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- PDB-3g2f: Crystal structure of the kinase domain of bone morphogenetic prot... -

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Basic information

Entry
Database: PDB / ID: 3g2f
TitleCrystal structure of the kinase domain of bone morphogenetic protein receptor type II (BMPR2) at 2.35 A resolution
ComponentsBone morphogenetic protein receptor type-2
KeywordsTRANSFERASE / kinase / Structural Genomics / Structural Genomics Consortium / SGC / ATP-binding / Disease mutation / Glycoprotein / Magnesium / Manganese / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / Receptor / Serine/threonine-protein kinase / Transmembrane
Function / homology
Function and homology information


semi-lunar valve development / activin receptor activity, type II / negative regulation of chondrocyte proliferation / lymphatic endothelial cell differentiation / regulation of lung blood pressure / pulmonary valve development / tricuspid valve morphogenesis / chondrocyte development / lung vasculature development / lymphangiogenesis ...semi-lunar valve development / activin receptor activity, type II / negative regulation of chondrocyte proliferation / lymphatic endothelial cell differentiation / regulation of lung blood pressure / pulmonary valve development / tricuspid valve morphogenesis / chondrocyte development / lung vasculature development / lymphangiogenesis / negative regulation of cell proliferation involved in heart valve morphogenesis / venous blood vessel development / aortic valve development / BMP binding / proteoglycan biosynthetic process / maternal placenta development / negative regulation of muscle cell differentiation / atrial septum morphogenesis / endocardial cushion development / positive regulation of cartilage development / endochondral bone morphogenesis / transforming growth factor beta receptor activity / retina vasculature development in camera-type eye / mitral valve morphogenesis / BMP receptor activity / positive regulation of axon extension involved in axon guidance / artery development / receptor protein serine/threonine kinase / Signaling by BMP / cellular response to BMP stimulus / endothelial cell apoptotic process / positive regulation of ossification / negative regulation of systemic arterial blood pressure / endothelial cell proliferation / limb development / anterior/posterior pattern specification / cell surface receptor protein serine/threonine kinase signaling pathway / negative regulation of vasoconstriction / lung alveolus development / ventricular septum morphogenesis / positive regulation of epithelial cell migration / blood vessel development / outflow tract morphogenesis / growth factor binding / positive regulation of SMAD protein signal transduction / mesoderm formation / blood vessel remodeling / positive regulation of osteoblast differentiation / BMP signaling pathway / positive regulation of bone mineralization / clathrin-coated pit / protein tyrosine kinase binding / cellular response to starvation / basal plasma membrane / caveola / negative regulation of smooth muscle cell proliferation / adherens junction / negative regulation of cell growth / cellular response to growth factor stimulus / osteoblast differentiation / regulation of cell population proliferation / postsynaptic density / receptor complex / cadherin binding / apical plasma membrane / axon / phosphorylation / dendrite / neuronal cell body / positive regulation of gene expression / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / nucleoplasm / ATP binding / metal ion binding / plasma membrane
Similarity search - Function
Activin types I and II receptor domain / Activin types I and II receptor domain / Ser/Thr protein kinase, TGFB receptor / Snake toxin-like superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase domain / Protein kinase, ATP binding site ...Activin types I and II receptor domain / Activin types I and II receptor domain / Ser/Thr protein kinase, TGFB receptor / Snake toxin-like superfamily / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / Bone morphogenetic protein receptor type-2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsChaikuad, A. / Thangaratnarajah, C. / Roos, A.K. / Filippakopoulos, P. / Salah, E. / Phillips, C. / Keates, T. / Fedorov, O. / Chalk, R. / Petrie, K. ...Chaikuad, A. / Thangaratnarajah, C. / Roos, A.K. / Filippakopoulos, P. / Salah, E. / Phillips, C. / Keates, T. / Fedorov, O. / Chalk, R. / Petrie, K. / Pike, A.C.W. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Weigelt, J. / Bountra, C. / Knapp, S. / Bullock, A. / Structural Genomics Consortium (SGC)
CitationJournal: Sci Rep / Year: 2019
Title: Structural consequences of BMPR2 kinase domain mutations causing pulmonary arterial hypertension.
Authors: Chaikuad, A. / Thangaratnarajah, C. / von Delft, F. / Bullock, A.N.
History
DepositionJan 31, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 17, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Jan 31, 2018Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.3Apr 17, 2019Group: Data collection / Derived calculations / Experimental preparation
Category: exptl_crystal_grow / struct_conn
Item: _exptl_crystal_grow.pdbx_details / _exptl_crystal_grow.temp / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Dec 18, 2019Group: Database references / Category: citation / struct_ref_seq_dif
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _struct_ref_seq_dif.details
Revision 1.5Sep 6, 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 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.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.pdbx_dist_value / _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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Bone morphogenetic protein receptor type-2
B: Bone morphogenetic protein receptor type-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,89512
Polymers77,5512
Non-polymers1,34310
Water2,198122
1
A: Bone morphogenetic protein receptor type-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5097
Polymers38,7761
Non-polymers7346
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Bone morphogenetic protein receptor type-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3855
Polymers38,7761
Non-polymers6104
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)94.540, 218.793, 44.187
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11B-82-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Bone morphogenetic protein receptor type-2 / Bone morphogenetic protein receptor type II / BMP type II receptor / BMPR-II


