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- PDB-3egh: Crystal structure of a complex between Protein Phosphatase 1 alph... -

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Basic information

Entry
Database: PDB / ID: 3egh
TitleCrystal structure of a complex between Protein Phosphatase 1 alpha (PP1), the PP1 binding and PDZ domains of Spinophilin and the small natural molecular toxin Nodularin-R
Components
  • Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
  • SpinophilinPPP1R9B
  • nodularin R
KeywordsHYDROLASE/HYDROLASE INHIBITOR / PP1 / Serine/Threonine Phosphatase / Post Synaptic Density / Inhibitor / Carbohydrate metabolism / Cell cycle / Cell division / Glycogen metabolism / Hydrolase / Iron / Manganese / Metal-binding / Phosphoprotein / Protein phosphatase / Actin-binding / Cell junction / Cell projection / Cytoskeleton / Developmental protein / Differentiation / Neurogenesis / Nucleus / Synapse / HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Function / homology
Function and homology information


protein localization to actin cytoskeleton / positive regulation of protein localization to actin cortical patch / response to L-phenylalanine derivative / cytoplasmic side of dendritic spine plasma membrane / regulation of opioid receptor signaling pathway / protein localization to cell periphery / cellular response to morphine / developmental process involved in reproduction / response to prostaglandin E / regulation of glycogen catabolic process ...protein localization to actin cytoskeleton / positive regulation of protein localization to actin cortical patch / response to L-phenylalanine derivative / cytoplasmic side of dendritic spine plasma membrane / regulation of opioid receptor signaling pathway / protein localization to cell periphery / cellular response to morphine / developmental process involved in reproduction / response to prostaglandin E / regulation of glycogen catabolic process / response to kainic acid / reproductive system development / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / cellular response to peptide / protein phosphatase 1 binding / cadherin binding involved in cell-cell adhesion / filopodium assembly / actin filament depolymerization / dendritic spine membrane / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of canonical Wnt signaling pathway / regulation of translational initiation / response to steroid hormone / protein phosphatase inhibitor activity / positive regulation of protein localization / myosin phosphatase activity / male mating behavior / protein serine/threonine phosphatase activity / cortical actin cytoskeleton / branching morphogenesis of an epithelial tube / glycogen metabolic process / dendritic spine neck / protein-serine/threonine phosphatase / dendritic spine head / dendrite development / entrainment of circadian clock by photoperiod / Triglyceride catabolism / phosphatase activity / phosphoprotein phosphatase activity / response to immobilization stress / cellular response to organic cyclic compound / DARPP-32 events / D2 dopamine receptor binding / response to amino acid / ribonucleoprotein complex binding / dephosphorylation / cellular response to epidermal growth factor stimulus / response to organonitrogen compound / response to amphetamine / protein dephosphorylation / Downregulation of TGF-beta receptor signaling / response to nicotine / filopodium / learning / actin filament organization / cellular response to estradiol stimulus / calcium-mediated signaling / hippocampus development / positive regulation of protein localization to plasma membrane / response to lead ion / adherens junction / lung development / regulation of protein phosphorylation / circadian regulation of gene expression / regulation of circadian rhythm / negative regulation of cell growth / response to organic cyclic compound / cerebral cortex development / ruffle membrane / kinase binding / neuron projection development / cell migration / actin filament binding / cellular response to xenobiotic stimulus / Circadian Clock / actin cytoskeleton / presynapse / response to estradiol / lamellipodium / actin binding / growth cone / perikaryon / transmembrane transporter binding / dendritic spine / postsynaptic density / nucleic acid binding / protein kinase activity / response to xenobiotic stimulus / cell cycle / cell division / neuronal cell body / dendrite / glutamatergic synapse / protein-containing complex binding / nucleolus / extracellular exosome / nucleoplasm / metal ion binding
Similarity search - Function
Neurabin-1/2, PDZ domain / Neurabin-like family / PDZ domain / Serine-threonine protein phosphatase, N-terminal / Serine-threonine protein phosphatase N-terminal domain / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 ...Neurabin-1/2, PDZ domain / Neurabin-like family / PDZ domain / Serine-threonine protein phosphatase, N-terminal / Serine-threonine protein phosphatase N-terminal domain / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / PDZ domain / Pdz3 Domain / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / 4-Layer Sandwich / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
NODULARIN-R / : / : / Neurabin-2 / Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Similarity search - Component
Biological speciesHomo sapiens (human)
Rattus norvegicus (Norway rat)
Nodularia spumigena (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2 Å
AuthorsRagusa, M.J. / Page, R. / Peti, W.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites.
Authors: Ragusa, M.J. / Dancheck, B. / Critton, D.A. / Nairn, A.C. / Page, R. / Peti, W.
History
DepositionSep 10, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 23, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance
Revision 1.2Dec 12, 2012Group: Other
Revision 1.3Apr 10, 2013Group: Derived calculations
Revision 1.4Oct 25, 2017Group: Advisory / Refinement description / Category: pdbx_validate_polymer_linkage / software
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / struct_conn / struct_ref_seq_dif
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_value_order / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
B: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
C: Spinophilin
D: Spinophilin
E: nodularin R
F: nodularin R
hetero molecules


