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- PDB-5udu: LarE, a sulfur transferase involved in synthesis of the cofactor ... -

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Basic information

Entry
Database: PDB / ID: 5udu
TitleLarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with manganese
ComponentsLactate racemization operon protein LarE
KeywordsTRANSFERASE / Lar / sulfur transferase / LarE / AMPylation / manganese / hexamer / trimer / PP-loop / ATP pyrophophatase domain / lactate / lactate racemization / lactate racemase
Function / homology
Function and homology information


intrinsic cysteine-dependent pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase / 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
: / PHOSPHATE ION / Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase
Similarity search - Component
Biological speciesLactobacillus plantarum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.792 Å
AuthorsFellner, M. / Desguin, B. / Hausinger, R.P. / Hu, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)CHE-1516126 United States
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017
Title: Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Authors: Fellner, M. / Desguin, B. / Hausinger, R.P. / Hu, J.
History
DepositionDec 28, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 23, 2017Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 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 / struct_ncs_dom_lim
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.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.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 / _struct_conn.ptnr2_label_seq_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Lactate racemization operon protein LarE
B: Lactate racemization operon protein LarE
C: Lactate racemization operon protein LarE
D: Lactate racemization operon protein LarE
E: Lactate racemization operon protein LarE
F: Lactate racemization operon protein LarE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)191,56920
Polymers190,3136
Non-polymers1,25614
Water2,378132
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16550 Å2
ΔGint-205 kcal/mol
Surface area63220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.949, 107.949, 320.406
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 and (name N...
21(chain B and ((resid 2 through 3 and (name N...
31(chain C and ((resid 2 through 3 and (name N...
41(chain D and (resid 2 through 18 or (resid 20...
51(chain E and ((resid 2 through 3 and (name N...
61(chain F and ((resid 2 through 3 and (name N...

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 and (name N...AA2 - 32 - 3
12ALAALAALAALA(chain A and ((resid 2 through 3 and (name N...AA2 - 2762 - 276
13ALAALAALAALA(chain A and ((resid 2 through 3 and (name N...AA2 - 2762 - 276
14ALAALAALAALA(chain A and ((resid 2 through 3 and (name N...AA2 - 2762 - 276
15ALAALAALAALA(chain A and ((resid 2 through 3 and (name N...AA2 - 2762 - 276
21ALAALATHRTHR(chain B and ((resid 2 through 3 and (name N...BB2 - 32 - 3
22ALAALAARGARG(chain B and ((resid 2 through 3 and (name N...BB2 - 2592 - 259
23ALAALAARGARG(chain B and ((resid 2 through 3 and (name N...BB2 - 2592 - 259
24ALAALAARGARG(chain B and ((resid 2 through 3 and (name N...BB2 - 2592 - 259
25ALAALAARGARG(chain B and ((resid 2 through 3 and (name N...BB2 - 2592 - 259
31ALAALATHRTHR(chain C and ((resid 2 through 3 and (name N...CC2 - 32 - 3
32ALAALAARGARG(chain C and ((resid 2 through 3 and (name N...CC2 - 2592 - 259
33ALAALAARGARG(chain C and ((resid 2 through 3 and (name N...CC2 - 2592 - 259
34ALAALAARGARG(chain C and ((resid 2 through 3 and (name N...CC2 - 2592 - 259
35ALAALAARGARG(chain C and ((resid 2 through 3 and (name N...CC2 - 2592 - 259
41ALAALALEULEU(chain D and (resid 2 through 18 or (resid 20...DD2 - 182 - 18
42ARGARGVALVAL(chain D and (resid 2 through 18 or (resid 20...DD20 - 2120 - 21
43ALAALAARGARG(chain D and (resid 2 through 18 or (resid 20...DD2 - 2592 - 259
44ALAALAARGARG(chain D and (resid 2 through 18 or (resid 20...DD2 - 2592 - 259
45ALAALAARGARG(chain D and (resid 2 through 18 or (resid 20...DD2 - 2592 - 259
46ALAALAARGARG(chain D and (resid 2 through 18 or (resid 20...DD2 - 2592 - 259
51ALAALATHRTHR(chain E and ((resid 2 through 3 and (name N...EE2 - 32 - 3
52ALAALASERSER(chain E and ((resid 2 through 3 and (name N...EE2 - 2802 - 280
53ALAALASERSER(chain E and ((resid 2 through 3 and (name N...EE2 - 2802 - 280
54ALAALASERSER(chain E and ((resid 2 through 3 and (name N...EE2 - 2802 - 280
55ALAALASERSER(chain E and ((resid 2 through 3 and (name N...EE2 - 2802 - 280
61ALAALATHRTHR(chain F and ((resid 2 through 3 and (name N...FF2 - 32 - 3
62ALAALASERSER(chain F and ((resid 2 through 3 and (name N...FF2 - 2602 - 260
63ALAALASERSER(chain F and ((resid 2 through 3 and (name N...FF2 - 2602 - 260
64ALAALASERSER(chain F and ((resid 2 through 3 and (name N...FF2 - 2602 - 260
65ALAALASERSER(chain F and ((resid 2 through 3 and (name N...FF2 - 2602 - 260

