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- PDB-6g3w: Crystal structure of the BIR3 - SERK2 complex from Arabidopsis th... -

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Basic information

Entry
Database: PDB / ID: 6g3w
TitleCrystal structure of the BIR3 - SERK2 complex from Arabidopsis thaliana.
Components
  • Probable inactive receptor kinase At1g27190
  • Somatic embryogenesis receptor kinase 2
KeywordsPROTEIN BINDING / leucine rich repeat receptor / membrane receptor / pseudokinase / ectodomain / receptor complex / negative regulator
Function / homology
Function and homology information


microsporogenesis / pollen maturation / brassinosteroid mediated signaling pathway / receptor serine/threonine kinase binding / non-specific serine/threonine protein kinase / protein kinase activity / phosphorylation / protein phosphorylation / protein serine kinase activity / signaling receptor binding ...microsporogenesis / pollen maturation / brassinosteroid mediated signaling pathway / receptor serine/threonine kinase binding / non-specific serine/threonine protein kinase / protein kinase activity / phosphorylation / protein phosphorylation / protein serine kinase activity / signaling receptor binding / protein serine/threonine kinase activity / lipid binding / ATP binding / nucleus / plasma membrane
Similarity search - Function
Leucine-rich repeat-containing N-terminal, plant-type / Leucine rich repeat N-terminal domain / Leucine Rich repeat / Leucine Rich Repeat / Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / Alpha-Beta Horseshoe / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Protein tyrosine and serine/threonine kinase ...Leucine-rich repeat-containing N-terminal, plant-type / Leucine rich repeat N-terminal domain / Leucine Rich repeat / Leucine Rich Repeat / Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) / Ribonuclease Inhibitor / Alpha-Beta Horseshoe / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Probable inactive receptor kinase At1g27190 / Somatic embryogenesis receptor kinase 2
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsHothorn, M. / Hohmann, U.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_176237 Switzerland
CitationJournal: Nat Plants / Year: 2018
Title: The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling.
Authors: Hohmann, U. / Nicolet, J. / Moretti, A. / Hothorn, L.A. / Hothorn, M.
History
DepositionMar 26, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 4, 2018Provider: repository / Type: Initial release
Revision 1.1May 16, 2018Group: Data collection / Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Sep 5, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 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 / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Somatic embryogenesis receptor kinase 2
B: Probable inactive receptor kinase At1g27190
C: Somatic embryogenesis receptor kinase 2
D: Probable inactive receptor kinase At1g27190
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,93815
Polymers90,2084
Non-polymers2,73111
Water2,576143
1
A: Somatic embryogenesis receptor kinase 2
B: Probable inactive receptor kinase At1g27190
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,8888
Polymers45,1042
Non-polymers1,7846
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Somatic embryogenesis receptor kinase 2
D: Probable inactive receptor kinase At1g27190
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,0517
Polymers45,1042
Non-polymers9475
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)50.184, 52.155, 308.892
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12B
22D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNPROPROAA30 - 2123 - 185
21ASNASNPROPROCC30 - 2123 - 185
12ASPASPGLYGLYBB26 - 2122 - 188
22ASPASPGLYGLYDD26 - 2122 - 188

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Somatic embryogenesis receptor kinase 2 / AtSERK2 / Somatic embryogenesis receptor-like kinase 2


Mass: 23975.844 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: SERK2, At1g34210, F23M19.11 / Plasmid: pfastbac / Cell line (production host): Tnao38 / Production host: Trichoplusia ni (cabbage looper)
References: UniProt: Q9XIC7, non-specific serine/threonine protein kinase
#2: Protein Probable inactive receptor kinase At1g27190


Mass: 21127.969 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At1g27190, T7N9.25 / Plasmid: pfastbac / Cell line (production host): Tnao38 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O04567

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Sugars , 2 types, 8 molecules

#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
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

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Non-polymers , 3 types, 146 molecules

#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 143 / 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: 2.4 Å3/Da / Density % sol: 48.65 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 25% (w/v) PEG 3,350, 0.2 M MgCl_2 x 6H_2O, 0.1 M Bis-Tris pH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.000027 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Feb 2, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.000027 Å / Relative weight: 1
ReflectionResolution: 2.2→49.41 Å / Num. obs: 42439 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 13 % / Biso Wilson estimate: 54 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.115 / Rsym value: 0.111 / Net I/σ(I): 17
Reflection shellResolution: 2.2→2.33 Å / Redundancy: 13 % / Mean I/σ(I) obs: 1.4 / Num. unique obs: 6697 / CC1/2: 0.71 / Rrim(I) all: 1.67 / Rsym value: 1.604 / % possible all: 99.7

