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- PDB-2wy3: Structure of the HCMV UL16-MICB complex elucidates select binding... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 2wy3
TitleStructure of the HCMV UL16-MICB complex elucidates select binding of a viral immunoevasin to diverse NKG2D ligands
Components
  • MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B
  • UNCHARACTERIZED PROTEIN UL16
KeywordsIMMUNE SYSTEM/VIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX / IMMUNE RESPONSE / INNATE IMMUNITY / STRUCTURAL MIMICRY / IMMUNOGLOBULIN DOMAIN / MEMBRANE / CYTOLYSIS / ULBP / NKG2D / NK CELL / CELL MEMBRANE / TRANSMEMBRANE / VIRAL IMMUNE EVASION / NATURAL KILLER CELL / CONVERGENT EVOLUTION
Function / homology
Function and homology information


evasion by virus of host natural killer cell activity / immune response-activating cell surface receptor signaling pathway / natural killer cell lectin-like receptor binding / negative regulation of defense response to virus by host / gamma-delta T cell activation / host cell membrane / response to retinoic acid / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / positive regulation of T cell mediated cytotoxicity ...evasion by virus of host natural killer cell activity / immune response-activating cell surface receptor signaling pathway / natural killer cell lectin-like receptor binding / negative regulation of defense response to virus by host / gamma-delta T cell activation / host cell membrane / response to retinoic acid / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / positive regulation of T cell mediated cytotoxicity / peptide antigen binding / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / response to heat / adaptive immune response / killing of cells of another organism / response to oxidative stress / membrane => GO:0016020 / immune response / external side of plasma membrane / signaling receptor binding / cell surface / extracellular space / plasma membrane
Similarity search - Function
Immunoglobulin-like - #1990 / Viral unique long protein 16 / Human cytomegalovirus, UL16 ectodomain / Viral unique long protein 16 / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Class I Histocompatibility antigen, domains alpha 1 and 2 / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein ...Immunoglobulin-like - #1990 / Viral unique long protein 16 / Human cytomegalovirus, UL16 ectodomain / Viral unique long protein 16 / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Class I Histocompatibility antigen, domains alpha 1 and 2 / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / Protein UL16 / MHC class I polypeptide-related sequence B
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
HUMAN HERPESVIRUS 5 STRAIN AD169
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsMueller, S. / Zocher, G. / Steinle, A. / Stehle, T.
CitationJournal: Plos Pathog. / Year: 2010
Title: Structure of the Hcmv Ul16-Micb Complex Elucidates Select Binding of a Viral Immunoevasin to Diverse Nkg2D Ligands.
Authors: Muller, S. / Zocher, G. / Steinle, A. / Stehle, T.
History
DepositionNov 11, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 2, 2010Provider: repository / Type: Initial release
Revision 1.1Jun 18, 2014Group: Refinement description / Version format compliance
Revision 1.2Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Dec 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B
B: UNCHARACTERIZED PROTEIN UL16
C: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B
D: UNCHARACTERIZED PROTEIN UL16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)114,52422
Polymers108,0284
Non-polymers6,49618
Water11,512639
1
A: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B
B: UNCHARACTERIZED PROTEIN UL16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,68111
Polymers54,0142
Non-polymers2,6679
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4070 Å2
ΔGint1.7 kcal/mol
Surface area16660 Å2
MethodPISA
2
C: MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B
D: UNCHARACTERIZED PROTEIN UL16
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,84311
Polymers54,0142
Non-polymers3,8299
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4080 Å2
ΔGint5.4 kcal/mol
Surface area16360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)58.120, 104.170, 146.800
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.5076, -0.02843, 0.8611), (0.02894, -0.9995, -0.01593), (0.8611, 0.01684, 0.5082)-50.64, 75.6, 28.66
2given(-0.5072, -0.03088, 0.8612), (0.02485, -0.9995, -0.0212), (0.8614, 0.01065, 0.5077)-50.73, 76.22, 28.81

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B / MHC CLASS I POLYPEPTIDE-RELATED SEQUENCE B ALLELE 002 / MIC-B


Mass: 36278.703 Da / Num. of mol.: 2 / Fragment: MHC CLASS I HOMOLOG DOMAIN, RESIDUES 24-341
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human)
Description: CDNA OF ALLELE 002 WAS ISOLATED FROM A IMR90 HUMAN LUNG FIBROBLAST LIBRARY
Cell: FIBROBLAST / Organ: LUNG / Plasmid: PET21A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ROSETTA 2 / References: UniProt: Q29980
#2: Protein UNCHARACTERIZED PROTEIN UL16 / UL16


