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- PDB-5tvg: Crystal structure of an alpha,alpha-trehalose-phosphate synthase ... -

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Basic information

Entry
Database: PDB / ID: 5tvg
TitleCrystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis
ComponentsAlpha,alpha-trehalose-phosphate synthase (UDP-forming)
KeywordsTRANSFERASE / structural genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


alpha,alpha-trehalose-phosphate synthase (UDP-forming) / alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity / trehalose biosynthetic process / nucleotide binding / metal ion binding
Similarity search - Function
Alpha,alpha-trehalose-phosphate synthase / Glycosyl transferase, family 20 / Glycosyltransferase family 20 / Glycogen Phosphorylase B; / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
URIDINE-5'-DIPHOSPHATE / Trehalose-6-phosphate synthase
Similarity search - Component
Biological speciesBurkholderia vietnamiensis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To Be Published
Title: Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis
Authors: Edwards, T.E. / Conrady, D.G. / Fairman, J.W. / Lorimer, D. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
History
DepositionNov 8, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 16, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Derived calculations / Refinement description / Category: pdbx_struct_oper_list / software / Item: _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Oct 4, 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
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
B: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
C: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
D: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
E: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
F: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
G: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
H: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)435,37732
Polymers430,8748
Non-polymers4,50324
Water14,214789
1
A: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
B: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
C: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
E: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)217,83918
Polymers215,4374
Non-polymers2,40214
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
F: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
G: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
H: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)217,53814
Polymers215,4374
Non-polymers2,10110
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
E: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)109,10411
Polymers107,7192
Non-polymers1,3859
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5170 Å2
ΔGint-44 kcal/mol
Surface area34010 Å2
MethodPISA
4
B: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
C: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)108,7357
Polymers107,7192
Non-polymers1,0175
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4430 Å2
ΔGint-46 kcal/mol
Surface area33900 Å2
MethodPISA
5
D: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
G: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)108,8278
Polymers107,7192
Non-polymers1,1096
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4650 Å2
ΔGint-44 kcal/mol
Surface area33330 Å2
MethodPISA
6
F: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
H: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)108,7116
Polymers107,7192
Non-polymers9934
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4190 Å2
ΔGint-36 kcal/mol
Surface area33490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.170, 103.020, 218.470
Angle α, β, γ (deg.)90.000, 96.420, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid 2 through 6 and (name N...
21(chain B and ((resid 2 through 6 and (name N...
31(chain C and ((resid 2 through 6 and (name N...
41(chain D and ((resid 2 through 6 and (name N...
51(chain E and ((resid 2 through 6 and (name N...
61(chain F and ((resid 2 through 6 and (name N...
71(chain G and ((resid 2 through 6 and (name N...
81(chain H and ((resid 2 through 6 and (name N...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and ((resid 2 through 6 and (name N...A2 - 6
121(chain A and ((resid 2 through 6 and (name N...A-4 - 500
131(chain A and ((resid 2 through 6 and (name N...A-4 - 500
141(chain A and ((resid 2 through 6 and (name N...A-4 - 500
151(chain A and ((resid 2 through 6 and (name N...A-4 - 500
211(chain B and ((resid 2 through 6 and (name N...B2 - 6
221(chain B and ((resid 2 through 6 and (name N...B0 - 500
231(chain B and ((resid 2 through 6 and (name N...B0 - 500
241(chain B and ((resid 2 through 6 and (name N...B0 - 500
251(chain B and ((resid 2 through 6 and (name N...B0 - 500
311(chain C and ((resid 2 through 6 and (name N...C2 - 6
321(chain C and ((resid 2 through 6 and (name N...C1 - 500
331(chain C and ((resid 2 through 6 and (name N...C1 - 500
341(chain C and ((resid 2 through 6 and (name N...C1 - 500
351(chain C and ((resid 2 through 6 and (name N...C1 - 500
411(chain D and ((resid 2 through 6 and (name N...D2 - 6
421(chain D and ((resid 2 through 6 and (name N...D-3 - 500
431(chain D and ((resid 2 through 6 and (name N...D-3 - 500
441(chain D and ((resid 2 through 6 and (name N...D-3 - 500
451(chain D and ((resid 2 through 6 and (name N...D-3 - 500
511(chain E and ((resid 2 through 6 and (name N...E2 - 6
521(chain E and ((resid 2 through 6 and (name N...E1 - 500
531(chain E and ((resid 2 through 6 and (name N...E1 - 500
541(chain E and ((resid 2 through 6 and (name N...E1 - 500
551(chain E and ((resid 2 through 6 and (name N...E1 - 500
611(chain F and ((resid 2 through 6 and (name N...F2 - 6
621(chain F and ((resid 2 through 6 and (name N...F1 - 460
631(chain F and ((resid 2 through 6 and (name N...F1 - 460
641(chain F and ((resid 2 through 6 and (name N...F1 - 460
651(chain F and ((resid 2 through 6 and (name N...F1 - 460
711(chain G and ((resid 2 through 6 and (name N...G2 - 6
721(chain G and ((resid 2 through 6 and (name N...G2 - 456
731(chain G and ((resid 2 through 6 and (name N...G2 - 456
741(chain G and ((resid 2 through 6 and (name N...G2 - 456
751(chain G and ((resid 2 through 6 and (name N...G2 - 456
811(chain H and ((resid 2 through 6 and (name N...H2 - 6
821(chain H and ((resid 2 through 6 and (name N...H2 - 458
831(chain H and ((resid 2 through 6 and (name N...H2 - 458
841(chain H and ((resid 2 through 6 and (name N...H2 - 458
851(chain H and ((resid 2 through 6 and (name N...H2 - 458