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Components

#1: Protein
Lactate racemization operon protein LarE


Mass: 31718.766 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (bacteria)
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1 / Gene: larE, lp_0109 / Plasmid: pGIR076 / Production host: Escherichia coli (E. coli) / Strain (production host): Arctic express DE3 / References: UniProt: F9UST4
#2: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mn
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 132 / 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: 2.45 Å3/Da / Density % sol: 49.84 % / Mosaicity: 0.16 °
Crystal growTemperature: 294.15 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 5 ul ~24 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) mixed with 5 ul of reservoir solution. Hanging drop reservoir contained 100 ul of 25.0% v/v pentaerythritol ethoxylate (15/4 EO/OH), ...Details: 5 ul ~24 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) mixed with 5 ul of reservoir solution. Hanging drop reservoir contained 100 ul of 25.0% v/v pentaerythritol ethoxylate (15/4 EO/OH), 50 mM HEPES pH 7.0, 50 mM ammonium sulfate. Crystal soaked 5 minutes in 30.0% v/v pentaerythritol ethoxylate (15/4 EO/OH), 50 mM BIS-TRIS pH 5.5, 50 mM ammonium sulfate, 38 mM manganese sulfate.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.9786 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 19, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 2.79→48.28 Å / Num. obs: 47833 / % possible obs: 99.5 % / Redundancy: 8 % / Biso Wilson estimate: 56.2 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.123 / Rpim(I) all: 0.046 / Rrim(I) all: 0.131 / Net I/σ(I): 16.2 / Num. measured all: 381207 / Scaling rejects: 0
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
2.79-2.8980.9360.684196.9
10.81-48.285.90.0330.999196.4

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.35 Å48.28 Å
Translation8.35 Å48.28 Å

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Processing

Software
NameVersionClassification
Aimless0.5.25data scaling
PHENIX1.11.1-2575refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASER2.6.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UDQ

