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- PDB-3ioj: Crystal structure of the Fucosylgalactoside alpha N-acetylgalacto... -

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Basic information

Entry
Database: PDB / ID: 3ioj
TitleCrystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with UDP
ComponentsHisto-blood group ABO system transferase
KeywordsTRANSFERASE / GTA / ABO / cisAB mutant / AA(Gly)B / ROSSMANN FOLD / UDP / SEMI-CLOSED CONFORMATION / BLOOD GROUP ANTIGEN / GLYCOPROTEIN / GLYCOSYLTRANSFERASE / GOLGI APPARATUS / MANGANESE / MEMBRANE / METAL-BINDING / POLYMORPHISM / SECRETED / SIGNAL-ANCHOR / TRANSMEMBRANE
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 / : / 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 / : / 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
: / URIDINE-5'-DIPHOSPHATE / Histo-blood group ABO system transferase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.651 Å
AuthorsPesnot, T. / Jorgensen, R. / Palcic, M.M. / Wagner, G.K.
CitationJournal: Nat.Chem.Biol. / Year: 2010
Title: Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.
Authors: Pesnot, T. / Jorgensen, R. / Palcic, M.M. / Wagner, G.K.
History
DepositionAug 14, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 7, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 12, 2014Group: Structure summary
Revision 1.3Nov 1, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Oct 13, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / diffrn_source ...database_2 / diffrn_source / pdbx_struct_conn_angle / struct_conn / 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 / _diffrn_source.pdbx_synchrotron_site / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _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.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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)70,79512
Polymers69,3082
Non-polymers1,48710
Water9,440524
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7650 Å2
ΔGint-86 kcal/mol
Surface area22230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)52.450, 77.536, 153.605
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
DetailsThe biological assembly is a dimer generated within the asymmetric unit.

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Histo-blood group ABO system transferase / NAGAT / Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / ...NAGAT / Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase / Histo-blood group A transferase / A transferase / Glycoprotein-fucosylgalactoside alpha-galactosyltransferase / Fucosylglycoprotein 3-alpha-galactosyltransferase / Histo-blood group B transferase / B transferase / Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form


Mass: 34654.008 Da / Num. of mol.: 2 / Fragment: Extracellular catalytic domain / Mutation: L266G, G268A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ABO / Plasmid: PCW DELTA 1AC / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21
References: UniProt: P16442, glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, fucosylgalactoside 3-alpha-galactosyltransferase

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Non-polymers , 5 types, 534 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


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 524 / 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: 2.25 Å3/Da / Density % sol: 45.41 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 50 mM MOPS pH 7, 50-200 mM ammonium sulfate, 50 mM MnCl2, and 6-9% PEG-3350, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 2, 2008 / Details: Double crystal Si[111], horizontally focussing
RadiationMonochromator: Double crystal Si[111], horizontally focussing
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.65→50 Å / Num. obs: 71372 / % possible obs: 93.5 % / Observed criterion σ(I): -3 / Redundancy: 6 % / Biso Wilson estimate: 18.5 Å2 / Rmerge(I) obs: 0.091 / Χ2: 1.013 / Net I/σ(I): 6.8
Reflection shellResolution: 1.65→1.71 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.564 / Mean I/σ(I) obs: 1.3 / Num. unique all: 4013 / Χ2: 0.638 / % possible all: 53.5

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å49.64 Å
Translation2.5 Å49.64 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER1.3.3phasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
MAR345dtbdata collection
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2RIT

2rit


Resolution: 1.651→33.126 Å / Occupancy max: 1 / Occupancy min: 0.25 / FOM work R set: 0.879 / SU ML: 1.34 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.193 3437 5.05 %RANDOM
Rwork0.163 ---
obs0.165 68016 89.34 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 49.811 Å2 / ksol: 0.388 e/Å3
Displacement parametersBiso max: 77.01 Å2 / Biso mean: 22.44 Å2 / Biso min: 8.24 Å2
Baniso -1Baniso -2Baniso -3
1--0.062 Å2-0 Å20 Å2
2---5.404 Å20 Å2
3---3.526 Å2
Refinement stepCycle: LAST / Resolution: 1.651→33.126 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4664 0 84 524 5272
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0094923
X-RAY DIFFRACTIONf_angle_d1.1976704
X-RAY DIFFRACTIONf_chiral_restr0.083721
X-RAY DIFFRACTIONf_plane_restr0.006843
X-RAY DIFFRACTIONf_dihedral_angle_d17.9331804
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 25

