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- PDB-3zgf: Crystal structure of the Fucosylgalactoside alpha N- acetylgalact... -

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Basic information

Entry
Database: PDB / ID: 3zgf
TitleCrystal structure of the Fucosylgalactoside alpha N- acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with in complex with NPE caged UDP-Gal (P2(1)2(1)2(1) space group)
ComponentsHISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE
KeywordsTRANSFERASE / GLYCOSYLTRANSFERASES
Function / homology
Function and homology information


fucosylgalactoside 3-alpha-galactosyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity / fucosylgalactoside 3-alpha-galactosyltransferase activity / ABO blood group biosynthesis / lipid glycosylation / Golgi cisterna membrane / protein glycosylation / antigen binding / manganese ion binding ...fucosylgalactoside 3-alpha-galactosyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity / fucosylgalactoside 3-alpha-galactosyltransferase activity / ABO blood group biosynthesis / lipid glycosylation / Golgi cisterna membrane / protein glycosylation / antigen binding / manganese ion binding / vesicle / carbohydrate metabolic process / Golgi membrane / nucleotide binding / Golgi apparatus / extracellular region
Similarity search - Function
Glycosyl transferase, family 6 / Glycosyltransferase family 6 / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Nucleotide-diphospho-sugar transferases / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
1-(2-NITROPHENYL)ETHYL UDP-GALACTOSE / : / URIDINE-5'-DIPHOSPHATE / Histo-blood group ABO system transferase
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.701 Å
AuthorsJorgensen, R. / Batot, G.O. / Hindsgaul, O. / Tanaka, H. / Perez, S. / Imberty, A. / Breton, C. / Royant, A. / Palcic, M.M.
CitationJournal: Acta Crystallogr.,Sect.F / Year: 2014
Title: Structures of a Human Blood Group Glycosyltransferase in Complex with a Photo-Activatable Udp-Gal Derivative Reveal Two Different Binding Conformations
Authors: Jorgensen, R. / Batot, G. / Mannerstedt, K. / Imberty, A. / Breton, C. / Hindsgaul, O. / Royant, A. / Palcic, M.M.
History
DepositionDec 17, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 6, 2014Group: Database references
Revision 1.2Aug 13, 2014Group: Database references
Revision 1.3Jan 17, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _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: HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE
B: HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,7178
Polymers69,3082
Non-polymers1,4096
Water9,494527
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5950 Å2
ΔGint-64 kcal/mol
Surface area22800 Å2
MethodPISA
Unit cell
Length a, b, c (Å)52.840, 78.450, 155.130
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (-0.9999, -0.006791, 0.0138), (0.008068, -0.9955, 0.09471), (0.01309, 0.09481, 0.9954)
Vector: 0.2076, -11.5858, 0.5584)

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein HISTO-BLOOD GROUP ABO SYSTEM TRANSFERASE / FUCOSYLGLYCOPROTEIN 3-ALPHA-GALACTOSYLTRANSFERASE / FUCOSYLGLYCOPROTEIN ALPHA-N- ...FUCOSYLGLYCOPROTEIN 3-ALPHA-GALACTOSYLTRANSFERASE / FUCOSYLGLYCOPROTEIN ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE / GLYCOPROTEIN-FUCOSYLGALACTOSIDE ALPHA-N-ACETYLGALACTOSAMINYLTRANSFER GLYCOPROTEIN-FUCOSYLGALACTOSIDE ALPHA-GALACTOSYLTRANSFERASE / HISTO-BLOOD GROUP A TRANSFERASE / A TRANSFERASE / HISTO-BLOOD GROUP B TRANSFERASE / B TRANSFERASE / NAGAT / FUCOSYLGLYCOPROTEIN ALPHA-N-ACETYLGALACTOSAMINYLTRANSFERASE SOLUBLE


Mass: 34654.008 Da / Num. of mol.: 2 / Fragment: EXTRACELLULAR CATALYTIC DOMAIN, RESIDUES 64-354 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): GOLD
References: UniProt: P16442, fucosylgalactoside 3-alpha-galactosyltransferase, glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase

