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- PDB-7kwf: Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56N mutant w... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7kwf
TitleDihydrodipicolinate synthase (DHDPS) from C.jejuni, H56N mutant with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site
Components(4-hydroxy-tetrahydrodipicolinate ...) x 2
KeywordsLYASE
Function / homology
Function and homology information


(R,S)-4-hydroxy-2-oxoglutarate aldolase activity / 4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / glyoxylate catabolic process / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / cytosol
Similarity search - Function
4-hydroxy-tetrahydrodipicolinate synthase, DapA / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase-type TIM barrel
Similarity search - Domain/homology
Chem-3VN / ACETATE ION / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / 4-hydroxy-tetrahydrodipicolinate synthase
Similarity search - Component
Biological speciesCampylobacter jejuni subsp. jejuni serotype O:2 (Campylobacter)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.82 Å
AuthorsSaran, S. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: To Be Published
Title: ALLOSTERIC SITE RESIDUE 'H56' CAPS THE INHIBITOR AT THE TIGHT DIMER INTERFACE FOR TRANSMITTING THE ALLOSTERIC INHIBITION SIGNALS IN Cj.DHDPS
Authors: Saran, S. / Skovpen, Y. / Yazdi, M.M. / Palmer, D.R.J. / Sanders, D.A.R.
History
DepositionNov 30, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Nov 29, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 4-hydroxy-tetrahydrodipicolinate synthase
B: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,34615
Polymers204,7606
Non-polymers1,5869
Water00
1
A: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules

A: 4-hydroxy-tetrahydrodipicolinate synthase
C: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,3568
Polymers136,5074
Non-polymers8494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_554-x,y,-z-1/21
Buried area10990 Å2
ΔGint-52 kcal/mol
Surface area40920 Å2
MethodPISA
2
B: 4-hydroxy-tetrahydrodipicolinate synthase
D: 4-hydroxy-tetrahydrodipicolinate synthase
E: 4-hydroxy-tetrahydrodipicolinate synthase
F: 4-hydroxy-tetrahydrodipicolinate synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,66811
Polymers136,5074
Non-polymers1,1617
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11830 Å2
ΔGint-50 kcal/mol
Surface area40060 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.260, 226.720, 201.530
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 through 70 or (resid 71...
21(chain B and (resid 3 through 70 or (resid 71...
31(chain C and (resid 3 through 73 or (resid 74...
41(chain D and (resid 3 through 70 or (resid 71...
51(chain E and (resid 3 through 70 or (resid 71...
61(chain F and (resid 3 through 70 or (resid 71...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LYSLYSCYSCYS(chain A and (resid 3 through 70 or (resid 71...AA3 - 7015 - 82
12LYSLYSLYSLYS(chain A and (resid 3 through 70 or (resid 71...AA7183
13LYSLYSPHEPHE(chain A and (resid 3 through 70 or (resid 71...AA3 - 29815 - 310
21LYSLYSCYSCYS(chain B and (resid 3 through 70 or (resid 71...BB3 - 7015 - 82
22LYSLYSLYSLYS(chain B and (resid 3 through 70 or (resid 71...BB7183
23LYSLYSPHEPHE(chain B and (resid 3 through 70 or (resid 71...BB3 - 29815 - 310
24LYSLYSPHEPHE(chain B and (resid 3 through 70 or (resid 71...BB3 - 29815 - 310
25LYSLYSPHEPHE(chain B and (resid 3 through 70 or (resid 71...BB3 - 29815 - 310
26LYSLYSPHEPHE(chain B and (resid 3 through 70 or (resid 71...BB3 - 29815 - 310
31LYSLYSTHRTHR(chain C and (resid 3 through 73 or (resid 74...CC3 - 7315 - 85
32LYSLYSLYSLYS(chain C and (resid 3 through 73 or (resid 74...CC7486
33HISHISPHEPHE(chain C and (resid 3 through 73 or (resid 74...CC-6 - 2986 - 310
34HISHISPHEPHE(chain C and (resid 3 through 73 or (resid 74...CC-6 - 2986 - 310
35HISHISPHEPHE(chain C and (resid 3 through 73 or (resid 74...CC-6 - 2986 - 310
36HISHISPHEPHE(chain C and (resid 3 through 73 or (resid 74...CC-6 - 2986 - 310
41LYSLYSCYSCYS(chain D and (resid 3 through 70 or (resid 71...DD3 - 7015 - 82
42LYSLYSLYSLYS(chain D and (resid 3 through 70 or (resid 71...DD7183
43HISHISPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD-5 - 2987 - 310
44HISHISPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD-5 - 2987 - 310
45HISHISPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD-5 - 2987 - 310
46HISHISPHEPHE(chain D and (resid 3 through 70 or (resid 71...DD-5 - 2987 - 310
51LYSLYSCYSCYS(chain E and (resid 3 through 70 or (resid 71...EE3 - 7015 - 82
52LYSLYSLYSLYS(chain E and (resid 3 through 70 or (resid 71...EE7183
53LYSLYSPHEPHE(chain E and (resid 3 through 70 or (resid 71...EE3 - 29815 - 310
54LYSLYSPHEPHE(chain E and (resid 3 through 70 or (resid 71...EE3 - 29815 - 310
55LYSLYSPHEPHE(chain E and (resid 3 through 70 or (resid 71...EE3 - 29815 - 310
56LYSLYSPHEPHE(chain E and (resid 3 through 70 or (resid 71...EE3 - 29815 - 310
61LYSLYSCYSCYS(chain F and (resid 3 through 70 or (resid 71...FF3 - 7015 - 82
62LYSLYSLYSLYS(chain F and (resid 3 through 70 or (resid 71...FF7183
63LYSLYSPHEPHE(chain F and (resid 3 through 70 or (resid 71...FF3 - 29815 - 310
64LYSLYSPHEPHE(chain F and (resid 3 through 70 or (resid 71...FF3 - 29815 - 310
65LYSLYSPHEPHE(chain F and (resid 3 through 70 or (resid 71...FF3 - 29815 - 310
66LYSLYSPHEPHE(chain F and (resid 3 through 70 or (resid 71...FF3 - 29815 - 310