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Components

#1: Protein
Alpha,alpha-trehalose-phosphate synthase (UDP-forming) / Osmoregulatory trehalose synthesis protein A / Trehalose-6-phosphate synthase


Mass: 53859.258 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia vietnamiensis (strain G4 / LMG 22486) (bacteria)
Strain: G4 / LMG 22486 / Gene: Bcep1808_2483 / Production host: Escherichia coli (E. coli)
References: UniProt: A4JGS8, alpha,alpha-trehalose-phosphate synthase (UDP-forming)
#2: Chemical
ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 789 / 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: 2.5 Å3/Da / Density % sol: 50.72 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: BuviA.00046.b.B1.PS02329 at 24.6 mg/mL with 2.5% glycerol, 3 mM UDP and 3 mM MgCl2 against JCSG+ screen condition D7 0.2 M Li2SO4, 0.1 M Tris pH 8.5, 40% MPD, crystal tracking ID 261935d7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 12, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 186193 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 3.2 % / Biso Wilson estimate: 39.32 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.063 / Net I/σ(I): 11.76
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique allCC1/2% possible all
2.3-2.363.20.4552.6213818137780.83599.7
2.36-2.420.3853.050.8799.6
2.42-2.490.3183.690.91399.6
2.49-2.570.2434.70.94399.6
2.57-2.660.2045.520.9699.6
2.66-2.750.1816.220.96699.2
2.75-2.850.1487.440.97399.5
2.85-2.970.1218.830.98399.4
2.97-3.10.10110.540.98799
3.1-3.250.0813.030.99199.3
3.25-3.430.06615.270.99498.9
3.43-3.640.05617.870.99598.7
3.64-3.890.05200.99598.3
3.89-4.20.04422.30.99698.1
4.2-4.60.0423.840.99798
4.6-5.140.03825.030.99797.9
5.14-5.940.03624.850.99797.9
5.94-7.270.03325.990.99897.5
7.27-10.290.02728.590.99996.8
10.290.02429.020.99991.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHENIX(1.11.1_2575)refinement
PDB_EXTRACT3.2data extraction
BALBESphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2WTX

