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- PDB-5foa: Crystal Structure of Human Complement C3b in complex with DAF (CCP2-4) -

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Basic information

Entry
Database: PDB / ID: 5foa
TitleCrystal Structure of Human Complement C3b in complex with DAF (CCP2-4)
Components
  • COMPLEMENT C3 BETA CHAIN
  • COMPLEMENT C3B ALPHA CHAIN
  • DECAY ACCELERATING FACTOR, CD55
KeywordsLIPID BINDING / COMPLEMENT SYSTEM / IMMUNE SYSTEM / PLASMA PROTEIN / REGULATORS OF COMPLEMENT ACTIVITY / DECAY-ACCELERATING ACTIVITY
Function / homology
Function and homology information


regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / regulation of complement-dependent cytotoxicity / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / regulation of complement activation ...regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / regulation of complement-dependent cytotoxicity / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / regulation of complement activation / complement-mediated synapse pruning / Alternative complement activation / respiratory burst / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment / positive regulation of CD4-positive, alpha-beta T cell activation / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of type IIa hypersensitivity / complement receptor mediated signaling pathway / positive regulation of CD4-positive, alpha-beta T cell proliferation / complement-dependent cytotoxicity / positive regulation of D-glucose transmembrane transport / complement activation / complement activation, alternative pathway / Class B/2 (Secretin family receptors) / endopeptidase inhibitor activity / neuron remodeling / amyloid-beta clearance / B cell activation / positive regulation of vascular endothelial growth factor production / ficolin-1-rich granule membrane / complement activation, classical pathway / Purinergic signaling in leishmaniasis infection / transport vesicle / side of membrane / COPI-mediated anterograde transport / endoplasmic reticulum-Golgi intermediate compartment membrane / Peptide ligand-binding receptors / secretory granule membrane / Regulation of Complement cascade / response to bacterium / Post-translational protein phosphorylation / fatty acid metabolic process / positive regulation of T cell cytokine production / positive regulation of receptor-mediated endocytosis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of protein phosphorylation / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / positive regulation of cytosolic calcium ion concentration / virus receptor activity / secretory granule lumen / G alpha (i) signalling events / blood microparticle / immune response / G protein-coupled receptor signaling pathway / membrane raft / receptor ligand activity / endoplasmic reticulum lumen / inflammatory response / signaling receptor binding / Golgi membrane / innate immune response / lipid binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
: / Complement C3-like, NTR domain / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 ...: / Complement C3-like, NTR domain / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / Anaphylatoxin, complement system domain / : / Anaphylatoxin domain signature. / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Macroglobulin domain MG4 / Macroglobulin domain MG4 / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Alpha-2-macroglobulin / Macroglobulin domain / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Immunoglobulin-like fold
Similarity search - Domain/homology
Complement C3 / Complement decay-accelerating factor
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.188 Å
AuthorsForneris, F. / Wu, J. / Xue, X. / Gros, P.
CitationJournal: Embo J. / Year: 2016
Title: Regulators of Complement Activity Mediate Inhibitory Mechanisms Through a Common C3B-Binding Mode.
Authors: Forneris, F. / Wu, J. / Xue, X. / Ricklin, D. / Lin, Z. / Sfyroera, G. / Tzekou, A. / Volokhina, E. / Granneman, J.C. / Hauhart, R. / Bertram, P. / Liszewski, M.K. / Atkinson, J.P. / Lambris, J.D. / Gros, P.
History
DepositionNov 18, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 6, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 1, 2016Group: Database references
Revision 1.2Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Revision 1.3Nov 6, 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: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA CHAIN
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3B ALPHA CHAIN
E: DECAY ACCELERATING FACTOR, CD55
F: DECAY ACCELERATING FACTOR, CD55


Theoretical massNumber of molelcules
Total (without water)393,5176
Polymers393,5176
Non-polymers00
Water00
1
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA CHAIN
E: DECAY ACCELERATING FACTOR, CD55