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.651-1.6730.326530.271061111437
1.673-1.6970.293750.2571346142147
1.697-1.7220.237860.2421703178959
1.722-1.7490.224950.2331981207670
1.749-1.7780.2811370.212238237580
1.778-1.8090.2281160.1942526264286
1.809-1.8420.2361390.182538267790
1.842-1.8770.2191280.1722674280293
1.877-1.9150.2151700.1582674284495
1.915-1.9570.1861280.1462763289195
1.957-2.0020.1861310.1452744287596
2.002-2.0530.1721510.1442771292297
2.053-2.1080.1821560.1542819297598
2.108-2.170.1661550.1552806296197
2.17-2.240.2091650.152815298099
2.24-2.320.2111370.1452835297298
2.32-2.4130.1781490.152860300999
2.413-2.5230.1781330.1572884301799
2.523-2.6560.2071740.1572843301799
2.656-2.8220.2051590.1672859301899
2.822-3.040.1791800.1662881306199
3.04-3.3450.1761450.15429413086100
3.345-3.8290.1611440.14529373081100
3.829-4.8210.1651520.13129843136100
4.821-33.1330.1971790.1863096327599
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)
10.3899-0.93440.86650.4641-0.07830.1048-0.0319-0.1640.01450.00460.0761-0.166-0.0881-0.2414-0.04570.1664-0.03970.01330.24280.00830.24049.96357.1518-22.587
23.6704-2.00681.05042.1322-1.61353.2477-0.2408-0.04270.3091-0.06530.4284-0.07820.2003-0.2437-0.13990.18980.04340.02290.21780.07370.17333.4988-3.6222-35.9716
30.6998-0.32690.1624-0.19260.14570.04560.11630.10670.134-0.0233-0.02920.0819-0.0454-0.0595-0.05340.11330.0032-0.010.14030.01190.09251.376-11.3368-27.4132
40.65690.277-0.1711.35340.89840.5440.0228-0.01210.15820.1837-0.11380.07250.0162-0.07640.06760.1195-0.0138-0.010.1584-0.00250.125313.2647-1.5415-18.5877
50.92191.14590.5561.21280.03650.49970.2951-0.1884-0.15910.2654-0.3355-0.11910.0003-0.02360.01350.1719-0.0589-0.0640.11440.01030.149515.8239-15.5593-9.4092
61.75530.3350.66990.7487-0.32490.84310.30350.0821-0.44460.0228-0.1756-0.2790.14950.1625-0.14920.15510.0102-0.0880.14210.00180.255623.9849-23.5574-16.7016
71.22550.65870.56330.9024-0.31980.7670.3994-0.1366-0.23220.2734-0.4417-0.1323-0.03090.14080.02210.1882-0.0738-0.09340.14090.06080.175820.2946-18.9214-7.8816
80.6657-0.2539-0.49222.4005-1.32070.59320.6017-0.421-0.27560.3864-0.7066-1.07470.12890.34040.04530.2539-0.0566-0.24720.18140.12480.490130.348-26.6301-8.9129
91.122-0.58150.44990.0038-0.45410.6570.4586-0.3192-0.51890.1109-0.1565-0.29280.28490.0304-0.24670.2783-0.1071-0.19440.16660.10420.252521.7972-23.908-5.4129
102.38280.4927-0.1520.9244-0.08871.29270.3221-0.3446-0.50930.4373-0.24990.16320.3088-0.122-0.17410.2716-0.0938-0.14670.17660.10540.189510.8252-28.9914-5.5126
111.63680.3630.460.40770.18011.01150.2248-0.0104-0.19910.098-0.0925-0.10930.0384-0.0101-0.10030.1511-0.003-0.04110.1140.00450.1216.4018-19.8483-17.0426
120.34450.25770.34260.0565-0.27550.3710.12630.0639-0.08570.0079-0.0392-0.01940.0924-0.0397-0.0380.1339-0.0083-0.03460.1291-0.02430.10316.212-18.4539-23.3343
130.4661-0.15690.39061.3392-0.36730.30350.18730.0393-0.3432-0.49510.07510.66150.282-0.1118-0.27060.2421-0.051-0.13740.1571-0.0040.2954-4.7591-33.558-23.9404
140.3075-0.37460.70750.9411-0.2850.83940.2186-0.033-0.3147-0.13890.1120.60190.3095-0.2189-0.28210.1604-0.0589-0.10560.17750.03450.2558-8.7013-31.2307-20.235