2wtx


Resolution: 2.3→46.536 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.75
RfactorNum. reflection% reflection
Rfree0.2245 2000 1.07 %
Rwork0.1784 --
obs0.1789 186127 98.91 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 153.47 Å2 / Biso mean: 59.9142 Å2 / Biso min: 19.45 Å2
Refinement stepCycle: final / Resolution: 2.3→46.536 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27774 0 281 790 28845
Biso mean--58.55 49.13 -
Num. residues----3621
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00828803
X-RAY DIFFRACTIONf_angle_d0.86539221
X-RAY DIFFRACTIONf_chiral_restr0.0544219
X-RAY DIFFRACTIONf_plane_restr0.0075170
X-RAY DIFFRACTIONf_dihedral_angle_d15.26216897
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A14703X-RAY DIFFRACTION6.589TORSIONAL
12B14703X-RAY DIFFRACTION6.589TORSIONAL
13C14703X-RAY DIFFRACTION6.589TORSIONAL
14D14703X-RAY DIFFRACTION6.589TORSIONAL
15E14703X-RAY DIFFRACTION6.589TORSIONAL
16F14703X-RAY DIFFRACTION6.589TORSIONAL
17G14703X-RAY DIFFRACTION6.589TORSIONAL
18H14703X-RAY DIFFRACTION6.589TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3-2.35750.30661430.24691312913272100
2.3575-2.42120.32051430.23841319213335100
2.4212-2.49250.28831430.22711318513328100
2.4925-2.57290.23581440.21061321213356100
2.5729-2.66490.25631430.2048132141335799
2.6649-2.77160.25851430.207131331327699
2.7716-2.89770.26971430.2053131541329799
2.8977-3.05040.24051430.2011131881333199
3.0504-3.24150.22251420.1936131271326999
3.2415-3.49170.22771440.1826131771332199
3.4917-3.84290.24871420.1683131331327598
3.8429-4.39870.18341420.1492130851322798
4.3987-5.54040.18681430.1455130741321798
5.5404-46.54590.20141420.1647131241326696
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)
11.33040.2328-0.10981.6743-0.13980.8867-0.0809-0.1780.01850.1750.0399-0.083-0.16250.03230.02730.63760.04630.0340.167-0.01190.3075-9.747711.49119.0268
24.9125-0.9523-0.49271.26130.10870.6754-0.06930.28070.3815-0.26350.0549-0.0331-0.2507-0.13390.02290.63450.01640.02330.17770.00310.3312-12.59256.87563.1399
30.5371-0.10810.02871.0235-0.17860.64510.022-0.07610.002-0.12020.0485-0.10490.02860.0551-0.04440.5327-0.01480.06210.1449-0.01070.34055.3945-10.2138.7959
41.8340.4167-0.30311.92840.44660.80040.097-0.1177-0.4512-0.077-0.01990.05670.2448-0.1236-0.06760.55020.0076-0.10630.23760.05640.3425-28.148-30.7906-0.3178
50.9463-0.0262-0.22421.20360.0733.62960.179-0.0745-0.0341-0.0856-0.06550.1898-0.0947-0.5226-0.10720.323-0.01-0.02250.26730.0460.2869-37.4026-17.330618.6778
62.0725-0.1415-0.09192.1022-0.25032.27360.1325-0.48120.3160.2321-0.02230.089-0.0689-0.0955-0.09050.508-0.1373-0.04560.6195-0.05970.3026-3.0606-17.44665.9163
70.9942-0.20860.02370.66360.03221.0710.1377-0.6012-0.22350.2264-0.01560.07820.4672-0.2438-0.09460.7238-0.2359-0.06340.64770.15990.3507-20.7908-32.400358.5186
82.3736-1.6178-0.83593.57680.78771.5194-0.02160.3420.0135-0.52560.2456-0.1364-0.46650.5163-0.2290.4833-0.16710.03010.8261-0.19340.3449-41.9206-45.839294.7108
91.22330.5621-0.06191.73560.31091.13650.0346-0.20740.01010.17290.18030.0027-0.07110.3244-0.1990.24570.0688-0.01780.6458-0.07030.3158-52.37-65.0294102.5186
101.90320.69350.0893.1509-1.13390.5133-0.04350.3591-0.5073-0.3740.133-0.17431.04490.0868-0.08261.45790.0113-0.10140.43740.03180.61171.6596-57.054637.2308
111.07280.4843-0.19632.1683-0.61921.07660.1029-0.2686-0.30650.12510.0123-0.28110.75210.38730.05940.79520.1324-0.11490.34430.06250.379415.2955-37.436138.9792
121.92790.2071-1.01342.2367-1.35811.4391-0.12450.02780.2339-0.3270.1534-0.0135-0.2043-0.0181-0.02210.7353-0.0987-0.13140.4958-0.04550.3386-46.3786-66.622844.1185