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Components

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4-hydroxy-tetrahydrodipicolinate ... , 2 types, 6 molecules ABFCDE

#1: Protein 4-hydroxy-tetrahydrodipicolinate synthase / HTPA synthase


Mass: 34161.215 Da / Num. of mol.: 3 / Mutation: H56N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase
#2: Protein 4-hydroxy-tetrahydrodipicolinate synthase / HTPA synthase


Mass: 34092.180 Da / Num. of mol.: 3 / Mutation: H56N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Strain: ATCC 700819 / NCTC 11168 / Gene: dapA, Cj0806 / Production host: Escherichia coli (E. coli)
References: UniProt: Q9PPB4, 4-hydroxy-tetrahydrodipicolinate synthase

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Non-polymers , 4 types, 9 molecules

#3: Chemical ChemComp-3VN / (2R,5R)-2,5-diamino-2,5-bis(4-aminobutyl)hexanedioic acid / bis-Lysine


Mass: 318.412 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C14H30N4O4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2 / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O4 / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY

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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: 2.38 Å3/Da / Density % sol: 48.28 %
Crystal growTemperature: 288.15 K / Method: microbatch
Details: 0.3 M Magnesium acetate, 12 % PEG 8000, 0.1 M Sodium acetate (pH 7.4), 120 mM R,R-bislysine

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jul 25, 2019
RadiationMonochromator: Double beam / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.82→49.4 Å / Num. obs: 47346 / % possible obs: 99.63 % / Redundancy: 15 % / CC1/2: 0.869 / Net I/σ(I): 3
Reflection shellResolution: 2.82→2.921 Å / Rmerge(I) obs: 1.437 / Num. unique obs: 4658 / % possible all: 99.59

