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- PDB-6b2m: LarE, a sulfur transferase involved in synthesis of the cofactor ... -

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Basic information

Entry
Database: PDB / ID: 6b2m
TitleLarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase in complex with coenzyme A
ComponentsATP-utilizing enzyme of the PP-loopsuperfamily
KeywordsTRANSFERASE / Lar / sulfur transferase / LarE / AMPylation / hexamer / trimer / PP-loop / ATP / magnesium / ATP pyrophophatase domain / lactate / lactate racemization / lactate racemase / coenzyme A
Function / homology
Function and homology information


pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase / NAD+ synthase (glutamine-hydrolyzing) activity / sulfurtransferase activity / lyase activity / ATP binding
Similarity search - Function
Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase LarE / NAD/GMP synthase / NAD synthase / Rossmann-like alpha/beta/alpha sandwich fold
Similarity search - Domain/homology
COENZYME A / PHOSPHATE ION / Lactate racemization operon protein LarE / Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase
Similarity search - Component
Biological speciesLactobacillus plantarum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.088 Å
AuthorsFellner, M. / Hausinger, R.P. / Hu, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)CHE-1516126 United States
CitationJournal: Biochemistry / Year: 2018
Title: Analysis of the Active Site Cysteine Residue of the Sacrificial Sulfur Insertase LarE from Lactobacillus plantarum.
Authors: Fellner, M. / Rankin, J.A. / Desguin, B. / Hu, J. / Hausinger, R.P.
History
DepositionSep 20, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 5, 2018Provider: repository / Type: Initial release
Revision 1.1Sep 12, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Oct 10, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Feb 20, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Oct 4, 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ATP-utilizing enzyme of the PP-loopsuperfamily
B: ATP-utilizing enzyme of the PP-loopsuperfamily
C: ATP-utilizing enzyme of the PP-loopsuperfamily
D: ATP-utilizing enzyme of the PP-loopsuperfamily
E: ATP-utilizing enzyme of the PP-loopsuperfamily
F: ATP-utilizing enzyme of the PP-loopsuperfamily
hetero molecules


Theoretical massNumber of molelcules
Total (without water)195,48818
Polymers190,3136
Non-polymers5,17512
Water10,899605
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14150 Å2
ΔGint-62 kcal/mol
Surface area62250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.362, 107.362, 319.849
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number91
Space group name H-MP4122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 2 through 3 or (resid 4...
21(chain B and (resid 2 through 3 or (resid 4...
31(chain C and (resid 2 through 3 or (resid 4...
41(chain D and (resid 2 through 18 or (resid 20...
51(chain E and (resid 2 through 3 or (resid 4...
61(chain F and (resid 2 through 3 or (resid 4...

