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- PDB-5d13: Third PDZ domain (PDZ3) of PSD-95 complexed with CFMOC-KKETEV peptide -

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Basic information

Entry
Database: PDB / ID: 5d13
TitleThird PDZ domain (PDZ3) of PSD-95 complexed with CFMOC-KKETEV peptide
Components
  • CFMOC-KKETEV peptide
  • Disks large homolog 4
Keywordssignaling protein/inhibitor / protein-peptide complex / signaling protein-inhibitor complex
Function / homology
Function and homology information


RHO GTPases activate CIT / positive regulation of AMPA glutamate receptor clustering / neuronal ion channel clustering / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / Neurexins and neuroligins / neuroligin family protein binding / structural constituent of postsynaptic density / synaptic vesicle maturation / positive regulation of neuron projection arborization ...RHO GTPases activate CIT / positive regulation of AMPA glutamate receptor clustering / neuronal ion channel clustering / P2Y1 nucleotide receptor binding / beta-1 adrenergic receptor binding / Neurexins and neuroligins / neuroligin family protein binding / structural constituent of postsynaptic density / synaptic vesicle maturation / positive regulation of neuron projection arborization / regulation of grooming behavior / receptor localization to synapse / vocalization behavior / cerebellar mossy fiber / LGI-ADAM interactions / proximal dendrite / neuron spine / Trafficking of AMPA receptors / protein localization to synapse / AMPA glutamate receptor clustering / cellular response to potassium ion / Activation of Ca-permeable Kainate Receptor / dendritic branch / positive regulation of dendrite morphogenesis / dendritic spine morphogenesis / negative regulation of receptor internalization / juxtaparanode region of axon / frizzled binding / acetylcholine receptor binding / neuron projection terminus / dendritic spine organization / regulation of NMDA receptor activity / positive regulation of synapse assembly / Synaptic adhesion-like molecules / NMDA selective glutamate receptor signaling pathway / RAF/MAP kinase cascade / beta-2 adrenergic receptor binding / neurotransmitter receptor localization to postsynaptic specialization membrane / cortical cytoskeleton / social behavior / locomotory exploration behavior / AMPA glutamate receptor complex / regulation of neuronal synaptic plasticity / neuromuscular process controlling balance / kinesin binding / excitatory synapse / positive regulation of excitatory postsynaptic potential / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of synaptic transmission / glutamate receptor binding / D1 dopamine receptor binding / regulation of postsynaptic membrane neurotransmitter receptor levels / ionotropic glutamate receptor binding / dendrite cytoplasm / cell periphery / PDZ domain binding / establishment of protein localization / regulation of long-term neuronal synaptic plasticity / synaptic membrane / postsynaptic density membrane / neuromuscular junction / cerebral cortex development / cell-cell adhesion / kinase binding / cell junction / synaptic vesicle / cell-cell junction / nervous system development / positive regulation of cytosolic calcium ion concentration / protein-containing complex assembly / scaffold protein binding / protein phosphatase binding / chemical synaptic transmission / dendritic spine / postsynaptic membrane / postsynapse / neuron projection / postsynaptic density / signaling receptor binding / synapse / dendrite / protein-containing complex binding / protein kinase binding / glutamatergic synapse / endoplasmic reticulum / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. ...Polyubiquitination (PEST) N-terminal domain of MAGUK / Disks large homologue 1, N-terminal PEST domain / Polyubiquitination (PEST) N-terminal domain of MAGUK / PDZ-associated domain of NMDA receptors / PDZ-associated domain of NMDA receptors / Disks large 1-like / : / Guanylate kinase, conserved site / Guanylate kinase-like signature. / Guanylate kinase-like domain profile. / Guanylate kinase-like domain / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / PDZ domain / Pdz3 Domain / PDZ domain / SH3 domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
CFMOC-KKETEV peptide / Disks large homolog 4
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.151 Å
AuthorsDe, S. / Spaller, M.R. / Olson, R.
CitationJournal: to be published
Title: Chemically-modified peptides as inhibitors of PDZ3 of PSD-95
Authors: Memic, A. / De, S. / Lakhani, B. / Beveridge, D.L. / Olson, R. / Spaller, M.R.
History
DepositionAug 3, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 17, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2023Group: 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 / diffrn_radiation_wavelength / pdbx_initial_refinement_model / pdbx_struct_oper_list / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id
Revision 2.0Apr 24, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / cell / entity / entity_poly / entity_src_gen / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_asym / struct_conn / struct_ref_seq
Item: _atom_site.auth_asym_id / _atom_site.group_PDB ..._atom_site.auth_asym_id / _atom_site.group_PDB / _atom_site.label_asym_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_seq_id / _cell.Z_PDB / _entity_poly.pdbx_strand_id / _entity_src_gen.gene_src_common_name / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_refine_tls_group.beg_auth_seq_id / _pdbx_refine_tls_group.end_auth_seq_id / _pdbx_refine_tls_group.selection_details / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id
Revision 3.0Jul 10, 2024Group: Data collection / Non-polymer description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / entity
Item: _chem_comp.formula / _chem_comp.formula_weight / _entity.formula_weight
Revision 3.1Oct 16, 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: Disks large homolog 4
B: Disks large homolog 4
C: Disks large homolog 4
D: Disks large homolog 4
G: CFMOC-KKETEV peptide
E: CFMOC-KKETEV peptide
H: CFMOC-KKETEV peptide
F: CFMOC-KKETEV peptide
I: CFMOC-KKETEV peptide