Mass: 17735.059 Da / Num. of mol.: 2 / Fragment: RESIDUES 27-184
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HUMAN HERPESVIRUS 5 STRAIN AD169 / Description: CDNA ISOLATED FROM HCMV STRAIN AD169 GENOME. / Plasmid: PCDNA3.1(-) / Cell line (production host): CHO LEC 3.2.8.1 / Organ (production host): OVARY / Production host: CRICETULUS GRISEUS (Chinese hamster) / References: UniProt: P16757

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Sugars , 1 types, 12 molecules

#5: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 3 types, 645 molecules

#3: Chemical ChemComp-PEU / 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL / PEG 8000


Mass: 1221.461 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C55H112O28 / Comment: precipitant*YM
#4: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 639 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE UNIPROT ACCESSION NUMBER Q29980 DOES NOT PROVIDE THE CORRECT AMINO ACID SEQUENCE OF THE MICB ...THE UNIPROT ACCESSION NUMBER Q29980 DOES NOT PROVIDE THE CORRECT AMINO ACID SEQUENCE OF THE MICB ALLELE 002. THIS CAN BE FOUND UNDER AAB71642 IN PUBMED PROTEIN SEARCH. ONLY THE ALPHA1 AND ALPHA2 DOMAINS (RESIDUES 1-181) OF THE ECTODOMAIN (1-276) WAS EXPRESSED. THIS IS A FRAGMENT OF THE FULL LENGTH PROTEIN (RESIDUES 1-318). SEQUENCE OF UNCHARACTERIZED PROTEIN UL16 CAN ALSO BE FOUND UNDER NP_039950 IN THE PUBMED PROTEIN SEARCH. ONLY THE ECTODOMAIN (RESIDUES 1-184) WAS EXPRESSED. THIS IS A FRAGMENT OF THE FULL LENGTH PROTEIN ( 1-230). DUE TO CLEAVAGE OF THE SIGNAL PEPTIDE (RESIDUES 1- 26) THE MATURE UL16 PROTEIN USED FOR CRYSTALLIZATION CONSISTS OF RESIDUES 27-184.

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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: 2.5 Å3/Da / Density % sol: 50.84 % / Description: NONE
Crystal growpH: 6.5
Details: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM CACODYLATE PH 6.5, 25 % PEG 8000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.0013
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 30, 2008
RadiationMonochromator: DCCM / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0013 Å / Relative weight: 1
ReflectionResolution: 1.8→50 Å / Num. obs: 82272 / % possible obs: 98.7 % / Observed criterion σ(I): 3.44 / Redundancy: 8.9 % / Biso Wilson estimate: 24.06 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 16.9
Reflection shellResolution: 1.8→1.85 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 3.44 / % possible all: 97.5