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
11ALAALATHRTHR(chain A and (resid 2 through 3 or (resid 4...AA2 - 32 - 3
12LEULEUALAALA(chain A and (resid 2 through 3 or (resid 4...AA4 - 54 - 5
13ALAALACOACOA(chain A and (resid 2 through 3 or (resid 4...AA - G2 - 5012
14ALAALACOACOA(chain A and (resid 2 through 3 or (resid 4...AA - G2 - 5012
15ALAALACOACOA(chain A and (resid 2 through 3 or (resid 4...AA - G2 - 5012
16ALAALACOACOA(chain A and (resid 2 through 3 or (resid 4...AA - G2 - 5012
21ALAALATHRTHR(chain B and (resid 2 through 3 or (resid 4...BB2 - 32 - 3
22LEULEUALAALA(chain B and (resid 2 through 3 or (resid 4...BB4 - 54 - 5
23ALAALACOACOA(chain B and (resid 2 through 3 or (resid 4...BB - I2 - 5012
24ALAALACOACOA(chain B and (resid 2 through 3 or (resid 4...BB - I2 - 5012
25ALAALACOACOA(chain B and (resid 2 through 3 or (resid 4...BB - I2 - 5012
26ALAALACOACOA(chain B and (resid 2 through 3 or (resid 4...BB - I2 - 5012
31ALAALATHRTHR(chain C and (resid 2 through 3 or (resid 4...CC2 - 32 - 3
32LEULEUALAALA(chain C and (resid 2 through 3 or (resid 4...CC4 - 54 - 5
33ALAALACOACOA(chain C and (resid 2 through 3 or (resid 4...CC - K2 - 5012
34ALAALACOACOA(chain C and (resid 2 through 3 or (resid 4...CC - K2 - 5012
35ALAALACOACOA(chain C and (resid 2 through 3 or (resid 4...CC - K2 - 5012
36ALAALACOACOA(chain C and (resid 2 through 3 or (resid 4...CC - K2 - 5012
41ALAALALEULEU(chain D and (resid 2 through 18 or (resid 20...DD2 - 182 - 18
42ARGARGARGARG(chain D and (resid 2 through 18 or (resid 20...DD2020
43ALAALACOACOA(chain D and (resid 2 through 18 or (resid 20...DD - M2 - 5012
44ALAALACOACOA(chain D and (resid 2 through 18 or (resid 20...DD - M2 - 5012
45ALAALACOACOA(chain D and (resid 2 through 18 or (resid 20...DD - M2 - 5012
46ALAALACOACOA(chain D and (resid 2 through 18 or (resid 20...DD - M2 - 5012
51ALAALATHRTHR(chain E and (resid 2 through 3 or (resid 4...EE2 - 32 - 3
52LEULEUALAALA(chain E and (resid 2 through 3 or (resid 4...EE4 - 54 - 5
53ALAALACOACOA(chain E and (resid 2 through 3 or (resid 4...EE - O2 - 5012
54ALAALACOACOA(chain E and (resid 2 through 3 or (resid 4...EE - O2 - 5012
55ALAALACOACOA(chain E and (resid 2 through 3 or (resid 4...EE - O2 - 5012
56ALAALACOACOA(chain E and (resid 2 through 3 or (resid 4...EE - O2 - 5012
61ALAALATHRTHR(chain F and (resid 2 through 3 or (resid 4...FF2 - 32 - 3
62LEULEUALAALA(chain F and (resid 2 through 3 or (resid 4...FF4 - 54 - 5
63ALAALACOACOA(chain F and (resid 2 through 3 or (resid 4...FF - Q2 - 5012
64ALAALACOACOA(chain F and (resid 2 through 3 or (resid 4...FF - Q2 - 5012
65ALAALACOACOA(chain F and (resid 2 through 3 or (resid 4...FF - Q2 - 5012
66ALAALACOACOA(chain F and (resid 2 through 3 or (resid 4...FF - Q2 - 5012

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Components

#1: Protein
ATP-utilizing enzyme of the PP-loopsuperfamily / Lactate racemization operon protein LarE / PP-loop superfamily ATP-binding protein / TIGR00268 family protein


Mass: 31718.766 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactobacillus plantarum (bacteria)
Gene: A8P51_04975, AVR82_02840, BIZ32_00440, IV39_GL000116, LPJSA22_00116, Nizo1839_0768, Nizo2891_3302, SRCM101060_01452
Plasmid: pGIR076 / Production host: Escherichia coli (E. coli) / Strain (production host): Arctic express DE3 / References: UniProt: A0A0G9FES3, UniProt: F9UST4*PLUS
#2: Chemical
ChemComp-COA / COENZYME A / Coenzyme A


Mass: 767.534 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 605 / 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: 2.42 Å3/Da / Density % sol: 49.21 % / Mosaicity: 0.19 °
Crystal growTemperature: 294.15 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 5 ul 28 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) containing 0.9 mM coenzyme A were mixed with 5 ul of reservoir solution. Hanging drop reservoir contained 100 ul of 30.0% v/v ...Details: 5 ul 28 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) containing 0.9 mM coenzyme A were mixed with 5 ul of reservoir solution. Hanging drop reservoir contained 100 ul of 30.0% v/v pentaerythritol ethoxylate (15/4 EO/OH), 50 mM BIS-TRIS pH 6.5, 100 mM ammonium sulfate.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.9787 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jul 31, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9787 Å / Relative weight: 1
ReflectionResolution: 2.09→47.95 Å / Num. obs: 111492 / % possible obs: 99.7 % / Redundancy: 6.1 % / Biso Wilson estimate: 33.46 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.091 / Rpim(I) all: 0.04 / Rrim(I) all: 0.1 / Net I/σ(I): 14.7 / Num. measured all: 679519 / Scaling rejects: 0
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.09-2.1260.993173352930.5090.4331.0831.897.1
11.43-47.954.90.02239317950.9990.0110.02543.797.2