Theoretical massNumber of molelcules
Total (without water)55,7289
Polymers55,7289
Non-polymers00
Water1,04558
1
A: Disks large homolog 4
E: CFMOC-KKETEV peptide


Theoretical massNumber of molelcules
Total (without water)13,6932
Polymers13,6932
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1190 Å2
ΔGint-4 kcal/mol
Surface area5740 Å2
MethodPISA
2
B: Disks large homolog 4
G: CFMOC-KKETEV peptide


Theoretical massNumber of molelcules
Total (without water)13,6932
Polymers13,6932
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1300 Å2
ΔGint-5 kcal/mol
Surface area5710 Å2
MethodPISA
3
C: Disks large homolog 4
H: CFMOC-KKETEV peptide
I: CFMOC-KKETEV peptide


Theoretical massNumber of molelcules
Total (without water)14,6483
Polymers14,6483
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Disks large homolog 4
F: CFMOC-KKETEV peptide


Theoretical massNumber of molelcules
Total (without water)13,6932
Polymers13,6932
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1140 Å2
ΔGint-4 kcal/mol
Surface area5310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.940, 84.940, 210.192
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number146
Space group name H-MH3

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Components

#1: Protein
Disks large homolog 4 / Postsynaptic density protein 95 / PSD-95 / Synapse-associated protein 90 / SAP90


Mass: 12738.067 Da / Num. of mol.: 4 / Fragment: unp residues 302-402
Source method: isolated from a genetically manipulated source
Details: GST-Fusion / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dlg4, Dlgh4, Psd95 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BLR-Gold / References: UniProt: P31016
#2: Protein/peptide
CFMOC-KKETEV peptide


Type: Oligopeptide / Class: Inhibitor / Mass: 955.103 Da / Num. of mol.: 5 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: CFMOC-KKETEV peptide
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 58 / 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: 2.67 Å3/Da / Density % sol: 53.89 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.2 / Details: 20 mM HEPES 100 mM NaCl 1.8 M tri-sodium citrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 6, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.15→36.5 Å / Num. obs: 30723 / % possible obs: 100 % / Redundancy: 6.7 % / CC1/2: 0.991 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.036 / Net I/σ(I): 10.5 / Num. measured all: 206411 / Scaling rejects: 45
Reflection shellResolution: 2.15→2.22 Å / Redundancy: 5 % / Rmerge(I) obs: 0.715 / Mean I/σ(I) obs: 1.5 / Num. measured all: 13352 / Num. unique all: 2650 / CC1/2: 0.881 / Rpim(I) all: 0.339 / Rejects: 0 / % possible all: 99.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
MOSFLM7.1.0data reduction
Aimless0.2.17data scaling
PHASER2.5.6phasing
PHENIX1.8.4refinement
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1TP3

