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- PDB-4m18: Crystal Structure of Surfactant Protein-D D325A/R343V mutant in c... -

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Basic information

Entry
Database: PDB / ID: 4m18
TitleCrystal Structure of Surfactant Protein-D D325A/R343V mutant in complex with trimannose (Man-a1,2Man-a1,2Man)
ComponentsPulmonary surfactant-associated protein D
KeywordsSUGAR BINDING PROTEIN / surfactant protein / carbohydrate recognition domain / lectin
Function / homology
Function and homology information


Toll Like Receptor TLR1:TLR2 Cascade / Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / Toll Like Receptor 4 (TLR4) Cascade / clathrin-coated endocytic vesicle / respiratory gaseous exchange by respiratory system / Regulation of TLR by endogenous ligand / Surfactant metabolism / collagen trimer / surfactant homeostasis ...Toll Like Receptor TLR1:TLR2 Cascade / Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / Toll Like Receptor 4 (TLR4) Cascade / clathrin-coated endocytic vesicle / respiratory gaseous exchange by respiratory system / Regulation of TLR by endogenous ligand / Surfactant metabolism / collagen trimer / surfactant homeostasis / Signal regulatory protein family interactions / negative regulation of interleukin-2 production / lung alveolus development / macrophage chemotaxis / endocytic vesicle / negative regulation of T cell proliferation / multivesicular body / regulation of cytokine production / receptor-mediated endocytosis / reactive oxygen species metabolic process / positive regulation of phagocytosis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / SARS-CoV-1 activates/modulates innate immune responses / carbohydrate binding / lysosome / defense response to bacterium / innate immune response / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Lung surfactant protein D coiled-coil trimerisation / Lung surfactant protein D coiled-coil trimerisation / Collectin, C-type lectin-like domain / : / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / C-type lectin, conserved site / C-type lectin domain signature. / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A ...Lung surfactant protein D coiled-coil trimerisation / Lung surfactant protein D coiled-coil trimerisation / Collectin, C-type lectin-like domain / : / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / C-type lectin, conserved site / C-type lectin domain signature. / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / C-type lectin fold / Roll / Alpha Beta
Similarity search - Domain/homology
2alpha-alpha-mannobiose / Pulmonary surfactant-associated protein D
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 3.203 Å
AuthorsGoh, B.C. / Rynkiewicz, M.J. / Cafarella, T.R. / White, M.R. / Hartshorn, K.L. / Allen, K. / Crouch, E.C. / Calin, O. / Seeberger, P.H. / Schulten, K. / Seaton, B.A.
CitationJournal: Biochemistry / Year: 2013
Title: Molecular mechanisms of inhibition of influenza by surfactant protein d revealed by large-scale molecular dynamics simulation.
Authors: Goh, B.C. / Rynkiewicz, M.J. / Cafarella, T.R. / White, M.R. / Hartshorn, K.L. / Allen, K. / Crouch, E.C. / Calin, O. / Seeberger, P.H. / Schulten, K. / Seaton, B.A.
History
DepositionAug 2, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 4, 2013Provider: repository / Type: Initial release
Revision 1.1Dec 11, 2013Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.pdbx_formal_charge / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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.ptnr2_auth_asym_id / _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.value / _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.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_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pulmonary surfactant-associated protein D
B: Pulmonary surfactant-associated protein D
C: Pulmonary surfactant-associated protein D
D: Pulmonary surfactant-associated protein D
E: Pulmonary surfactant-associated protein D
F: Pulmonary surfactant-associated protein D
G: Pulmonary surfactant-associated protein D
H: Pulmonary surfactant-associated protein D
I: Pulmonary surfactant-associated protein D
J: Pulmonary surfactant-associated protein D
K: Pulmonary surfactant-associated protein D
L: Pulmonary surfactant-associated protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)197,83262
Polymers190,58012
Non-polymers7,25250
Water25214
1
A: Pulmonary surfactant-associated protein D
B: Pulmonary surfactant-associated protein D
C: Pulmonary surfactant-associated protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,39716
Polymers47,6453
Non-polymers1,75213
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8110 Å2
ΔGint-137 kcal/mol
Surface area19040 Å2
MethodPISA
2
D: Pulmonary surfactant-associated protein D
E: Pulmonary surfactant-associated protein D
F: Pulmonary surfactant-associated protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,51915
Polymers47,6453
Non-polymers1,87412
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8450 Å2
ΔGint-127 kcal/mol
Surface area19510 Å2
MethodPISA
3
G: Pulmonary surfactant-associated protein D
H: Pulmonary surfactant-associated protein D
I: Pulmonary surfactant-associated protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,55916
Polymers47,6453
Non-polymers1,91413
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8310 Å2
ΔGint-133 kcal/mol
Surface area19310 Å2
MethodPISA
4
J: Pulmonary surfactant-associated protein D
K: Pulmonary surfactant-associated protein D
L: Pulmonary surfactant-associated protein D
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,35715
Polymers47,6453
Non-polymers1,71212
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7810 Å2
ΔGint-127 kcal/mol
Surface area19130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.833, 159.454, 159.894
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
Pulmonary surfactant-associated protein D / PSP-D / SP-D / Collectin-7 / Lung surfactant protein D