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.32 Å47.75 Å
Translation8.32 Å47.75 Å

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Processing

Software
NameVersionClassification
PHENIXrefinement
Aimless0.5.27data scaling
PHASER2.6.0phasing
PDB_EXTRACT3.22data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UDQ

5udq


Resolution: 2.088→47.746 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 23.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2335 10496 4.96 %
Rwork0.1946 200931 -
obs0.1966 211427 99.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 150.38 Å2 / Biso mean: 43.7285 Å2 / Biso min: 16.28 Å2
Refinement stepCycle: final / Resolution: 2.088→47.746 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11607 0 318 605 12530
Biso mean--57.14 42.37 -
Num. residues----1525
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00812140
X-RAY DIFFRACTIONf_angle_d0.95116519
X-RAY DIFFRACTIONf_chiral_restr0.0551910
X-RAY DIFFRACTIONf_plane_restr0.0062100
X-RAY DIFFRACTIONf_dihedral_angle_d4.9938313
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6330X-RAY DIFFRACTION8.845TORSIONAL
12B6330X-RAY DIFFRACTION8.845TORSIONAL
13C6330X-RAY DIFFRACTION8.845TORSIONAL
14D6330X-RAY DIFFRACTION8.845TORSIONAL
15E6330X-RAY DIFFRACTION8.845TORSIONAL
16F6330X-RAY DIFFRACTION8.845TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.0877-2.11140.35853540.3086455680995
2.1114-2.13630.33763540.297966717025100
2.1363-2.16230.31353390.280567887127100
2.1623-2.18970.31683080.26767217029100
2.1897-2.21850.28693500.270566517001100
2.2185-2.24890.31923460.270867297075100
2.2489-2.2810.30673770.255767237100100
2.281-2.31510.27683370.232966877024100
2.3151-2.35130.29183390.237667417080100
2.3513-2.38980.3173290.235567827111100
2.3898-2.4310.27423250.230467067031100
2.431-2.47520.30853480.229667257073100
2.4752-2.52280.29173970.2266557052100
2.5228-2.57430.28153100.216867737083100
2.5743-2.63030.25523460.208967347080100
2.6303-2.69150.26163360.205467277063100
2.6915-2.75880.26463360.212167927128100
2.7588-2.83330.27853450.218766867031100
2.8333-2.91670.26123710.199666837054100
2.9167-3.01080.24933340.20267007034100
3.0108-3.11840.26173120.213567857097100
3.1184-3.24330.23223030.200567727075100
3.2433-3.39080.24733940.194466487042100
3.3908-3.56950.21023960.17866847080100
3.5695-3.79310.21663790.174966717050100
3.7931-4.08580.20573270.161867067033100
4.0858-4.49670.1753980.14776629702799
4.4967-5.14670.16774220.14156575699799
5.1467-6.48180.20483640.17166667703199
6.4818-47.75890.18893200.17436665698599
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)
11.88761.81950.00036.1854-0.43032.14920.06730.0279-0.1141-0.0189-0.0064-0.22070.29590.0915-0.0630.35160.0650.07050.24820.0090.198434.7941-51.0873-16.8163
20.8561.38070.195.09550.0850.19540.0586-0.20710.14020.3112-0.00160.5715-0.0886-0.212-0.0610.32190.0570.05860.36970.03440.280829.5628-46.7175-18.0372
36.6361-0.6057-0.70312.01630.87543.00510.02660.3562-0.0528-0.2762-0.08560.18250.1039-0.07510.05730.2930.01870.01380.15090.01530.208531.2103-23.1296-3.4906
42.7286-0.823-1.34743.09542.98938.96240.04550.0418-0.53540.0162-0.0650.03440.4098-0.03650.02860.182-0.0225-0.02950.1817-0.00350.309144.1263-60.856516.9432
