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- PDB-7kzd: Crystal structure of KabA from Bacillus cereus UW85 in complex wi... -

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Basic information

Entry
Database: PDB / ID: 7kzd
TitleCrystal structure of KabA from Bacillus cereus UW85 in complex with the reduced internal aldimine and with bound Glutarate
ComponentsAminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
KeywordsBIOSYNTHETIC PROTEIN / TRANSFERASE / Kanosamine / Biosynthesis / Aminotransferase / KabA
Function / homology
Function and homology information


polysaccharide biosynthetic process / transaminase activity / pyridoxal phosphate binding
Similarity search - Function
: / NTD biosynthesis operon protein NtdA, N-terminal domain / DegT/DnrJ/EryC1/StrS aminotransferase / DegT/DnrJ/EryC1/StrS aminotransferase family / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
GLUTARIC ACID / Chem-PLR / KabA
Similarity search - Component
Biological speciesBacillus cereus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsPrasertanan, T. / Palmer, D.R.J. / Sanders, D.A.R.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada) Canada
CitationJournal: J.Struct.Biol. / Year: 2021
Title: Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85.
Authors: Prasertanan, T. / Palmer, D.R.J. / Sanders, D.A.R.
History
DepositionDec 10, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 26, 2021Provider: repository / Type: Initial release
Revision 1.1Jun 2, 2021Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.title
Revision 1.2Oct 18, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.3Mar 13, 2024Group: Source and taxonomy / Category: entity_src_gen

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
B: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
C: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
D: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
E: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
F: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
G: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
H: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
hetero molecules


Theoretical massNumber of molelcules
Total (without water)413,12066
Polymers407,8718
Non-polymers5,24958
Water29,3101627
1
A: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
C: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
hetero molecules


  • defined by author&software
  • Evidence: gel filtration, The data suggest that KabA is of high purity and is a tetramer in solution using size exclusion chromatography to estimate molecular weight corresponded to the observed ...Evidence: gel filtration, The data suggest that KabA is of high purity and is a tetramer in solution using size exclusion chromatography to estimate molecular weight corresponded to the observed molecular weight based on Native (non-denaturing) gel electrophoresis analysis
  • 103 kDa, 2 polymers
  • Search similar-shape structures of this assembly by Omokage search (details)
Theoretical massNumber of molelcules
Total (without water)103,31117
Polymers101,9682
Non-polymers1,34315
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7770 Å2
ΔGint-10 kcal/mol
Surface area34170 Å2
MethodPISA
2
B: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
D: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,55921
Polymers101,9682
Non-polymers1,59219
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8940 Å2
ΔGint5 kcal/mol
Surface area34420 Å2
MethodPISA
3
E: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
H: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,12514
Polymers101,9682
Non-polymers1,15712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8080 Å2
ΔGint-3 kcal/mol
Surface area34670 Å2
MethodPISA
4
F: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
G: Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,12514
Polymers101,9682
Non-polymers1,15712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7870 Å2
ΔGint-7 kcal/mol
Surface area34760 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.940, 93.580, 106.890
Angle α, β, γ (deg.)108.840, 92.330, 90.080
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme / KabA


Mass: 50983.910 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus cereus (bacteria) / Gene: kabA, GE376_30835 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: C0JRF5, aspartate transaminase
#2: Chemical
ChemComp-PLR / (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE / 4'-DEOXYPYRIDOXINE PHOSPHATE


Mass: 233.158 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C8H12NO5P / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 46 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-GUA / GLUTARIC ACID


Mass: 132.115 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C5H8O4 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1627 / Source method: isolated from a natural source / Formula: H2O
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: 2.16 Å3/Da / Density % sol: 42.93 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: PEG 4000, Sodium Chloride

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.814 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 18, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.814 Å / Relative weight: 1
ReflectionResolution: 1.9→48.413 Å / Num. obs: 257845 / % possible obs: 95.92 % / Redundancy: 2.1 % / CC1/2: 0.994 / Rrim(I) all: 0.091 / Net I/σ(I): 6.86
Reflection shellResolution: 1.9→1.968 Å / Mean I/σ(I) obs: 1.9 / Num. unique obs: 25515 / CC1/2: 0.716 / Rrim(I) all: 0.641 / % possible all: 95.28

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Processing

Software
NameVersionClassification
PHENIXdev_2398refinement
PDB_EXTRACT3.27data extraction
MOLREPphasing
AutoProcessdata reduction
AutoProcessdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7KZ3

