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- PDB-4gyy: Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4gyy
TitleCrystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate
Components
  • Casein kinase II subunit alphaCasein kinase 2
  • UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Keywordstransferase/peptide / OGT / O-GlcNAc / GT-B / glycosyltransferase / GlcNAcylation / 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 neurotransmitter receptor localization to postsynaptic specialization membrane / regulation of glycolytic process / RIPK1-mediated regulated necrosis / regulation of synapse assembly / regulation of gluconeogenesis / Receptor Mediated Mitophagy / positive regulation of stem cell population maintenance / Sin3-type complex / Formation of WDR5-containing histone-modifying complexes / Synthesis of PC / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of proteolysis / phosphatidylinositol-3,4,5-trisphosphate binding / mitophagy / negative regulation of apoptotic signaling pathway / hemopoiesis / positive regulation of Wnt signaling pathway / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / histone acetyltransferase complex / chaperone-mediated protein folding / positive regulation of lipid biosynthetic process / negative regulation of 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 / cellular response to glucose stimulus / mitochondrial membrane / negative regulation of transforming growth factor beta receptor signaling pathway / peptidyl-threonine phosphorylation / Hsp90 protein binding / circadian regulation of gene expression / response to insulin / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / Regulation of necroptotic cell death / PML body / protein processing / chromatin DNA binding / Wnt signaling pathway / Regulation of PTEN stability and activity / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / positive regulation of protein catabolic process / UCH proteinases / rhythmic process / KEAP1-NFE2L2 pathway / double-strand break repair / positive regulation of cold-induced thermogenesis / chromatin organization / kinase activity / HATs acetylate histones / positive regulation of cell growth / peptidyl-serine phosphorylation / Regulation of TP53 Activity through Phosphorylation / negative regulation of translation / protein stabilization / regulation of cell cycle / non-specific serine/threonine protein kinase / 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
Chem-12V / 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: 1.85 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 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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 / _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: 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)166,2819
Polymers164,7464
Non-polymers1,5355
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)83,1895
Polymers82,3732
Non-polymers8163
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1490 Å2
ΔGint-13 kcal/mol
Surface area29080 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)83,0934
Polymers82,3732
Non-polymers7192
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1490 Å2
ΔGint-13 kcal/mol
Surface area28370 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)166,37710
Polymers164,7464
Non-polymers1,6316
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7690 Å2
ΔGint-42 kcal/mol
Surface area53440 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)166,1858
Polymers164,7464
Non-polymers1,4394
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area7730 Å2
ΔGint-43 kcal/mol
Surface area52000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.520, 136.480, 152.770
Angle α, β, γ (deg.)90.00, 103.51, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11A-2000-

HOH

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Components

#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 / Casein kinase 2 / 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
#3: Chemical ChemComp-12V / (2S,3R,4R,5S,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-thiopyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate / URIDINE DIPHOSPHO-5-THIO-N-ACETYLGLUCOSAMINE


Mass: 623.419 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H27N3O16P2S
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


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


Mass: 18.015 Da / Num. of mol.: 836 / 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: 3.03 Å3/Da / Density % sol: 59.42 %
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: X25 / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 11, 2011
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.85→59.95 Å / Num. all: 166242 / Num. obs: 166242 / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2
Reflection shellResolution: 1.85→1.95 Å / % possible all: 99.5

