidylinositol-3,4,5-trisphosphate binding / positive regulation of proteolysis / mitophagy / negative regulation of apoptotic signaling pathway / hemopoiesis / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of Wnt signaling pathway / histone acetyltransferase complex / negative regulation of double-strand break repair via homologous recombination / positive regulation of lipid biosynthetic process / chaperone-mediated protein folding / negative regulation of protein ubiquitination / positive regulation of TORC1 signaling / negative regulation of ubiquitin-dependent protein catabolic process / negative regulation of cell migration / response to nutrient / Signal transduction by L1 / cell projection / positive regulation of translation / mitochondrial membrane / cellular response to glucose stimulus / peptidyl-threonine phosphorylation / negative regulation of transforming growth factor beta receptor signaling pathway / circadian regulation of gene expression / Hsp90 protein binding / response to insulin / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / Regulation of necroptotic cell death / protein processing / chromatin DNA binding / 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 / UCH proteinases / KEAP1-NFE2L2 pathway / double-strand break repair / rhythmic process / chromatin organization / kinase activity / positive regulation of cold-induced thermogenesis / HATs acetylate histones / positive regulation of cell growth / peptidyl-serine phosphorylation / Regulation of TP53 Activity through Phosphorylation / protein stabilization / negative regulation of translation / non-specific serine/threonine protein kinase / regulation of cell cycle / cell cycle / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / glutamatergic synapse / apoptotic process / DNA damage response / positive regulation of cell population proliferation / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / ATP binding / identical protein binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Signal recognition particle alu RNA binding heterodimer, srp9/1 - #150 / Rossmann fold - #11380 / Signal recognition particle alu RNA binding heterodimer, srp9/1 / O-GlcNAc transferase, C-terminal / Glycosyl transferase family 41 / TPR repeat / Tetratricopeptide repeat / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / Casein Kinase 2, subunit alpha ...Signal recognition particle alu RNA binding heterodimer, srp9/1 - #150 / Rossmann fold - #11380 / Signal recognition particle alu RNA binding heterodimer, srp9/1 / O-GlcNAc transferase, C-terminal / Glycosyl transferase family 41 / TPR repeat / Tetratricopeptide repeat / Tetratricopeptide repeat 1 / 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: 2.05 Å
AuthorsJanetzko, J. / Lazarus, M.B. / Walker, S.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM094263 United States
CitationJournal: Nat.Chem.Biol. / Year: 2016
Title: How the glycosyltransferase OGT catalyzes amide bond cleavage.
Authors: Janetzko, J. / Trauger, S.A. / Lazarus, M.B. / Walker, S.
History
DepositionJan 8, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 14, 2016Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2016Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Derived calculations / Category: pdbx_audit_support / pdbx_struct_oper_list
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / 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_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
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: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules


Theoretical massNumber of molelcules
Total (without water)165,68611
Polymers164,1484
Non-polymers1,5397
Water13,908772
1
A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules


Theoretical massNumber of molelcules
Total (without water)82,8916
Polymers82,0742
Non-polymers8174
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-46 kcal/mol
Surface area28780 Å2
MethodPISA
2
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules


Theoretical massNumber of molelcules
Total (without water)82,7955
Polymers82,0742
Non-polymers7213
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3140 Å2
ΔGint-34 kcal/mol
Surface area27970 Å2
MethodPISA
3
A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules

A: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
B: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules


Theoretical massNumber of molelcules
Total (without water)165,78312
Polymers164,1484
Non-polymers1,6358
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area11420 Å2
ΔGint-110 kcal/mol
Surface area52730 Å2
MethodPISA
4
C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules

C: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
D: TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET
hetero molecules


Theoretical massNumber of molelcules
Total (without water)165,59010
Polymers164,1484
Non-polymers1,4436
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area10980 Å2
ΔGint-82 kcal/mol
Surface area51240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.350, 137.190, 153.070
Angle α, β, γ (deg.)90.000, 103.050, 90.000
Int Tables number5
Space group name H-MI121

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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: 80675.219 Da / Num. of mol.: 2 / Mutation: D554N
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 TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET


