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- PDB-6c72: Crystal structure of a tailspike protein gp49 from Acinetobacter ... -

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Basic information

Entry
Database: PDB / ID: 6c72
TitleCrystal structure of a tailspike protein gp49 from Acinetobacter baumannii bacteriophage Fri1, a capsular polysaccharide depolymerase
ComponentsParticle-associated glycoside hydrolase
KeywordsHYDROLASE / glycosidase / Fri1 / tailspike / Acinetobacter baumannii
Function / homologysymbiont entry into host cell via disruption of host cell glycocalyx / symbiont entry into host cell via disruption of host cell envelope / virus tail / Pectin lyase fold / Pectin lyase fold/virulence factor / metal ion binding / Tail spike protein
Function and homology information
Biological speciesAcinetobacter phage Fri1 (virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.396 Å
AuthorsButh, S.A. / Garcon, A. / Popova, A.V. / Shneider, M.M. / Leiman, P.G.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
SNF310030_144243 Switzerland
CitationJournal: To Be Published
Title: Exopolysaccharide degrading enzymes - specificity determinants of Acinetobacter baumannii phages
Authors: Buth, S.A. / Shneider, M.M. / Popova, A.V. / Shashkov, A.S. / Senchenkova, S.N. / Knirel, Y. / Leiman, P.G.
History
DepositionJan 19, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2019Provider: repository / Type: Initial release
Revision 1.1Mar 13, 2024Group: 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_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.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_alt_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _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.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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_symmetry / _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 1.2Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Particle-associated glycoside hydrolase
B: Particle-associated glycoside hydrolase
C: Particle-associated glycoside hydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)198,15643
Polymers195,5403
Non-polymers2,61640
Water28,5001582
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23830 Å2
ΔGint-1049 kcal/mol
Surface area58710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)73.462, 98.664, 148.704
Angle α, β, γ (deg.)90.000, 91.810, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 204 through 235 or resid 237...
21(chain B and (resid 204 through 235 or resid 237...
31(chain C and (resid 204 through 235 or resid 237...

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
11SERSERGLYGLY(chain A and (resid 204 through 235 or resid 237...AA204 - 23518 - 49
12GLYGLYHISHIS(chain A and (resid 204 through 235 or resid 237...AA237 - 27251 - 86
13LYSLYSLEULEU(chain A and (resid 204 through 235 or resid 237...AA274 - 28388 - 97
14ALAALAALAALA(chain A and (resid 204 through 235 or resid 237...AA28599
15LEULEUTYRTYR(chain A and (resid 204 through 235 or resid 237...AA287 - 361101 - 175
16HISHISALAALA(chain A and (resid 204 through 235 or resid 237...AA363 - 552177 - 366
17GLYGLYASNASN(chain A and (resid 204 through 235 or resid 237...AA554 - 612368 - 426
18PHEPHEPHEPHE(chain A and (resid 204 through 235 or resid 237...AA614 - 619428 - 433
19ASNASNPHEPHE(chain A and (resid 204 through 235 or resid 237...AA621 - 685435 - 499
110GLUGLUPROPRO(chain A and (resid 204 through 235 or resid 237...AA687 - 738501 - 552
111TYRTYRLEULEU(chain A and (resid 204 through 235 or resid 237...AA740 - 782554 - 596
21SERSERGLYGLY(chain B and (resid 204 through 235 or resid 237...BB204 - 23518 - 49
22GLYGLYHISHIS(chain B and (resid 204 through 235 or resid 237...BB237 - 27251 - 86
23LYSLYSLEULEU(chain B and (resid 204 through 235 or resid 237...BB274 - 28388 - 97
24ALAALAALAALA(chain B and (resid 204 through 235 or resid 237...BB28599
25LEULEUTYRTYR(chain B and (resid 204 through 235 or resid 237...BB287 - 361101 - 175
26HISHISALAALA(chain B and (resid 204 through 235 or resid 237...BB363 - 552177 - 366
27GLYGLYASNASN(chain B and (resid 204 through 235 or resid 237...BB554 - 612368 - 426
28PHEPHEPHEPHE(chain B and (resid 204 through 235 or resid 237...BB614 - 619428 - 433
29ASNASNPHEPHE(chain B and (resid 204 through 235 or resid 237...BB621 - 685435 - 499
210GLUGLUPROPRO(chain B and (resid 204 through 235 or resid 237...BB687 - 738501 - 552
211TYRTYRLEULEU(chain B and (resid 204 through 235 or resid 237...BB740 - 782554 - 596
31SERSERGLYGLY(chain C and (resid 204 through 235 or resid 237...CC204 - 23518 - 49
32GLYGLYHISHIS(chain C and (resid 204 through 235 or resid 237...CC237 - 27251 - 86
33LYSLYSLEULEU(chain C and (resid 204 through 235 or resid 237...CC274 - 28388 - 97
34ALAALAALAALA(chain C and (resid 204 through 235 or resid 237...CC28599
35LEULEUTYRTYR(chain C and (resid 204 through 235 or resid 237...CC287 - 361101 - 175
36HISHISALAALA(chain C and (resid 204 through 235 or resid 237...CC363 - 552177 - 366
37GLYGLYASNASN(chain C and (resid 204 through 235 or resid 237...CC554 - 612368 - 426
38PHEPHEPHEPHE(chain C and (resid 204 through 235 or resid 237...CC614 - 619428 - 433
39ASNASNPHEPHE(chain C and (resid 204 through 235 or resid 237...CC621 - 685435 - 499
310GLUGLUPROPRO(chain C and (resid 204 through 235 or resid 237...CC687 - 738501 - 552
311TYRTYRLEULEU(chain C and (resid 204 through 235 or resid 237...CC740 - 782554 - 596