Mass: 38775.547 Da / Num. of mol.: 2 / Fragment: UNP residues 189-517, protein kinase domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BMPR2, PPH1 / Plasmid: pNIC-CH / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3
References: UniProt: Q13873, receptor protein serine/threonine kinase

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Non-polymers , 5 types, 132 molecules

#2: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 122 / 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: 2.95 Å3/Da / Density % sol: 58.25 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 0.3M ammonium_sulfate, 25% w/v PEG 8000, 0.1M Cacodylate pH6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 7, 2008 / Details: Dynamically bendable mirror
RadiationMonochromator: LN2 cooled fixed-exit Si(111) monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.35→47.35 Å / Num. all: 39276 / Num. obs: 39276 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 2 / Redundancy: 5.5 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 8.5
Reflection shellResolution: 2.35→2.47 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.677 / Mean I/σ(I) obs: 2.1 / Num. unique all: 5592 / % possible all: 100

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Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.5.0055refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2QLU

2qlu


Resolution: 2.35→47.35 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.919 / SU B: 15.057 / SU ML: 0.171 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 2 / ESU R: 0.275 / ESU R Free: 0.219 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24649 1976 5 %RANDOM
Rwork0.20785 ---
obs0.20978 37363 99.92 %-
all-39276 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.827 Å2
Baniso -1Baniso -2Baniso -3
1--0.56 Å20 Å20 Å2
2---1.67 Å20 Å2
3---2.22 Å2
Refine analyzeLuzzati coordinate error obs: 0.47 Å
Refinement stepCycle: LAST / Resolution: 2.35→47.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4910 0 82 122 5114
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0225114
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2951.9796907
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.8695610
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.88323.373255
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.44815891
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.7791549
X-RAY DIFFRACTIONr_chiral_restr0.090.2744
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213862
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5891.53033
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.09324888
X-RAY DIFFRACTIONr_scbond_it1.81932081
X-RAY DIFFRACTIONr_scangle_it2.394.52016
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Auth asym-IDNumberTypeRms dev position (Å)Weight position
A275tight positional0.290.05
A483medium positional0.630.5
A57loose positional0.25