132.0504-0.8716-0.02591.271-0.18422.155-0.1346-0.52570.1492-0.21130.279-0.14880.22350.4157-0.12770.5385-0.00330.02050.6058-0.1770.377-29.2444-82.102556.5949
140.8924-0.3212-0.221.2811-0.15020.0971-0.08850.0891-0.0374-0.45190.1093-0.08670.15340.2308-0.03430.7576-0.02490.02930.5742-0.10630.3536-29.3891-86.939244.3241
153.93810.85170.17734.3347-0.40862.3019-0.2664-0.002-0.7417-0.26490.13240.41860.4991-0.09410.11770.5713-0.04380.06830.4035-0.12860.6477-57.4556-107.39360.0416
161.510.0381-0.10442.15570.93382.3369-0.16660.1415-0.2956-0.34220.060.45120.1195-0.46710.10590.3364-0.0766-0.11080.5751-0.02860.463-71.5833-84.864268.8319
173.28530.6341-2.0213.0002-1.81121.94530.22090.5659-1.05490.1077-0.1207-0.62730.03680.3616-0.01880.81090.5971-0.40671.3741-0.42280.9663-17.4838-99.9035108.4158
181.55840.595-0.87960.7529-0.90241.1012-0.3040.3823-0.94990.03340.6194-1.25720.43780.3234-0.18350.95940.4337-0.16731.2346-0.51191.3007-25.7525-108.5355103.6327
192.64171.6191-0.78252.8391-0.2421.76760.2330.7459-0.6073-0.19550.2575-0.28570.6346-0.0973-0.50350.85480.4152-0.22281.228-0.19950.5223-36.844-87.97498.5255
200.96390.2492-0.11240.66930.22841.37020.1081-0.1009-0.63470.3540.1003-0.18740.49190.1638-0.24790.93620.5637-0.37011.2153-0.10590.763-30.8063-96.4734112.6182
210.40730.34670.10430.3593-0.05040.27180.0311-0.0368-0.27310.23830.1957-0.48780.22130.6686-0.06580.5560.579-0.32661.5472-0.25520.4224-22.4964-81.9817104.1848
221.1303-0.5524-0.61781.08740.42861.7251-0.1229-0.2626-0.05330.03640.3519-0.16620.12760.6188-0.0840.4680.1744-0.01141.3357-0.40670.4721-22.519-78.467277.8681
231.9322-0.7686-0.84371.20190.5830.5420.0197-0.085-0.1499-0.0960.1052-0.24330.40860.7064-0.08440.54060.421-0.06991.7424-0.38880.5434-13.483-80.943389.4473
240.2770.06880.17220.2893-0.08610.450.11690.0388-0.22870.19910.3013-0.54990.04510.8160.1180.41530.3053-0.30111.9245-0.56720.7612-10.4704-75.976397.2111
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -4 through 188 )A-4 - 188
2X-RAY DIFFRACTION2chain 'A' and (resid 189 through 240 )A189 - 240
3X-RAY DIFFRACTION3chain 'A' and (resid 241 through 463 )A241 - 463
4X-RAY DIFFRACTION4chain 'B' and (resid 0 through 188 )B0 - 188
5X-RAY DIFFRACTION5chain 'B' and (resid 189 through 464 )B189 - 464
6X-RAY DIFFRACTION6chain 'C' and (resid 1 through 188 )C1 - 188
7X-RAY DIFFRACTION7chain 'C' and (resid 189 through 468 )C189 - 468
8X-RAY DIFFRACTION8chain 'D' and (resid -3 through 144 )D-3 - 144
9X-RAY DIFFRACTION9chain 'D' and (resid 145 through 456 )D145 - 456
10X-RAY DIFFRACTION10chain 'E' and (resid 1 through 170 )E1 - 170
11X-RAY DIFFRACTION11chain 'E' and (resid 171 through 456 )E171 - 456
12X-RAY DIFFRACTION12chain 'F' and (resid 1 through 201 )F1 - 201
13X-RAY DIFFRACTION13chain 'F' and (resid 202 through 343 )F202 - 343
14X-RAY DIFFRACTION14chain 'F' and (resid 344 through 460 )F344 - 460
15X-RAY DIFFRACTION15chain 'G' and (resid 2 through 217 )G2 - 217
16X-RAY DIFFRACTION16chain 'G' and (resid 218 through 456 )G218 - 456
17X-RAY DIFFRACTION17chain 'H' and (resid 2 through 42 )H2 - 42
18X-RAY DIFFRACTION18chain 'H' and (resid 43 through 70 )H43 - 70
19X-RAY DIFFRACTION19chain 'H' and (resid 71 through 100 )H71 - 100
20X-RAY DIFFRACTION20chain 'H' and (resid 101 through 154 )H101 - 154
21X-RAY DIFFRACTION21chain 'H' and (resid 155 through 271 )H155 - 271
22X-RAY DIFFRACTION22chain 'H' and (resid 272 through 343 )H272 - 343
23X-RAY DIFFRACTION23chain 'H' and (resid 344 through 367 )H344 - 367
24X-RAY DIFFRACTION24chain 'H' and (resid 368 through 458 )H368 - 458

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