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- PDB-7ayn: Crystal structure of the lectin domain of the FimH variant Arg98A... -

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Basic information

Entry
Database: PDB / ID: 7ayn
TitleCrystal structure of the lectin domain of the FimH variant Arg98Ala, in complex with Methyl 3-chloro-4-D-mannopyranosyloxy-3-biphenylcarboxylate
ComponentsType 1 fimbrin D-mannose specific adhesin
KeywordsCELL ADHESION / adhesin / FimH / UPEC / bladder infection / carbohydrate / lectin
Function / homology
Function and homology information


pilus tip / mechanosensory behavior / cell adhesion involved in single-species biofilm formation / pilus / cell-substrate adhesion / D-mannose binding / host cell membrane / cell adhesion
Similarity search - Function
FimH, mannose-binding domain / FimH, mannose binding / Fimbrial-type adhesion domain / Fimbrial protein / : / Fimbrial-type adhesion domain superfamily / Adhesion domain superfamily
Similarity search - Domain/homology
Chem-SBQ / Type 1 fimbrin D-mannose specific adhesin
Similarity search - Component
Biological speciesEscherichia coli K12 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.42 Å
AuthorsJakob, R.P. / Tomasic, T. / Rabbani, S. / Reisner, A. / Jakopin, Z. / Maier, T. / Ernst, B. / Anderluh, M.
CitationJournal: Eur.J.Med.Chem. / Year: 2020
Title: Does targeting Arg98 of FimH lead to high affinity antagonists?
Authors: Tomasic, T. / Rabbani, S. / Jakob, R.P. / Reisner, A. / Jakopin, Z. / Maier, T. / Ernst, B. / Anderluh, M.
History
DepositionNov 12, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 23, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 30, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID
Revision 1.2Jan 31, 2024Group: 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
Revision 1.3Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Type 1 fimbrin D-mannose specific adhesin
B: Type 1 fimbrin D-mannose specific adhesin
C: Type 1 fimbrin D-mannose specific adhesin
D: Type 1 fimbrin D-mannose specific adhesin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,27012
Polymers67,3234
Non-polymers1,9488
Water17,222956
1
A: Type 1 fimbrin D-mannose specific adhesin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,3804
Polymers16,8311
Non-polymers5493
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Type 1 fimbrin D-mannose specific adhesin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,3183
Polymers16,8311
Non-polymers4872
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Type 1 fimbrin D-mannose specific adhesin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,2562
Polymers16,8311
Non-polymers4251
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Type 1 fimbrin D-mannose specific adhesin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,3183
Polymers16,8311
Non-polymers4872
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)54.652, 32.926, 177.442
Angle α, β, γ (deg.)90.000, 96.560, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 1 through 16 or resid 18...
21(chain B and (resid 1 through 16 or resid 18...
31(chain C and (resid 1 through 16 or resid 18...
41(chain D and (resid 1 through 16 or resid 18...