Theoretical massNumber of molelcules
Total (without water)196,7583
Polymers196,7583
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area13970 Å2
ΔGint-80 kcal/mol
Surface area96000 Å2
MethodPQS
2
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3B ALPHA CHAIN
F: DECAY ACCELERATING FACTOR, CD55


Theoretical massNumber of molelcules
Total (without water)196,7583
Polymers196,7583
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14990 Å2
ΔGint-79 kcal/mol
Surface area94280 Å2
MethodPQS
Unit cell
Length a, b, c (Å)117.429, 142.378, 323.697
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21221

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Components

#1: Protein COMPLEMENT C3 BETA CHAIN / C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PRO


Mass: 71393.320 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 23-667 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#2: Protein COMPLEMENT C3B ALPHA CHAIN / C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PRO


Mass: 104074.148 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 749-1663 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#3: Protein DECAY ACCELERATING FACTOR, CD55 / DECAY ACCELERATING FACTOR /


Mass: 21290.883 Da / Num. of mol.: 2 / Fragment: CCP DOMAINS 2-4, UNP RESIDUES 97-285
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / References: UniProt: P08174
Has protein modificationY
Sequence detailsRESIDUES GS AT N-TERMINUS AND AAA AT C-TERMINUS ARE ADDED BY CLONING. RESIDUE 1013 HAS BEEN ...RESIDUES GS AT N-TERMINUS AND AAA AT C-TERMINUS ARE ADDED BY CLONING. RESIDUE 1013 HAS BEEN CONVERTED FROM GLN TO GLU IN CONVERSION OF C3 PROTEIN TO C3B

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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: 3.49 Å3/Da / Density % sol: 64.8 % / Description: NONE
Crystal growDetails: 60MM MGCL2 30MM BIS-TRIS PH 5.5 6.5% PEG 3350 3% MESO-ERHYTROL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.975
DetectorType: DECTRUS PILATUS / Detector: PIXEL
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.975 Å / Relative weight: 1
ReflectionResolution: 4.2→117.83 Å / Num. obs: 39033 / % possible obs: 96.5 % / Observed criterion σ(I): 1.5 / Redundancy: 4.1 % / Biso Wilson estimate: 133.88 Å2 / Rmerge(I) obs: 0.15 / Net I/σ(I): 6.3
Reflection shellResolution: 4.2→4.43 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.59 / Mean I/σ(I) obs: 2.3 / % possible all: 92.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2I07, 1OK3