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Components

#1: Protein Particle-associated glycoside hydrolase / Tail spike protein


Mass: 65179.918 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acinetobacter phage Fri1 (virus) / Gene: Fri1_49 / Plasmid: PTSL
Details (production host): PET-23a DERIVATIVE WITH SLYD LEADER
Production host: Escherichia coli (E. coli) / Strain (production host): B834/DE3 / References: UniProt: A0A0H4TJ34
#2: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 40 / Source method: obtained synthetically / Formula: Zn
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1582 / 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: 2.84 Å3/Da / Density % sol: 56.71 % / Description: thin plates
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 15% PEG 8000, 50 mM NaCl, 100 mM Tris HCl pH8.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9796 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 30, 2013
RadiationMonochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9796 Å / Relative weight: 1
ReflectionResolution: 2.396→49.332 Å / Num. all: 81953 / Num. obs: 81953 / % possible obs: 98.2 % / Redundancy: 4.7 % / Biso Wilson estimate: 30.82 Å2 / Rpim(I) all: 0.043 / Rrim(I) all: 0.095 / Rsym value: 0.075 / Net I/av σ(I): 8.8 / Net I/σ(I): 16 / Num. measured all: 388727
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsRpim(I) allRrim(I) allRsym value% possible all
2.4-2.534.70.4051.9112240.230.510.40592.5
2.53-2.684.80.2792.7113340.1560.3480.27998.9
2.68-2.864.60.1953.7106870.1110.2420.19599
2.86-3.0950.1364.999900.0730.1670.13699.2
3.09-3.394.90.0867.791600.0460.1050.08699.2
3.39-3.794.60.05711.383290.0320.0720.05799.4
3.79-4.374.90.04514.473840.0250.0570.04599.4
4.37-5.364.60.03716.462580.0220.0490.03799.5
5.36-7.584.80.04115.948760.0240.0550.04199.7
7.58-49.3324.50.02425.927110.0170.0370.02499.1

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å46.82 Å
Translation2.5 Å46.82 Å

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Processing

Software
NameVersionClassification
PDB_EXTRACT3.24data extraction
XDSMarch 30, 2013data reduction
SCALA3.3.20data scaling
PHENIX1.12_2829refinement
PHASER2.5.2phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: in house model