150.72460.11350.2060.6525-0.67380.20190.1260.0002-0.1668-0.0177-0.06-0.0670.00120.0849-0.04170.1549-0.0108-0.06230.1293-0.01220.13645.3951-21.6486-17.8938
161.9809-0.859-2.00935.9240.8047-2.02640.2589-0.86330.36491.09940.00180.3199-0.2433-0.13-0.07660.2905-0.05430.00530.24830.00910.13742.3337-18.1151-5.4998
170.61830.27030.38890.5402-0.170.70690.1967-0.1688-0.2650.23120.00670.06720.1851-0.0737-0.17160.2469-0.0724-0.0760.19540.08940.2510.0666-32.1948-6.6376
180.92560.10280.62080.19520.14080.82030.2216-0.0874-0.3248-0.026-0.08180.10920.2237-0.0726-0.19260.155-0.0419-0.08230.12580.0240.1979-0.5417-28.0364-16.2908
190.23510.02440.02880.52430.91581.23230.12640.0409-0.101-0.0530.0456-0.12970.18390.0309-0.06420.1490.0272-0.02810.1287-0.0330.113113.3945-21.5867-31.3307
201.6699-0.3251-0.03760.00040.39941.10620.14180.2298-0.2692-0.05840.0831-0.06470.33880.1872-0.18880.16660.0566-0.02440.1379-0.05050.158217.2487-21.0186-28.166
211.94290.5594-1.11571.2193-0.66950.5320.1478-0.29330.08780.14910.04940.28170.2708-0.0017-0.17490.1722-0.03-0.06340.19650.01760.1805-8.7067-19.3982-24.035
220.1125-0.25540.15220.2990.1895-0.27010.08930.0864-0.0906-0.0967-0.0251-0.0680.0820.0134-0.03050.1053-0.001-0.00620.1522-0.00310.0794-2.1535-3.1347-29.1962
230.6506-0.1550.26350.593-0.19580.41910.03-0.1442-0.2350.1794-0.07070.00520.1270.05970.01140.1352-0.0278-0.01180.14320.01740.1206-13.3065-11.1979-18.5888
240.55861.15360.2170.96090.51110.55380.0423-0.21470.13530.2663-0.06610.49630.0315-0.1060.0380.1255-0.01920.03920.1531-0.01410.1968-17.47448.5185-11.0861
250.4150.8804-0.15730.89730.13390.39770.0246-0.0480.22550.0025-0.03130.3297-0.0109-0.16470.01060.0883-0.00870.01230.1424-0.00970.1708-24.46567.3328-17.9585
260.45970.31070.04531.5270.2680.420.1102-0.18240.19330.3774-0.20250.67440.0647-0.1160.11630.1477-0.03830.08250.173-0.07890.2828-24.397911.6926-8.764
270.09680.86180.4943.42340.68070.28160.0933-0.08840.23550.2702-0.0880.57460.0096-0.024-0.00770.179-0.05050.0710.1615-0.03440.1753-25.76414.5422-8.0955
281.6619-1.6180.7127-0.4504-1.2861.67380.08120.08080.99390.4998-0.29290.2654-0.2379-0.01240.24890.3361-0.07140.12770.2356-0.07090.4738-16.830524.2753-5.7648
292.81451.42770.2053-0.0563-1.26552.1566-0.11950.40041.13760.0224-0.00110.132-0.52930.17520.13060.2854-0.0402-0.00480.22810.02660.4507-10.550724.396-13.9494
302.3016-0.0119-0.12123.57480.90981.69160.0038-0.59410.38330.7499-0.2505-0.058-0.3043-0.12110.1660.2284-0.03320.0150.231-0.08760.1692-10.366513.9564-2.4122
310.70610.45250.05530.3150.08161.30770.1484-0.1570.08980.1519-0.17330.16640.11530.04940.0480.1482-0.05180.02990.1555-0.02880.1066-13.40225.8207-7.6247
322.14710.62230.07872.5397-1.29611.10930.13910.21680.3531-0.3706-0.11530.1066-0.1659-0.0069-0.04710.125-00.00450.15150.03320.1439-21.13259.1585-25.4156
330.470.16130.20730.05010.55240.11860.05460.04170.0732-0.0505-0.02620.00770.00340.0397-0.010.1108-0.0023-0.00680.13330.02090.1086-7.05374.8997-24.3463
340.7334-0.4594-0.35610.95250.37221.138-0.01710.13410.2925-0.25890.0618-0.5537-0.19210.0936-0.02540.1563-0.0340.020.15690.04390.26374.485320.1354-26.1784
350.2245-0.5799-0.00732.23240.56570.42210.0124-0.03370.42410.05250.1301-0.9522-0.16640.3036-0.18710.1408-0.0476-0.00860.18740.03190.37558.704820.3478-21.4866
