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- PDB-3u0y: Crystal structure of the Fucosylgalactoside alpha N-acetylgalacto... -

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Basic information

Entry
Database: PDB / ID: 3u0y
TitleCrystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with compound 382 and UDP
ComponentsHisto-blood group ABO system transferase
Keywordstransferase/transferase inhibitor / ROSSMANN FOLD / "SEMI CLOSED" CONFORMATION / GLYCOSYLTRANSFERASE / TRANSFERASE GTB / ABO / BLOOD GROUP ANTIGEN / GLYCOPROTEIN / METAL-BINDING / MANGANESE / UDP-GAL / H-ANTIGEN ACCEPTOR / MEMBRANE / transferase / transferase-transferase inhibitor complex
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-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine / : / 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: 1.6 Å
AuthorsPalcic, M.M. / Jorgensen, R.
CitationJournal: To be Published
Title: A novel compound from a molecular fragment library screen inhibits glycosyltransferases by displacing the metal ion and interfering with substrate binding
Authors: Jorgensen, R. / Grimm, L.L. / Sindhuwinata, N. / Peters, T. / Palcic, M.M.
History
DepositionSep 29, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 24, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 12, 2014Group: Structure summary
Revision 1.2Sep 13, 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 / 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 / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _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: Histo-blood group ABO system transferase
B: Histo-blood group ABO system transferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,18713
Polymers69,3082
Non-polymers1,87911
Water8,053447
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7720 Å2
ΔGint-72 kcal/mol
Surface area22110 Å2
MethodPISA
2
A: Histo-blood group ABO system transferase
hetero molecules

B: Histo-blood group ABO system transferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,18713
Polymers69,3082
Non-polymers1,87911
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_556x,y,z+11
Buried area4360 Å2
ΔGint-53 kcal/mol
Surface area25460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)77.630, 152.740, 52.990
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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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-acetylgalactosaminyltransferase / Glycoprotein-fucosylgalactoside alpha-galactosyltransferase / Histo-blood group A transferase / A transferase / Histo-blood group B transferase / B transferase / NAGAT / Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form


Mass: 34654.008 Da / Num. of mol.: 2 / Fragment: unp residues 64-354 / 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 (E. coli) / Strain (production host): BL21
References: UniProt: P16442, glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, fucosylgalactoside 3-alpha-galactosyltransferase

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Non-polymers , 6 types, 458 molecules

#2: Chemical ChemComp-GTI / 1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine


Mass: 246.331 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H14N4S
#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.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 447 / 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: 2.34 Å3/Da / Density % sol: 47.37 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 50 mM MOPS pH 7, 50-200 mM ammonium sulfate, 50 mM MnCl2, 6-9% PEG-3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.918 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Jan 15, 2010 / Details: mirrors
RadiationMonochromator: Double Crystal Monochromator - Si-111 crystal
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918 Å / Relative weight: 1
ReflectionResolution: 1.6→20 Å / Num. all: 84041 / Num. obs: 82147 / % possible obs: 97.7 % / Observed criterion σ(I): -3 / Redundancy: 6.6 % / Biso Wilson estimate: 24.807 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 18.07
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique allNum. unique obs% possible all
1.6-1.75.70.682.5878197137421313095.5
1.7-1.86.10.4274.2966502109251060597.1
1.8-26.60.2238.22104567158631551497.8
2-2.37.10.10916.76103726146671441098.2
2.3-2.57.30.07723.49455876240618299.1
2.5-37.30.05930.47678929348923598.8
3-3.57.20.04140.67343764800475799.1
3.5-410.80.03347.29192362699267899.2
4-570.0351.92191862727269798.9
5-76.90.02850.67129361866185399.3
7-106.60.02551.52485473172799.5
10-2050.02250.01217743335982.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 33.28 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å19.86 Å
Translation2.5 Å19.86 Å

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASER2.1.4phasing
PHENIX1.6_289refinement
PDB_EXTRACT3.1data extraction
MxCuBEdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2RIT

2rit


Resolution: 1.6→19.86 Å / Occupancy max: 1 / Occupancy min: 0.12 / FOM work R set: 0.8794 / SU ML: 0.18 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 18.97 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1939 2465 3 %Random
Rwork0.1658 ---
obs0.1667 82079 97.82 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 59.283 Å2 / ksol: 0.419 e/Å3
Displacement parametersBiso max: 115.62 Å2 / Biso mean: 23.0109 Å2 / Biso min: 6.03 Å2
Baniso -1Baniso -2Baniso -3
1-0.0011 Å20 Å20 Å2
2---0.0012 Å20 Å2
3---0.0001 Å2
Refinement stepCycle: LAST / Resolution: 1.6→19.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4675 0 114 447 5236
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.015038
X-RAY DIFFRACTIONf_angle_d1.2826870
X-RAY DIFFRACTIONf_chiral_restr0.087735
X-RAY DIFFRACTIONf_plane_restr0.006869
X-RAY DIFFRACTIONf_dihedral_angle_d16.2221866
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 18