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Non-polymers , 5 types, 533 molecules

#2: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#3: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE / Uridine diphosphate


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-IUG / 1-(2-NITROPHENYL)ETHYL UDP-GALACTOSE


Mass: 702.430 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H30N3O19P2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 527 / 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: 2.3 Å3/Da / Density % sol: 46 % / Description: NONE
Crystal growpH: 7
Details: 7-12% POLYETHYLENE GLYCOL 3350, 0.1 - 0.3 M AMMONIUM SULPHATE, 0.05 M MNCL2, 0.05 M MOPS PH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-5 / Wavelength: 0.90772
DetectorType: MARRESEARCH SX-165 / Detector: CCD / Details: MULTILAYER MIRROR
RadiationMonochromator: BENT SI (220) CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.90772 Å / Relative weight: 1
ReflectionResolution: 1.7→20 Å / Num. obs: 71207 / % possible obs: 99 % / Observed criterion σ(I): 2.96 / Redundancy: 7 % / Biso Wilson estimate: 20.24 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 14.94
Reflection shellResolution: 1.7→1.85 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.63 / Mean I/σ(I) obs: 2.96 / % possible all: 96.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2RIT

2rit


Resolution: 1.701→19.984 Å / SU ML: 0.25 / σ(F): 1.99 / Phase error: 21.98 / Stereochemistry target values: ML / Details: C-TERMINAL FROM RESIDUE 346 DISORDERED
RfactorNum. reflection% reflection
Rfree0.2173 2134 3 %
Rwork0.1816 --
obs0.1827 71129 99.34 %
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 38.364 Å2 / ksol: 0.351 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.1346 Å20 Å20 Å2
2--0.0282 Å20 Å2
3---0.1064 Å2
Refinement stepCycle: LAST / Resolution: 1.701→19.984 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4697 0 83 527 5307
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0094951
X-RAY DIFFRACTIONf_angle_d1.1076757
X-RAY DIFFRACTIONf_dihedral_angle_d15.4961829
X-RAY DIFFRACTIONf_chiral_restr0.079726
X-RAY DIFFRACTIONf_plane_restr0.006849
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7012-1.74070.41861270.33784110X-RAY DIFFRACTION90
1.7407-1.78420.29171430.27274589X-RAY DIFFRACTION100
1.7842-1.83250.30031410.23944555X-RAY DIFFRACTION100
1.8325-1.88630.24861410.21754583X-RAY DIFFRACTION100
1.8863-1.94720.26341400.20864559X-RAY DIFFRACTION100
1.9472-2.01670.21871430.19224612X-RAY DIFFRACTION100
2.0167-2.09740.26921410.18774571X-RAY DIFFRACTION100
2.0974-2.19270.24281430.18874609X-RAY DIFFRACTION100
2.1927-2.30820.24321430.17984625X-RAY DIFFRACTION100
2.3082-2.45250.21421420.18484591X-RAY DIFFRACTION100
2.4525-2.64150.23681420.1834658X-RAY DIFFRACTION100
2.6415-2.90660.23321440.18924640X-RAY DIFFRACTION100