5udq


Resolution: 2.792→48.276 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.92 / Phase error: 25.45
RfactorNum. reflection% reflection
Rfree0.2495 4429 4.96 %
Rwork0.1945 --
obs0.1973 44655 99.41 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 174.62 Å2 / Biso mean: 62.7776 Å2 / Biso min: 17.97 Å2
Refinement stepCycle: final / Resolution: 2.792→48.276 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11547 0 62 134 11743
Biso mean--61.87 45.46 -
Num. residues----1516
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00711834
X-RAY DIFFRACTIONf_angle_d0.89616045
X-RAY DIFFRACTIONf_chiral_restr0.0591870
X-RAY DIFFRACTIONf_plane_restr0.0072076
X-RAY DIFFRACTIONf_dihedral_angle_d15.4274149
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6129X-RAY DIFFRACTION11.868TORSIONAL
12B6129X-RAY DIFFRACTION11.868TORSIONAL
13C6129X-RAY DIFFRACTION11.868TORSIONAL
14D6129X-RAY DIFFRACTION11.868TORSIONAL
15E6129X-RAY DIFFRACTION11.868TORSIONAL
16F6129X-RAY DIFFRACTION11.868TORSIONAL
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 (%)
2.7923-2.8240.39891700.35012564273490
2.824-2.85730.41421460.327128352981100
2.8573-2.89210.36471430.313728442987100
2.8921-2.92870.36311260.277229023028100
2.9287-2.96720.33381450.277328122957100
2.9672-3.00790.33271500.263928452995100
3.0079-3.05080.36691250.256328923017100
3.0508-3.09640.32721490.259628312980100
3.0964-3.14480.3721190.268828482967100
3.1448-3.19630.38441290.263328783007100
3.1963-3.25140.29241590.263328583017100
3.2514-3.31050.33181590.246928162975100
3.3105-3.37420.28321730.215528473020100
3.3742-3.4430.27471790.210127782957100
3.443-3.51790.27151570.198128292986100
3.5179-3.59970.27551320.197128993031100
3.5997-3.68970.25271460.191627942940100
3.6897-3.78940.28581390.196228532992100
3.7894-3.90080.27791340.177228733007100
3.9008-4.02670.21291480.1628643012100
4.0267-4.17050.20241390.157428322971100
4.1705-4.33740.2131610.146628262987100
4.3374-4.53470.19121300.14428292959100
4.5347-4.77360.17211710.146928333004100
4.7736-5.07230.19531730.14228042977100
5.0723-5.46350.20071370.15542833297099
5.4635-6.01240.24271270.17882861298899
6.0124-6.88020.24971580.19352804296299
6.8802-8.66020.1831550.17932819297499
8.6602-48.28350.21291500.18652778292897
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)
13.20110.4272-0.15044.635-0.54022.6279-0.11350.33260.29651.40920.60250.17-0.188-0.1389-0.53580.7150.2962-0.09730.6206-0.04080.33119.1441-3.0696-16.7635
20.09970.6114-0.47255.9179-2.40030.793-0.3379-0.0053-0.0140.90370.6582-0.9468-0.19230.0806-0.33050.66610.1534-0.20010.7098-0.23710.53924.5235-7.6565-18.7532
35.4839-1.55561.40743.6639-0.49194.05160.07990.4884-0.0095-0.2373-0.095-0.16010.03790.2809-0.00610.34320.0632-0.03750.3368-0.01520.322.2499-31.012-3.1843
41.09760.2231-0.25364.072-4.19426.21850.1893-0.01150.2660.3287-0.1622-0.2476-0.67210.1305-0.04930.4144-0.04090.08460.3201-0.05940.48319.42.258822.1536
58.99540.3009-1.05244.8529-6.53229.08920.2405-0.5490.31440.28960.51250.0865-0.5229-1.054-0.53640.45280.05310.03730.493-0.02220.3528-1.2343-0.178828.8933
67.44372.2577-0.45872.69210.95425.6440.2390.5338-0.235-0.2776-0.28370.29650.1308-0.68090.04760.72370.05050.09450.36710.10850.59175.44711.569311.9052
70.61892.3584-0.99368.2545-5.25955.94320.0791-0.1140.1491-0.70410.166-0.24010.32290.029-0.10350.36120.00420.04010.3126-0.05730.439410.3682-12.524824.5614
84.76370.0988-1.5394.32793.14157.10410.0094-0.1763-0.1922-0.1865-0.10820.07430.00090.00390.12960.2275-0.0177-0.04620.18370.00890.332117.2201-25.483828.2875