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4LY8

4ly8


Resolution: 2.82→49.4 Å / SU ML: 0.52 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 35.7 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3336 2368 5 %
Rwork0.2749 44961 -
obs0.2778 47329 99.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 80.07 Å2 / Biso mean: 30.7041 Å2 / Biso min: 13.06 Å2
Refinement stepCycle: final / Resolution: 2.82→49.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13759 0 108 0 13867
Biso mean--30.82 --
Num. residues----1793
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5316X-RAY DIFFRACTION1.086TORSIONAL
12B5316X-RAY DIFFRACTION1.086TORSIONAL
13C5316X-RAY DIFFRACTION1.086TORSIONAL
14D5316X-RAY DIFFRACTION1.086TORSIONAL
15E5316X-RAY DIFFRACTION1.086TORSIONAL
16F5316X-RAY DIFFRACTION1.086TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.82-2.880.49151380.3844260799
2.88-2.940.45441370.36282620100
2.94-3.010.37341370.35682599100
3.01-3.080.41371370.33312600100
3.08-3.170.40931390.33032641100
3.17-3.260.36171380.32972623100
3.26-3.370.37841380.31522616100
3.37-3.490.38111370.3167260599
3.49-3.630.38231380.29792626100
3.63-3.790.33751400.26692652100
3.79-3.990.30691380.25822624100
3.99-4.240.3091390.24572636100
4.24-4.570.30241390.23312656100
4.57-5.030.25251410.23042672100
5.03-5.750.29451410.24132679100
5.75-7.240.33281420.24492699100
7.24-100.21311490.1957280699
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)
11.5785-0.17070.60470.4371-0.26160.89470.0450.55990.43360.279-0.0645-0.122-0.06620.26240.07260.3894-0.11220.04920.1564-0.11190.208320.879535.8582-27.6125
20.1780.0014-0.37220.2184-0.06930.60160.0152-0.13490.3058-0.1089-0.108-0.14360.13630.0391-0.034-0.3915-0.25090.12650.45330.10520.230221.261938.7698-25.9952
32.2895-2.0789-0.71696.79022.64731.2913-0.5183-0.52490.07930.37420.05450.41940.02640.61240.38780.15360.0398-0.00820.29420.00870.34629.582333.3276-27.2328
40.29750.17320.43980.55321.73674.65460.0886-0.15-0.30840.1253-0.0349-0.60710.21640.8797-0.12720.2868-0.0201-0.14370.23980.02640.229125.676924.7728-28.6092
52.19410.5842-0.55391.2670.51633.1282-0.53620.20160.19030.11360.0791-0.0695-0.5825-0.67150.17580.25250.0590.0170.13950.03290.350318.482518.1443-37.2952
61.9801-0.8487-0.38842.4395-0.89711.98970.2346-0.16030.09970.0731-0.3320.0840.00250.27980.14180.1681-0.0390.00940.2252-0.0140.232211.507119.3036-32.8313
70.36550.1767-0.22572.66920.5485-0.05830.0301-0.14130.03680.474-0.111-0.06870.1677-0.27720.0370.2519-0.04370.04120.3588-0.05030.20453.317128.9447-24.7804
81.5924-0.2991-0.68213.53031.78191.9313-0.0889-0.03660.77970.68910.2098-0.12890.272-0.0649-0.0557-0.0124-0.0349-0.03310.2682-0.00590.3332-0.989540.2441-26.6655
91.7659-1.2953-1.48371.23250.55191.8049-0.13790.0387-0.6390.175-0.02670.2259-0.09450.15080.24710.27870.01650.00380.243-0.03830.250117.382646.9717-36.9611
101.21171.0750.76970.94540.80631.69290.2326-0.11370.36030.0543-0.2517-0.49740.173-0.45920.32610.1950.12010.02960.3542-0.15050.41567.719352.3869-31.2055
111.1258-0.26470.15131.10221.29731.9845-0.0339-0.016-0.0230.19460.02840.11030.0216-0.2298-0.02330.20780.0171-0.02230.19020.0380.2037-78.729248.115219.4742
