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- PDB-6dwe: Crystal structure of tryptophan synthase from M. tuberculosis - a... -

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Basic information

Entry
Database: PDB / ID: 6dwe
TitleCrystal structure of tryptophan synthase from M. tuberculosis - aminoacrylate- and BRD0059-bound form
Components(Tryptophan synthase ...) x 2
KeywordsLYASE/LYASE INHIBITOR / PLP / heterotetramer / amino acid biosynthesis / substrate channeling / allostery / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID / LYASE-LYASE INHIBITOR complex
Function / homology
Function and homology information


tryptophan synthase / tryptophan synthase activity / L-tryptophan metabolic process / L-tryptophan biosynthetic process / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Tryptophan synthase, alpha chain / Tryptophan synthase, alpha chain, active site / Tryptophan synthase alpha chain / Tryptophan synthase alpha chain signature. / Tryptophan synthase, beta chain, conserved site / Tryptophan synthase, beta chain / Tryptophan synthase beta chain/beta chain-like / Tryptophan synthase beta chain pyridoxal-phosphate attachment site. / Rossmann fold - #1100 / Pyridoxal-phosphate dependent enzyme ...Tryptophan synthase, alpha chain / Tryptophan synthase, alpha chain, active site / Tryptophan synthase alpha chain / Tryptophan synthase alpha chain signature. / Tryptophan synthase, beta chain, conserved site / Tryptophan synthase, beta chain / Tryptophan synthase beta chain/beta chain-like / Tryptophan synthase beta chain pyridoxal-phosphate attachment site. / Rossmann fold - #1100 / Pyridoxal-phosphate dependent enzyme / Pyridoxal-phosphate dependent enzyme / Tryptophan synthase beta subunit-like PLP-dependent enzyme / Ribulose-phosphate binding barrel / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / : / FORMIC ACID / Chem-HDJ / MALONIC ACID / MALONATE ION / Chem-P1T / TRIETHYLENE GLYCOL / Tryptophan synthase beta chain / Tryptophan synthase alpha chain
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.691 Å
AuthorsChang, C. / Michalska, K. / Maltseva, N.I. / Jedrzejczak, R. / McCarren, P. / Nag, P.P. / Joachimiak, A. / Satchell, K. / Center for Structural Genomics of Infectious Diseases (CSGID)
CitationJournal: To be Published
Title: Crystal structure of tryptophan synthase from M. tuberculosis - closed form with BRD6309 bound
Authors: Chang, C. / Michalska, K. / Maltseva, N.I. / Jedrzejczak, R. / McCarren, P. / Nag, P.P. / Joachimiak, A. / Satchell, K.
History
DepositionJun 26, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 11, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 17, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support
Revision 1.2Oct 11, 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_conn_type
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_asym_id / _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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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.ptnr1_symmetry / _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_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_conn_type.id
Revision 1.3Dec 25, 2024Group: Advisory / Derived calculations / Structure summary
Category: pdbx_entry_details / pdbx_validate_close_contact ...pdbx_entry_details / pdbx_validate_close_contact / struct_conn / struct_conn_type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tryptophan synthase alpha chain
B: Tryptophan synthase beta chain
G: Tryptophan synthase alpha chain
H: Tryptophan synthase beta chain
E: Tryptophan synthase alpha chain
F: Tryptophan synthase beta chain
C: Tryptophan synthase alpha chain
D: Tryptophan synthase beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)293,91569
Polymers287,6568
Non-polymers6,25961
Water13,709761
1
A: Tryptophan synthase alpha chain
B: Tryptophan synthase beta chain
C: Tryptophan synthase alpha chain
D: Tryptophan synthase beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,91133
Polymers143,8284
Non-polymers3,08329
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
G: Tryptophan synthase alpha chain
H: Tryptophan synthase beta chain
E: Tryptophan synthase alpha chain
F: Tryptophan synthase beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)147,00436
Polymers143,8284
Non-polymers3,17532
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)135.093, 159.396, 165.226
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Tryptophan synthase ... , 2 types, 8 molecules AGECBHFD

#1: Protein
Tryptophan synthase alpha chain


Mass: 28579.449 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: trpA, Rv1613, MTCY01B2.05 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P9WFY1, tryptophan synthase
#2: Protein
Tryptophan synthase beta chain


Mass: 43334.598 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv / Gene: trpB, Rv1612, MTCY01B2.04 / Plasmid: pMCSG81 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P9WFX9, tryptophan synthase

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Non-polymers , 10 types, 822 molecules