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection allNum. reflection obs% reflection obs (%)
1.6-1.63080.26961300.26341924322432295
1.6308-1.6640.31351330.249343014434443495
1.664-1.70020.261320.234442624394439496
1.7002-1.73970.27231350.223843594494449497
1.7397-1.78320.23251340.203443394473447397
1.7832-1.83140.2221340.188843324466446697
1.8314-1.88520.20431360.170343944530453098
1.8852-1.9460.1811360.152243884524452498
1.946-2.01550.18921360.145444034539453998
2.0155-2.09610.1691370.146644374574457498
2.0961-2.19140.1781370.147944194556455698
2.1914-2.30680.1781370.145744464583458398
2.3068-2.45110.19611380.149744474585458599
2.4511-2.63990.20471390.148744984637463799
2.6399-2.90490.16261400.15545034643464399
2.9049-3.32350.16621400.145145254665466599
3.3235-4.18080.15661420.143545844726472699
4.1808-19.86150.19291490.177247854934493499
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)
10.6181-0.4477-0.18261.9291-1.49571.5088-0.3873-0.01570.00790.17250.33180.23060.0009-0.17010.02490.306-0.0416-0.01520.1972-0.02780.1797-15.7646-12.89416.4866
23.29580.7590.08360.2826-0.71392.7615-0.2044-0.1391-0.40160.11570.2749-0.0955-0.38440.1867-0.01320.2057-0.0913-0.05330.1820.09110.20073.3762-15.750111.3857
30.0455-0.20630.23650.8484-0.48610.81630.04420.0159-0.0514-0.0025-0.1473-0.2686-0.07110.10820.08460.0717-0.0218-0.00820.15710.04320.138-2.8711-26.29669.0952
41.23630.4487-0.12620.6975-0.54930.58090.1315-0.02270.03970.2375-0.1255-0.0014-0.29710.0345-0.00320.1476-0.0191-0.02070.10650.00710.0852-14.3905-20.111521.2027
50.293-1.07350.09814.2751-0.07630.03820.130.0249-0.1223-0.1441-0.13830.5084-0.01970.01590.01950.06810.00130.00560.0939-0.00670.121-19.0423-35.041723.5758
61.25620.38650.04183.1088-1.79812.339-0-0.2028-0.13060.2133-0.18-0.24690.15160.0710.12110.121-0.0148-0.01310.12820.03930.0914-8.6699-41.425232.0593
71.061-1.321-0.14735.34570.67851.3020.04960.0312-0.16940.4161-0.18680.58390.1292-0.10420.13890.1171-0.0320.01980.0976-0.01170.1108-18.8059-39.485328.3421
80.27430.37360.51152.70140.86830.58060.0275-0.1299-0.09811.0216-0.2780.12460.2389-0.10720.19560.3755-0.01580.0570.10920.02120.1414-14.9584-46.994538.3367
91.8544-0.0915-0.7860.2377-0.75313.0024-0.24620.0994-0.46010.04360.00020.03620.4203-0.1790.22370.1487-0.04380.05640.106-0.01660.1929-18.9127-45.607829.7155
101.9640.57010.00120.9174-0.69662.96380.05440.1652-0.4141-0.107-0.21140.09760.5099-0.08360.16850.1445-0.0340.03320.0799-0.01050.1567-17.6127-50.333418.712
110.908-0.1125-0.02910.728-0.06260.32250.0070.1438-0.05250.0767-0.0874-0.0466-0.02120.06530.06030.0387-0.0111-0.0160.07980.02020.0799-9.6891-37.852224.2316
120.08550.4319-0.49891.215-0.60491.771-0.0389-0.0108-0.0579-0.109-0.1556-0.31860.01420.27310.17010.04360.00340.00210.15470.04930.1437-4.3386-34.368813.8694
132.36080.8905-2.57682.1846-1.8334.0117-0.4266-0.2029-0.403-1.1072-0.4366-1.0561.14090.7670.84750.42670.18540.31080.20270.11980.33041.1064-48.30852.7099
141.33930.1491-1.38111.9386-1.74533.4606-0.4512-0.0587-0.4295-1.7889-0.3515-0.76211.22760.45280.73990.70090.16330.31160.18170.03340.2566-3.311-47.2555-1.4849
151.45330.4797-0.24420.4683-0.06270.18-0.0810.0455-0.0475-0.0418-0.0816-0.1050.2002-0.00190.12330.04250.02990.03450.10680.02750.099-8.4608-39.211313.0712
163.0023-3.99770.90917.79030.88853.42150.43581.16740.079-2.0214-0.33211.0466-0.1773-1.0543-0.07740.10060.0179-0.03790.24750.00790.1416-21.5823-40.258810.3051
171.2456-0.4523-0.9790.7402-0.3452.0806-0.14270.0512-0.3117-0.2452-0.22230.34410.822-0.11450.34060.37290.03060.05940.1275-0.02550.1883-15.6401-52.9577.8121
181.3691-0.0169-0.66451.2993-1.18671.9653-0.0546-0.0019-0.2485-0.3912-0.1782-0.17580.44380.15990.22470.1720.05670.06010.10250.02180.1417-7.947-45.71137.0763
