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- PDB-5fo9: Crystal Structure of Human Complement C3b in Complex with CR1 (CC... -

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Basic information

Entry
Database: PDB / ID: 5fo9
TitleCrystal Structure of Human Complement C3b in Complex with CR1 (CCP15- 17)
Components
  • COMPLEMENT C3 BETA CHAIN
  • COMPLEMENT C3B ALPHA' CHAIN
  • COMPLEMENT RECEPTOR TYPE 1
KeywordsLIPID BINDING PROTEIN / COMPLEMENT SYSTEM / IMMUNE SYSTEM / PLASMA PROTEIN / REGULATORS OF COMPLEMENT ACTIVITY / COFACTOR ACTIVITY / DECAY ACCELERATING ACTIVITY
Function / homology
Function and homology information


complement component C4b receptor activity / immune complex clearance by erythrocytes / complement component C3b receptor activity / positive regulation of serine-type endopeptidase activity / negative regulation of complement activation, alternative pathway / complement component C4b binding / negative regulation of immunoglobulin production / negative regulation of activation of membrane attack complex / negative regulation of complement activation, classical pathway / negative regulation of complement-dependent cytotoxicity ...complement component C4b receptor activity / immune complex clearance by erythrocytes / complement component C3b receptor activity / positive regulation of serine-type endopeptidase activity / negative regulation of complement activation, alternative pathway / complement component C4b binding / negative regulation of immunoglobulin production / negative regulation of activation of membrane attack complex / negative regulation of complement activation, classical pathway / negative regulation of complement-dependent cytotoxicity / negative regulation of complement activation / ATP export / T cell mediated immunity / oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / plasma membrane organization / complement component C3b binding / negative regulation of plasma cell differentiation / RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / negative regulation of serine-type endopeptidase activity / Alternative complement activation / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of phagocytosis, engulfment / complement receptor mediated signaling pathway / Activation of C3 and C5 / positive regulation of type IIa hypersensitivity / positive regulation of regulatory T cell differentiation / positive regulation of glucose transmembrane transport / complement-dependent cytotoxicity / complement activation, alternative pathway / complement activation / negative regulation of interleukin-2 production / neuron remodeling / endopeptidase inhibitor activity / amyloid-beta clearance / plasma membrane raft / ficolin-1-rich granule membrane / negative regulation of type II interferon production / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / complement activation, classical pathway / negative regulation of T cell proliferation / Peptide ligand-binding receptors / secretory granule membrane / fatty acid metabolic process / Regulation of Complement cascade / Post-translational protein phosphorylation / response to bacterium / 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 angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / virus receptor activity / G alpha (i) signalling events / blood microparticle / secretory granule lumen / cytoskeleton / immune response / inflammatory response / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / positive regulation of cell population proliferation / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / : ...Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / : / : / Complement component 3, CUB domain 2 / Complement component 3, CUB domain 1 / Complement C3-like, NTR domain / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin/fibulin / Anaphylatoxin, complement system / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Glycosyltransferase - #20 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin / Macroglobulin domain / 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 / Other non-globular / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/SCR/CCP superfamily / Sushi/CCP/SCR domain profile. / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Single Sheet / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Jelly Rolls / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Complement C3 / Complement receptor type 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 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 1.2Jul 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 1.3Jan 10, 2024Group: 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: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA' CHAIN
C: COMPLEMENT RECEPTOR TYPE 1
D: COMPLEMENT C3 BETA CHAIN
E: COMPLEMENT C3B ALPHA' CHAIN
F: COMPLEMENT RECEPTOR TYPE 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)394,6128
Polymers394,1706
Non-polymers4422
Water0
1
D: COMPLEMENT C3 BETA CHAIN
E: COMPLEMENT C3B ALPHA' CHAIN
F: COMPLEMENT RECEPTOR TYPE 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)197,3064
Polymers197,0853
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14260 Å2
ΔGint-63.7 kcal/mol
Surface area80500 Å2
MethodPISA
2
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA' CHAIN
C: COMPLEMENT RECEPTOR TYPE 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)197,3064
Polymers197,0853
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15680 Å2
ΔGint-96.7 kcal/mol
Surface area97530 Å2
MethodPQS
Unit cell
Length a, b, c (Å)104.320, 113.710, 138.520
Angle α, β, γ (deg.)82.74, 71.77, 80.95
Int Tables number1
Space group name H-MP1