56.64276.6467.9612.07927.04059.7326-0.0563-0.1882-0.0461-0.23190.09510.1639-0.3889-0.5772-0.12310.3387-0.01920.060.37050.04330.357534.6759-53.668826.0868
66.35425.49936.28638.73517.23427.46740.5478-0.3579-0.00020.8101-0.448-0.21560.58140.1669-0.0940.2297-0.00460.06350.31560.04010.310751.0975-48.105533.2403
74.31944.74853.98978.45636.77916.2522-0.0407-0.1615-0.26510.45380.1769-0.31560.1950.2144-0.120.20630.04310.02270.34220.02230.274554.5132-54.77829.1976
89.2669-2.41243.21513.9956-2.69537.2668-0.21710.34080.85010.7925-0.0105-0.1728-1.44280.70210.26820.5118-0.04450.00960.252-0.04140.321453.088-56.860517.6132
92.1576-7.11477.47127.6181-4.36129.12320.17050.84040.3533-0.3037-0.3058-0.3009-0.52160.26760.13640.42540.04070.03720.36050.01120.289844.5855-54.21726.7584
100.32362.14211.42948.42595.79235.2271-0.16650.08840.0996-0.82880.01880.1997-0.40940.23220.12280.31420.05760.03360.26280.04020.313943.3742-41.739824.7667
112.4521-8.74688.34098.73-8.4612.57650.0757-0.22690.0803-0.1841-0.1881-0.14730.32670.03680.20410.17570.00940.03780.372-0.04110.207637.6855-35.781533.4489
122.9923-1.01760.76884.1619-2.23213.8759-0.06690.07630.0977-0.0847-0.01410.039-0.08090.04870.12440.2068-0.03150.01320.1793-0.02320.195835.221-27.438826.5633
138.96083.39460.17926.119-4.65469.5654-0.0579-0.10380.1397-0.1099-0.0898-0.1545-0.14240.5010.16920.1140.036-0.00290.13060.00660.209940.0316-24.252128.6817
145.0838-3.8910.88197.6606-0.81121.80550.0467-0.00150.1665-0.31610.019-0.20370.13070.0366-0.04890.2428-0.02950.02120.1557-0.02840.171112.3481-61.32747.7877
155.6766-4.2128-3.62787.95736.71349.0986-0.1022-0.62630.23120.50640.21120.58570.12890.0942-0.06330.2456-0.03350.07440.2687-0.01340.3109-3.7432-53.00615.646
169.2277-1.2335-0.36447.0755-4.14085.2538-0.3283-1.05810.12521.02280.22060.4354-0.1551-0.04470.19460.35920.01950.04180.26340.01450.276.1852-63.154119.0103
172.14627.6312-0.34568.73531.59839.83550.0194-0.4293-0.18010.6649-0.0381-0.49530.2779-0.16230.04050.29950.0787-0.01450.24620.01940.299921.2253-62.713719.2386
188.7201-1.381-2.2823.77782.41421.858-0.4238-0.88370.2568-0.08250.47190.08780.03410.32990.01390.3264-0.0221-0.03250.31840.03660.28918.7796-44.242115.5116
193.32011.6546-0.40153.279-0.40741.80010.00460.0844-0.2036-0.13170.04160.02750.10680.0576-0.04230.27570.0330.00630.1823-0.02240.23349.8394-28.888112.0013
208.4426-1.5973.75525.71993.08477.651-0.1942-0.9974-0.65650.52090.36090.10320.6542-0.5522-0.16970.2491-0.03960.09390.23330.06450.30878.322-27.132719.8174
219.2499-2.1601-0.07598.99970.13836.6371-0.8936-0.8385-0.03340.55630.61461.8819-0.8457-0.92410.29130.82790.2124-0.02650.48710.05620.734531.040722.93833.8917
222.9961-2.55420.51546.8097-1.37643.2244-0.0632-0.21650.4512-0.29390.0463-0.4864-0.63290.0603-0.01940.5887-0.1307-0.06670.3345-0.02880.343547.010311.585634.9958
231.7515-1.9432-0.37574.17690.17641.57590.07190.04740.0038-0.22930.07130.4872-0.6173-0.3614-0.13180.6522-0.0368-0.06620.49740.0510.503734.449910.054333.9138
247.27790.96930.31184.5485-0.26093.2336-0.0888-0.11720.3063-0.08780.0303-0.0863-0.26540.21330.06450.2406-0.03550.00160.16890.0130.170142.3052-11.837223.2581