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1JE6

1je6


Resolution: 1.8→49.087 Å / SU ML: 0.24 / σ(F): 1.99 / Phase error: 19.02 / Stereochemistry target values: ML
Details: CHAIN A RESIDUES 149-151 AND 176- -181 ARE DISORDERED. CHAIN B 164-184 ARE DISORDERED. CHAIN C RESIDUES 148-149 AND 176-181 ARE DISORDERED. CHAIN D RESIDUES 160-184 ARE DISORDERED. MET0 IN ...Details: CHAIN A RESIDUES 149-151 AND 176- -181 ARE DISORDERED. CHAIN B 164-184 ARE DISORDERED. CHAIN C RESIDUES 148-149 AND 176-181 ARE DISORDERED. CHAIN D RESIDUES 160-184 ARE DISORDERED. MET0 IN CHAIN A IS NOT PART OF THE MATURE EUCARYOTIC MICB SEQUENCE BUT AN E.COLI ARTEFACT. MET140 IN CHAIN A AND CHAIN C WAS MODELLED AS AN ALANINE IN BOTH CASES
RfactorNum. reflection% reflection
Rfree0.2133 4114 5 %
Rwork0.177 --
obs0.1788 82271 98.68 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.518 Å2 / ksol: 0.375 e/Å3
Displacement parametersBiso mean: 33.92 Å2
Baniso -1Baniso -2Baniso -3
1-4.6447 Å2-0 Å2-0 Å2
2---0.5617 Å20 Å2
3----4.083 Å2
Refinement stepCycle: LAST / Resolution: 1.8→49.087 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4914 0 229 639 5782
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0065481
X-RAY DIFFRACTIONf_angle_d1.0577451
X-RAY DIFFRACTIONf_dihedral_angle_d14.7692086
X-RAY DIFFRACTIONf_chiral_restr0.077846
X-RAY DIFFRACTIONf_plane_restr0.004942
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.82120.21951380.21162625X-RAY DIFFRACTION98
1.8212-1.84340.23571380.19832613X-RAY DIFFRACTION97
1.8434-1.86670.2261390.19482657X-RAY DIFFRACTION98
1.8667-1.89130.22751380.19612615X-RAY DIFFRACTION97
1.8913-1.91720.23071380.18442610X-RAY DIFFRACTION98
1.9172-1.94460.25921410.18432681X-RAY DIFFRACTION98
1.9446-1.97360.20681380.17882628X-RAY DIFFRACTION98
1.9736-2.00450.25161400.17272658X-RAY DIFFRACTION98
2.0045-2.03730.19061380.16732635X-RAY DIFFRACTION99
2.0373-2.07240.21241420.15992684X-RAY DIFFRACTION99
2.0724-2.11010.20821380.16592630X-RAY DIFFRACTION98
2.1101-2.15070.18051420.15972690X-RAY DIFFRACTION99
2.1507-2.19460.20031400.15382673X-RAY DIFFRACTION99
2.1946-2.24230.17311410.16162664X-RAY DIFFRACTION99
2.2423-2.29450.22091410.16012687X-RAY DIFFRACTION99
2.2945-2.35190.22161420.16822690X-RAY DIFFRACTION99
2.3519-2.41550.23131420.16952702X-RAY DIFFRACTION99
2.4155-2.48650.22661410.16922679X-RAY DIFFRACTION99
2.4865-2.56680.18641420.16652693X-RAY DIFFRACTION99
2.5668-2.65850.21821420.17662715X-RAY DIFFRACTION99
2.6585-2.7650.20211430.17452715X-RAY DIFFRACTION99
2.765-2.89080.231430.17322718X-RAY DIFFRACTION99
2.8908-3.04320.24211440.18072732X-RAY DIFFRACTION100
3.0432-3.23380.1921440.172738X-RAY DIFFRACTION99
3.2338-3.48340.19961440.15542733X-RAY DIFFRACTION99
3.4834-3.83390.18211450.14512759X-RAY DIFFRACTION99
3.8339-4.38830.16441470.14492776X-RAY DIFFRACTION100
4.3883-5.52760.20271470.15222799X-RAY DIFFRACTION100
5.5276-49.10510.2351560.23092958X-RAY DIFFRACTION99
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)
12.68890.5431.11720.30710.82752.0066-0.00710.3072-0.3937-0.17920.2416-0.18120.28720.2566-0.24660.2910.0002-0.02360.1848-0.04010.141617.448948.704989.1082
21.71580.64430.36321.07110.88143.23540.1127-0.0365-0.0434-0.03690.01960.01380.29590.1234-0.13310.2270.0376-0.01940.1062-0.00880.127618.605649.106596.4055
30.90530.11771.25350.11381.24032.71370.0040.0278-0.0015-0.32860.02040.0247-0.39910.0567-0.01950.3352-0.0179-0.04620.1199-0.01790.125614.603757.959881.2229
40.9883-1.1732-1.8183-0.13767.86564.7948-0.8795-0.2022-0.19130.69750.51640.5134-0.68310.03510.22050.74060.3628-0.00380.4647-0.03030.20170.332757.785183.778
51.7787-0.82420.75020.80480.39661.33620.11-0.1483-0.3218-0.2959-0.05930.13350.0038-0.22040.01950.2243-0.0281-0.01630.2363-0.05990.186819.516564.170396.0208
60.8528-0.97670.77485.6371-2.52573.0020.45790.26890.0963-0.5533-0.53740.4863-0.0456-0.12660.05160.26590.17-0.01030.31230.0330.212116.029324.99189.3752
70.5364-0.87940.91462.588-0.64533.60970.1770.02490.41230.0046-0.19280.3923-0.5289-0.4796-0.05490.16330.0874-0.01320.19040.00910.19718.325427.209395.8164
83.6356-3.2351-1.4392-2.7256-1.92324.87840.35580.36282.68490.75850.65451.8755-1.57070.3584-0.92220.616-0.14880.07530.18470.23910.875927.425335.251894.4403