7kz3


Resolution: 1.9→48.413 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 27.84 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2486 12881 5 %
Rwork0.2071 244573 -
obs0.2092 257454 95.93 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 173.02 Å2 / Biso mean: 39.4364 Å2 / Biso min: 14.5 Å2
Refinement stepCycle: final / Resolution: 1.9→48.413 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28358 0 220 1639 30217
Biso mean--59.66 39.15 -
Num. residues----3504
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00729121
X-RAY DIFFRACTIONf_angle_d0.89839188
X-RAY DIFFRACTIONf_chiral_restr0.0534404
X-RAY DIFFRACTIONf_plane_restr0.0055004
X-RAY DIFFRACTIONf_dihedral_angle_d16.30917876
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.9-1.92160.35144190.3015798695
1.9216-1.94420.31524300.2798817195
1.9442-1.96790.31734250.2687807896
1.9679-1.99280.31434310.2751817496
1.9928-2.0190.3024280.2595815996
2.019-2.04670.3074270.2539810096
2.0467-2.07590.29024270.2466812095
2.0759-2.10690.28494270.2431811696
2.1069-2.13990.29424310.2356818196
2.1399-2.17490.27174290.228816296
2.1749-2.21240.28734290.2296813996
2.2124-2.25270.28094280.2245812796
2.2527-2.2960.26754330.2186822896
2.296-2.34290.28034300.2258816896
2.3429-2.39380.28074290.2241815896
2.3938-2.44950.26994290.2171815396
2.4495-2.51070.26734280.2227814096
2.5107-2.57860.26694300.2156817696
2.5786-2.65450.26164300.2141815796
2.6545-2.74020.26014310.2131819296
2.7402-2.83810.2674310.2144817696
2.8381-2.95170.25664330.2151822897
2.9517-3.0860.25814310.2123819196
3.086-3.24870.24344320.2042820096
3.2487-3.45220.21794300.1908817896
3.4522-3.71860.2324270.187810496
3.7186-4.09270.20294300.1732817996
4.0927-4.68450.19474320.1671819496
4.6845-5.90030.2264320.1889821097
5.9003-48.4130.24324320.2047802895
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)
13.9013-0.0472-0.86423.38420.01513.7836-0.0207-0.4169-0.41980.34950.02020.4457-0.0761-0.7011-0.00450.2672-0.01910.05760.43390.03860.3985-12.5569-5.134117.4492
22.0045-0.17710.26770.8547-0.01071.4796-0.0626-0.0457-0.10180.0243-0.07540.04380.0611-0.01140.08860.22520.02090.01680.16830.00760.28018.6836-0.19275.78
30.8610.01980.09973.52630.59683.50870.11380.4194-0.4149-0.4639-0.15690.24650.283-0.08020.04110.34080.0243-0.04510.2854-0.10140.38051.4931-5.4029-15.1403
42.8163-0.3739-0.37721.52350.51952.51290.01010.0359-0.39750.0154-0.0298-0.06120.20670.16280.0030.23420.01670.00490.1370.02190.265713.9447-7.3655-0.334
52.1986-0.68110.34581.3306-0.09031.36360.06050.24710.1067-0.2128-0.15360.237-0.1408-0.22570.01190.26250.041-0.03510.2251-0.01610.2774-7.818410.5841-2.6715
64.50970.1939-0.25721.85650.05573.63180.0576-0.3122-0.22370.184-0.05290.4390.0029-0.45680.01210.2472-0.05330.01730.29490.06080.369934.304440.337317.4491
71.56170.06490.50720.7056-0.30791.13660.00490.0246-0.0139-0.0442-0.07430.1162-0.0952-0.1262-0.00910.20950.04310.00110.1480.00910.195555.440246.45865.8203
82.3148-1.0863-0.16253.9424-0.03334.0245-0.0170.2726-0.1687-0.3596-0.11650.3855-0.0523-0.30550.05170.31050.0976-0.06970.3645-0.0460.23849.260247.6867-14.835
92.0779-0.76710.05641.1729-0.00820.97570.15340.376-0.0568-0.2181-0.15480.1926-0.0722-0.1411-0.00640.25130.027-0.04440.2383-0.0060.267346.166648.5572-4.069