#3: Chemical
ChemComp-MLI / MALONATE ION


Mass: 102.046 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H2O4
#4: Chemical...
ChemComp-FMT / FORMIC ACID


Mass: 46.025 Da / Num. of mol.: 33 / Source method: obtained synthetically / Formula: CH2O2
#5: Chemical
ChemComp-P1T / 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID


Mass: 318.220 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C11H15N2O7P
#6: Chemical
ChemComp-CS / CESIUM ION


Mass: 132.905 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Cs
#7: Chemical
ChemComp-HDJ / (2R,3S,4R)-3-(2',6'-difluoro-4'-methyl[1,1'-biphenyl]-4-yl)-4-(fluoromethyl)azetidine-2-carbonitrile


Mass: 316.320 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C18H15F3N2
#8: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#9: Chemical ChemComp-MLA / MALONIC ACID / DICARBOXYLIC ACID C3 / PROPANEDIOLIC ACID / METHANEDICARBOXYLIC ACID


Mass: 104.061 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O4
#10: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#11: Chemical ChemComp-PGE / TRIETHYLENE GLYCOL


Mass: 150.173 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O4
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 761 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationN

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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: 3.09 Å3/Da / Density % sol: 60.22 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop
Details: 8% Tacsimate, pH 8.0, 20% PEG3350, 100 mM sodium malonate, pH 7.0
PH range: 7.0~8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97926 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 10, 2016
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97926 Å / Relative weight: 1
ReflectionResolution: 2.691→30 Å / Num. obs: 98448 / % possible obs: 99.3 % / Redundancy: 6.3 % / Biso Wilson estimate: 43.2 Å2 / Rmerge(I) obs: 0.163 / Rpim(I) all: 0.07 / Rrim(I) all: 0.178 / Χ2: 0.775 / Net I/σ(I): 4.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.691-2.755.10.74546480.610.3520.8270.68994.5
2.75-2.85.40.63547200.7270.2940.7030.69397
2.8-2.855.50.61548100.7530.2830.680.71997.7
2.85-2.915.70.57848320.7770.2630.6380.71898.4
2.91-2.975.80.56248570.7790.2550.6190.71199.2
2.97-3.0460.50448890.8380.2280.5550.70299.7
3.04-3.126.10.45949040.8550.2060.5050.72399.5
3.12-3.25.70.39249180.8810.1820.4340.73799.8
3.2-3.295.90.35448970.9180.160.390.74999.9
3.29-3.470.29649400.9590.1210.320.742100
3.4-3.5270.25549110.970.1040.2760.754100
3.52-3.6670.19949590.9810.0810.2150.746100
3.66-3.836.90.16849340.9860.0690.1810.777100
3.83-4.036.80.13849550.990.0570.1490.79399.9
4.03-4.286.70.11549590.9930.0480.1250.79199.9
4.28-4.616.20.09149690.9950.0390.0990.82499.8
4.61-5.076.10.08449870.9950.0370.0920.831100
5.07-5.870.10550230.9940.0430.1130.811100
5.8-7.36.70.08350710.9960.0350.090.829100
7.3-306.20.04852650.9980.0210.0521.07399.8

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
PHENIX1.12_2829refinement
PDB_EXTRACT3.24data extraction
HKL-3000data reduction
HKL-3000phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 5TCJ