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
11PHEPHEGLYGLY(chain A and (resid 1 through 16 or resid 18...AA1 - 161 - 16
12ALAALALEULEU(chain A and (resid 1 through 16 or resid 18...AA18 - 6818 - 68
13PHEPHESBQSBQ(chain A and (resid 1 through 16 or resid 18...AA - E1 - 3011
14TYRTYRASPASP(chain A and (resid 1 through 16 or resid 18...AA82 - 10082 - 100
15PROPROASNASN(chain A and (resid 1 through 16 or resid 18...AA102 - 138102 - 138
16ASPASPTHRTHR(chain A and (resid 1 through 16 or resid 18...AA140 - 158140 - 158
21PHEPHEGLYGLY(chain B and (resid 1 through 16 or resid 18...BB1 - 161 - 16
22ALAALALEULEU(chain B and (resid 1 through 16 or resid 18...BB18 - 6818 - 68
23ASNASNSERSER(chain B and (resid 1 through 16 or resid 18...BB70 - 8070 - 80
24PROPROASNASN(chain B and (resid 1 through 16 or resid 18...BB102 - 138102 - 138
25ASPASPTHRTHR(chain B and (resid 1 through 16 or resid 18...BB140 - 158140 - 158
31PHEPHEGLYGLY(chain C and (resid 1 through 16 or resid 18...CC1 - 161 - 16
32ALAALALEULEU(chain C and (resid 1 through 16 or resid 18...CC18 - 6818 - 68
33ASNASNSERSER(chain C and (resid 1 through 16 or resid 18...CC70 - 8070 - 80
34PROPROASNASN(chain C and (resid 1 through 16 or resid 18...CC102 - 138102 - 138
35ASPASPTHRTHR(chain C and (resid 1 through 16 or resid 18...CC140 - 158140 - 158
41PHEPHEGLYGLY(chain D and (resid 1 through 16 or resid 18...DD1 - 161 - 16
42ALAALALEULEU(chain D and (resid 1 through 16 or resid 18...DD18 - 6818 - 68
43ASNASNSERSER(chain D and (resid 1 through 16 or resid 18...DD70 - 8070 - 80
44PROPROASNASN(chain D and (resid 1 through 16 or resid 18...DD102 - 138102 - 138
45ASPASPTHRTHR(chain D and (resid 1 through 16 or resid 18...DD140 - 158140 - 158

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Components

#1: Protein
Type 1 fimbrin D-mannose specific adhesin / Protein FimH


Mass: 16830.711 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K12 (bacteria) / Gene: fimH, b4320, JW4283 / Plasmid: pTRC99a / Production host: Escherichia coli (E. coli) / Strain (production host): HM125 / References: UniProt: P08191
#2: Chemical
ChemComp-SBQ / methyl 3-[3-chloranyl-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-phenyl]benzoate


Mass: 424.829 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H21ClO8 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 956 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.36 Å3/Da / Density % sol: 47.79 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 6% Tacsimate pH 6.0, 12% PEG3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00004 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 13, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00004 Å / Relative weight: 1
ReflectionResolution: 1.42→50.298 Å / Num. obs: 118005 / % possible obs: 98.5 % / Redundancy: 6.7 % / CC1/2: 0.997 / Rpim(I) all: 0.061 / Net I/σ(I): 7.5
Reflection shellResolution: 1.42→1.47 Å / Redundancy: 6.7 % / Mean I/σ(I) obs: 1.1 / Num. unique obs: 11668 / CC1/2: 0.401 / Rpim(I) all: 1.606 / % possible all: 99.5

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Processing

Software
NameVersionClassification
PHENIX1.12rc1_2801refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4X50