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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: 1.85→59.946 Å / SU ML: 0.55 / σ(F): 1.35 / Phase error: 24.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2374 8349 5.03 %RANDOM
Rwork0.2177 ---
all0.2187 166242 --
obs0.2187 166049 99.51 %-
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 36.903 Å2 / ksol: 0.383 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-1.9363 Å2-0 Å28.2616 Å2
2---6.7918 Å20 Å2
3---4.8556 Å2
Refinement stepCycle: LAST / Resolution: 1.85→59.946 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10972 0 93 836 11901
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00411413
X-RAY DIFFRACTIONf_angle_d0.80615523
X-RAY DIFFRACTIONf_dihedral_angle_d11.5354274
X-RAY DIFFRACTIONf_chiral_restr0.0561718
X-RAY DIFFRACTIONf_plane_restr0.0042010
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.85-1.8710.33772550.30235272X-RAY DIFFRACTION99
1.871-1.8930.32242980.29065241X-RAY DIFFRACTION99
1.893-1.91610.30232880.27525174X-RAY DIFFRACTION99
1.9161-1.94040.29092920.25325172X-RAY DIFFRACTION99
1.9404-1.96590.27532580.24635262X-RAY DIFFRACTION99
1.9659-1.99290.22952820.21945220X-RAY DIFFRACTION99
1.9929-2.02130.24492970.21125190X-RAY DIFFRACTION99
2.0213-2.05150.27682600.21835307X-RAY DIFFRACTION100
2.0515-2.08360.23812600.20745260X-RAY DIFFRACTION100
2.0836-2.11770.22022640.20625272X-RAY DIFFRACTION100
2.1177-2.15420.25332790.20535279X-RAY DIFFRACTION99
2.1542-2.19340.24082650.20795240X-RAY DIFFRACTION99
2.1934-2.23560.24222790.20925192X-RAY DIFFRACTION99
2.2356-2.28120.25573040.21425255X-RAY DIFFRACTION99
2.2812-2.33080.23942640.20835258X-RAY DIFFRACTION100
2.3308-2.38510.24532830.22255245X-RAY DIFFRACTION100
2.3851-2.44470.25593070.21975259X-RAY DIFFRACTION100
2.4447-2.51080.23692880.21865210X-RAY DIFFRACTION100
2.5108-2.58470.25222770.22245292X-RAY DIFFRACTION100
2.5847-2.66810.25972530.22235265X-RAY DIFFRACTION100
2.6681-2.76350.23952590.22655308X-RAY DIFFRACTION100
2.7635-2.87410.25622550.22845288X-RAY DIFFRACTION99
2.8741-3.00490.23722940.22375228X-RAY DIFFRACTION99
3.0049-3.16330.23312790.22015262X-RAY DIFFRACTION100
3.1633-3.36150.24112930.21485285X-RAY DIFFRACTION100
3.3615-3.6210.19163000.20155246X-RAY DIFFRACTION100
3.621-3.98540.2162650.19135261X-RAY DIFFRACTION99
3.9854-4.56190.20662820.18515307X-RAY DIFFRACTION100
4.5619-5.74680.21232740.20565272X-RAY DIFFRACTION99
5.7468-59.9770.25662950.26665378X-RAY DIFFRACTION100
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)
13.1513-0.53751.1575.00290.86433.09810.0189-0.23720.0973-0.625-0.03390.6944-0.1241-0.94960.20990.3929-0.0599-0.23150.55920.1680.4139-12.892435.415-36.3153
21.02210.1975-0.06132.24070.2542.0713-0.02290.2540.0974-0.24330.11270.3094-0.0317-0.1421-0.01970.13290.0229-0.04320.30930.00830.1779-2.410535.9318-22.9131
31.76970.5594-1.95140.4501-0.2462.6150.12350.06910.2036-0.0331-0.00710.0836-0.2342-0.0676-0.07690.16660.05410.01870.16880.05060.1848-11.776547.9003-3.6901
41.95120.21330.62611.78450.45780.81210.05980.22530.2245-0.6614-0.00270.3452-0.2524-0.1494-0.04830.30950.0871-0.0660.21280.06190.235-27.869742.3885-6.6623
50.7911-0.07520.03461.5866-0.10571.23670.04610.23750.0279-0.5348-0.05850.25270.1306-0.0791-0.00660.24910.0402-0.08740.1467-0.00750.126-25.533816.5188-3.8618