1tp3


Resolution: 2.151→36.499 Å / FOM work R set: 0.7143 / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 33.77 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2565 1530 4.99 %
Rwork0.2101 29148 -
obs0.2125 30678 99.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 188.56 Å2 / Biso mean: 76.05 Å2 / Biso min: 30.7 Å2
Refinement stepCycle: final / Resolution: 2.151→36.499 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3064 0 41 58 3163
Biso mean--58.77 56.15 -
Num. residues----429
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.013143
X-RAY DIFFRACTIONf_angle_d1.194267
X-RAY DIFFRACTIONf_chiral_restr0.049468
X-RAY DIFFRACTIONf_plane_restr0.007575
X-RAY DIFFRACTIONf_dihedral_angle_d15.4561092
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 11 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.1511-2.22060.36261310.342226722803
2.2206-2.29990.34911110.310526762787
2.2999-2.3920.31391610.267126182779
2.392-2.50080.28261410.260926642805
2.5008-2.63260.26951510.248826122763
2.6326-2.79750.29131480.258126272775
2.7975-3.01340.28591370.236826732810
3.0134-3.31650.28781480.235926252773
3.3165-3.7960.2551350.199126632798
3.796-4.78080.21491380.162526712809
4.7808-36.50390.22511290.180226472776
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)
14.65464.7486-4.67884.8836-4.63814.6352-0.05662.038-0.2936-2.31110.2824-0.46940.38320.1457-0.37180.9063-0.0195-0.02960.77650.10890.853109.281-13.094-32.387
21.7633-3.4774-0.09567.74662.16249.02960.9885-0.7981-2.8591-0.36330.54880.85393.5413-2.4517-1.2591.0964-0.2529-0.40680.8460.31551.1072103.52-26.192-22.428
33.1821-1.57180.8638.1729-0.95442.1170.1368-0.4141-0.12570.0009-0.08030.1438-0.31260.6156-0.03210.3897-0.0203-0.01180.6287-0.05170.7459114.961-15.599-18.053
44.58272.70891.66136.5822.02097.81570.30.03-0.0078-0.88760.4007-0.4696-0.45350.3736-0.52210.41060.02650.02340.40880.0040.6856109.299-15.116-24.552
55.37464.19126.13763.75333.83618.50520.2683-0.87471.2630.9773-0.87950.95810.5133-0.70280.69450.5004-0.07350.04360.5337-0.02180.7244105.552-14.985-13.695
69.1388-0.11452.41796.175-3.17728.2834-0.0060.72371.46350.2161-0.3037-0.5128-0.67871.07340.35220.4833-0.03320.05880.4217-0.03870.6316116.603-13.428-22.163
75.3981-4.91363.22294.7799-1.57047.3271.21841.76680.3046-1.5372-0.8818-0.22290.16560.181-0.14710.58290.0483-0.00620.3895-0.03370.561384.98-21.102-16.017
85.27550.4482-2.56425.9206-1.04076.65350.0187-0.16750.5084-0.3389-0.0299-0.4913-0.13910.5455-0.07540.3897-0.0080.03270.2355-0.06850.65489.237-15.386-4.745
95.3627-0.69721.09763.43462.87342.9245-0.43421.3735-0.1041-0.16470.48210.0377-1.2072-0.0384-0.12520.6452-0.08290.02510.40020.06020.76486.035-13.704-13.116
102.9536-1.4609-0.09695.2171-1.16053.00030.10410.11450.1508-0.2005-0.03380.08050.3314-0.0165-0.1050.4134-0.0147-0.03220.2314-0.05510.490985.832-24.158-4.5
116.4183-1.25490.01215.39785.97197.9818-0.3327-0.6428-0.39870.8828-0.61590.7510.8756-0.78010.9560.56070.03480.00680.4452-0.11020.887575.434-7.456-2.796
124.8649-4.272-1.62823.80781.82037.18860.2570.34690.733-0.6024-0.51-1.4768-0.42680.57430.37310.3591-0.02060.02170.40440.06980.7392104.907-37.4530.585
137.2313-1.47551.27074.1392-1.26214.6638-0.1819-0.57450.13441.24940.1384-1.1939-0.33140.26590.0260.5230.0551-0.22910.3616-0.05080.539698.225-38.7679.867
141.3758-1.04130.73081.7989-0.42232.0683-0.5868-1.10361.14382.14350.1884-2.0333-0.44770.6550.50561.07210.1415-0.69390.873-0.19051.0801106.39-35.91617.546
152.0896-0.4386-0.04846.30670.93513.9392-0.9666-0.62471.13042.03750.8477-2.0186-0.28890.55470.17830.65910.0263-0.29880.4363-0.12031.0281103.688-33.7318.311
162.61673.1071-3.14123.607-3.7113.6632-0.3609-0.6965-0.68820.3208-0.4462-1.88850.38140.03860.6840.53720.053-0.130.4908-0.00010.6448101.385-54.62311.803