Theoretical massNumber of molelcules
Total (without water)114,11914
Polymers113,5316
Non-polymers5888
Water8,665481
1
A: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
C: Spinophilin
E: nodularin R
hetero molecules

B: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
D: Spinophilin
F: nodularin R
hetero molecules


Theoretical massNumber of molelcules
Total (without water)114,11914
Polymers113,5316
Non-polymers5888
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_445x-1/2,y-1/2,z1
Buried area12430 Å2
ΔGint-66 kcal/mol
Surface area33560 Å2
MethodPISA
2
A: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
C: Spinophilin
E: nodularin R
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,2449
Polymers56,7653
Non-polymers4786
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6290 Å2
ΔGint-34 kcal/mol
Surface area19400 Å2
MethodPISA
3
B: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
D: Spinophilin
F: nodularin R
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,8755
Polymers56,7653
Non-polymers1102
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5390 Å2
ΔGint-30 kcal/mol
Surface area14910 Å2
MethodPISA
Unit cell
Length a, b, c (Å)119.409, 84.426, 109.314
Angle α, β, γ (deg.)90.00, 93.58, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-542-

HOH

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Serine/threonine-protein phosphatase PP1-alpha catalytic subunit / PP-1A


Mass: 37349.844 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP1CA, PPP1A / Plasmid: RP1B / Production host: Escherichia coli (E. coli)
References: UniProt: P62136, protein-serine/threonine phosphatase
#2: Protein Spinophilin / PPP1R9B / Neurabin-II / Neurabin-2 / Protein phosphatase 1 regulatory subunit 9B / Neural tissue-specific F- ...Neurabin-II / Neurabin-2 / Protein phosphatase 1 regulatory subunit 9B / Neural tissue-specific F-actin-binding protein II / p130 / PP1bp134


Mass: 18571.566 Da / Num. of mol.: 2 / Fragment: PP1 binding and PDZ domains
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ppp1r9b / Plasmid: RP1B / Production host: Escherichia coli (E. coli) / References: UniProt: O35274

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Protein/peptide , 1 types, 2 molecules EF

#3: Protein/peptide nodularin R / Nodularin


Type: Oligopeptide / Class: Toxin / Mass: 843.985 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Nodularia spumigena (bacteria) / References: NOR: NOR00279, NODULARIN-R

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Non-polymers , 3 types, 489 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mn
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 481 / Source method: isolated from a natural source / Formula: H2O