Mass: 1398.562 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68400*PLUS
#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, 777 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.: 772 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.16 Å3/Da / Density % sol: 61.02 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 1.6 M Lithium Sulfate, 0.1 M Bis Tris Propane pH 7.0
PH range: 7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.09999 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 17, 2012
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.09999 Å / Relative weight: 1
ReflectionResolution: 2.05→40.93 Å / Num. obs: 117637 / % possible obs: 95.2 % / Redundancy: 2.7 % / CC1/2: 0.976 / Rmerge(I) obs: 0.097 / Rpim(I) all: 0.066 / Net I/σ(I): 5.9 / Num. measured all: 313938 / Scaling rejects: 140
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) all% possible all
2.05-2.092.30.3241.91233452710.5210.24386.3
11.23-40.933.20.07810.824937810.9890.04997.9

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Processing

Software
NameVersionClassification
SCALA0.5.12data scaling
PHENIXrefinement
PDB_EXTRACT3.15data extraction
PHASERphasing
CBASSdata collection
iMOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3PE4

3pe4


Resolution: 2.05→40.925 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2374 5893 5.02 %
Rwork0.2172 111524 -
obs0.2182 117417 94.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 96.28 Å2 / Biso mean: 32.3017 Å2 / Biso min: 9.39 Å2
Refinement stepCycle: final / Resolution: 2.05→40.925 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11018 0 93 772 11883
Biso mean--21.8 33.6 -
Num. residues----1397
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00411462
X-RAY DIFFRACTIONf_angle_d0.66115576
X-RAY DIFFRACTIONf_chiral_restr0.0451718
X-RAY DIFFRACTIONf_plane_restr0.0052017
X-RAY DIFFRACTIONf_dihedral_angle_d11.8566983
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.05-2.07330.28611610.25493366352787
2.0733-2.09770.26691520.24173348350085
2.0977-2.12330.26061810.23093362354386
2.1233-2.15020.26751790.23013380355988
2.1502-2.17840.25041780.22583478365689
2.1784-2.20830.27441880.23183412360088
2.2083-2.23980.24281790.23543464364389
2.2398-2.27330.26292120.23263494370690
2.2733-2.30880.28141910.23723565375691
2.3088-2.34660.22511750.23113626380193
2.3466-2.38710.29611990.23563662386194
2.3871-2.43050.25352010.23733714391595
2.4305-2.47720.28172280.24423730395896
2.4772-2.52780.2521880.24333786397497
2.5278-2.58270.25392170.24183794401198
2.5827-2.64280.30571850.23693851403698
2.6428-2.70890.30871720.24943887405999
2.7089-2.78210.26731950.247138984093100
2.7821-2.8640.27031970.237539294126100
2.864-2.95640.23532160.22763890410699
2.9564-3.0620.23852150.22383836405199
3.062-3.18460.25841970.226339224119100
3.1846-3.32940.24382120.21413851406398
3.3294-3.50490.21072200.20263841406199
3.5049-3.72430.20292220.19183856407899
3.7243-4.01170.1881940.18133924411899
4.0117-4.41490.19932100.17473877408798
4.4149-5.05280.20591820.18443913409599
5.0528-6.36210.22082270.21893902412999
6.3621-40.93320.23342200.23423966418699
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)
13.1007-0.94582.21044.19570.3192.6633-0.1882-0.39120.1665-0.89460.30041.020.0233-1.0527-0.15860.70150.0508-0.3380.70960.17630.6763-12.791835.6321-36.4893
21.34020.22650.61963.66150.10613.10570.02370.23670.0218-0.33090.06170.3921-0.0709-0.1291-0.09260.19030.0493-0.01090.36070.01120.2289-2.510135.9428-22.8402
33.69581.0313-3.75360.6758-0.57024.60230.13450.14570.2391-0.0159-0.01320.0482-0.2389-0.0749-0.1230.24920.05210.06240.18980.04550.2355-11.797547.8391-3.7452