252.92652.981-1.71627.3599-3.34213.8650.3653-0.13260.77310.2189-0.20430.8507-0.7856-0.2723-0.15230.47980.09030.00230.3375-0.06760.4337-0.080711.877527.4986
261.36231.68640.27018.0585-2.62981.0164-0.21790.23130.3867-0.6320.12960.1305-0.1814-0.13030.08470.52930.06590.01410.38510.01970.35713.33938.226319.8766
272.4081-0.276-0.01652.12520.61455.38760.08220.11690.0408-0.1606-0.09130.142-0.1695-0.20690.00140.18190.00740.00580.1498-0.01150.2359.7903-14.624421.6295
281.0578-0.04030.21514.61072.06322.77420.00580.18360.074-0.4435-0.0396-0.1947-0.03480.01520.03910.38890.02810.05560.18210.06390.278928.12521.3216-4.5409
294.46252.57141.92514.94281.38247.7481-0.040.5215-0.3351-0.66240.188-0.91770.69280.8897-0.14840.40980.04560.11550.2570.01380.448938.776523.9599-2.3213
300.8689-0.0352-2.08480.0574-0.19372.21390.10110.0497-0.05270.73980.06270.16890.9923-0.1995-0.19560.68120.05450.00290.2864-0.00140.396930.30717.593310.3639
313.49370.8073-1.35565.067-1.92243.2949-0.00530.17640.1537-0.15410.0441-0.1988-0.3208-0.0095-0.04640.25130.0250.00680.1427-0.01080.209725.6519-7.507-3.378
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 95 )A2 - 95
2X-RAY DIFFRACTION2chain 'A' and (resid 96 through 189 )A96 - 189
3X-RAY DIFFRACTION3chain 'A' and (resid 190 through 279 )A190 - 279
4X-RAY DIFFRACTION4chain 'B' and (resid 2 through 58 )B2 - 58
5X-RAY DIFFRACTION5chain 'B' and (resid 59 through 72 )B59 - 72
6X-RAY DIFFRACTION6chain 'B' and (resid 73 through 95 )B73 - 95
7X-RAY DIFFRACTION7chain 'B' and (resid 96 through 115 )B96 - 115
8X-RAY DIFFRACTION8chain 'B' and (resid 116 through 146 )B116 - 146
9X-RAY DIFFRACTION9chain 'B' and (resid 147 through 164 )B147 - 164
10X-RAY DIFFRACTION10chain 'B' and (resid 165 through 189 )B165 - 189
11X-RAY DIFFRACTION11chain 'B' and (resid 190 through 205 )B190 - 205
12X-RAY DIFFRACTION12chain 'B' and (resid 206 through 245 )B206 - 245
13X-RAY DIFFRACTION13chain 'B' and (resid 246 through 259 )B246 - 259
14X-RAY DIFFRACTION14chain 'C' and (resid 2 through 81 )C2 - 81
15X-RAY DIFFRACTION15chain 'C' and (resid 82 through 115 )C82 - 115
16X-RAY DIFFRACTION16chain 'C' and (resid 116 through 146 )C116 - 146
17X-RAY DIFFRACTION17chain 'C' and (resid 147 through 164 )C147 - 164
18X-RAY DIFFRACTION18chain 'C' and (resid 165 through 189 )C165 - 189
19X-RAY DIFFRACTION19chain 'C' and (resid 190 through 245 )C190 - 245
20X-RAY DIFFRACTION20chain 'C' and (resid 246 through 263 )C246 - 263
21X-RAY DIFFRACTION21chain 'D' and (resid 2 through 42 )D2 - 42
22X-RAY DIFFRACTION22chain 'D' and (resid 43 through 115 )D43 - 115
23X-RAY DIFFRACTION23chain 'D' and (resid 116 through 189 )D116 - 189
24X-RAY DIFFRACTION24chain 'D' and (resid 190 through 259 )D190 - 259
25X-RAY DIFFRACTION25chain 'E' and (resid 2 through 115 )E2 - 115
26X-RAY DIFFRACTION26chain 'E' and (resid 116 through 189 )E116 - 189
27X-RAY DIFFRACTION27chain 'E' and (resid 190 through 280 )E190 - 280
28X-RAY DIFFRACTION28chain 'F' and (resid 2 through 115 )F2 - 115
29X-RAY DIFFRACTION29chain 'F' and (resid 116 through 154 )F116 - 154
30X-RAY DIFFRACTION30chain 'F' and (resid 155 through 177 )F155 - 177
31X-RAY DIFFRACTION31chain 'F' and (resid 178 through 259 )F178 - 259

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