4x50


Resolution: 1.42→50.298 Å / SU ML: 0.14 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 20.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.184 1988 1.68 %
Rwork0.1589 116017 -
obs0.1593 118005 98.55 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 102.82 Å2 / Biso mean: 27.2998 Å2 / Biso min: 7.84 Å2
Refinement stepCycle: final / Resolution: 1.42→50.298 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4756 0 240 959 5955
Biso mean--22.78 41.71 -
Num. residues----632
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0115046
X-RAY DIFFRACTIONf_angle_d1.1356949
X-RAY DIFFRACTIONf_chiral_restr0.087814
X-RAY DIFFRACTIONf_plane_restr0.009951
X-RAY DIFFRACTIONf_dihedral_angle_d12.0871797
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3532X-RAY DIFFRACTION5.952TORSIONAL
12B3532X-RAY DIFFRACTION5.952TORSIONAL
13C3532X-RAY DIFFRACTION5.952TORSIONAL
14D3532X-RAY DIFFRACTION5.952TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.42-1.45550.29611390.3048818699
1.4555-1.49490.291390.2681825598
1.4949-1.53890.25541400.2397810899
1.5389-1.58850.2341390.2157822798
1.5885-1.64530.26761490.2026821498
1.6453-1.71120.23471350.1976809897
1.7112-1.78910.24431410.182825299
1.7891-1.88340.2061440.1707832599
1.8834-2.00140.18041420.1529830199
2.0014-2.15590.15911410.1457830099
2.1559-2.37290.16441380.1416826597
2.3729-2.71620.17991470.14588377100
2.7162-3.42210.16551440.13578500100
3.4221-50.2980.15321500.14860998
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)
11.464-0.69860.1851.6288-0.0891.76140-0.1063-0.16510.1340.05870.17780.0401-0.2694-0.04510.1158-0.00450.00270.10010.01980.1438-15.2922-2.65476.9533
20.9919-0.40810.82050.4867-0.63631.4932-0.0253-0.1303-0.0278-0.00050.05280.0048-0.1121-0.19540.0180.1359-0.0011-0.00170.09810.00120.11-27.5944-2.652-8.8637
31.77280.19732.85140.26630.99856.4334-0.1436-0.17580.0889-0.10030.03910.0288-0.2745-0.35590.02780.16380.0141-0.0060.20240.0090.1594-24.81014.0212-8.2411
44.73660.78451.35680.81220.12961.81690.0837-0.2948-0.01360.0877-0.023-0.032-0.1059-0.0304-0.01950.11120.00310.00170.0775-0.00760.1105-9.21856.1858.626
51.84730.44311.15890.55730.20.9250.00020.128-0.0856-0.02320.0174-0.03170.00790.04590.00720.1051-0.00550.00850.10430.00710.0992-15.483-1.4017-11.5267
60.71720.13960.86821.3170.22712.3611-0.04410.1120.0669-0.13330.0582-0.0394-0.16320.1025-0.00550.1281-0.01050.00550.11550.00810.1112-10.09155.1298-10.0665
71.32790.2280.82240.05790.362.3433-0.0315-0.1020.1785-0.114-0.0084-0.0194-0.2525-0.09160.0920.13580.0102-0.00140.0938-0.00710.1327-14.15548.13734.5667
82.9140.97761.41951.98580.82623.6623-0.10430.0023-0.2025-0.2065-0.00880.03030.0032-0.25060.08620.14620.00020.00860.1315-0.00790.1355-25.04480.158-18.453
92.5401-0.57671.77022.0144-2.07835.14430.04670.1217-0.1954-0.0877-0.0003-0.05120.271-0.1388-0.00130.1327-0.00940.00780.1288-0.00130.1489-31.0962-9.9196-13.2681
101.40910.54250.5180.68140.27040.56870.03570.078-0.08460.03420.0174-0.05470.03640.0661-0.060.10780.0007-0.00310.06350.00410.1025-9.2069-3.0029-0.8947
111.6982-0.2043-0.19423.0155-1.03054.2074-0.0977-0.0712-0.0349-0.1969-0.08650.15050.2258-0.4234-0.09640.1574-0.0153-0.02340.1490.00460.1533-34.8958-5.0437-14.9306