B275tight thermal0.660.5
B483medium thermal0.752
B57loose thermal0.6310
LS refinement shellResolution: 2.35→2.411 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.326 155 -
Rwork0.29 2683 -
obs--99.79 %
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)
18.0131-2.9312-2.057912.07511.76447.16840.1993-0.5550.760.27570.0325-0.5908-0.94190.0545-0.23180.3113-0.0276-0.0490.0529-0.07820.256479.69975.41938.131
24.3056-0.9405-0.87898.8881-1.67347.02810.0094-0.16950.6630.0518-0.0473-0.6238-0.3084-0.13210.03790.3326-0.049-0.03660.0306-0.06590.428580.5672.28231.973
32.456-0.39090.0486.57671.4551.7440.0482-0.14520.4174-0.3288-0.18690.5207-0.3724-0.27230.13870.26450.0512-0.04390.054-0.02580.208869.44965.48826.603
411.84578.2804-4.06019.1157-3.80562.05060.0051-0.00510.6459-0.19110.0094-0.2835-0.2561-0.1731-0.01450.38110.07560.02630.11390.00030.379679.5380.34629.238
51.853-1.4159-0.04944.304-0.32141.40080.0621-0.27040.03020.40740.00560.1069-0.0505-0.0793-0.06780.2004-0.0560.02490.064-0.01250.023675.19854.93734.435
66.6188-1.29350.59934.08240.35651.53830.4550.31040.2518-0.5419-0.3590.40970.0293-0.1512-0.0960.2918-0.0071-0.04220.071-0.01170.100767.44959.2821.004
74.0372-0.29291.95724.8949-0.40226.17980.01630.15180.2097-0.1929-0.1795-0.0829-0.5317-0.07360.16330.24950.01460.02460.023-0.01530.101974.66158.8526.947
86.81261.9568-0.32917.195.42757.08480.27680.31970.2923-0.8889-0.2521-0.5394-0.28730.1042-0.02470.39240.09340.17190.1670.1190.210786.01351.94618.317
90.0066-0.0365-0.14280.61892.30029.4417-0.04580.0313-0.0024-0.3443-0.11050.1201-0.74510.20.15641.12080.1566-0.08730.6366-0.03790.354777.15350.9637.763
101.8267-1.88210.01023.7425-1.56794.3810.1320.0426-0.1428-0.1969-0.0569-0.11530.1259-0.045-0.07510.2548-0.0414-0.01960.02890.0030.138179.5745.70927.168
115.85142.4103-2.06310.1708-5.418411.9091-0.0151-0.5265-0.32660.7951-0.1911-0.94370.21870.53370.20620.17480.0301-0.0890.12530.03090.104888.73940.96838.567
129.3590.30582.02679.7336-0.97852.56570.34260.37770.1878-0.7282-0.2477-0.85770.19880.5605-0.09490.1750.05720.17360.1256-0.00440.220592.88345.80119.503
1318.4709-1.74794.55564.9444-1.523114.82490.008-0.5989-1.18910.0487-0.0287-0.05221.2264-0.31870.02070.2883-0.02470.00680.17670.07880.332785.41631.83132.825
142.3960.4029-1.24547.0821-2.01381.21050.05080.2121-0.6861-0.7007-0.29110.08980.3351-0.04280.24020.441-0.0111-0.09470.0996-0.05610.32676.78136.83523.516
153.01740.3755-2.576111.8814-8.274212.89030.0242-0.1315-0.47920.15230.11910.48410.4544-0.2197-0.14330.1582-0.0774-0.0090.0609-0.01550.264767.93738.85233.061
167.2354-4.8324-3.002514.4197-0.51378.8871-0.4425-0.0206-0.2241.0970.4120.42360.54250.04110.03050.336-0.078-0.03740.08150.04010.683455.448-12.20334.183
173.97130.2865-0.73838.99822.38981.5787-0.2185-0.0769-0.77940.86960.075-0.50250.91140.15190.14350.75150.09120.1560.04190.04651.359560.697-11.24528.48
181.83783.0543-1.42375.2671-3.28028.91240.41590.1515-1.02020.85680.1242-1.52360.59320.9677-0.54010.79730.2978-0.12410.2628-0.01892.02871.754-4.80630.67