66.0062-0.927-1.39085.1792.93156.0351-0.1404-0.90840.26360.618-0.2470.2974-0.5389-0.13180.19590.48680.03570.02570.2242-0.00490.1384-19.651422.385837.5038
70.0103-0.1120.05411.6746-0.78950.3701-0.1372-0.2761-0.17680.7920.06280.465-0.0654-0.0809-0.0250.44410.04550.16910.20.03660.125-18.511717.648538.4657
81.87290.83082.14620.80570.88662.4688-0.2231-0.50560.43720.21480.2413-0.2399-0.53650.05360.09320.7441-0.06180.02020.6129-0.23660.2722-11.476120.830145.6961
90.7596-0.27580.03411.5721-0.38620.74370.0356-0.10080.15020.24910.01160.0291-0.126-0.0003-0.02880.10420.0080.03860.1017-0.02780.0809-15.151232.979424.2707
100.1402-0.3452-0.15440.97580.43880.87010.0594-0.04010.11060.1411-0.04160.50250.0085-0.1718-0.00020.10690.01840.06240.1466-0.02660.2599-32.507927.929620.3964
112.1892-1.14531.63261.1366-0.07642.2962-0.12080.0553-0.0527-0.29980.13670.82050.1146-0.5093-0.22470.2951-0.0363-0.24070.3413-0.00760.4804-40.873713.0457-3.857
125.1801-1.03791.42872.2258-0.69281.70870.20530.273-0.32490.0509-0.1386-0.25790.25040.5659-0.08360.13280.04880.00280.2242-0.00350.1628-8.219127.868811.2995
134.1963-0.83610.33292.10221.88432.1186-0.01210.53110.6753-0.5659-0.3491-0.6178-0.55070.70440.37180.30620.01470.04720.26850.03910.2418-16.706132.4162-4.6978
142.6423-0.2108-0.23951.613-1.07040.7654-0.1243-0.08550.09070.2953-0.1564-0.5653-0.24040.17490.24230.46390.1316-0.28380.8644-0.25710.974137.531-21.64651.5525
153.2849-0.1926-0.83333.75870.26712.4145-0.0368-0.24890.03610.2481-0.0016-0.5257-0.07090.6345-0.0010.2102-0.0127-0.02940.3640.04490.191421.0386-24.72520.7376
161.53690.4509-1.63710.999-0.01233.2775-0.1503-0.0167-0.17820.00490.048-0.03210.23750.06110.08990.22580.04380.02360.1710.02420.16817.8552-36.38347.8009
171.8950.28480.75571.2840.51311.7683-0.0742-0.1375-0.2530.18090.0021-0.42730.21280.16230.06670.20990.0631-0.00630.19260.06610.23695.7783-32.776325.0925
180.96920.0173-0.01781.5747-0.00520.7963-0.0099-0.05540.06670.10260.0123-0.4526-0.00090.19310.00580.11250.002-0.04960.16310.01630.22116.2436-5.262624.7992
196.74482.4416-0.57524.6473-1.69535.6270.0317-0.3054-0.33170.2102-0.07060.87050.3559-0.78120.03120.15250.00070.09040.2609-0.00660.4019-35.74-12.677124.1058
200.6832-0.813-0.17811.09730.17840.06090.1064-0.03810.08340.5336-0.07190.6868-0.1678-0.2425-0.06630.1960.0180.11720.21330.0130.3607-36.3538-4.839420.9602
215.50340.39025.82823.0948-1.18548.1125-0.25140.4071-0.7276-0.12080.58170.67980.5331-0.5431-0.15360.2315-0.04950.11290.4235-0.01930.6283-42.0251-9.049719.2113
220.6188-0.39410.05291.581-0.34960.9196-0.0222-0.0146-0.1306-0.00540.00490.31090.1738-0.1152-0.00010.0866-0.02470.04570.0960.0080.1068-23.1544-21.729817.1906
230.7026-0.28530.01031.6793-0.16420.6727-0.0329-0.1374-0.01060.4123-0.00990.0516-0.0110.07960.06040.2109-0.00230.01710.15490.03180.1149-12.4159-18.353232.3099
240.71790.1556-0.16930.953-0.00280.3859-0.1982-0.3580.16830.62390.0925-0.04130.0613-0.0111-0.02330.2264-0.00530.01910.11750.055-0.0003-10.4468-10.983237.222
252.0724-0.61191.63942.1077-0.8064.4-0.12120.45760.2096-0.29-0.10370.0587-0.26890.0440.16980.1714-0.005-0.0080.23970.04240.1158-10.6258-16.71089.1116
265.5589-5.2061-3.50235.37192.19165.03370.31980.7294-0.4673-0.5834-0.446-0.17140.50880.12390.06780.24850.04480.02820.2461-0.00650.18956.1648-21.194715.9338
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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