103.82681.1199-2.47622.67030.41044.776-0.3028-0.0643-0.12260.10710.0881-0.6762-0.3080.48420.18220.3135-0.1101-0.05590.3325-0.01210.609145.16218.869719.4823
111.96150.09070.70670.88130.16751.6334-0.0349-0.10410.02530.01570.0558-0.1616-0.11620.37030.02340.2701-0.0079-0.01490.32420.00650.309531.30339.007612.4997
121.4877-0.15810.26691.92040.63260.9319-0.04440.5104-0.0264-0.36020.086-0.3669-0.17010.75910.04350.3398-0.07820.06260.7041-0.02730.398439.54836.9462-5.4433
134.60662.11192.36213.20950.0013.9977-0.13260.49840.3904-0.3640.08060.1702-0.487-0.07910.07670.3870.04530.01190.30850.05110.329418.582414.6153-6.7242
140.025-0.03110.1481.81740.24461.76050.06840.1994-0.26790.04440.0405-0.65490.0990.90950.4040.19890.0954-0.09110.5663-0.05930.535846.3175-1.271513.1674
153.37320.03291.43262.04040.05681.70930.17190.936-0.6447-0.4008-0.1176-0.23530.09540.1389-0.31540.48280.2467-0.04110.7618-0.26390.686539.042-11.458-5.1844
161.726-0.944-0.07181.88910.44482.4243-0.03060.3435-0.4564-0.021-0.0402-0.27730.1660.46380.18670.22680.092-0.05470.51380.00920.550248.1414-7.697913.3092
179.3365.78695.50495.39661.07716.9342-0.78630.5529-0.1885-0.87730.34870.0551-0.587-0.46580.34621.12190.32890.07371.5573-0.12050.43432.3094-2.47357.1273
182.70150.60190.63073.2756-0.18383.1548-0.1231-0.21370.59310.5990.035-0.4492-0.52850.4860.04170.4234-0.0597-0.04030.3971-0.0990.498991.040265.594423.1513
190.96210.7719-0.46061.45420.28220.6960.0729-0.15470.14530.0945-0.0871-0.01530.02290.12540.0490.23890.0423-0.0190.2721-0.02840.160872.570954.919317.494
201.0507-0.35360.30191.3440.10221.46320.07030.55450.0479-0.2195-0.0004-0.2697-0.17470.5616-0.05220.266-0.05460.02870.50970.01870.241783.557555.4291-5.8005
214.53672.63221.7952.5438-0.56864.7178-0.07660.35720.3528-0.2510.21490.4112-0.3515-0.4302-0.15090.32140.05630.01140.30720.04880.307264.586461.8251-6.5865
223.3463-1.1055-0.22361.86090.35530.9380.05040.3564-0.06480.0317-0.0436-0.30020.03450.2629-0.02730.1928-0.0003-0.03220.2902-0.03540.269593.163647.399713.0941
234.39890.19590.93812.8687-0.70560.3984-0.06851.1596-0.4612-0.42480.1556-0.01670.09650.4185-0.18860.28390.0886-0.08690.5693-0.17170.552188.386937.2664-5.1253
243.2166-0.94630.13262.33120.93086.08390.1216-0.0528-0.370.0816-0.1684-0.00790.1833-0.1014-0.06540.1409-0.0349-0.05160.25730.03130.267894.873141.610618.4653
2520.50092.00010.02220.44598.9340.05040.3459-0.1838-0.2026-0.0124-0.12290.28310.07490.01340.94350.16720.21960.757-0.34540.63979.435545.52657.1021
264.1733-0.5738-0.99682.64240.68233.55760.15950.5471-0.5717-0.2204-0.1535-0.57270.22590.68350.04610.26820.04850.03620.42770.03340.4389-11.9412-20.1714-59.781
271.19910.23430.26460.6719-0.06031.0040.01220.0555-0.0381-0.0104-0.1049-0.0856-0.06740.02730.10030.2994-0.03680.02250.1991-0.01680.2965-28.3414-12.2862-52.3258
280.326-0.78190.19862.6459-0.27952.90540.0238-0.5318-0.44720.4056-0.2709-0.19640.3130.24060.13110.3446-0.0969-0.04650.31460.10220.2712-22.892-16.1998-28.8668
290.62850.4249-0.27791.08640.09451.48970.0381-0.0571-0.24210.1404-0.0781-0.07090.2690.01240.00370.2608-0.04670.01920.14120.00630.2067-34.6874-20.906-41.7019
301.43590.61920.57181.75660.6611.79520.0706-0.15910.10710.3109-0.1533-0.2245-0.01810.1899-0.010.2688-0.0737-0.0280.22980.03740.2936-15.8382-1.8871-42.0945
312.9571-1.63411.19151.31810.17983.37280.20770.2629-0.7177-0.1589-0.0686-0.2604-0.07850.1456-0.13260.21470.02230.00490.270.0040.568233.69925.4972-59.9854