5tcj


Resolution: 2.691→29.899 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 20.32
RfactorNum. reflection% reflection
Rfree0.2024 1955 1.99 %
Rwork0.1555 --
obs0.1564 98346 99.1 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 185.5 Å2 / Biso mean: 41.9582 Å2 / Biso min: 1.07 Å2
Refinement stepCycle: final / Resolution: 2.691→29.899 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19112 0 352 762 20226
Biso mean--53.7 39.36 -
Num. residues----2597
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00219928
X-RAY DIFFRACTIONf_angle_d0.75127037
X-RAY DIFFRACTIONf_chiral_restr0.0423016
X-RAY DIFFRACTIONf_plane_restr0.0043600
X-RAY DIFFRACTIONf_dihedral_angle_d17.36611698
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6913-2.75860.3591200.25856434655493
2.7586-2.83310.33811250.22936714683998
2.8331-2.91640.25851500.21266696684698
2.9164-3.01050.24781410.213468847025100
3.0105-3.1180.28561340.204868436977100
3.118-3.24270.25591520.190868777029100
3.2427-3.390.23261650.172368697034100
3.39-3.56850.2061290.159269137042100
3.5685-3.79170.19781610.140769237084100
3.7917-4.08380.18021410.13169477088100
4.0838-4.49350.16451440.116369377081100
4.4935-5.14090.13911200.114170207140100
5.1409-6.46610.16361530.144570377190100
6.4661-29.90130.16021200.139672977417100
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)
10.0987-0.04780.08720.1143-0.05160.07020.13950.0229-0.03090.0627-0.0545-0.1459-0.01320.04510.00090.1760.01730.01740.28120.05090.371789.2945-13.083621.8847
20.048-0.01190.05630.0082-0.01890.063-0.0819-0.00580.13960.0623-0.0471-0.1977-0.20780.1824-0.02030.1746-0.05080.02480.27220.06790.396987.2855-1.373821.2376
30.0657-0.04040.02280.0310.01010.0350.00470.2530.05940.0711-0.0326-0.109-0.0269-0.0281-00.24180.02420.03450.30320.07240.326879.2641-8.08899.0901
40.0679-0.0328-0.04210.01010.01530.0235-0.00120.223-0.3675-0.0397-0.1676-0.15620.19840.0822-0.00410.26940.07990.00780.3188-0.02070.436189.2209-23.921515.1051
50.0082-0.0121-0.01760.025-0.0070.0372-0.01170.15510.0059-0.06860.05860.1432-0.14270.02560.00030.15190.01550.00190.20.04360.157558.0095-5.344411.2925
60.00980.0608-0.06930.0974-0.10540.11160.0359-0.04-0.0272-0.07860.00980.0246-0.0539-0.08610.00020.14120.01390.01230.1281-0.00740.126942.5184-10.24126.2343
70.07460.00890.01190.0295-0.00890.02230.0777-0.2032-0.16750.0347-0.1037-0.1541-0.00170.025-00.16330.0117-0.00970.22490.06510.235959.124-17.85429.2086
80.19580.1244-0.18630.29640.07340.22950.0501-0.03960.02450.0242-0.0143-0.0372-0.07920.025900.152-0.00380.00070.16640.01840.128851.22072.43933.193
90.12210.02410.08380.2651-0.11330.11870.18150.0351-0.1188-0.10340.01280.29540.0836-0.04790.0460.11860.03710.00820.2146-0.0420.3461-20.913314.52419.4822
100.0249-0.0095-0.00870.05060.04330.04720.1312-0.04450.01410.0181-0.01570.1372-0.0550.049-00.17950.02630.01150.2748-0.00270.2804-12.062322.195312.185
110.02710.00270.00290.0116-0.01980.03090.051-0.0828-0.25480.12460.02960.1271-0.09120.068600.2824-0.04940.03910.2485-0.03450.3002-8.596918.407722.417
120.2174-0.1083-0.10720.10930.02510.0720.0357-0.3077-0.24490.03070.0850.3420.10940.0408-0.00540.2031-0.0465-0.00790.31130.0550.4885-22.22155.899618.8924
130.0504-0.00690.03240.04260.02090.03620.0128-0.1369-0.0285-0.0240.0174-0.0035-0.14050.09470.00080.1217-0.02570.02380.217-0.01990.122511.29146.455719.8697
140.1734-0.0965-0.16350.46560.12230.43970.0343-0.0272-0.0119-0.0782-0.04610.032-0.056-0.004500.1071-0.011200.132-0.00810.117316.97793.39280.468
150.02020.01990.04320.06480.05830.0707-0.27840.2482-0.1147-0.62030.1833-0.10080.15090.0311-0.07670.9992-0.27830.21880.3857-0.2220.198635.4491-38.5477-49.1031
160.53910.02650.3269-0.00080.02260.2152-0.32450.1586-0.1386-0.43920.0072-0.26620.275-0.044-0.42130.7374-0.0420.34050.2163-0.08880.318144.6209-41.8458-38.7779