120.7034-0.5349-0.15021.0559-0.8061.19130.09620.0738-0.40180.26320.0810.2485-0.1592-0.0554-0.01210.049-0.0886-0.09150.37670.05660.2674-82.531140.581110.8638
130.860.4191-1.07391.22560.0831.9158-0.00260.07530.00490.12150.04640.02680.1815-0.1436-0.06460.20840.0038-0.01650.17370.03610.1673-68.957535.12914.7187
140.84220.30840.38260.48010.43041.1056-0.12170.22850.09650.03520.03810.1014-0.11170.21790.12370.11260.01250.02560.25210.01960.3736-59.222552.994112.9066
151.24271.67690.10563.9777-1.18151.5096-0.0605-0.19310.3841-0.00420.02230.25850.07090.10280.04190.1228-0.0244-0.00650.1816-0.02070.2528-69.275245.080831.6239
162.519-0.40920.06072.32330.40621.6301-0.1451-0.1153-0.06780.62880.44410.14440.52060.0144-0.23890.43130.0104-0.03360.2638-0.00350.2316-60.552553.913331.3511
171.1564-1.1716-0.97190.73380.68351.2610.10880.19-0.1638-0.0748-0.2091-0.13690.00980.28820.27420.1963-0.0310.01860.23120.01350.228428.728523.9429-62.6257
183.25380.37380.33463.21560.08672.0024-0.4357-0.571-0.51830.02510.05070.0716-1.01271.05660.05410.1931-0.0240.00950.3965-0.05770.543736.864622.7825-57.1476
190.823-0.0814-0.63412.69551.28142.8609-0.1388-0.08610.180.1976-0.80630.1078-0.42810.0041-0.27760.150.0702-0.10890.2550.23320.263932.293431.5602-57.9954
201.7564-1.7495-0.00582.02280.43541.3414-0.19710.03120.08440.04070.1208-0.0577-0.10410.10690.01750.1419-0.04530.01780.18320.02360.175520.536737.7817-57.6272
211.73860.49811.412.4193-0.43621.10780.05490.1688-0.2603-0.0226-0.0823-0.0434-0.0690.0040.02080.13760.02730.0240.2555-0.04110.211413.51724.4396-71.6114
220.4384-0.21210.46780.37420.82483.5732-0.1020.0263-0.02230.0591-0.01990.2639-0.13530.19620.14690.3689-0.0338-0.01720.18950.06360.300818.7617.4076-57.8603
232.30730.71590.1872.53710.22050.70840.16230.0299-0.1699-0.1058-0.2474-0.0232-0.02390.1134-0.00740.142-0.01150.02370.31810.04140.217-27.77436.1867-3.4564
244.74460.9091-0.95431.54972.04224.68690.0764-0.5721-0.01440.1538-0.1978-0.4859-0.12150.27770.25360.3026-0.0256-0.0890.35290.06610.3984-18.886235.50820.4633
250.5795-0.6705-0.71880.49410.46340.3589-0.03380.20120.10470.12230.0538-0.2205-0.0199-0.1146-0.00530.1882-0.0234-0.03180.21620.0160.2695-32.300141.652614.4738
26-0.0254-0.8019-0.06891.87990.2947-0.06450.01640.0539-0.0423-0.2276-0.01080.03580.0188-0.07060.01130.2171-0.0330.01680.2565-0.00520.2635-42.164935.4559-5.9586
270.79640.31740.70062.32190.91060.85450.2890.27040.04060.3783-0.1678-1.02220.58730.42240.1016-0.14780.07660.08160.41710.11320.4239-22.778413.668229.0056
280.01620.36750.08141.2124-0.21672.0946-0.192-0.2069-0.19310.02860.2016-0.1827-0.17910.0375-0.03290.25590.01830.04780.27120.03470.2487-29.710111.793513.9697
295.59080.346-2.57480.412-0.07524.5389-0.65560.8843-0.39490.0741-0.29050.20230.3421-0.35640.24880.44160.0235-0.05270.1280.02940.2149-39.57875.655613.0056
300.95050.18540.2058-0.01120.06210.1223-0.0882-0.07120.00610.02220.05810.0266-0.0628-0.00730.00620.295-0.0019-0.01040.14850.0260.2484-38.672414.693934.0512
311.2554-0.71250.05540.61050.48781.2240.23020.1642-0.0763-0.0879-0.11590.12360.121-0.3771-0.07890.2192-0.0466-0.02030.2320.0190.3613-78.97558.109222.0906
322.8616-3.3455-1.09065.90284.29435.0362-0.5612-0.501-0.17420.82290.29350.74570.6576-0.5841-0.36810.0437-0.0692-0.05060.3610.1210.4662-86.396812.90825.726