2.9066-3.32550.22231440.17754659X-RAY DIFFRACTION100
3.3255-4.18350.17441470.15644721X-RAY DIFFRACTION100
4.1835-19.98530.15821530.14934913X-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)
14.19581.12312.47114.27771.48553.78480.0572-0.0090.3141-0.032-0.0576-0.2975-0.18470.150.02030.1073-0.01650.04850.18350.03910.13648.59175.4291-26.8262
22.12560.2348-0.06481.18841.29491.46320.11020.26950.0927-0.208-0.03570.0923-0.0069-0.0522-0.05860.15620.0184-0.03690.19080.00240.08011.6032-11.5742-28.7777
36.164-1.25281.64922.8658-0.2197.72470.0648-0.31590.25090.5983-0.0562-0.2837-0.12560.28060.00620.1706-0.0518-0.02950.15990.01120.132213.3587-1.8115-17.9438
41.0889-0.06650.41380.3524-0.21140.66360.15920.0573-0.25460.0956-0.0052-0.14670.18060.15850.04330.2029-0.0064-0.1920.1384-0.02420.301520.8595-26.8847-12.8882
53.7361-1.88440.83264.2692-1.25592.21270.12690.3819-0.1670.1984-0.1466-0.50590.1730.3553-0.00750.11880.0132-0.07670.1543-0.02720.19923.4734-15.3825-17.4421
66.5619-2.32480.66312.5025-2.31774.93380.2006-0.3687-0.01990.4376-0.0009-0.206-0.19720.1117-0.27460.256-0.0774-0.09090.17450.01090.143420.6137-16.9826-7.5493
70.7748-0.67480.7951.3691-0.65241.1513-0.06160.06170.11410.0923-0.1254-0.3309-0.15350.17970.18550.3533-0.0532-0.29960.18290.09530.517126.5932-30.0781-7.0112
82.3502-1.73780.65852.7010.03792.55790.3842-0.3595-0.24580.3954-0.1398-0.71710.39780.0857-0.3170.2152-0.0586-0.10430.14550.00310.27327.9364-14.1777-9.8487
90.3225-0.13750.15070.1156-0.2070.42630.08220.0064-0.10620.1403-0.0542-0.11840.04160.0141-0.26380.3321-0.0487-0.2750.14730.060.309114.1641-35.2137-7.7795
100.7929-0.36840.85540.649-0.46151.59350.0296-0.1863-0.08280.20510.0145-0.071-0.0231-0.1046-0.04790.4266-0.0898-0.15330.17870.07340.15559.485-27.1153-3.4815
113.9463-2.5457-0.17142.6980.48431.1752-0.0731-0.6388-0.30840.41860.153-0.0050.3242-0.0814-0.07570.3851-0.0997-0.08030.20240.04940.092712.4023-17.1603-2.0752
123.46051.0282-0.49865.5674-2.0463.01260.0320.2655-0.514-0.1861-0.0761-0.42910.29350.03190.01980.13950.0174-0.06610.1647-0.05540.16718.2748-21.9368-20.9418
131.04860.3747-0.71731.7331-0.0811.24010.12510.1851-0.16060.057-0.01120.07640.2114-0.0519-0.09390.16170.0179-0.06920.1441-0.02180.11254.7942-19.972-23.9303
141.02420.5680.24581.26270.18480.46590.1584-0.0584-0.30460.0694-0.01260.10690.2215-0.09370.05130.2533-0.1269-0.15840.13670.00250.2652-7.0314-33.7494-21.1858
151.9247-0.23370.21690.7669-0.32280.61060.20580.1037-0.18970.1274-0.0564-0.06550.16350.0558-0.12630.198-0.0311-0.07530.1429-0.01750.14783.9964-22.1667-18.7702
163.6851-0.01781.31592.1492-0.7652.12470.2636-0.433-0.12430.8961-0.06190.1634-0.0469-0.1764-0.19220.3413-0.0545-0.03470.19690.01330.13221.7848-23.7001-5.918
171.8143-0.1396-3.11876.88351.895.75670.2539-0.3108-0.58490.1413-0.1224-0.12550.30570.0986-0.11230.3307-0.1041-0.15450.210.07460.3378-1.4541-39.4456-9.156