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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: 2.42 Å3/Da / Density % sol: 49.1 %
Crystal growTemperature: 277 K / pH: 6.5
Details: 0.1M MES, 15% PEG 550 MME, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 1
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 19, 2008
Details: DOUBLE CRYSTAL CHANNEL CUT, SI(111), 1M LONG RH COATED TOROIDAL MIRROR FOR VERTICAL HORIZONTAL FOCUSING
RadiationMonochromator: SI(111) CHANNEL CUT MONOCHROMETER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→40 Å / Num. obs: 70101 / % possible obs: 98.1 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 26.55 Å2 / Rsym value: 0.066
Reflection shellResolution: 2→2.07 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 3.45 / Rsym value: 0.281 / % possible all: 82.5

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACT3.006data extraction
HKL-2000data reduction
HKL-2000data scaling
REFMAC5.2.0019phasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2→40 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.929 / Occupancy max: 1 / Occupancy min: 0.25 / SU B: 9.321 / SU ML: 0.129 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.169 / ESU R Free: 0.157 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.235 3528 5 %RANDOM
Rwork0.192 ---
obs0.195 66573 96.3 %-
all-69145 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 30.11 Å2
Baniso -1Baniso -2Baniso -3
1--0.35 Å20 Å21.11 Å2
2--0.7 Å20 Å2
3----0.21 Å2
Refinement stepCycle: LAST / Resolution: 2→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6436 0 28 481 6945
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0226650
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5441.9929014
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2245824
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.58124.092303
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.136151080
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.0121541
X-RAY DIFFRACTIONr_chiral_restr0.1090.2990
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.025109
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2010.22943
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.310.24567
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1550.2441
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1720.248
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1230.223
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.8041.54186
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.24326537
X-RAY DIFFRACTIONr_scbond_it2.1632774
X-RAY DIFFRACTIONr_scangle_it3.2224.52470
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.06 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.23 172 -
Rwork0.221 3657 -
obs--71.17 %
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)
111.1664-4.50456.50415.4478-6.107513.4299-0.0120.57280.4115-0.0994-0.1083-0.138-0.32640.49120.1203-0.094-0.06490.0119-0.11130.0135-0.09380.1535-15.5211-17.2649
22.6431.1233-3.86873.518-3.86911.2088-0.18330.153-0.2171-0.15280.0225-0.11080.43270.15750.1608-0.1692-0.0248-0.0119-0.1537-0.034-0.1211-0.3956-29.0296-14.5946
32.7042-3.0323-0.31827.66570.37182.6173-0.2732-0.5047-0.04640.84480.16650.1020.135-0.08030.1067-0.1304-0.02420.0036-0.10550.0041-0.1343-12.7906-27.44583.1117