174.40393.93551.79534.73444.15476.43420.43621.84361.2345-0.6252-0.07-0.46640.2191.1411-0.06471.15930.0720.09191.470.3190.9701107.93-15.37820.018
189.187-5.99923.50324.0057-2.66992.48341.4709-0.1027-1.65160.1897-0.1608-0.5962.188-1.0724-1.49450.7603-0.2644-0.12721.1831-0.02160.8291107.59-24.49131.715
198.18044.49244.40258.20821.90092.5664-0.792-1.3581.43331.52370.629-2.15010.06850.98970.13490.90210.0886-0.27331.1157-0.09590.9938114.93-15.96334.045
208.9409-1.04748.90373.38720.41389.63122.22622.3742-2.6106-3.1488-0.95550.19082.71621.1726-1.481.5560.341-0.56991.4843-0.42811.2976109.823-28.95123.558
216.3835-1.2736.18743.14271.51278.5878-0.19963.16660.6055-1.7132-0.4767-0.9311-1.32170.05440.75870.6693-0.01610.05851.3760.05460.9391110.556-15.91325.924
225.7972-1.18011.51077.4744-0.70234.8873-0.8996-2.11682.03930.52480.6642-0.4603-1.0512-0.68460.53351.01010.5006-0.31662.1391-0.38751.2507103.657-10.03533.674
239.952.78192.56677.85640.52543.2475-0.7767-0.77792.3603-0.6474-0.50780.2534-0.20890.42911.16160.67380.0813-0.03391.49290.13710.6674104.526-17.01231.261
244.9719-2.29143.81594.637-1.70362.8555-0.65031.84080.58250.14840.69230.50270.1167-0.70160.4650.9072-0.34590.26331.63360.26841.5933124.836-13.14133.304
255.5429-5.4984-4.88455.45934.78544.78470.2986-0.57952.0910.4744-0.1064-0.2265-0.46740.0252-0.02590.46760.0123-0.01210.4493-0.19920.641288.727-14.2412.929
262.00741.96511.97671.92521.99788.09431.53050.55311.5356-0.5159-0.17350.04080.95960.7466-0.97270.5090.07110.07130.4117-0.04711.162486.928-35.849-2.512
275.4392-4.8244.48045.206-6.22649.16710.4682-0.16770.30040.3334-0.027-0.96720.68210.7861-0.52980.66990.0143-0.17080.7820.02180.9501112.951-20.989-14.14
282.8395-0.7909-1.12114.1976-3.55234.155-1.00610.2247-0.88330.9317-0.5175-0.5688-0.4842-0.20441.61261.08470.27730.04710.6934-0.00350.804194.431-41.0718.157
295.9391-4.5559-0.72345.0468-1.69724.2511-0.5986-1.70011.9438-0.77021.50341.06651.6271-0.7662-0.5870.9139-0.1185-0.4631.33350.04430.893112.899-22.05137.932
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 307:317 )A307 - 317
2X-RAY DIFFRACTION2( CHAIN A AND RESID 318:324 )A318 - 324
3X-RAY DIFFRACTION3( CHAIN A AND RESID 325:341 )A325 - 341
4X-RAY DIFFRACTION4( CHAIN A AND RESID 342:371 )A342 - 371
5X-RAY DIFFRACTION5( CHAIN A AND RESID 372:380 )A372 - 380
6X-RAY DIFFRACTION6( CHAIN A AND RESID 381:406 )A381 - 406
7X-RAY DIFFRACTION7( CHAIN B AND RESID 307:317 )B307 - 317
8X-RAY DIFFRACTION8( CHAIN B AND RESID 318:350 )B318 - 350
9X-RAY DIFFRACTION9( CHAIN B AND RESID 351:356 )B351 - 356
10X-RAY DIFFRACTION10( CHAIN B AND RESID 357:393 )B357 - 393
11X-RAY DIFFRACTION11( CHAIN B AND RESID 394:406 )B394 - 406
12X-RAY DIFFRACTION12( CHAIN C AND RESID 306:317 )C306 - 317
13X-RAY DIFFRACTION13( CHAIN C AND RESID 318:362 )C318 - 362
14X-RAY DIFFRACTION14( CHAIN C AND RESID 363:380 )C363 - 380
15X-RAY DIFFRACTION15( CHAIN C AND RESID 381:393 )C381 - 393
16X-RAY DIFFRACTION16( CHAIN C AND RESID 394:406 )C394 - 406
17X-RAY DIFFRACTION17( CHAIN D AND RESID 307:317 )D307 - 317
18X-RAY DIFFRACTION18( CHAIN D AND RESID 318:329 )D318 - 329
19X-RAY DIFFRACTION19( CHAIN D AND RESID 330:341 )D330 - 341
20X-RAY DIFFRACTION20( CHAIN D AND RESID 342:350 )D342 - 350
21X-RAY DIFFRACTION21( CHAIN D AND RESID 351:362 )D351 - 362
22X-RAY DIFFRACTION22( CHAIN D AND RESID 363:371 )D363 - 371
23X-RAY DIFFRACTION23( CHAIN D AND RESID 372:393 )D372 - 393
24X-RAY DIFFRACTION24( CHAIN D AND RESID 394:406 )D394 - 406
25X-RAY DIFFRACTION25( CHAIN G AND RESID 420:425 )G420 - 425
26X-RAY DIFFRACTION26( CHAIN I AND RESID 502:502 )I502
27X-RAY DIFFRACTION27( CHAIN E AND RESID 420:425 )E420 - 425
28X-RAY DIFFRACTION28( CHAIN H AND RESID 420:425 )H420 - 425
29X-RAY DIFFRACTION29( CHAIN F AND RESID 420:425 )F420 - 425

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