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Components

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


Mass: 71393.320 Da / Num. of mol.: 2 / Fragment: 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


Mass: 104074.148 Da / Num. of mol.: 2 / Fragment: CCP DOMAINS, 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 COMPLEMENT RECEPTOR TYPE 1 / C3B/C4B RECEPTOR / COMPLEMENT CR1 / CD35


Mass: 21617.527 Da / Num. of mol.: 2 / Fragment: RESIDUES 942-1136
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: KOMAGATAELLA PASTORIS (fungus) / References: UniProt: P17927
#4: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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
Sequence detailsRESIDUE 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: 4.27 Å3/Da / Density % sol: 71.2 % / Description: NONE
Crystal growDetails: 8% PEG 3350 35MM BIS-TRIS PH 5.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.873
DetectorType: DECTRIS PILATUS / Detector: PIXEL
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.873 Å / Relative weight: 1
ReflectionResolution: 3.3→60.15 Å / Num. obs: 88061 / % possible obs: 98.4 % / Observed criterion σ(I): 1.5 / Redundancy: 1.9 % / Biso Wilson estimate: 74.36 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 3.8
Reflection shellResolution: 3.3→3.48 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 1.4 / % possible all: 98.2

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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, 1GKN, 1GKG

2i07

1gkn

1gkg


Resolution: 3.3→60.153 Å / SU ML: 0.51 / σ(F): 1.96 / Phase error: 31.69 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2913 4423 5 %
Rwork0.2505 --
obs0.2525 88022 98.37 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 143 Å2
Refinement stepCycle: LAST / Resolution: 3.3→60.153 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27378 0 28 0 27406
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00328012
X-RAY DIFFRACTIONf_angle_d0.82937968
X-RAY DIFFRACTIONf_dihedral_angle_d12.96410474
X-RAY DIFFRACTIONf_chiral_restr0.0564296
X-RAY DIFFRACTIONf_plane_restr0.0044914
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3-3.33750.39651630.34942739X-RAY DIFFRACTION98
3.3375-3.37680.38841410.33412794X-RAY DIFFRACTION98
3.3768-3.41790.32011490.31682724X-RAY DIFFRACTION98
3.4179-3.46120.30941190.31072919X-RAY DIFFRACTION98
3.4612-3.50670.36621630.31962675X-RAY DIFFRACTION98
3.5067-3.55480.38231330.31692840X-RAY DIFFRACTION98
3.5548-3.60550.36861330.30592777X-RAY DIFFRACTION98
3.6055-3.65940.34881520.30312790X-RAY DIFFRACTION98
3.6594-3.71650.34621460.29432788X-RAY DIFFRACTION98
3.7165-3.77750.35371480.29392780X-RAY DIFFRACTION98
3.7775-3.84260.32081480.27452813X-RAY DIFFRACTION98
3.8426-3.91240.30191500.27312770X-RAY DIFFRACTION98
3.9124-3.98770.32681330.28142787X-RAY DIFFRACTION98
3.9877-4.06910.36531430.27422801X-RAY DIFFRACTION98
4.0691-4.15750.31231450.25852789X-RAY DIFFRACTION98
4.1575-4.25420.29611560.25252768X-RAY DIFFRACTION98