93.4111-1.11160.98831.7014-0.1746-1.81510.17560.16450.0134-0.1504-0.12360.0769-0.10280.1748-0.04070.16390.0431-0.00880.1724-0.00910.175723.402325.011194.0344
102.0471-2.12910.41921.7466-0.00661.51460.19460.3299-0.4139-0.2586-0.24580.73890.0468-0.60250.1070.24920.0385-0.10840.3598-0.05920.302112.137514.606487.795
111.5931.3145-1.63390.69340.8656-0.67930.12660.9610.0196-0.75230.2010.3496-0.5141-0.6253-0.17050.50120.1917-0.26970.6976-0.10370.33269.629115.806974.7051
122.00570.14442.10822.8057-2.6308-5.45360.42640.7846-0.6462-1.6331-1.06160.007-0.05960.26640.43420.85170.2494-0.05980.4663-0.13070.086923.328313.163976.4897
130.6801-1.3575-1.27531.97510.93881.59160.10960.1558-0.0214-0.0954-0.09110.2126-0.1882-0.4081-0.02910.16860.00960.00220.24040.02730.189921.076811.184898.0976
142.7475-0.70011.0779-0.08620.78380.3396-0.1155-0.85080.17340.08810.10470.217-0.2862-0.03140.07690.2270.02930.06680.3284-0.00460.23992.529976.0589118.4574
152.006-0.5234-0.42560.8513-1.8134-0.9697-0.3002-0.261-0.09050.21790.2111-0.03870.00460.23110.09460.2091-0.035-0.0110.15710.0010.137320.705872.6158116.0115
161.17170.13190.0081.3318-0.17551.04970.0520.0392-0.0571-0.0062-0.02220.1337-0.1225-0.0754-0.02830.1043-0.0048-0.01020.12630.00250.157814.353373.4336108.1887
170.8391-0.50230.89891.582-0.11412.3379-0.11620.16550.1391-0.23660.07340.337-0.3171-0.30170.06610.13980.0066-0.04520.14950.01230.15277.895976.3535101.9661
181.19020.3190.07330.74510.32640.3664-0.12960.32780.0007-0.24210.18540.0367-0.0739-0.1077-0.03080.1843-0.0401-0.00190.1596-0.0140.135713.880669.4122101.1327
191.4279-1.4771.2360.07180.04220.5308-0.0967-0.302-0.17960.02970.0110.0321-0.035-0.11570.0730.1313-0.02070.02020.1552-0.00070.149215.072772.8926114.0179
202.62140.7342-4.75461.07661.69733.2589-0.68430.6194-0.6603-0.18810.0241-0.3251.42270.03160.68260.4953-0.00970.15990.3583-0.07420.340432.046973.315297.3377
21-2.9221-1.67431.91121.76-0.80583.66760.09290.09120.1656-0.2869-0.0044-0.37620.23010.9695-0.05860.10740.04310.04950.32690.02330.276549.8055-0.989892.0453
220.6731-0.6486-0.04781.5970.9960.82320.0248-0.18760.16390.16760.0881-0.6090.22150.3354-0.06210.2076-0.0064-0.07620.1714-0.00140.238242.40831.4841105.5265
230.53260.2778-0.02070.60010.30081.22520.0427-0.00780.0143-0.06880.0313-0.0154-0.0937-0.0316-0.06380.151-0.00190.03420.095-0.00080.113234.70483.249197.0874
241.1007-0.0803-0.4560.1575-0.04351.2993-0.02210.0349-0.187-0.31510.0557-0.04660.27660.049-0.01960.2053-0.02430.01530.0948-0.00150.136633.8088-3.991389.5712
250.6846-0.6137-1.3456-0.3312-3.35584.9040.20040.14060.17370.0144-0.2273-0.064-0.5918-0.08930.00510.1869-0.0130.01740.09540.02310.103832.549911.638385.877
260.4297-0.50330.10990.67880.45710.97610.0421-0.0025-0.0179-0.0310.0083-0.02050.04620.0039-0.04830.0901-0.01850.01130.07740.00690.103634.54932.366398.0176
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:25)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 26:84)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 85:139)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 140:148)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 152:175)
6X-RAY DIFFRACTION6(CHAIN C AND RESID 0:17)
7X-RAY DIFFRACTION7(CHAIN C AND RESID 18:37)
8X-RAY DIFFRACTION8(CHAIN C AND RESID 38:41)
9X-RAY DIFFRACTION9(CHAIN C AND RESID 42:90)
10X-RAY DIFFRACTION10(CHAIN C AND RESID 91:124)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 125:139)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 140:156)
13X-RAY DIFFRACTION13(CHAIN C AND RESID 157:175)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 27:42)
15X-RAY DIFFRACTION15(CHAIN B AND RESID 43:55)
16X-RAY DIFFRACTION16(CHAIN B AND RESID 56:87)
17X-RAY DIFFRACTION17(CHAIN B AND RESID 88:115)
18X-RAY DIFFRACTION18(CHAIN B AND RESID 116:134)
19X-RAY DIFFRACTION19(CHAIN B AND RESID 135:156)
20X-RAY DIFFRACTION20(CHAIN B AND RESID 157:163)
21X-RAY DIFFRACTION21(CHAIN D AND RESID 27:43)
22X-RAY DIFFRACTION22(CHAIN D AND RESID 44:52)
23X-RAY DIFFRACTION23(CHAIN D AND RESID 53:84)
24X-RAY DIFFRACTION24(CHAIN D AND RESID 85:110)
25X-RAY DIFFRACTION25(CHAIN D AND RESID 111:117)
26X-RAY DIFFRACTION26(CHAIN D AND RESID 118:159)

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