Resolution: 2.396→49.332 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.92 / Phase error: 21.52
RfactorNum. reflection% reflectionSelection details
Rfree0.2031 8051 5.01 %random selection
Rwork0.1545 ---
obs0.1569 160570 97.86 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 149.85 Å2 / Biso mean: 36.6404 Å2 / Biso min: 18.23 Å2
Refinement stepCycle: final / Resolution: 2.396→49.332 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13353 0 48 1582 14983
Biso mean--67.09 40.18 -
Num. residues----1737
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00613693
X-RAY DIFFRACTIONf_angle_d0.78818660
X-RAY DIFFRACTIONf_chiral_restr0.0532176
X-RAY DIFFRACTIONf_plane_restr0.0052403
X-RAY DIFFRACTIONf_dihedral_angle_d9.5217984
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A7851X-RAY DIFFRACTION6.643TORSIONAL
12B7851X-RAY DIFFRACTION6.643TORSIONAL
13C7851X-RAY DIFFRACTION6.643TORSIONAL
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 (%)
2.3957-2.42290.37772000.30623763396373
2.4229-2.45140.32482750.24495180545598
2.4514-2.48130.2682680.22425058532699
2.4813-2.51270.2662680.21855140540898
2.5127-2.54580.262680.2035088535699
2.5458-2.58060.22562650.1965090535599
2.5806-2.61750.24872720.20015215548798
2.6175-2.65660.23622700.19945070534099
2.6566-2.69810.23392690.19135094536398
2.6981-2.74230.27442740.19335189546399
2.7423-2.78960.24542700.1845073534399
2.7896-2.84030.21162720.18075144541699
2.8403-2.89490.27772690.18195098536799
2.8949-2.9540.23172740.17715141541599
2.954-3.01820.22652700.18465134540499
3.0182-3.08840.24662750.17445203547899
3.0884-3.16570.21052660.16785079534598
3.1657-3.25120.22272660.16245123538999
3.2512-3.34690.21722730.16445175544899
3.3469-3.45490.20292740.15465097537199
3.4549-3.57830.19482670.14055096536399
3.5783-3.72160.18242750.1315204547999
3.7216-3.89090.15772700.12265135540599
3.8909-4.09590.16852710.12365165543699
4.0959-4.35240.15112710.10565115538699
4.3524-4.68820.13892700.09925120539099
4.6882-5.15960.14542690.10685129539899
5.1596-5.90510.17962750.12375127540299
5.9051-7.43570.1832730.14615177545099
7.4357-49.34240.20192720.17745097536998
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)
13.5153-0.9015-1.54564.3516-0.36970.8237-0.3544-0.30110.00091.7607-0.19340.72780.9467-0.69990.22160.9261-0.08140.30010.4682-0.0740.584224.568755.1261147.2037
26.3038-2.1584-4.16532.26961.80577.8227-0.467-0.6180.36440.47030.09920.11020.16350.17490.36910.37950.01630.08570.3231-0.07990.48429.349262.0078143.2948
30.65741.46840.94353.22841.99432.85730.1404-0.14480.18460.1392-0.15160.2887-0.1339-0.25280.03680.30530.03140.1120.31060.00270.474830.555956.1577126.7703
40.384-0.11320.16152.1636-0.74720.6801-0.0117-0.1118-0.1685-0.03240.15650.39670.0777-0.1535-0.14810.2691-0.03350.03970.34270.00280.428536.666935.7064120.1034
50.6172-0.0954-0.0162.36960.15331.38490.0819-0.01040.11750.12360.02280.1412-0.0687-0.0856-0.09590.26150.01110.07930.26320.02730.377339.994655.635112.3578
61.01910.26750.25371.28091.00570.8148-0.00950.13030.1554-0.06790.07660.0349-0.026-0.064-0.07060.256-0.00820.03940.27290.03490.307346.049152.9609100.7186
72.7421-0.0004-0.3422.5858-0.27911.60470.05850.1511-0.0126-0.0405-0.01240.020.01150.0389-0.03940.2835-0.00010.01920.29740.00550.258255.782645.892290.6755
80.85040.7764-0.46710.9109-0.23450.30170.0592-0.06930.12210.1029-0.00830.03920.0276-0.0457-0.04120.30690.0044-0.00250.2808-0.00660.287386.533355.907677.4089
92.7688-0.90542.47551.6604-1.10833.6597-0.04970.02540.10460.0260.02330.0198-0.0537-0.00880.03570.25340.01810.05290.22460.00530.291996.102462.354263.5425
107.3963-1.36070.0112.4444-1.09883.55260.2984-0.3754-0.19420.62570.06150.32990.0949-0.8332-0.31740.6292-0.13190.20190.6274-0.10260.395642.087155.4271160.0624
114.337-0.1595-1.80673.4865-0.95567.7438-0.0879-0.7649-0.32040.71380.03720.07020.3819-0.15240.01020.5647-0.05240.11420.4810.00720.32849.459249.9962158.2675
121.30650.13560.21372.0213-0.53220.37980.0966-0.25160.18890.19530.02550.1855-0.2846-0.0021-0.12490.4501-0.04690.10050.3829-0.08030.291757.132261.1184146.1279
131.1391-0.36960.19820.60650.00221.4594-0.0886-0.20340.23810.10460.04610.114-0.3098-0.1831-0.00130.4068-0.01630.09790.2485-0.02270.422947.548270.1272127.9937