190.6036-0.49410.63210.3190.0620.5204-0.06680.36230.38780.1044-0.0389-0.3386-0.04060.08110.12220.0064-0.005-0.03550.17340.05810.22654.2982-34.7120.8439
200.16840.30830.16361.1047-0.15760.6246-0.0601-0.0866-0.02440.1713-0.114-0.4131-0.06430.26590.17630.06-0.0309-0.05350.17540.07810.19431.1819-33.12724.6041
212.8242.11660.28693.244-0.3360.2019-0.3871-0.3071-0.3865-0.8596-0.0515-0.444-0.2330.07120.34070.31720.09330.1440.22640.05930.2182-1.9837-34.4807-1.0092
220.00130.07130.37270.8617-0.42952.09570.0230.0610.00330.0198-0.1068-0.2513-0.03720.33080.08180.064-0.021-0.00840.1710.0250.1189-3.9197-17.72785.6255
231.05150.3931-0.29350.3343-0.59941.09440.0995-0.0203-0.0905-0.0808-0.0902-0.08340.32940.13250.00660.16490.01240.00760.11880.01110.0954-11.2116-29.0905-5.644
241.4815-0.1265-0.18820.95760.22720.17730.05480.0360.0429-0.1839-0.05260.4633-0.0113-0.1880.00160.1476-0.0022-0.03960.1183-0.00650.121-24.5233-15.0351-9.5394
251.6717-1.08740.67111.03-0.93331.4591-0.01780.16520.1841-0.2455-0.0697-0.124-0.06280.01050.07850.1819-0-0.020.11470.00910.0918-17.7008-12.0192-16.5577
261.1498-0.5391-0.08521.078-0.37140.97610.1590.158-0.2093-0.3833-0.15630.39390.0201-0.2111-0.02460.17290.0419-0.07270.1114-0.02250.1479-27.8776-10.813-16.8874
271.25510.19760.32892.0016-0.79260.65330.0813-0.01610.0609-0.3616-0.13640.33740.1481-0.2019-0.00980.20380.0177-0.06910.1184-0.0250.145-26.162-17.722-18.2685
284.4436-0.57771.83040.97760.50812.8272-0.4588-0.55120.2424-0.06010.17170.1487-1.0657-0.72440.34090.55470.2401-0.05690.4856-0.13440.5105-34.84930.3371-9.2173
293.2421-0.60032.38840.1715-0.65944.9466-0.29280.36590.82870.2062-0.01330.4326-1.8164-0.14870.31340.60290.0064-0.04050.20250.0430.4-27.45342.7468-2.5887
300.23690.34560.92375.6208-1.04026.4720.21310.3564-0.4526-0.6628-0.00371.59630.5503-1.6611-0.17740.1868-0.0177-0.01660.42290.02880.4497-34.7155-10.8149-2.2523
310.7804-0.33990.31530.9196-1.05871.05140.1281-0.03790.0192-0.18750.0310.5782-0.0296-0.0999-0.13550.1453-0.0233-0.03790.12030.00490.2101-26.943-16.705-5.7565
322.255-0.2929-0.670.20720.47471.59570.05180.08760.2931-0.1951-0.0843-0.2294-0.34050.08390.02890.1965-0.01280.00740.1350.03380.1537-11.4977-7.6138-13.3985
330.4911-0.30450.3113-0.0027-0.30011.0832-0.0333-0.01760.08240.0025-0.0193-0.0461-0.0610.18260.03740.0776-0.03130.00170.11220.0090.0904-11.2084-12.06320.8262
340.4112-0.04030.31980.3093-0.27841.0587-0.2843-0.44230.59020.74040.1883-0.2955-0.57240.18940.13130.427-0.0158-0.08930.1548-0.06310.2567-14.81462.811112.6781
352.7659-1.87910.97761.3435-0.89191.0718-0.6438-0.52330.36890.82570.33380.0438-0.7196-0.22570.26990.4250.0795-0.04980.2038-0.08330.2133-19.37991.335216.815
360.6811-0.26190.70661.57550.07131.2692-0.058-0.09280.0695-0.0045-0.02170.0281-0.1961-0.03340.08770.1284-0.02150.00090.1033-0.00810.0994-16.5839-9.5024.9723
370.9088-1.4193-0.18342.80110.88471.5967-0.13670.0173-0.17650.3790.11340.5131-0.0277-0.51070.01570.14830.05780.05450.18740.01770.1772-30.5627-7.05516.8209
381.30360.4126-0.10951.33170.98141.3704-0.0613-0.05430.2526-0.0510.04080.122-0.3782-0.07270.01340.20150.0267-0.0070.0752-0.00690.1154-21.7504-3.19228.7723
390.88961.193-0.58781.9095-0.5173-0.0183-0.0154-0.11560.0239-0.0683-0.0058-0.09280.0360.12990.00230.0897-0.0434-0.00310.08350.01360.0805-5.435-7.7848-4.7493
400.64350.8532-1.00031.4848-1.26361.5068-0.0734-0.00370.023-0.0319-0.0937-0.2157-0.080.25460.12950.1413-0.0359-0.00570.13880.02910.1643-6.0025-9.8242-9.1646
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 60:76)A60 - 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 - 355
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 - 355

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