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Processing

Software
NameVersionClassification
REFMAC5.8.0218refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6fg8, 4z61

6fg8

4z61


Resolution: 2.2→49.41 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.937 / SU B: 16.233 / SU ML: 0.192 / Cross valid method: THROUGHOUT / ESU R: 0.292 / ESU R Free: 0.214 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2481 2122 5 %RANDOM
Rwork0.21698 ---
obs0.21852 40314 99.93 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 61.234 Å2
Baniso -1Baniso -2Baniso -3
1-1.21 Å20 Å20 Å2
2--1.96 Å2-0 Å2
3----3.17 Å2
Refinement stepCycle: 1 / Resolution: 2.2→49.41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5634 0 176 143 5953
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0195934
X-RAY DIFFRACTIONr_bond_other_d0.0010.025445
X-RAY DIFFRACTIONr_angle_refined_deg1.4342.0258093
X-RAY DIFFRACTIONr_angle_other_deg0.808312756
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9575744
X-RAY DIFFRACTIONr_dihedral_angle_2_deg43.42725.641234
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.1715977
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.8231529
X-RAY DIFFRACTIONr_chiral_restr0.0740.2972
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0216481
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021042
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_it1.2143.4162982
X-RAY DIFFRACTIONr_mcbond_other1.2143.4162981
X-RAY DIFFRACTIONr_mcangle_it1.9775.1173721
X-RAY DIFFRACTIONr_mcangle_other1.9765.1173722
X-RAY DIFFRACTIONr_scbond_it1.6683.7792952
X-RAY DIFFRACTIONr_scbond_other1.6683.782953
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.7855.6184372
X-RAY DIFFRACTIONr_long_range_B_refined6.07167.11624038
X-RAY DIFFRACTIONr_long_range_B_other6.06867.08424012
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A56220.11
12C56220.11
21B52660.13
22D52660.13
LS refinement shellResolution: 2.2→2.257 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.356 154 -
Rwork0.361 2928 -
obs--99.32 %
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)
17.55140.23612.8342.8573-1.15336.51460.07270.50620.2271-0.73880.14840.0915-0.31310.2643-0.22110.3073-0.09080.03060.17660.05520.1157-1.934522.0522119.1556
25.92181.5582.29653.1157-0.38384.992-0.11420.67240.4622-0.35790.1463-0.2464-0.63980.6453-0.03210.2283-0.05640.08280.12590.01280.12531.343220.7859125.6341
34.89691.34930.73612.40441.02873.07490.08140.3301-0.2313-0.03850.0489-0.21930.22490.1204-0.13040.0480.0158-0.00780.0375-0.02510.0359-8.53237.6766127.416
48.3371.4588-1.60852.0773.27037.31440.2409-0.7558-1.00150.3338-0.1507-0.35640.44830.0324-0.09020.2394-0.0249-0.07820.12820.03950.1908-11.34031.5286136.5994
56.67871.1409-0.35396.4194-1.72645.01060.0502-0.2951-0.640.2358-0.0110.41070.8771-0.7241-0.03930.2255-0.112-0.00230.201-0.03280.1466-22.8121-1.1188133.6574
63.71430.25421.63652.77893.187317.4168-0.19020.18190.1633-0.2620.18520.064-0.3397-0.07920.00490.07650.00890.01920.1035-0.01250.2253-24.574419.898153.2013
71.4650.8622-0.20193.28010.73076.8695-0.03140.07340.2759-0.27720.10040.051-0.6054-0.2458-0.0690.06940.0202-0.00350.0416-0.02750.1397-17.340119.6451150.8444