2i07

1ok3


Resolution: 4.188→110.39 Å / SU ML: 0.64 / σ(F): 1.34 / Phase error: 32.64 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3073 1953 5 %
Rwork0.2695 --
obs0.2714 38966 95.55 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 192 Å2
Refinement stepCycle: LAST / Resolution: 4.188→110.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27275 0 0 0 27275
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01527873
X-RAY DIFFRACTIONf_angle_d2.06537776
X-RAY DIFFRACTIONf_dihedral_angle_d15.45610420
X-RAY DIFFRACTIONf_chiral_restr0.0914259
X-RAY DIFFRACTIONf_plane_restr0.0134896
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.188-4.29280.36541390.33922197X-RAY DIFFRACTION83
4.2928-4.40880.36781460.31672490X-RAY DIFFRACTION93
4.4088-4.53860.33841190.29452580X-RAY DIFFRACTION93
4.5386-4.6850.32831270.29022540X-RAY DIFFRACTION94
4.685-4.85250.32831500.26672589X-RAY DIFFRACTION95
4.8525-5.04680.33881380.27262625X-RAY DIFFRACTION96
5.0468-5.27650.31931350.26592675X-RAY DIFFRACTION97
5.2765-5.55460.30481240.28292677X-RAY DIFFRACTION97
5.5546-5.90260.35861500.29352731X-RAY DIFFRACTION99
5.9026-6.35830.32771280.29452734X-RAY DIFFRACTION99
6.3583-6.99810.30231430.29122747X-RAY DIFFRACTION99
6.9981-8.01050.30191460.27192780X-RAY DIFFRACTION99
8.0105-10.09130.25531530.21272783X-RAY DIFFRACTION99
10.0913-110.42810.2721550.25012865X-RAY DIFFRACTION96
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)
1-0.0001-0.00320.00540.00180.00070.0033-0.05180.0855-0.0614-0.0098-0.0101-0.00570.03210.0137-0.00041.3530.1517-0.21441.1707-0.03421.3675116.1321-15.212519.5735
20.00390.0010.00070.00840.00150.00050.04310.0208-0.0112-0.02080.028-0.0023-0.0313-0.0567-0.00021.58070.11920.19141.567-0.12261.2507110.4725-4.344115.8248
30.00710.0002-0.00110.00340.0017-0.00110.01810.00550.05830.00610.01260.05420.0333-0.0018-0.00011.6796-0.14040.16961.62740.02251.7955124.3951-10.300513.7614
40.0957-0.0584-0.03790.07150.00880.02120.0125-0.040.0836-0.0890.0731-0.0320.1260.0040.01010.5410.1582-0.020.52080.20730.4065100.385518.991530.6761
50.0148-0.0101-0.02010.03530.01230.0241-0.0287-0.0269-0.05680.0338-0.04650.0060.0237-0.0038-0.00180.60610.07220.02480.54750.2070.292982.133946.659442.8769
60.003-0.0007-0.00580.00940.00270.0025-0.0458-0.01710.0302-0.0053-0.0165-0.0326-0.0121-0.0358-0.00010.7257-0.20640.24430.7964-0.06410.931279.642760.017645.6015
70.0281-0.0104-0.01050.0087-0.0110.02090.06420.0154-0.01460.03260.0561-0.0199-0.024-0.01820.10240.1625-0.2579-0.12540.3033-0.1785-0.035889.888649.471746.6329
80.0012-0.0026-0.00690.00270.01160.0035-0.09260.0244-0.0640.0325-0.12140.06650.018-0.13400.6193-0.11830.26430.44710.11790.568108.5137-12.405565.0569
90.00330.00950.01010.00470.0057-0-0.0949-0.01930.03440.08490.0085-0.052-0.0038-0.03870.00030.36790.2566-0.07980.4080.09180.5638112.8649-9.967667.7392
100.00360.0025-0.00650.01350.00760.0247-0.0928-0.0611-0.050.12030.03870.03040.0484-0.07240.04430.51110.2372-0.17710.58850.32150.4954124.510322.762168.4787