140.9826-0.1573-0.4310.663-0.32221.30790.0757-0.0510.12260.12850.0254-0.032-0.16340.1588-0.06070.3548-0.04660.05070.3163-0.05290.347467.149661.7611131.7992
150.4606-0.15260.07880.5083-0.6081.04240.0967-0.0360.17840.0623-0.0829-0.0686-0.09140.1003-0.04060.3078-0.03940.04760.3094-0.04450.385173.547664.7025120.3719
160.7480.06820.04120.8163-0.05551.49040.08410.03340.0804-0.0626-0.0158-0.1044-0.11670.1083-0.08260.316-0.04770.09160.2968-0.00020.404575.789366.5774104.8604
170.4021-0.1089-0.43350.02410.07020.58160.0443-0.10960.0526-0.02090.0341-0.05210.08450.0795-0.07030.38880.01990.04610.31510.02860.380491.986245.796380.9429
184.56052.24761.41732.13360.70371.57730.12690.0771-0.07490.16660.0029-0.28370.17150.1586-0.13440.31480.0698-0.01310.2535-0.00630.3186105.597442.111469.2289
196.85141.4022-0.79020.9533-0.55883.6032-0.022-0.97741.08310.4849-0.05780.5633-0.0403-0.36740.05070.65790.03850.30670.5686-0.07530.669432.740135.8258153.3044
206.09952.2866-1.13180.9482-0.58735.6297-0.15690.10870.52970.24180.27970.9411-0.1049-0.503-0.11720.3923-0.00130.1890.40840.06970.626630.494434.1722144.3572
212.1926-0.94941.45952.0761-0.88041.8946-0.0847-0.2645-0.03670.31210.04430.1664-0.0543-0.1368-0.00530.3011-0.01780.09490.34540.02070.320547.153729.996138.5833
221.54631.07540.89691.95920.92041.87080.0302-0.32280.00070.2614-0.09240.0668-0.060.05790.05430.29180.00660.00660.34080.01320.290666.313441.2857141.3591
231.29380.3353-0.28680.5792-0.03721.4693-0.0151-0.07940.00590.0464-0.03060.00280.04680.04390.02470.259-0.01050.03040.24980.00070.295357.904929.7031125.1063
241.35910.250.30160.3381-0.12961.088-0.0040.062-0.04850.0156-0.0262-0.02570.15610.20610.04160.26280.01820.01430.2661-0.00830.281868.106929.4614116.3917
250.52510.53230.1681.5470.38271.6898-0.00390.0214-0.0161-0.0635-0.0155-0.2020.04210.13560.02190.24750.03270.04310.30590.00470.345780.385734.9781108.2579
260.0864-0.02170.1231-0.01070.07191.0780.003-0.03290.0381-0.0442-0.00490.02880.0691-0.09170.02530.33510.00490.06050.3349-0.01040.368881.62845.292874.7371
272.2256-0.01430.83124.88690.26731.45980.02680.0463-0.14070.2347-0.02840.17480.11870.06390.01020.2625-0.01220.06930.23830.0130.254985.863942.721257.0979
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 204 through 239 )A204 - 239
2X-RAY DIFFRACTION2chain 'A' and (resid 240 through 281 )A240 - 281
3X-RAY DIFFRACTION3chain 'A' and (resid 282 through 334 )A282 - 334
4X-RAY DIFFRACTION4chain 'A' and (resid 335 through 375 )A335 - 375
5X-RAY DIFFRACTION5chain 'A' and (resid 376 through 475 )A376 - 475
6X-RAY DIFFRACTION6chain 'A' and (resid 476 through 543 )A476 - 543
7X-RAY DIFFRACTION7chain 'A' and (resid 544 through 636 )A544 - 636
8X-RAY DIFFRACTION8chain 'A' and (resid 637 through 694 )A637 - 694
9X-RAY DIFFRACTION9chain 'A' and (resid 695 through 782 )A695 - 782
10X-RAY DIFFRACTION10chain 'B' and (resid 204 through 239 )B204 - 239
11X-RAY DIFFRACTION11chain 'B' and (resid 240 through 281 )B240 - 281
12X-RAY DIFFRACTION12chain 'B' and (resid 282 through 334 )B282 - 334
13X-RAY DIFFRACTION13chain 'B' and (resid 335 through 375 )B335 - 375
14X-RAY DIFFRACTION14chain 'B' and (resid 376 through 475 )B376 - 475
15X-RAY DIFFRACTION15chain 'B' and (resid 476 through 543 )B476 - 543
16X-RAY DIFFRACTION16chain 'B' and (resid 544 through 636 )B544 - 636
17X-RAY DIFFRACTION17chain 'B' and (resid 637 through 694 )B637 - 694
18X-RAY DIFFRACTION18chain 'B' and (resid 695 through 782 )B695 - 782
19X-RAY DIFFRACTION19chain 'C' and (resid 204 through 239 )C204 - 239
20X-RAY DIFFRACTION20chain 'C' and (resid 240 through 281 )C240 - 281
21X-RAY DIFFRACTION21chain 'C' and (resid 282 through 334 )C282 - 334
22X-RAY DIFFRACTION22chain 'C' and (resid 335 through 375 )C335 - 375
23X-RAY DIFFRACTION23chain 'C' and (resid 376 through 475 )C376 - 475
24X-RAY DIFFRACTION24chain 'C' and (resid 476 through 543 )C476 - 543
25X-RAY DIFFRACTION25chain 'C' and (resid 544 through 636 )C544 - 636
26X-RAY DIFFRACTION26chain 'C' and (resid 637 through 694 )C637 - 694
27X-RAY DIFFRACTION27chain 'C' and (resid 695 through 782 )C695 - 782

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