122.41050.4749-1.64772.13290.46592.90110.06690.1330.4066-0.11070.39340.7309-0.0657-0.514-0.34440.1470.00110.00550.19110.110.3155-15.3748-0.540721.5123
131.18040.448-0.32180.595-0.45491.51760.11860.08450.3981-0.07830.19090.22190.0774-0.404-0.27630.15510.01590.02410.22630.0320.2298-27.7901-4.708537.2209
141.55280.4198-0.88290.2043-0.52191.31340.0133-0.03660.0665-0.00590.02320.02250.1177-0.0818-0.00340.1614-0.01250.01350.146-0.00470.1466-12.9659-8.62225.0535
152.4479-0.0208-2.02140.7318-0.07461.87580.3167-0.5830.36170.1106-0.10180.0864-0.27390.3772-0.15240.2016-0.05650.04260.2999-0.06170.1752-15.1004-3.12739.5992
160.43310.2371-0.59560.9362-0.0062.66050.1673-0.50360.14170.228-0.063-0.0511-0.02160.5767-0.13360.2533-0.0484-0.00290.3443-0.00490.1457-8.5587-8.443738.0003
171.16990.4219-1.03870.39810.15282.1896-0.1049-0.0135-0.15060.00990.0245-0.05480.0718-0.13590.05960.17530.00140.01120.1561-0.00550.1449-11.7389-11.198423.3404
182.2778-0.2888-2.08451.1260.60383.40480.0094-0.40810.12080.2061-0.08590.22450.1566-0.11680.09060.1735-0.03980.03040.3586-0.05290.157-24.433-6.909746.3272
190.50550.3591-0.78450.343-0.27652.1160.38830.06690.537-0.11490.08930.1894-0.3241-0.2527-0.42850.23230.00580.21860.22190.06040.7068-32.58921.602741.3679
203.2580.1521-1.94441.3132-0.51052.63960.2715-0.43570.36050.14460.01890.1178-0.28770.2797-0.27470.1734-0.0280.0350.1387-0.02650.1473-9.3430.575329.3767
213.47771.1606-1.12394.3467-2.54755.81230.36030.1140.90960.27040.16110.5413-0.5735-0.4644-0.50280.21590.02870.10370.26270.03930.4212-35.0564-3.961242.6772
224.7336-0.7366-0.96274.7002-0.2491.6331-0.1831-0.23360.20460.46120.3302-0.52770.20360.1493-0.05050.18930.0361-0.04650.2717-0.05180.1788-8.2927-16.052263.5764
233.8160.6969-0.98840.4211-0.00060.8851-0.10170.0437-0.2481-0.00430.0413-0.08350.052-0.03720.07220.1532-0.01370.00570.2457-0.00590.1563-1.8908-21.347256.2236
243.15590.5681-1.03080.7159-0.3791.947-0.14240.4633-0.16-0.09150.1296-0.0580.1283-0.16050.01720.1744-0.03820.00590.3181-0.03980.1697-2.436-23.666549.8164
253.14150.2558-0.86250.5407-0.30271.4282-0.06340.25290.0448-0.01490.078-0.0252-0.0347-0.05850.00560.1192-0.019-0.00110.2229-0.01830.09862.4135-16.996552.7944
260.89530.7122-0.10581.96360.66561.85780.0095-0.0264-0.11360.02550.1384-0.15010.1815-0.1724-0.13980.18720.005-0.01370.3179-0.00550.1405-16.513-18.267375.8583
270.35640.0470.04480.17750.4711.17280.03710.02730.0755-0.03740.0777-0.0233-0.04010.1603-0.1390.2275-0.00570.00810.2676-0.00690.1533-14.5669-17.855696.5883
280.8568-0.38450.55930.39660.18872.57850.04890.08520.08340.02720.0640.0418-0.14890.1247-0.05430.2222-0.009-0.00940.30760.01910.1666-19.2243-10.194378.8658
290.2416-0.43260.72870.8113-1.23582.37690.0166-0.064-0.0389-0.07880.04010.10150.1454-0.6645-0.00160.23350.00230.01180.42740.00590.1686-26.4679-16.616491.1561
300.59080.1299-0.48870.7448-0.03132.11680.0363-0.02990.09080.19730.16790.3547-0.4203-0.9159-0.09940.28870.07440.04390.54330.00170.2034-30.007-10.057687.0616