360.36490.10910.13730.62530.28380.14780.00410.03910.13810.018-0.0388-0.1062-0.03130.05560.03070.09610.0030.00430.11660.02070.1253-2.94579.1531-20.2034
370.80570.48890.18082.43860.67060.3529-0.0003-0.3070.1580.4938-0.1182-0.3276-0.03940.01930.0750.1591-0.0081-0.04910.155-0.0350.1701-1.01815.7875-8.113
381.04430.06650.2893-0.0892-0.35721.0967-0.0707-0.04130.31180.0978-0.0101-0.1878-0.2523-0.00050.08220.1374-0.017-0.03550.1268-0.00020.21130.76216.8337-17.5446
39-0.1944-0.04260.25650.5073-0.55391.09320.03160.07830.0415-0.08470.06190.0886-0.1086-0.0005-0.02570.1343-0.0048-0.00610.15540.0420.0985-12.61826.9792-31.2438
401.7981-0.54290.11051.375-0.24710.87520.07470.21230.2762-0.24860.08060.1045-0.0579-0.0748-0.13190.15710.0097-0.02350.15360.03680.1407-17.51617.3161-29.1551
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 63:76)A63 - 76
2X-RAY DIFFRACTION2(chain A and resid 77:82)A77 - 82
3X-RAY DIFFRACTION3(chain A and resid 83:98)A83 - 98
4X-RAY DIFFRACTION4(chain A and resid 99:111)A99 - 111
5X-RAY DIFFRACTION5(chain A and resid 112:122)A112 - 122
6X-RAY DIFFRACTION6(chain A and resid 123:143)A123 - 143
7X-RAY DIFFRACTION7(chain A and resid 144:154)A144 - 154
8X-RAY DIFFRACTION8(chain A and resid 155:163)A155 - 163
9X-RAY DIFFRACTION9(chain A and resid 164:178)A164 - 178
10X-RAY DIFFRACTION10(chain A and resid 179:203)A179 - 203
11X-RAY DIFFRACTION11(chain A and resid 204:218)A204 - 218
12X-RAY DIFFRACTION12(chain A and resid 219:241)A219 - 241
13X-RAY DIFFRACTION13(chain A and resid 242:250)A242 - 250
14X-RAY DIFFRACTION14(chain A and resid 251:262)A251 - 262
15X-RAY DIFFRACTION15(chain A and resid 263:274)A263 - 274
16X-RAY DIFFRACTION16(chain A and resid 275:279)A275 - 279
17X-RAY DIFFRACTION17(chain A and resid 280:293)A280 - 293
18X-RAY DIFFRACTION18(chain A and resid 294:318)A294 - 318
19X-RAY DIFFRACTION19(chain A and resid 319:335)A319 - 335
20X-RAY DIFFRACTION20(chain A and resid 336:346)A336 - 346
21X-RAY DIFFRACTION21(chain B and resid 63:79)B63 - 79
22X-RAY DIFFRACTION22(chain B and resid 80:97)B80 - 97
23X-RAY DIFFRACTION23(chain B and resid 98:111)B98 - 111
24X-RAY DIFFRACTION24(chain B and resid 112:125)B112 - 125
25X-RAY DIFFRACTION25(chain B and resid 126:145)B126 - 145
26X-RAY DIFFRACTION26(chain B and resid 146:162)B146 - 162
27X-RAY DIFFRACTION27(chain B and resid 163:173)B163 - 173
28X-RAY DIFFRACTION28(chain B and resid 174:178)B174 - 178
29X-RAY DIFFRACTION29(chain B and resid 179:189)B179 - 189
30X-RAY DIFFRACTION30(chain B and resid 190:198)B190 - 198
31X-RAY DIFFRACTION31(chain B and resid 199:212)B199 - 212
32X-RAY DIFFRACTION32(chain B and resid 213:217)B213 - 217
33X-RAY DIFFRACTION33(chain B and resid 218:241)B218 - 241
34X-RAY DIFFRACTION34(chain B and resid 242:250)B242 - 250
35X-RAY DIFFRACTION35(chain B and resid 251:259)B251 - 259
36X-RAY DIFFRACTION36(chain B and resid 260:274)B260 - 274
37X-RAY DIFFRACTION37(chain B and resid 275:292)B275 - 292
38X-RAY DIFFRACTION38(chain B and resid 293:316)B293 - 316
39X-RAY DIFFRACTION39(chain B and resid 317:335)B317 - 335
40X-RAY DIFFRACTION40(chain B and resid 336:346)B336 - 346

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