197.44677.0295.259110.48154.7879.89790.1705-0.0818-0.08920.4483-0.4104-0.23090.41950.45830.23990.45440.0460.01170.0867-0.04610.678858.107-19.19726.42
200.81912.59220.01828.96171.17522.56330.1653-0.1281-0.43780.9587-0.295-1.06390.30990.17510.12980.4915-0.0306-0.00040.07330.20080.871462.4179.6835.243
2117.0494-4.26781.51563.2026-0.08670.70540.07430.24140.13180.02840.023-0.72070.3240.4409-0.09730.52710.08530.16860.3974-0.06890.863279.0071.06321.926
224.20172.88130.51029.81050.94313.67060.0407-0.0597-0.5454-0.01290.2577-0.50250.0248-0.4379-0.29840.3938-0.08220.07310.0850.01650.775759.8944.82728.951
232.8544-0.07761.94329.08193.16089.5968-0.1352-0.0614-0.53170.2857-0.0771-0.44270.34530.49050.21230.3598-0.05-0.00510.06410.07660.868665.0452.31429.308
246.3303-1.12360.52981.7354-1.12072.6287-0.15071.3529-0.6591-0.9987-0.021-0.64990.49030.43260.17170.9435-0.19620.30790.4446-0.28221.150865.1137.08311.432
252.79131.4037-0.66773.9195-0.07326.92-0.2870.0097-0.523-0.37460.184-0.3298-0.10560.250.1030.3865-0.0960.05950.03910.03440.724560.96814.89224.868
266.83643.99364.01946.43792.990810.6586-0.2296-0.46980.18940.0623-0.31950.7693-0.4144-0.62430.54910.24620.03580.02830.05330.0190.587749.21219.14930.37
2710.15652.98680.281610.0281-0.94587.8847-0.17871.0736-0.3427-1.17160.35250.0708-0.4124-0.212-0.17380.5138-0.0983-0.06150.1567-0.08350.440950.12314.00211.456
282.05212.63792.33975.56790.84244.986-0.5881-0.28490.4172-0.488-0.06810.3848-1.1717-0.41960.65620.611-0.1084-0.030.2977-0.04690.788555.15528.18327.165
291.33633.18690.93517.76382.27780.7179-0.55480.2377-0.1896-1.15670.4325-0.2461-0.39380.20860.12220.6412-0.23970.08860.3220.12411.056866.54322.07722.276
304.8897-4.5898-0.211614.71586.2186.607-0.1862-0.3413-0.32990.51930.14730.1817-0.10930.2780.03890.3453-0.17040.01840.14680.09460.462267.2526.65937.422
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A198 - 211
2X-RAY DIFFRACTION2A212 - 238
3X-RAY DIFFRACTION3A239 - 259
4X-RAY DIFFRACTION4A260 - 273
5X-RAY DIFFRACTION5A274 - 319
6X-RAY DIFFRACTION6A320 - 336
7X-RAY DIFFRACTION7A337 - 376
8X-RAY DIFFRACTION8A377 - 387
9X-RAY DIFFRACTION9A388 - 398
10X-RAY DIFFRACTION10A399 - 422
11X-RAY DIFFRACTION11A423 - 435
12X-RAY DIFFRACTION12A436 - 461
13X-RAY DIFFRACTION13A462 - 468
14X-RAY DIFFRACTION14A469 - 493
15X-RAY DIFFRACTION15A494 - 509
16X-RAY DIFFRACTION16B200 - 213
17X-RAY DIFFRACTION17B214 - 245
18X-RAY DIFFRACTION18B246 - 264
19X-RAY DIFFRACTION19B265 - 279
20X-RAY DIFFRACTION20B280 - 316
21X-RAY DIFFRACTION21B317 - 332
22X-RAY DIFFRACTION22B333 - 342
23X-RAY DIFFRACTION23B343 - 356
24X-RAY DIFFRACTION24B357 - 399
25X-RAY DIFFRACTION25B400 - 421
26X-RAY DIFFRACTION26B422 - 440
27X-RAY DIFFRACTION27B441 - 458
28X-RAY DIFFRACTION28B459 - 470
29X-RAY DIFFRACTION29B471 - 498
30X-RAY DIFFRACTION30B499 - 513

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