322.246-0.06020.50880.0587-0.36591.19250.05910.4206-0.0923-0.0532-0.1003-0.3319-0.15130.24770.03630.3138-0.00340.03480.34740.0210.379526.120840.3593-63.8733
331.4640.7850.58030.92820.31582.08180.05-0.2419-0.22590.0912-0.18840.01750.0704-0.03210.14590.2832-0.0403-0.0110.19680.0380.351110.323928.6811-42.4246
340.0393-0.11920.04081.2009-0.24692.74870.1653-0.4619-0.62930.3311-0.3147-0.39420.23740.26130.22550.3781-0.0933-0.10250.42510.18130.445523.31230.1474-29.0944
350.62150.4985-0.71690.5285-0.20661.11240.0479-0.1209-0.43030.0748-0.1627-0.23980.1020.01960.00080.2287-0.0392-0.04510.17850.06870.342311.077425.6371-41.7823
362.060.880.67511.33030.29321.21280.1794-0.4357-0.03970.2981-0.1856-0.3044-0.04750.1474-0.00570.2582-0.0744-0.06090.26180.03820.351530.085643.026-43.2993
372.14230.39180.59762.26410.91671.74930.2739-0.47580.04040.2802-0.1379-0.386-0.10240.282-0.22740.2826-0.1275-0.07870.31660.08440.387932.598846.5589-40.3653
382.1439-1.3253-0.37763.20490.29842.7131-0.07250.35570.5606-0.62530.00270.389-0.3286-0.3710.04160.32350.0427-0.06320.29960.08710.4366-22.028853.2212-67.723
391.6185-0.15210.03760.6449-0.39731.19510.0185-0.06820.07680.0735-0.0306-0.0724-0.076-0.12770.00180.2206-0.0009-0.01790.1905-0.04680.2294-5.279441.9602-51.1962
400.58190.45440.15171.167-0.49962.2913-0.0383-0.38290.1020.22140.00840.1476-0.1985-0.55640.00910.2620.0533-0.00410.4753-0.07880.2316-17.493742.9737-39.6481
411.993-1.19451.71522.39630.18195.38150.0752-0.19820.36110.2462-0.0942-0.409-0.28120.3252-0.0340.2894-0.0896-0.0240.2813-0.050.36544.505349.2142-37.9023
421.45550.32790.34741.6242-0.06330.8030.1021-0.2244-0.14720.0935-0.0490.1890.0686-0.1999-0.09610.1853-0.0099-0.00870.28010.01340.2254-23.009131.0871-54.2453
439.4678-2.9223-4.37145.35084.06393.6747-1.73910.22910.61291.51820.6626-1.5152-0.27290.06221.10091.3936-0.04210.19830.52360.30921.1459-8.210932.4429-51.0951
440.6872-0.505-0.78155.5574-1.38782.0251-0.15720.00060.3684-0.08110.08970.3999-0.7683-0.73020.02230.35050.1472-0.05330.5376-0.03520.6288-68.87046.5558-64.2333
451.4337-0.05480.30790.9440.06791.25820.02020.0010.18770.0021-0.05680.182-0.1593-0.36850.03990.27740.02660.01420.2497-0.03220.3126-55.1092-4.8922-54.2812
461.0008-0.1434-0.79471.4414-0.48832.38930.0096-0.32060.06410.32090.02940.2921-0.2419-0.6419-0.0870.35650.02740.08420.584-0.10290.382-64.3592-4.5467-40.2821
472.1409-0.81531.05051.48260.2743.8607-0.0232-0.14730.56090.4169-0.0783-0.0989-0.22250.1850.12570.4283-0.06670.02850.2868-0.07050.3841-42.38162.0026-37.7071
480.59070.04160.6262.2549-0.09071.66880.0197-0.1422-0.0102-0.0441-00.64330.1637-0.6220.04240.2306-0.0363-0.00610.4005-0.02690.4223-69.9127-13.8679-58.0901
491.4350.19981.05662.044-0.04810.85410.1852-0.3612-0.20550.2011-0.08770.28450.4938-0.428600.3009-0.13460.02660.57740.01160.431-67.5018-22.022-49.9038
502-3.03729.10940.6234-1.86975.6080.0496-0.0405-0.04470.2892-0.0714-0.19510.153-0.1155-0.00171.5035-0.09270.19510.74960.48910.9456-55.3528-14.9009-51.3347
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 67 )A6 - 67
2X-RAY DIFFRACTION2chain 'A' and (resid 68 through 158 )A68 - 158
3X-RAY DIFFRACTION3chain 'A' and (resid 159 through 229 )A159 - 229
4X-RAY DIFFRACTION4chain 'A' and (resid 230 through 303 and resid 501)A230 - 303