310.64940.099-0.03950.02-0.05891.4215-0.01610.18240.18920.0012-0.02170.1187-0.2589-0.24770.09870.24910.0348-0.00380.28320.01640.1804-18.6194-7.443977.0608
321.5345-0.24840.52271.9408-1.45784.34460.117-0.1936-0.14250.1625-0.00940.2251-0.0011-0.20280.05410.2489-0.00290.01570.3705-0.00730.1628-22.1486-15.3365102.3039
331.0888-0.5271-0.58861.36152.00693.6315-0.0184-0.0964-0.24070.1794-0.00430.11490.4342-0.06230.04920.2536-0.02460.01620.31220.00430.1741-14.3411-25.5376101.3211
340.8762-0.37670.82760.8956-0.60522.3650.0001-0.00410.0033-0.00170.05540.09010.1314-0.5631-0.08320.1835-0.01380.00370.36260.00330.1233-25.7993-18.53279.2451
353.3597-0.4206-1.20673.29131.81614.4099-0.1086-0.2675-0.22620.30720.10330.00610.15950.001-0.11060.25660.0250.00530.28730.0140.1484-12.1367-20.6289104.8068
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 15 )A1 - 15
2X-RAY DIFFRACTION2chain 'A' and (resid 16 through 32 )A16 - 32
3X-RAY DIFFRACTION3chain 'A' and (resid 33 through 40 )A33 - 40
4X-RAY DIFFRACTION4chain 'A' and (resid 41 through 53 )A41 - 53
5X-RAY DIFFRACTION5chain 'A' and (resid 54 through 77 )A54 - 77
6X-RAY DIFFRACTION6chain 'A' and (resid 78 through 95 )A78 - 95
7X-RAY DIFFRACTION7chain 'A' and (resid 96 through 104 )A96 - 104
8X-RAY DIFFRACTION8chain 'A' and (resid 105 through 116 )A105 - 116
9X-RAY DIFFRACTION9chain 'A' and (resid 117 through 124 )A117 - 124
10X-RAY DIFFRACTION10chain 'A' and (resid 125 through 150 )A125 - 150
11X-RAY DIFFRACTION11chain 'A' and (resid 151 through 158 )A151 - 158
12X-RAY DIFFRACTION12chain 'B' and (resid 1 through 15 )B1 - 15
13X-RAY DIFFRACTION13chain 'B' and (resid 16 through 32 )B16 - 32
14X-RAY DIFFRACTION14chain 'B' and (resid 33 through 53 )B33 - 53
15X-RAY DIFFRACTION15chain 'B' and (resid 54 through 77 )B54 - 77
16X-RAY DIFFRACTION16chain 'B' and (resid 78 through 95 )B78 - 95
17X-RAY DIFFRACTION17chain 'B' and (resid 96 through 104 )B96 - 104
18X-RAY DIFFRACTION18chain 'B' and (resid 105 through 116 )B105 - 116
19X-RAY DIFFRACTION19chain 'B' and (resid 117 through 124 )B117 - 124
20X-RAY DIFFRACTION20chain 'B' and (resid 125 through 150 )B125 - 150
21X-RAY DIFFRACTION21chain 'B' and (resid 151 through 158 )B151 - 158
22X-RAY DIFFRACTION22chain 'C' and (resid 1 through 15 )C1 - 15
23X-RAY DIFFRACTION23chain 'C' and (resid 16 through 64 )C16 - 64
24X-RAY DIFFRACTION24chain 'C' and (resid 65 through 104 )C65 - 104
25X-RAY DIFFRACTION25chain 'C' and (resid 105 through 158 )C105 - 158
26X-RAY DIFFRACTION26chain 'D' and (resid 1 through 15 )D1 - 15
27X-RAY DIFFRACTION27chain 'D' and (resid 16 through 32 )D16 - 32
28X-RAY DIFFRACTION28chain 'D' and (resid 33 through 53 )D33 - 53
29X-RAY DIFFRACTION29chain 'D' and (resid 54 through 77 )D54 - 77
30X-RAY DIFFRACTION30chain 'D' and (resid 78 through 95 )D78 - 95
31X-RAY DIFFRACTION31chain 'D' and (resid 96 through 104 )D96 - 104
32X-RAY DIFFRACTION32chain 'D' and (resid 105 through 116 )D105 - 116
33X-RAY DIFFRACTION33chain 'D' and (resid 117 through 124 )D117 - 124
34X-RAY DIFFRACTION34chain 'D' and (resid 125 through 150 )D125 - 150
35X-RAY DIFFRACTION35chain 'D' and (resid 151 through 158 )D151 - 158

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