4.2542-4.36060.2641470.23772811X-RAY DIFFRACTION99
4.3606-4.47840.27371560.23482787X-RAY DIFFRACTION99
4.4784-4.61020.31331630.23692772X-RAY DIFFRACTION99
4.6102-4.75890.26781470.21752806X-RAY DIFFRACTION99
4.7589-4.92890.25041610.21062766X-RAY DIFFRACTION99
4.9289-5.12620.23981480.21022781X-RAY DIFFRACTION99
5.1262-5.35930.27051370.21632813X-RAY DIFFRACTION98
5.3593-5.64170.27991420.22362775X-RAY DIFFRACTION98
5.6417-5.99490.27271380.2362848X-RAY DIFFRACTION99
5.9949-6.45720.28911680.24662740X-RAY DIFFRACTION99
6.4572-7.10610.28211640.23312792X-RAY DIFFRACTION99
7.1061-8.13220.25341440.22322812X-RAY DIFFRACTION99
8.1322-10.23760.1951280.20812792X-RAY DIFFRACTION98
10.2376-60.16260.25091580.22452750X-RAY DIFFRACTION97
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)
10.1666-0.15840.11790.3714-0.02820.06060.01010.25140.0395-0.01890.03070.35850.2001-0.0861-00.7603-0.0924-0.01120.9558-0.10431.1403-29.0713-12.57-10.2701
20.462-0.4058-0.35130.1068-0.51220.161-0.1016-0.0003-0.0027-0.01140.0154-0.0327-0.25070.1481-00.62160.0416-0.11450.4016-0.00770.7323-27.6487-26.111931.3379
30.74810.4283-0.19060.5459-0.33630.45290.00410.087-0.09920.0515-0.0074-0.1798-0.13020.2135-0.13080.5547-0.04380.00440.5221-0.11170.8771-11.7942-12.34311.3657
40.17230.1518-0.06720.1578-0.14290.2131-0.01250.2565-0.06380.02050.1915-0.8177-0.37120.1228-0.01560.50020.0067-0.01260.45760.01381.120733.49719.675715.9129
50.6862-0.0953-0.23120.2591-0.36070.588-0.3311-0.0162-0.30590.08630.1529-0.039-0.1243-0.0469-0.20470.66990.0218-0.1430.58540.18120.5306-2.057428.605840.0692
60.14110.04240.09510.07210.03750.03020.06090.0373-0.30390.2663-0.49570.14550.1901-0.4163-00.6047-0.21020.12850.908-0.28691.0177-6.666115.89378.3086
70.27-0.4081-0.1843-0.0462-0.04870.1273-0.45930.4437-0.5378-0.17370.507-0.1532-0.02870.20050.16620.5962-0.0141-0.04950.54910.12160.9110.84677.591718.3082
80.29910.04650.23110.6811-0.51020.6919-0.0836-0.05420.22580.21420.16850.04420.045-0.19820.06920.7877-0.04650.16910.6643-0.20630.7061-43.4252-22.830933.279
90.11860.07780.31730.5709-0.58460.4510.3010.2714-0.0441-0.1272-0.05680.09270.1305-0.13070.08591.39740.14380.01951.6739-0.00131.5035-41.2537-32.3956-39.1729
100.73890.1233-0.29730.1243-0.44610.2563-0.07140.0180.12650.09460.0545-0.0530.1797-0.2270.07760.88310.05780.09740.5851-0.13530.6195-41.7249-40.99723.9832
110.1212-0.0648-0.08980.0839-0.14030.0402-1.00990.4437-0.51090.17310.1426-0.33030.1647-0.7272-0.02211.314-0.04360.61861.577-0.28920.8203-75.0844-37.140573.5775
120.00470.0455-0.00170.0218-0.0361-0.0025-0.09360.23360.07970.0093-0.268-0.072-0.07010.2415-02.55410.22760.00562.0023-0.3062.1703-57.926313.667470.1552
130.3654-0.07390.21820.16220.09270.0271-0.23210.14150.2860.17560.06280.4142-0.0904-0.31110.08350.92430.21280.05280.8614-0.0871.1099-56.8864-10.562724.6544
141.3219-0.4559-0.1947-0.07010.24080.3069-0.1037-0.7069-0.29040.10230.2292-0.1651-0.1940.19660.17340.82740.16360.04050.9280.18470.34944.177227.116158.1495
152.03440.1695-0.20710.5886-0.31720.88070.79320.16550.44110.4271-0.31470.2107-0.38960.46930.82590.4061-0.25020.01360.1807-0.08450.409561.01234.55517.0603