96.2439-1.047-0.23923.4546-1.88982.56290.20790.2103-0.4075-0.42190.10350.4530.2106-0.2019-0.27970.80380.02990.01170.3801-0.02220.513441.61437.38957.755
102.1905-4.47170.41879.2502-0.94030.9765-0.1979-0.42060.34790.3270.3166-0.3267-0.1877-0.2176-0.13250.4445-0.03530.02870.5577-0.03530.523147.94930.757616.9026
111.03791.0258-1.51553.0208-0.59853.73380.0192-0.04560.03-0.15270.0264-0.0688-0.1023-0.1546-0.04430.31760.0396-0.08910.30170.00730.429944.5155-25.771512.9223
122.5159-4.0705-0.62526.1601-0.19182.08920.0215-0.1081-0.0305-0.35960.0108-0.09580.67950.1434-0.01860.7974-0.08140.06810.3505-0.04780.513413.0572-70.495532.6173
131.8053-2.3891-0.89374.22080.222.4434-0.1107-0.16110.02450.10540.1791-0.2470.73880.1929-0.07370.7064-0.1068-0.03430.4213-0.0650.505515.8809-65.082536.175
146.96680.7364-0.80693.75340.58523.792-0.06220.0916-0.3366-0.32280.0686-0.04480.3075-0.1575-0.01020.3608-0.0388-0.01140.1758-0.0040.336611.6423-42.444423.1428
151.56331.30880.53716.85012.03161.66690.24330.0375-0.49190.7431-0.1572-0.47840.79770.2393-0.08970.72470.1021-0.09380.4896-0.02680.592654.3256-66.40127.097
160.05650.02470.08443.56862.13631.74050.03130.4035-0.2160.2827-0.0228-0.12250.50660.24230.00380.47370.053-0.0580.526-0.07760.621450.5632-62.549419.6666
174.4173-0.529-2.32375.7461-1.47152.8144-0.0654-0.28080.28620.0750.09450.02290.30370.2338-0.01590.33660.0095-0.09350.3773-0.00690.286641.9674-39.627626.7997
185.7102-1.5543-1.7173.9606-0.09737.82570.04361.0809-0.2923-0.9785-0.3115-0.26520.17780.8650.25760.57380.02570.04720.66310.03080.609248.2148-38.909112.5151
191.35260.10930.2644.8966-1.65712.5426-0.12920.13610.0213-0.1915-0.03380.04810.08370.00160.17420.56540.0713-0.13270.3024-0.1390.459925.5679-75.6779-4.6966
207.8854-1.5072-2.43286.6139-0.05134.24460.48670.4176-0.055-0.1707-0.06210.6532-0.2694-0.9186-0.32240.59370.0602-0.06350.2432-0.03450.513716.2489-78.69932.6862
210.5995-1.32731.00139.0308-7.0985.88470.10970.002-0.13730.40220.17780.4149-0.57920.0796-0.24070.5390.0067-0.15060.416-0.09960.445524.5955-61.5846-2.4571
224.229-1.9771-0.48484.7421-1.12932.9717-0.15730.0725-0.22350.06660.2104-0.17150.3534-0.0678-0.04240.38080.0214-0.06250.2648-0.05530.315929.2678-45.6952-2.0148
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 276 )A190 - 276
4X-RAY DIFFRACTION4chain 'B' and (resid 2 through 95 )B2 - 95
5X-RAY DIFFRACTION5chain 'B' and (resid 96 through 114 )B96 - 114
6X-RAY DIFFRACTION6chain 'B' and (resid 115 through 164 )B115 - 164
7X-RAY DIFFRACTION7chain 'B' and (resid 165 through 189 )B165 - 189
8X-RAY DIFFRACTION8chain 'B' and (resid 190 through 259 )B190 - 259
9X-RAY DIFFRACTION9chain 'C' and (resid 2 through 81 )C2 - 81
10X-RAY DIFFRACTION10chain 'C' and (resid 82 through 189 )C82 - 189
11X-RAY DIFFRACTION11chain 'C' and (resid 190 through 259 )C190 - 259
12X-RAY DIFFRACTION12chain 'D' and (resid 2 through 95 )D2 - 95
13X-RAY DIFFRACTION13chain 'D' and (resid 96 through 189 )D96 - 189
14X-RAY DIFFRACTION14chain 'D' and (resid 190 through 259 )D190 - 259
15X-RAY DIFFRACTION15chain 'E' and (resid 2 through 115 )E2 - 115
16X-RAY DIFFRACTION16chain 'E' and (resid 116 through 189 )E116 - 189
17X-RAY DIFFRACTION17chain 'E' and (resid 190 through 245 )E190 - 245
18X-RAY DIFFRACTION18chain 'E' and (resid 246 through 280 )E246 - 280
19X-RAY DIFFRACTION19chain 'F' and (resid 2 through 115 )F2 - 115
20X-RAY DIFFRACTION20chain 'F' and (resid 116 through 164 )F116 - 164
21X-RAY DIFFRACTION21chain 'F' and (resid 165 through 189 )F165 - 189
22X-RAY DIFFRACTION22chain 'F' and (resid 190 through 260 )F190 - 260

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