110.0242-0.035-0.09390.02030.00560.1689-0.19720.0782-0.0092-0.03360.0117-0.09760.02380.1596-0.13290.0606-0.1404-0.00890.1447-0.07490.4759135.187730.256244.7706
120.0410.029-0.01830.0118-0.01710.03630.00970.09510.01250.01980.0096-0.0779-0.10110.14180.00850.2423-0.13750.02270.4306-0.16180.2322141.663122.875337.5658
130.03030.00630.00230.00260.00120.00870.03250.0192-0.029-0.0250.07260.0642-0.00520.04590.0020.98690.12650.0980.7724-0.130.4616124.96395.102430.7819
140.01480.00130.01210.01960.01390.0026-0.08120.0648-0.0641-0.0458-0.06230.0104-0.01660.1162-0.00020.43540.0869-0.02190.498-0.14780.6916125.5567-5.027733.682
150.0516-0.01240.04090.0260.05140.0470.13080.1099-0.2479-0.07580.1001-0.05010.26640.02660.1981-0.23920.059-0.3561-0.0868-0.00550.0082113.69163.14749.0096
160.00770.0183-0.0190.0776-0.0227-0.007-0.01050.01380.03910.1008-0.1093-0.1008-0.2413-0.1984-0.0301-0.0563-0.0830.1150.06960.03560.3933123.747251.641255.5132
170.01270.07710.07740.08610.04140.0862-0.1144-0.0055-0.147-0.04650.0965-0.04720.27850.1324-0.0611.22080.0836-0.22920.6320.17770.4339134.8675-10.796690.7414
180.12880.06460.12320.1068-0.0130.3018-0.32430.17040.0941-0.0946-0.0646-0.3652-0.4213-0.187-0.21760.6214-0.4134-0.22690.20430.02020.5598147.964771.326664.8383
190.0752-0.0043-0.0628-0.00890.02990.0272-0.0398-0.1811-0.15160.06770.0029-0.0222-0.10190.14050.0710.17570.25180.38560.33170.08040.150196.871780.092928.5889
200.0551-0.02190.0003-0.001-0.00310.0297-0.023-0.25870.00320.20120.0441-0.1850.00090.07610.0987-0.2189-0.05190.07810.1780.28040.004886.928543.95054.6913
210.16330.011-0.1424-0.02110.03510.19720.1860.01590.3226-0.07090.268-0.0415-0.36710.01631.0317-0.52170.21120.5634-0.24210.1978-0.1941103.336667.60824.2226
22-0.003-0.0034-0.00160.0020.00330.0054-0.01260.00640.0534-0.0508-0.07170.008-0.0302-0.013-0.00030.97020.24590.11360.6985-0.03910.244986.886178.777154.2952
230.0097-0.0036-0.0010.0047-0.00290.0065-0.02430.0068-0.01080.01640.011-0.0331-0.01550.050300.80090.04480.14880.74870.20720.497997.313471.038752.8176
240.0257-0.00430.00610.0023-0.00180.00430.03340.03740.00980.00660.04280.01630.00210.00730.00040.98640.31480.00780.7780.15940.845183.832373.031345.3178
250.0191-0.017-0.00340.0142-0.00260.00030.0120.0175-0.0072-0.0398-0.0323-0.0084-0.0956-0.04380.00080.5601-0.03860.16710.53860.13430.5613106.912152.89563.582
260.01560.00340.00490.00450.00640.00410.04780.0135-0.05170.0505-0.0237-0.0320.0423-0.021-0.00550.61920.3161-0.22650.39-0.05950.1908103.598245.459471.1397
270.00810.00160.00530.0242-0.00890.01230.0309-0.0003-0.03920.04990.0364-0.01570.06030.04940.00030.8290.104-0.11530.89930.09220.8875107.505653.056573.3535
280.0044-0.0087-0.00170.0135-0.00240.0104-0.00230.01980.04320.05730.01630.0008-0.01340.02440.00021.41670.20640.22171.19710.04611.1311119.526521.783888.4836
290.0025-0.0018-0.00190.001700.0038-0.0309-0.012-0.02140.0044-0.064-0.0051-0.0151-0.00070.00031.54560.1843-0.08731.35650.16991.2464121.22298.287890.8347
300.00110.0004-0.00110.0105-0.00110.0024-0.0172-0.0092-0.04130.0058-0.0225-0.01470.04990.00910.00011.21390.15590.09371.07660.02981.0572108.612724.02583.663