Mass: 15881.684 Da / Num. of mol.: 12
Fragment: neck and carbohydrate recognition domain (UNP residues 229-375)
Mutation: D325A/R343V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: COLEC7, PSPD, SFTP4, SFTPD / Plasmid: pET30A(+) / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta blue / References: UniProt: P35247
#2: Polysaccharide
alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose


Type: oligosaccharide / Mass: 504.438 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-2DManpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,3,2/[a1122h-1a_1-5]/1-1-1/a2-b1_b2-c1WURCSPDB2Glycan 1.1.0
[][a-D-Manp]{[(2+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose / 2alpha-alpha-mannobiose


Type: oligosaccharide, Oligosaccharide / Class: Metabolism / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: 2alpha-alpha-mannobiose
DescriptorTypeProgram
DManpa1-2DManpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a1122h-1a_1-5]/1-1/a2-b1WURCSPDB2Glycan 1.1.0
[][a-D-Manp]{[(2+1)][a-D-Manp]{}}LINUCSPDB-CARE
#4: Chemical...
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 38 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Formula: H2O
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: 3.61 Å3/Da / Density % sol: 65.89 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: Purified D325A+R343V (12-15 mg/mL in 20 mM HEPES, pH 7.5, 150 mM sodium chloride, 10 mM calcium acetate) + reservoir solution (0.1 M HEPES, pH 7.5, 0.25 M sodium chloride, 20-22% w/v PEG3350) ...Details: Purified D325A+R343V (12-15 mg/mL in 20 mM HEPES, pH 7.5, 150 mM sodium chloride, 10 mM calcium acetate) + reservoir solution (0.1 M HEPES, pH 7.5, 0.25 M sodium chloride, 20-22% w/v PEG3350), VAPOR DIFFUSION, HANGING DROP, temperature 290K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 14, 2011
RadiationMonochromator: double mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 3.2→15.024 Å / Num. obs: 45301 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Biso Wilson estimate: 32.85 Å2 / Rmerge(I) obs: 0.169 / Χ2: 1.068 / Net I/σ(I): 5.4
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
3.2-3.313.50.43144061.033198.1
3.31-3.443.70.3244071.05199
3.44-3.63.90.26444701.068199.4
3.6-3.794.20.24145151.075199.8
3.79-4.024.40.20345121.0621100
4.02-4.324.60.15445241.031100
4.32-4.744.60.12145111.0221100
4.74-5.44.60.12545901.0631100
5.4-6.74.60.13746221.11100
6.7-15.0244.40.0647441.1621100

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHENIX1.8_1069refinement
PDB_EXTRACT3.11data extraction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB ENTRY 4M17