5X-RAY DIFFRACTION5chain 'A' and (resid 304 through 443 )A304 - 443
6X-RAY DIFFRACTION6chain 'B' and (resid 5 through 67 )B5 - 67
7X-RAY DIFFRACTION7chain 'B' and (resid 68 through 158 )B68 - 158
8X-RAY DIFFRACTION8chain 'B' and (resid 159 through 185 )B159 - 185
9X-RAY DIFFRACTION9chain 'B' and (resid 186 through 443 and resid 501)B186 - 443
10X-RAY DIFFRACTION10chain 'C' and (resid 6 through 47 )C6 - 47
11X-RAY DIFFRACTION11chain 'C' and (resid 48 through 158 )C48 - 158
12X-RAY DIFFRACTION12chain 'C' and (resid 159 through 262 and resid 502)C159 - 262
13X-RAY DIFFRACTION13chain 'C' and (resid 263 through 303 )C263 - 303
14X-RAY DIFFRACTION14chain 'C' and (resid 304 through 378 )C304 - 378
15X-RAY DIFFRACTION15chain 'C' and (resid 379 through 407 )C379 - 407
16X-RAY DIFFRACTION16chain 'C' and (resid 408 through 443 )C408 - 443
17X-RAY DIFFRACTION17chain 'C' and (resid 501 through 501 )C502
18X-RAY DIFFRACTION18chain 'D' and (resid 6 through 67 )D6 - 67
19X-RAY DIFFRACTION19chain 'D' and (resid 68 through 121 )D68 - 121
20X-RAY DIFFRACTION20chain 'D' and (resid 122 through 262 and resid 502)D122 - 262
21X-RAY DIFFRACTION21chain 'D' and (resid 263 through 303 )D263 - 303
22X-RAY DIFFRACTION22chain 'D' and (resid 304 through 378 )D304 - 378
23X-RAY DIFFRACTION23chain 'D' and (resid 379 through 415 )D379 - 415
24X-RAY DIFFRACTION24chain 'D' and (resid 416 through 443 )D416 - 443
25X-RAY DIFFRACTION25chain 'D' and (resid 501 through 501 )D502
26X-RAY DIFFRACTION26chain 'E' and (resid 7 through 47 )E7 - 47
27X-RAY DIFFRACTION27chain 'E' and (resid 48 through 168 )E48 - 168
28X-RAY DIFFRACTION28chain 'E' and (resid 169 through 211 )E169 - 211
29X-RAY DIFFRACTION29chain 'E' and (resid 212 through 303 and resid 501)E212 - 303
30X-RAY DIFFRACTION30chain 'E' and (resid 304 through 443 )E304 - 443
31X-RAY DIFFRACTION31chain 'F' and (resid 7 through 47 )F7 - 47
32X-RAY DIFFRACTION32chain 'F' and (resid 48 through 101 )F48 - 101
33X-RAY DIFFRACTION33chain 'F' and (resid 102 through 168 )F102 - 168
34X-RAY DIFFRACTION34chain 'F' and (resid 169 through 211 )F169 - 211
35X-RAY DIFFRACTION35chain 'F' and (resid 212 through 303 and resid 501)F212 - 303
36X-RAY DIFFRACTION36chain 'F' and (resid 304 through 401 )F304 - 401
37X-RAY DIFFRACTION37chain 'F' and (resid 402 through 443 )F402 - 443
38X-RAY DIFFRACTION38chain 'G' and (resid 5 through 67 )G5 - 67
39X-RAY DIFFRACTION39chain 'G' and (resid 68 through 168 )G68 - 168
40X-RAY DIFFRACTION40chain 'G' and (resid 169 through 262 and resid 501)G169 - 262
41X-RAY DIFFRACTION41chain 'G' and (resid 263 through 303 )G263 - 303
42X-RAY DIFFRACTION42chain 'G' and (resid 304 through 443 )G304 - 443
43X-RAY DIFFRACTION43chain 'F' and (resid 502 through 502 )F502
44X-RAY DIFFRACTION44chain 'H' and (resid 6 through 47 )H6 - 47
45X-RAY DIFFRACTION45chain 'H' and (resid 48 through 175 )H48 - 175
46X-RAY DIFFRACTION46chain 'H' and (resid 176 through 262 and resid 501)H176 - 262
47X-RAY DIFFRACTION47chain 'H' and (resid 263 through 303 )H263 - 303
48X-RAY DIFFRACTION48chain 'H' and (resid 304 through 378 )H304 - 378
49X-RAY DIFFRACTION49chain 'H' and (resid 379 through 443 )H379 - 443
50X-RAY DIFFRACTION50chain 'E' and (resid 502 through 502 )E502

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