331.52880.53610.47070.14080.03171.75920.2362-0.95090.07320.3885-0.1168-0.06-0.1667-0.537-0.33780.1558-0.01030.04320.32420.11440.3033-80.693617.016332.0661
343.0552-0.65350.58971.14650.20490.8953-0.0920.0186-0.10550.07830.04290.04240.184-0.0655-0.06220.16910.0185-0.02840.19740.01410.2061-68.418522.378833.8401
351.5120.50050.78270.6503-0.43721.2787-0.20070.0312-0.018-0.1321-0.0216-0.0241-0.184-0.16160.1770.22590.00730.01080.1432-0.00440.3049-62.01445.774524.2964
360.74590.06110.13251.3285-1.18921.0230.07140.0317-0.1956-0.22570.06940.47160.1269-0.1748-0.23350.22560.0022-0.05780.2772-0.00180.3654-71.93736.36397.0643
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 23 )A3 - 23
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 55 )A24 - 55
3X-RAY DIFFRACTION3chain 'A' and (resid 56 through 70 )A56 - 70
4X-RAY DIFFRACTION4chain 'A' and (resid 71 through 99 )A71 - 99
5X-RAY DIFFRACTION5chain 'A' and (resid 100 through 129 )A100 - 129
6X-RAY DIFFRACTION6chain 'A' and (resid 130 through 171 )A130 - 171
7X-RAY DIFFRACTION7chain 'A' and (resid 172 through 229 )A172 - 229
8X-RAY DIFFRACTION8chain 'A' and (resid 230 through 248 )A230 - 248
9X-RAY DIFFRACTION9chain 'A' and (resid 249 through 279 )A249 - 279
10X-RAY DIFFRACTION10chain 'A' and (resid 280 through 298 )A280 - 298
11X-RAY DIFFRACTION11chain 'B' and (resid 3 through 70 )B3 - 70
12X-RAY DIFFRACTION12chain 'B' and (resid 71 through 99 )B71 - 99
13X-RAY DIFFRACTION13chain 'B' and (resid 100 through 191 )B100 - 191
14X-RAY DIFFRACTION14chain 'B' and (resid 192 through 248 )B192 - 248
15X-RAY DIFFRACTION15chain 'B' and (resid 249 through 279 )B249 - 279
16X-RAY DIFFRACTION16chain 'B' and (resid 280 through 298 )B280 - 298
17X-RAY DIFFRACTION17chain 'C' and (resid -6 through 55 )C-6 - 55
18X-RAY DIFFRACTION18chain 'C' and (resid 56 through 70 )C56 - 70
19X-RAY DIFFRACTION19chain 'C' and (resid 71 through 98 )C71 - 98
20X-RAY DIFFRACTION20chain 'C' and (resid 99 through 171 )C99 - 171
21X-RAY DIFFRACTION21chain 'C' and (resid 172 through 248 )C172 - 248
22X-RAY DIFFRACTION22chain 'C' and (resid 249 through 298 )C249 - 298
23X-RAY DIFFRACTION23chain 'D' and (resid 3 through 55 )D3 - 55
24X-RAY DIFFRACTION24chain 'D' and (resid 56 through 70 )D56 - 70
25X-RAY DIFFRACTION25chain 'D' and (resid 71 through 191 )D71 - 191
26X-RAY DIFFRACTION26chain 'D' and (resid 192 through 298 )D192 - 298
27X-RAY DIFFRACTION27chain 'E' and (resid 3 through 70 )E3 - 70
28X-RAY DIFFRACTION28chain 'E' and (resid 71 through 148 )E71 - 148
29X-RAY DIFFRACTION29chain 'E' and (resid 149 through 171 )E149 - 171
30X-RAY DIFFRACTION30chain 'E' and (resid 172 through 298 )E172 - 298
31X-RAY DIFFRACTION31chain 'F' and (resid 3 through 55 )F3 - 55
32X-RAY DIFFRACTION32chain 'F' and (resid 56 through 70 )F56 - 70
33X-RAY DIFFRACTION33chain 'F' and (resid 71 through 98 )F71 - 98
34X-RAY DIFFRACTION34chain 'F' and (resid 99 through 171 )F99 - 171
35X-RAY DIFFRACTION35chain 'F' and (resid 172 through 262 )F172 - 262
36X-RAY DIFFRACTION36chain 'F' and (resid 263 through 298 )F263 - 298

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