160.3742-0.47340.01540.1249-0.06670.2515-0.0339-0.0053-0.2137-0.09170.2980.1252-0.05870.29080.10230.6629-0.21860.18230.474-0.03760.535644.492341.716825.0397
170.01820.02690.00170.1229-0.12390.2913-0.083-0.39370.24720.1712-0.1106-0.0679-0.19130.0884-0.0011.3617-0.16390.41951.7307-0.1740.977412.022945.988756.8683
180.1022-0.17380.02820.3109-0.25990.5021-0.3569-0.43920.3846-0.30110.1791.9944-0.4767-0.1795-0.01210.60010.34820.66421.19710.0048-1.2919-23.140343.51164.5479
190.2064-0.25720.05720.35350.02720.1293-0.04560.0608-0.2654-0.40880.52510.3995-0.03080.75570.03720.7818-0.174-0.1122.1604-0.20650.0356-3.664949.4653101.9665
20-0.0038-0.01580.0083-0.0047-0.00140.001-0.0218-0.0765-0.15380.05850.15120.07520.0544-0.0369-02.02720.6918-0.24342.06650.62552.4819-16.4777-2.976894.9138
21-0.02920.10290.02380.09730.06170.0535-0.2123-0.2541-0.222-0.06830.15070.1402-0.2760.16540.06291.5380.156-0.0611.88280.66551.7946-3.05075.533978.7027
220.020.03530.03360.03050.07270.03830.0713-0.02940.06040.2628-0.19470.2139-0.0473-0.215601.3836-0.2260.04692.2467-0.10021.719134.82223.614753.699
23-0.00330.00920.0078-0.0138-0.0157-0.0006-0.0313-0.20750.01010.0078-0.0983-0.0715-0.1931-0.167101.80780.05780.30611.87730.43691.840345.981129.396938.5201
240.0035-0.0036-0.01240.02050.0007-0.0040.0879-0.2083-0.1330.07170.058-0.15250.0226-0.1802-0.00011.51940.2563-0.27261.7080.2841.558438.677215.011349.8
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 23 THROUGH 134 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 135 THROUGH 322 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 323 THROUGH 664 )
4X-RAY DIFFRACTION4CHAIN 'D' AND (RESID 23 THROUGH 124 )
5X-RAY DIFFRACTION5CHAIN 'D' AND (RESID 125 THROUGH 356 )
6X-RAY DIFFRACTION6CHAIN 'D' AND (RESID 357 THROUGH 437 )
7X-RAY DIFFRACTION7CHAIN 'D' AND (RESID 438 THROUGH 664 )
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESID 752 THROUGH 1031 )
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESID 1032 THROUGH 1178 )
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESID 1179 THROUGH 1513 )
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESID 1514 THROUGH 1663 )
12X-RAY DIFFRACTION12CHAIN 'C' AND (RESID 941 THROUGH 988 )
13X-RAY DIFFRACTION13CHAIN 'C' AND (RESID 989 THROUGH 1133 )
14X-RAY DIFFRACTION14CHAIN 'E' AND (RESID 752 THROUGH 1012 )
15X-RAY DIFFRACTION15CHAIN 'E' AND (RESID 1013 THROUGH 1243 )
16X-RAY DIFFRACTION16CHAIN 'E' AND (RESID 1244 THROUGH 1312 )
17X-RAY DIFFRACTION17CHAIN 'E' AND (RESID 1313 THROUGH 1382 )
18X-RAY DIFFRACTION18CHAIN 'E' AND (RESID 1383 THROUGH 1513 )
19X-RAY DIFFRACTION19CHAIN 'E' AND (RESID 1514 THROUGH 1663 )
20X-RAY DIFFRACTION20CHAIN 'F' AND (RESID 941 THROUGH 960 )
21X-RAY DIFFRACTION21CHAIN 'F' AND (RESID 961 THROUGH 1059 )
22X-RAY DIFFRACTION22CHAIN 'F' AND (RESID 1060 THROUGH 1089 )
23X-RAY DIFFRACTION23CHAIN 'F' AND (RESID 1090 THROUGH 1105 )
24X-RAY DIFFRACTION24CHAIN 'F' AND (RESID 1106 THROUGH 1133 )

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