42.32890.139-0.63251.0120.0611.8396-0.07720.15720.0044-0.02660.03130.18470.1252-0.4410.0459-0.1399-0.0345-0.0116-0.0839-0.0078-0.1452-19.5087-26.5479-9.3694
52.63840.25280.21852.6262-0.874911.0717-0.04660.19130.4103-0.0737-0.0550.1957-0.3605-0.03230.1015-0.12040.1104-0.0078-0.03840.020.0807-22.1013-11.7471-8.3009
69.61788.9021-6.306322.8389-23.446925.37630.4590.53390.9723-0.0163-0.28650.5398-0.4291-0.772-0.17250.0667-0.08940.00230.0882-0.09830.0578-27.1728-30.2873-21.8162
713.3981-1.93640.01547.9018-0.67559.5440.05760.3490.0681-0.0114-0.11240.7362-0.0548-0.94660.0548-0.10.0550.0382-0.03860.0038-0.09381.5232-17.9389-38.4055
82.48211.4790.86925.40773.94725.9962-0.0066-0.13660.18240.0516-0.03480.2611-0.0884-0.15930.0414-0.1520.01670.014-0.10470.0073-0.11665.9375-22.8076-34.6984
91.99560.3784-0.81511.6433-0.02972.0521-0.0243-0.01030.13360.02110.05140.0541-0.0444-0.001-0.0271-0.16660.001-0.004-0.1882-0.0272-0.176615.7817-22.6334-41.1478
101.81550.3537-0.71771.71390.16651.4699-0.03250.0148-0.139-0.03720.0234-0.21350.10970.14180.0092-0.11280.0235-0.0115-0.1748-0.0018-0.148729.1484-28.7086-48.3423
112.65870.70491.6252.210.3817.21840.1901-0.04110.1143-0.00220.00910.0528-0.2949-0.1846-0.1992-0.1373-0.03180.0276-0.2242-0.0164-0.043526.8676-10.7163-45.6034
1216.04047.79593.633817.777714.711112.97160.599-1.36940.268-0.2728-0.1425-0.8411-0.39110.3074-0.45650.04020.0267-0.10420.07980.0784-0.00731.7806-30.9502-33.1457
139.1701-2.622-2.05935.2453.62282.51010.5315-0.15650.8724-0.5521-0.0514-0.1317-0.75870.4405-0.48010.1650.1623-0.06270.13730.11880.284-20.3897-2.3142-11.2536
143.0904-0.0792-1.4983.90190.64656.17530.14030.05010.4223-0.02420.16120.2-0.2206-0.3367-0.3015-0.19220.1069-0.1179-0.05910.03890.0769-23.0343-11.0503-9.0312
157.6955-7.2714-1.836816.78913.005212.3267-0.40340.0679-0.80840.14560.09360.77670.9686-0.65450.30980.1345-0.23230.02850.1619-0.0706-0.0235-17.0639-40.7608-29.4226
166.5955-0.0971-0.41021.51170.19221.7154-0.0223-0.0159-1.203-0.0466-0.074-0.33070.27980.43710.09630.1884-0.02640.00070.10290.02560.2595-4.5675-51.1521-40.686
1710.37030.8404-3.15151.83020.51332.296-0.2723-0.0773-0.2830.12280.1452-0.51240.13090.1420.12720.0842-0.0793-0.03880.03540.04780.0257-2.4095-44.0675-40.5753
1810.2542.8894-4.61284.4519-4.25727.61260.4670.41520.46670.0478-0.1226-0.0202-0.7432-0.5257-0.3445-0.0328-0.0902-0.0841-0.166-0.02130.028228.2159-3.0376-44.5577
191.62090.3456-0.7373.1002-1.00942.64230.0424-0.1805-0.07670.28880.0196-0.05050.170.0755-0.062-0.15890.003-0.0893-0.0748-0.0497-0.070325.3964-20.3022-36.9492
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA7 - 267 - 26
2X-RAY DIFFRACTION2AA27 - 4627 - 46
3X-RAY DIFFRACTION3AA47 - 5947 - 59
4X-RAY DIFFRACTION4AA60 - 27260 - 272
5X-RAY DIFFRACTION5AA273 - 300273 - 300
6X-RAY DIFFRACTION6AO331
7X-RAY DIFFRACTION7BB7 - 177 - 17
8X-RAY DIFFRACTION8BB18 - 4418 - 44
9X-RAY DIFFRACTION9BB45 - 14545 - 145
10X-RAY DIFFRACTION10BB146 - 274146 - 274
11X-RAY DIFFRACTION11BB275 - 300275 - 300
12X-RAY DIFFRACTION12BO331
13X-RAY DIFFRACTION13CC424 - 44011 - 27
14X-RAY DIFFRACTION14CC441 - 47328 - 60
15X-RAY DIFFRACTION15CC474 - 49061 - 77
16X-RAY DIFFRACTION16CC491 - 55378 - 140
17X-RAY DIFFRACTION17CC554 - 583141 - 170
18X-RAY DIFFRACTION18DD424 - 44311 - 30
19X-RAY DIFFRACTION19DD444 - 48931 - 76

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