81.78150.1180.23122.1189-0.54034.4822-0.13730.0079-0.0196-0.08860.0765-0.00380.4082-0.18880.06070.0555-0.02570.02710.0196-0.03450.1007-22.34163.4936158.4984
912.46677.1675-4.60448.7191-3.88694.85080.1418-0.2529-0.91020.3-0.1686-0.32520.5079-0.47220.02690.4304-0.0339-0.00070.2118-0.02530.3301-19.8993-8.7858150.926
102.71-0.3215-2.32584.6295-2.04458.5495-0.02410.1532-0.702-0.5231-0.0523-0.140.90060.3030.07630.38170.0685-0.0110.0432-0.07820.3663-17.7231-12.1033162.5051
119.6291.1414-0.964711.68080.91893.98270.26020.0955-0.87590.4307-0.3963-0.14290.4772-0.3420.13610.35170.01980.01660.09420.02090.3592-16.2928-17.4251168.6596
123.72680.10511.34086.2874-1.12482.4562-0.0284-0.0398-0.34780.01480.14740.11330.3539-0.0727-0.1190.2452-0.01190.01080.2904-0.02940.2243-26.5981-9.4112112.0342
132.40370.638-1.41354.79793.7158.4248-0.08350.1375-0.2370.1414-0.04960.53880.7153-0.58350.13310.1354-0.1203-0.04050.5071-0.06130.2873-34.0106-5.9488108.754
142.5131.72830.39554.3772.10376.2063-0.10450.4188-0.066-0.03330.03740.09520.35-0.44870.06710.0657-0.072-0.04130.3592-0.0120.0653-22.43670.3847105.3405
152.91551.4294-3.71216.013.03629.2129-0.0668-0.0104-0.4780.49530.028-0.83880.62750.15090.03880.23780.0357-0.04440.3703-0.07170.161-9.4236-0.4257102.7146
165.16283.3012-2.3385.9694-1.6226.8231-0.22630.92820.0415-0.84290.6087-0.5846-1.29950.496-0.38240.5586-0.23610.14720.5366-0.03820.1772-10.371210.092197.7121
176.89864.66271.951110.42164.99062.43230.9461-0.28190.66690.6465-0.7699-0.35270.1381-0.3255-0.17620.8518-0.1208-0.14020.75420.06570.3983-4.631915.2185100.5037
1810.6607-0.0536.82913.54193.91388.80230.1419-0.1168-0.10030.065-0.21640.22370.2479-0.22150.07450.41620.026-0.01890.43850.0030.3697-27.960520.611474.9585
196.2726-0.4829-0.01950.5168-1.58035.99040.01160.0610.11940.23530.1250.1466-0.5304-0.5074-0.13670.50950.06020.01620.7280.08130.3485-30.467314.121181.1608
204.20570.61591.55710.42660.655510.70720.2093-0.072-0.0920.3120.0909-0.01550.00150.1224-0.30030.26650.0901-0.00610.39160.11550.285-22.349615.264875.6842
213.5808-0.78840.0740.568-1.08174.74150.1631-0.16850.40050.3675-0.1877-0.1134-0.63670.63070.02460.5737-0.1205-0.03470.64110.18330.266-12.417818.300274.9467
222.59662.05871.01051.91481.23446.48920.24680.0032-0.06050.3443-0.0978-0.37080.45750.8184-0.14890.51550.03120.00690.8460.190.4683-0.295313.318568.7428
231.89130.9828-2.88660.9139-2.52877.0322-0.0657-0.123-0.82710.1092-0.2812-0.071-0.29220.71970.34690.5283-0.00570.06060.82320.0350.750910.32099.012861.187
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A26 - 52
2X-RAY DIFFRACTION2A53 - 89
3X-RAY DIFFRACTION3A90 - 164
4X-RAY DIFFRACTION4A165 - 176
5X-RAY DIFFRACTION5A177 - 213
6X-RAY DIFFRACTION6B25 - 37
7X-RAY DIFFRACTION7B38 - 76
8X-RAY DIFFRACTION8B77 - 165
9X-RAY DIFFRACTION9B166 - 173
10X-RAY DIFFRACTION10B174 - 196
11X-RAY DIFFRACTION11B197 - 213
12X-RAY DIFFRACTION12C30 - 39
13X-RAY DIFFRACTION13C40 - 71
14X-RAY DIFFRACTION14C72 - 135
15X-RAY DIFFRACTION15C136 - 144
16X-RAY DIFFRACTION16C145 - 207
17X-RAY DIFFRACTION17C208 - 214
18X-RAY DIFFRACTION18D30 - 38
19X-RAY DIFFRACTION19D39 - 71
20X-RAY DIFFRACTION20D72 - 91
21X-RAY DIFFRACTION21D92 - 153
22X-RAY DIFFRACTION22D154 - 204
23X-RAY DIFFRACTION23D205 - 213

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