310.0034-0.00360.00310.0105-0.01040.00960.0052-0.00750.0016-0.00010.0002-0.0062-0.0070.0118-0.00031.43360.03060.16911.50570.20661.4565114.27489.288992.6761
320.0771-0.0706-0.0020.0664-0.0120.10560.11530.1016-0.0486-0.0245-0.01050.0310.1722-0.05320.1812-0.03470.2794-0.22540.350.19760.444899.090727.640315.0449
330.24830.289-0.16960.1946-0.15720.28240.10370.04730.06980.00350.1679-0.1069-0.0797-0.38890.52580.3620.69150.43090.13280.10730.133575.442565.52429.1251
340.05740.0290.09770.067-0.00810.10050.16280.14620.35020.07410.12940.19620.2023-0.19480.15990.68920.16580.56690.6780.21280.790961.382779.470339.8987
350.2502-0.12390.04830.2156-0.03090.1415-0.00310.126-0.42470.17620.21870.31670.13580.06420.28690.1649-0.00650.128-0.07650.23070.281769.57650.46128.7661
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'F' AND (RESID 97 THROUGH 123 )
2X-RAY DIFFRACTION2CHAIN 'F' AND (RESID 124 THROUGH 144 )
3X-RAY DIFFRACTION3CHAIN 'F' AND (RESID 145 THROUGH 157 )
4X-RAY DIFFRACTION4CHAIN 'F' AND (RESID 158 THROUGH 222 )
5X-RAY DIFFRACTION5CHAIN 'F' AND (RESID 223 THROUGH 247 )
6X-RAY DIFFRACTION6CHAIN 'F' AND (RESID 248 THROUGH 263 )
7X-RAY DIFFRACTION7CHAIN 'F' AND (RESID 264 THROUGH 285 )
8X-RAY DIFFRACTION8CHAIN 'A' AND (RESID 23 THROUGH 76 )
9X-RAY DIFFRACTION9CHAIN 'A' AND (RESID 77 THROUGH 124 )
10X-RAY DIFFRACTION10CHAIN 'A' AND (RESID 125 THROUGH 210 )
11X-RAY DIFFRACTION11CHAIN 'A' AND (RESID 211 THROUGH 277 )
12X-RAY DIFFRACTION12CHAIN 'A' AND (RESID 278 THROUGH 369 )
13X-RAY DIFFRACTION13CHAIN 'A' AND (RESID 370 THROUGH 411 )
14X-RAY DIFFRACTION14CHAIN 'A' AND (RESID 412 THROUGH 469 )
15X-RAY DIFFRACTION15CHAIN 'A' AND (RESID 470 THROUGH 664 )
16X-RAY DIFFRACTION16CHAIN 'B' AND (RESID 752 THROUGH 932 )
17X-RAY DIFFRACTION17CHAIN 'B' AND (RESID 932 THROUGH 1360 )
18X-RAY DIFFRACTION18CHAIN 'B' AND (RESID 1361 THROUGH 1663 )
19X-RAY DIFFRACTION19CHAIN 'C' AND (RESID 23 THROUGH 134 )
20X-RAY DIFFRACTION20CHAIN 'C' AND (RESID 135 THROUGH 322 )
21X-RAY DIFFRACTION21CHAIN 'C' AND (RESID 323 THROUGH 664 )
22X-RAY DIFFRACTION22CHAIN 'E' AND (RESID 97 THROUGH 123 )
23X-RAY DIFFRACTION23CHAIN 'E' AND (RESID 124 THROUGH 144 )
24X-RAY DIFFRACTION24CHAIN 'E' AND (RESID 145 THROUGH 157 )
25X-RAY DIFFRACTION25CHAIN 'E' AND (RESID 158 THROUGH 171 )
26X-RAY DIFFRACTION26CHAIN 'E' AND (RESID 172 THROUGH 206 )
27X-RAY DIFFRACTION27CHAIN 'E' AND (RESID 207 THROUGH 222 )
28X-RAY DIFFRACTION28CHAIN 'E' AND (RESID 223 THROUGH 247 )
29X-RAY DIFFRACTION29CHAIN 'E' AND (RESID 248 THROUGH 263 )
30X-RAY DIFFRACTION30CHAIN 'E' AND (RESID 264 THROUGH 276 )
31X-RAY DIFFRACTION31CHAIN 'E' AND (RESID 277 THROUGH 285 )
32X-RAY DIFFRACTION32CHAIN 'D' AND (RESID 752 THROUGH 853 )
33X-RAY DIFFRACTION33CHAIN 'D' AND (RESID 854 THROUGH 1152 )
34X-RAY DIFFRACTION34CHAIN 'D' AND (RESID 1153 THROUGH 1349 )
35X-RAY DIFFRACTION35CHAIN 'D' AND (RESID 1350 THROUGH 1663 )

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