4m17


Resolution: 3.203→15.024 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.34 / σ(F): 1.34 / Phase error: 21.02 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2222 1991 4.4 %RANDOM
Rwork0.1868 ---
obs0.1884 45242 99.33 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 159.02 Å2 / Biso mean: 49.2482 Å2 / Biso min: 11.62 Å2
Refinement stepCycle: LAST / Resolution: 3.203→15.024 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13049 0 424 14 13487
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01413980
X-RAY DIFFRACTIONf_angle_d0.75319299
X-RAY DIFFRACTIONf_chiral_restr0.0452123
X-RAY DIFFRACTIONf_plane_restr0.0052410
X-RAY DIFFRACTIONf_dihedral_angle_d19.1375080
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.203-3.28220.31751340.2852883301794
3.2822-3.370.30271400.25243057319799
3.37-3.4680.27681400.23783025316599
3.468-3.57850.26921400.2223054319499
3.5785-3.70450.29091400.208530733213100
3.7045-3.85040.25581420.212430893231100
3.8504-4.02250.19651450.188130773222100
4.0225-4.23010.20441370.168430753212100
4.2301-4.48840.19261470.146731273274100
4.4884-4.82430.19151440.141531093253100
4.8243-5.29050.15451410.145731063247100
5.2905-6.01260.19621450.166131613306100
6.0126-7.42020.22491470.196131623309100
7.4202-15.02370.16191490.146632533402100
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)
18.78742.77032.67583.04740.09475.04830.08-1.07220.49330.3525-0.3959-1.0247-0.55180.04040.29070.46010.0564-0.06440.3597-0.01310.5026-18.58721.3638-16.4972
21.79610.5355-0.15912.93381.1443.12780.04290.2076-0.1997-0.0021-0.022-0.14110.13750.1741-0.01120.21840.03220.05540.2963-0.03220.2611-23.46611.9224-41.8043
35.6837-2.08233.60434.0514-2.76728.74480.3045-1.22210.071.07910.0009-1.11751.3064-0.0724-0.4270.7315-0.0217-0.16850.5427-0.07620.5963-10.44125.4966-21.6302
40.94470.0959-0.00232.2526-0.06952.18550.06840.02720.37060.1839-0.0570.1978-0.1666-0.1123-0.01710.2916-0.03030.01980.20830.01780.4105-41.656928.7745-27.5861
51.6489-0.13670.8512.74921.47067.8459-0.4774-1.0279-0.19440.70460.0903-0.69330.22850.41990.27320.40920.0318-0.15960.6280.01720.5867-11.253314.8385-20.3326
62.78930.1319-0.30251.58190.00571.23930.18260.76870.4068-0.8165-0.3428-0.8405-0.03490.13330.13060.4250.12120.16070.5530.14540.5768-11.828335.0564-46.4043
76.2103-1.7758-0.17136.9063-1.32462.6955-0.1302-0.3242-1.4719-0.713-0.1237-0.27920.93240.62320.08280.47250.16110.03710.62610.08570.5531-36.4973-18.1424-27.4719
81.86560.4652-0.06552.26180.28142.08280.0893-0.28370.06480.1275-0.024-0.1991-0.39270.1494-0.05030.2725-0.0510.03450.2713-0.02750.2705-41.32229.5388-8.5497
94.8997-2.73650.5421.6319-0.59221.29810.202-0.30090.04-0.3142-0.1365-0.89620.76640.20420.01210.56910.0889-0.0090.3429-0.06360.8945-42.7362-23.0172-20.7076
101.450.8445-0.37142.5864-0.05392.2939-0.06340.24890.1509-0.22350.10710.0320.11410.0339-0.02410.1986-0.0199-0.00430.2333-0.00340.2942-50.40841.816-41.9381
112.9826-2.4092-1.79634.47062.56531.56980.3162-0.1086-0.1060.0539-0.2532-0.80110.56560.8118-0.0710.6750.1852-0.07440.42180.11830.5535-35.1047-16.7808-17.0215
122.51840.4117-0.79221.2702-0.5533.28020.0351-0.3386-0.12940.1038-0.11170.19750.2407-0.29010.04970.24890.00880.01190.2822-0.00750.2591-68.3836-12.6393-14.6839
134.60012.2514-1.01418.6301-1.9123.0592-0.10530.4853-1.05630.80070.35940.07490.9127-0.5899-0.48660.7045-0.0843-0.05370.502-0.05470.4935-69.9464-19.466812.242