180.70160.6206-0.20424.3394-0.3360.73130.13750.066-0.16450.13140.05750.16130.2517-0.0845-0.06020.169-0.0399-0.08830.13010.00170.1322-0.0131-25.5247-17.3919
191.4481.3725-1.18882.71051.35966.54890.02810.1677-0.1877-0.03510.1501-0.28490.23350.1533-0.14220.11950.0236-0.0650.2013-0.06770.160113.7105-22.4455-32.0659
201.1705-0.24050.02843.0297-2.14163.07470.1561-0.1606-0.6823-0.42710.1448-0.13640.85410.0548-0.08020.29790.0452-0.11290.2211-0.0050.391517.9399-29.5079-24.9895
213.27680.9694-1.43182.7865-0.45130.76610.1421-0.0838-0.2123-0.0474-0.06250.28330.2668-0.1124-0.05750.1998-0.0407-0.07510.2711-0.00850.1183-8.66-19.4862-26.6253
222.9307-0.07970.83841.1631-0.98911.04680.02540.1821-0.0696-0.2231-0.0321-0.01120.0605-0.0718-0.00590.177-0.009-0.0240.2137-0.0030.0768-1.7845-2.8134-29.1262
233.9001-1.688-1.4453.91110.11341.76060.1421-0.4816-0.37720.4703-0.13070.24650.10640.0490.00280.1617-0.0838-0.01170.20690.02370.1608-13.2804-11.2935-17.247
241.7349-0.07540.44070.03240.2172.0179-0.0269-0.08790.2315-0.0234-0.08110.3689-0.0558-0.11660.10220.09160.00360.03020.1324-0.01040.3226-21.038413.75-14.552
250.3923-0.712-0.78353.77520.39582.0187-0.06260.1621-0.072-0.04270.09270.52940.167-0.3882-0.01370.0824-0.03960.00510.1879-0.01120.1942-23.51321.8864-17.963
269.1302-0.80641.17323.88763.50076.02940.1229-0.342-0.16510.611-0.04560.6110.3748-0.2334-0.09720.1408-0.04480.06410.17480.00960.1903-20.59284.4424-8.2387
273.8163-1.38180.41760.5317-0.41232.18290.0340.1437-0.25390.0034-0.10420.24160.1158-0.44230.04760.1244-0.04490.12380.2174-0.12090.4322-26.732917.396-8.9512
282.0383-1.3056-0.98742.7899-0.49823.40960.277-0.2335-0.03210.59280.08581.1407-0.2278-0.2392-0.35160.2376-0.0410.12120.17970.02170.4299-27.87141.3373-10.2626
290.8896-0.2712-0.13220.92880.55750.61350.1262-0.11930.77270.3439-0.01270.2809-0.21610.004-0.20780.1676-0.00560.03750.1527-0.06530.3851-14.396122.6018-10.7155
303.7338-1.5293-1.63236.0623-4.13357.4168-0.0473-0.41480.40570.5658-0.0973-0.1159-0.4181-0.0990.18560.1945-0.02190.00370.1735-0.09370.2004-9.498914.95-5.2248
311.0542-0.69840.05241.19321.20832.1134-0.0646-0.47080.06180.48190.1320.12990.066-0.01880.06960.2803-0.02210.07390.1959-0.02410.0944-12.29695.1688-2.7936
322.97440.81331.49757.18513.0553.017-0.03360.1390.4006-0.3107-0.2310.5104-0.0933-0.23620.27810.07560.00570.02880.16380.02760.1448-18.47338.053-22.1015
331.9073-0.0960.58761.6750.98790.9181-0.00610.1670.235-0.18360.0340.0427-0.09050.0263-0.01420.1038-0.0169-0.01740.14730.01980.0866-4.93155.9732-25.03
340.78030.0634-1.21242.0138-0.06221.94620.08880.04840.5081-0.21730.0331-0.4412-0.29790.1969-0.02540.158-0.0320.00240.13840.06960.32966.823420.0031-23.9077
353.483-0.1667-1.49861.78610.89031.58310.1179-0.01480.28020.0724-0.0477-0.0196-0.12330.0001-0.0560.0882-0.0064-0.00670.09690.01160.1061-4.06388.6549-20.1021