44.84340.38211.17775.41040.54582.01330.09170.46220.2914-0.69040.08330.3435-0.2377-0.04-0.1660.33070.0885-0.02370.28030.04890.2689-28.135942.2839-6.7159
51.0547-0.22180.042.0648-0.23671.51820.08650.27520.022-0.567-0.06660.26510.1562-0.0985-0.01610.33530.0557-0.05510.2257-0.02150.1979-25.611916.4683-3.6429
67.0996-0.5336-0.70992.7426-1.6054.8387-0.2001-1.24510.51451.1157-0.4210.6303-0.3998-0.23550.56170.5780.05290.1050.4384-0.00890.2892-19.441923.379938.5965
70.10710.0961-0.06020.9875-0.82660.6931-0.199-0.4772-0.23551.00360.2280.73830.0688-0.28640.01180.48320.04590.16630.35940.0320.3062-18.802317.742938.7543
81.47670.57461.19790.37540.29241.1617-0.2797-0.47230.50360.33750.3771-0.4345-0.56130.20190.01281.0436-0.21560.01510.9304-0.39310.4491-11.34920.964645.7467
91.2508-0.6245-0.01612.2853-0.54671.03050.0457-0.15040.19240.24450.0095-0.0951-0.14140.0336-0.04170.169-0.00210.04980.1567-0.04340.1603-15.115733.038224.2474
100.1261-0.1120.15681.07250.69881.2910.0352-0.02070.04440.1393-0.03580.42030.0173-0.16260.02450.16950.0270.0750.1938-0.02150.2818-32.543827.865820.5533
112.4663-1.41081.60870.8821-0.53962.9672-0.26920.2143-0.1298-0.22620.08631.05790.1345-0.72450.01760.4288-0.0164-0.23820.4147-0.02860.5526-40.917312.887-3.5477
123.429-0.15791.96742.8229-0.9493.25280.3574-0.0565-0.2264-0.1375-0.163-0.480.34050.5879-0.17930.15730.06230.02360.2658-0.01720.1745-8.275827.888911.3
132.82160.50942.88595.3048-1.08153.45080.12010.99860.8955-0.7475-0.1086-0.9073-0.48930.82770.04830.35930.10420.09080.39490.08420.3627-17.06632.2079-4.3305
143.88141.74920.20152.1709-0.81751.2973-0.5076-0.07580.38190.51620.1982-1.1317-0.45080.30210.29580.52180.0088-0.3721.0345-0.18351.131837.6796-22.1541.2321
154.3192-0.1363-1.29794.819-0.87762.63080.0179-0.19060.03930.3283-0.2872-0.5941-0.17811.00440.31770.2992-0.0391-0.00250.54670.08930.250421.045-25.07060.4206
162.02340.7428-2.10330.842-0.13136.2899-0.1159-0.0282-0.1078-0.02420.0234-0.00740.25330.16590.09650.28490.06310.04780.19230.01040.19717.9193-36.37097.7204
172.88930.28021.62352.49660.92262.4834-0.1075-0.0838-0.18520.30920.027-0.38130.22980.20930.06290.27430.06310.03320.22610.07950.23216.1247-32.562825.4142
181.4648-0.05320.00372.0554-0.17121.0030.0067-0.08970.10210.1157-0.0525-0.5469-0.01750.24620.04610.1736-0.0036-0.01860.19210.03590.28936.3142-5.199924.8557
196.1216-0.4710.79924.3485-1.37958.11840.1647-0.7069-0.50140.1938-0.25981.31710.7368-1.00170.09690.3534-0.00860.17030.35230.00370.5549-36.2253-13.307824.2784
202.5702-1.2092-0.77673.38640.82411.19730.0227-0.33530.12740.81630.03610.6343-0.1143-0.4185-0.07360.31580.01680.1130.31580.02460.3641-36.2657-5.149622.5898
217.50851.66144.01412.3312-0.25969.3509-0.46670.7355-0.6906-0.41570.55531.17721.0433-1.0995-0.07860.5149-0.15150.06220.5855-0.07330.7456-41.9957-9.006819.5694
221.0581-0.75660.03422.7922-0.57481.2954-0.00460.0474-0.149-0.10280.01260.37660.1956-0.1828-0.02440.1645-0.03970.03630.1529-0.00680.1716-22.996-21.714117.4134
231.3679-0.59930.32291.9683-0.28380.75640.0546-0.1647-0.01160.3272-0.06220.06990.01490.05920.01520.2731-0.01810.04040.19850.03290.1615-12.1786-18.272932.5197
241.69910.5799-0.09831.7089-0.08740.54760.0118-0.3470.20120.534-0.0693-0.00530.08130.0534-0.02020.32570.00070.03020.20640.02040.116-10.3319-10.893537.3668
255.039-2.10813.75993.3124-0.8513.82160.25820.44620.3483-0.5885-0.16270.1256-0.0755-0.1034-0.130.2507-0.01110.03850.2640.04230.1334-10.5224-16.67889.3169
265.095-5.17971.55386.92120.08173.43950.02160.6113-0.581-1.1766-0.1335-0.58010.7260.91780.06950.38490.02060.13050.3359-0.00840.35.9507-21.02216.3292
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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