143.01441.1771-1.02091.4407-0.51372.7917-0.37140.2125-0.30030.02060.0768-0.32890.37790.43520.26910.30480.0358-0.00830.45520.05010.2649-38.823-9.85759.9568
152.78650.78250.64899.19621.30572.0074-0.25510.3112-0.7283-0.18480.17081.24860.9315-1.17760.01270.6374-0.2575-0.00040.75950.05310.573-69.3354-21.70822.626
162.1946-0.4574-0.60111.9953-0.52362.48940.13040.11020.19440.04320.12180.2033-0.447-0.3092-0.23150.31630.06370.05150.3605-0.0250.284-70.20786.2234.3115
175.61211.47491.07816.48210.92472.01940.1109-0.0816-0.5772-0.1270.04610.83090.79730.1302-0.16770.7324-0.0815-0.08380.44390.02070.3374-61.0415-23.798815.8226
181.87271.1074-1.22091.6633-0.10223.80590.2463-0.52850.32090.35310.10590.0963-0.18650.3518-0.30320.29710.0660.02120.4527-0.06370.4145-57.7017-1.352738.4124
192.01111.7413-1.99132.4523-2.37975.93490.66230.63130.3607-0.5728-0.4824-0.1221-0.6422-0.1413-0.26830.67120.19710.05050.56850.00160.4606-64.4308-24.14-58.8231
201.540.17740.10661.59510.00511.4251-0.07040.1527-0.1969-0.12090.2971.1625-0.1194-0.1668-0.19970.34510.0063-0.08440.27080.00380.8896-95.9637-26.5917-53.3953
213.9226-1.32280.47121.04990.34297.94570.16550.888-0.4502-1.1089-0.5225-0.5986-0.23250.75350.25710.58990.0520.2550.3927-0.11150.7075-65.4179-13.7621-60.3151
222.20820.39740.43552.4471-0.57921.56740.1246-0.0209-0.36970.2999-0.2085-0.15120.23650.0480.0740.3299-0.0456-0.05690.2445-0.04520.3874-67.0137-31.8386-33.432
235.8799-1.4426-2.47733.241.9284.243-0.05460.6122-0.3341-0.3514-0.3942-0.0940.49980.08180.35210.52450.0528-0.0230.38-0.00960.385-72.1532-20.6826-64.889
242.0944-1.09530.36342.8942-0.21272.4716-0.0438-0.12760.3059-0.1524-0.0510.0003-0.454-0.35350.07110.26250.0251-0.04690.2518-0.04540.2796-77.22561.4561-41.5401
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 214 through 232 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 233 through 355 )A0
3X-RAY DIFFRACTION3chain 'B' and (resid 214 through 232 )B0
4X-RAY DIFFRACTION4chain 'B' and (resid 233 through 355 )B0
5X-RAY DIFFRACTION5chain 'C' and (resid 212 through 232 )C0
6X-RAY DIFFRACTION6chain 'C' and (resid 233 through 355 )C0
7X-RAY DIFFRACTION7chain 'D' and (resid 211 through 232 )D0
8X-RAY DIFFRACTION8chain 'D' and (resid 233 through 355 )D0
9X-RAY DIFFRACTION9chain 'E' and (resid 211 through 232 )E0
10X-RAY DIFFRACTION10chain 'E' and (resid 233 through 355 )E0
11X-RAY DIFFRACTION11chain 'F' and (resid 211 through 232 )F0
12X-RAY DIFFRACTION12chain 'F' and (resid 233 through 355 )F0
13X-RAY DIFFRACTION13chain 'G' and (resid 213 through 232 )G0
14X-RAY DIFFRACTION14chain 'G' and (resid 233 through 355 )G0
15X-RAY DIFFRACTION15chain 'H' and (resid 211 through 232 )H0
16X-RAY DIFFRACTION16chain 'H' and (resid 233 through 355 )H0
17X-RAY DIFFRACTION17chain 'I' and (resid 214 through 232 )I0
18X-RAY DIFFRACTION18chain 'I' and (resid 233 through 355 )I0
19X-RAY DIFFRACTION19chain 'J' and (resid 214 through 232 )J0
20X-RAY DIFFRACTION20chain 'J' and (resid 233 through 355 )J0
21X-RAY DIFFRACTION21chain 'K' and (resid 213 through 232 )K0
22X-RAY DIFFRACTION22chain 'K' and (resid 233 through 355 )K0
23X-RAY DIFFRACTION23chain 'L' and (resid 213 through 232 )L0
24X-RAY DIFFRACTION24chain 'L' and (resid 233 through 355 )L0

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