363.59930.9472-0.64985.2694-1.10374.97340.1093-0.56650.26910.7659-0.09-0.5982-0.07750.35880.01460.1608-0.0209-0.04090.2091-0.04560.1243-1.721211.5367-7.5405
370.98481.09930.9821.94730.0792.4165-0.0989-0.05750.45640.0079-0.03280.3409-0.293-0.04180.12990.17670.0012-0.09590.1461-0.08340.50751.366126.9021-12.5695
382.8002-0.1363-0.2945.44050.74191.92470.03780.0740.366-0.0114-0.0501-0.1626-0.03260.02930.01890.0949-0.0181-0.01180.12240.02620.0986-0.079412.1283-19.1119
391.93941.74060.74792.3228-0.23356.46450.12160.18180.1398-0.20180.05490.2678-0.1031-0.0533-0.14770.11210.0098-0.02730.17590.06340.1267-13.62027.5404-33.4247
404.66980.3028-0.0063.47150.05124.74440.0660.40390.0787-0.4672-0.01720.3848-0.0983-0.35590.03920.1379-0.0048-0.07010.1840.03410.1081-17.19835.6586-29.7179
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 64:80)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 81:97)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 98:113)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 114:132)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 133:145)
6X-RAY DIFFRACTION6(CHAIN A AND RESID 146:151)
7X-RAY DIFFRACTION7(CHAIN A AND RESID 152:161)
8X-RAY DIFFRACTION8(CHAIN A AND RESID 162:169)
9X-RAY DIFFRACTION9(CHAIN A AND RESID 170:188)
10X-RAY DIFFRACTION10(CHAIN A AND RESID 189:196)
11X-RAY DIFFRACTION11(CHAIN A AND RESID 197:207)
12X-RAY DIFFRACTION12(CHAIN A AND RESID 208:219)
13X-RAY DIFFRACTION13(CHAIN A AND RESID 220:242)
14X-RAY DIFFRACTION14(CHAIN A AND RESID 243:260)
15X-RAY DIFFRACTION15(CHAIN A AND RESID 261:274)
16X-RAY DIFFRACTION16(CHAIN A AND RESID 275:286)
17X-RAY DIFFRACTION17(CHAIN A AND RESID 287:298)
18X-RAY DIFFRACTION18(CHAIN A AND RESID 299:319)
19X-RAY DIFFRACTION19(CHAIN A AND RESID 320:335)
20X-RAY DIFFRACTION20(CHAIN A AND RESID 336:354)
21X-RAY DIFFRACTION21(CHAIN B AND RESID 65:80)
22X-RAY DIFFRACTION22(CHAIN B AND RESID 81:97)
23X-RAY DIFFRACTION23(CHAIN B AND RESID 98:113)
24X-RAY DIFFRACTION24(CHAIN B AND RESID 114:132)
25X-RAY DIFFRACTION25(CHAIN B AND RESID 133:145)
26X-RAY DIFFRACTION26(CHAIN B AND RESID 146:151)
27X-RAY DIFFRACTION27(CHAIN B AND RESID 152:161)
28X-RAY DIFFRACTION28(CHAIN B AND RESID 162:169)
29X-RAY DIFFRACTION29(CHAIN B AND RESID 170:188)
30X-RAY DIFFRACTION30(CHAIN B AND RESID 189:196)
31X-RAY DIFFRACTION31(CHAIN B AND RESID 197:207)
32X-RAY DIFFRACTION32(CHAIN B AND RESID 208:219)
33X-RAY DIFFRACTION33(CHAIN B AND RESID 220:242)
34X-RAY DIFFRACTION34(CHAIN B AND RESID 243:260)
35X-RAY DIFFRACTION35(CHAIN B AND RESID 261:274)
36X-RAY DIFFRACTION36(CHAIN B AND RESID 275:286)
37X-RAY DIFFRACTION37(CHAIN B AND RESID 287:298)
38X-RAY DIFFRACTION38(CHAIN B AND RESID 299:319)
39X-RAY DIFFRACTION39(CHAIN B AND RESID 320:335)
40X-RAY DIFFRACTION40(CHAIN B AND RESID 336:345)

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