170.08650.02980.12720.32350.01020.3508-0.32210.3861-0.033-0.89840.1749-0.2660.25330.1935-0.2320.9137-0.37590.29850.5933-0.050.122644.9023-28.1021-51.9465
180.009-0.0022-0.00460.00690.00870.007-0.07950.0323-0.0834-0.18020.0965-0.0770.06780.188800.34190.11610.0830.32130.00060.314646.8857-33.8042-18.659
190.01410.0129-0.02090.0326-0.02210.02450.0049-0.11150.031-0.06720.0425-0.2496-0.03940.109-0.00010.15590.0180.04470.23140.00540.200747.7086-14.7876-15.7078
200.1731-0.1009-0.11910.4380.05340.36-0.0445-0.0051-0.0219-0.1035-0.04310.01920.1245-0.0586-00.1678-0.01410.02470.111-0.01720.15329.9264-24.5516-12.8482
210.03110.0084-0.03720.0102-0.00160.03150.0119-0.0484-0.0817-0.03740.05350.10130.1737-0.1494-00.1856-0.0433-0.00560.21350.00870.194817.102-22.9552-5.3759
220.23540.108-0.01630.35860.09130.04130.0174-0.0747-0.04880.6069-0.03950.0236-0.1476-0.15370.05260.5489-0.02670.17470.29570.01780.215410.1298-29.792882.6532
230.0858-0.0631-0.01790.0631-0.02010.0495-0.03160.0229-0.00240.2969-0.03950.1733-0.074-0.0182-0.00030.2677-0.04430.09130.19510.02350.292810.7234-34.579671.9071
240.0219-0.0016-0.00030.00810.00210.0195-0.0546-0.015-0.03940.0170.04330.1416-0.210.0243-0.00010.2781-0.0130.14570.2075-0.02550.35820.4074-25.948669.0046
250.29940.2033-0.18590.1472-0.13260.13980.1613-0.03010.17770.6271-0.05730.3713-0.2293-0.15940.1680.7613-0.01990.17060.2134-0.11570.190510.0437-18.322482.9402
260.0168-0.0054-0.00980.00260.00070.0061-0.05130.0641-0.1060.0397-0.07050.0804-0.1052-0.128900.1605-0.0461-0.00510.3755-0.03730.24616.2735-22.924849.4075
270.24690.1899-0.09970.2997-0.04410.18040.01920.00110.01570.0198-0.038-0.0068-0.0243-0.090700.1222-0.00650.00430.1720.00520.145824.0141-16.088644.2206
280.03160.058-0.07650.1068-0.02510.1919-0.0523-0.0555-0.0337-0.0211-0.0146-0.02760.23440.011200.1829-0.00990.02650.16390.02550.202827.9244-32.36742.5946
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 8 through 85 )A8 - 85
2X-RAY DIFFRACTION2chain 'A' and (resid 86 through 126 )A86 - 126
3X-RAY DIFFRACTION3chain 'A' and (resid 127 through 197 )A127 - 197
4X-RAY DIFFRACTION4chain 'A' and (resid 198 through 267 )A198 - 267
5X-RAY DIFFRACTION5chain 'B' and (resid 5 through 50 )B5 - 50
6X-RAY DIFFRACTION6chain 'B' and (resid 51 through 140 )B51 - 140
7X-RAY DIFFRACTION7chain 'B' and (resid 141 through 210 )B141 - 210
8X-RAY DIFFRACTION8chain 'B' and (resid 211 through 408 )B211 - 408
9X-RAY DIFFRACTION9chain 'G' and (resid 9 through 85 )G9 - 85
10X-RAY DIFFRACTION10chain 'G' and (resid 86 through 142 )G86 - 142
11X-RAY DIFFRACTION11chain 'G' and (resid 143 through 165 )G143 - 165
12X-RAY DIFFRACTION12chain 'G' and (resid 166 through 267 )G166 - 267
13X-RAY DIFFRACTION13chain 'H' and (resid 4 through 50 )H4 - 50
14X-RAY DIFFRACTION14chain 'H' and (resid 51 through 407 )H51 - 407
15X-RAY DIFFRACTION15chain 'E' and (resid 9 through 97 )E9 - 97
16X-RAY DIFFRACTION16chain 'E' and (resid 98 through 165 )E98 - 165
17X-RAY DIFFRACTION17chain 'E' and (resid 166 through 265 )E166 - 265
18X-RAY DIFFRACTION18chain 'F' and (resid 9 through 31 )F9 - 31
19X-RAY DIFFRACTION19chain 'F' and (resid 32 through 64 )F32 - 64
20X-RAY DIFFRACTION20chain 'F' and (resid 65 through 379 )F65 - 379
21X-RAY DIFFRACTION21chain 'F' and (resid 380 through 407 )F380 - 407
22X-RAY DIFFRACTION22chain 'C' and (resid 8 through 69 )C8 - 69
23X-RAY DIFFRACTION23chain 'C' and (resid 70 through 142 )C70 - 142
24X-RAY DIFFRACTION24chain 'C' and (resid 143 through 165 )C143 - 165
25X-RAY DIFFRACTION25chain 'C' and (resid 166 through 266 )C166 - 266
26X-RAY DIFFRACTION26chain 'D' and (resid 9 through 31 )D9 - 31
27X-RAY DIFFRACTION27chain 'D' and (resid 32 through 271 )D32 - 271
28X-RAY DIFFRACTION28chain 'D' and (resid 272 through 407 )D272 - 407

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