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- PDB-2w73: High-resolution structure of the complex between calmodulin and a... -

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Basic information

Entry
Database: PDB / ID: 2w73
TitleHigh-resolution structure of the complex between calmodulin and a peptide from calcineurin A
Components
  • CALMODULIN
  • SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
KeywordsMETAL BINDING PROTEIN / METAL-BINDING PROTEIN / PROTEIN PHOSPHATASE / ALTERNATIVE SPLICING / PHOSPHOPROTEIN / UBL CONJUGATION / CALMODULIN-BINDING / CALCIUM / HYDROLASE / CALMODULIN / ACETYLATION / METHYLATION / POLYMORPHISM / METAL-BINDING / ZINC / IRON / DIMER / EF HAND / NUCLEUS
Function / homology
Function and homology information


negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress / positive regulation of calcium ion import across plasma membrane / calmodulin-dependent protein phosphatase activity / calcineurin complex ...negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress / positive regulation of calcium ion import across plasma membrane / calmodulin-dependent protein phosphatase activity / calcineurin complex / positive regulation of connective tissue replacement / negative regulation of dendrite morphogenesis / calcineurin-mediated signaling / slit diaphragm / protein serine/threonine phosphatase complex / peptidyl-serine dephosphorylation / renal filtration / calcineurin-NFAT signaling cascade / skeletal muscle tissue regeneration / : / transition between fast and slow fiber / positive regulation of calcineurin-NFAT signaling cascade / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / cardiac muscle hypertrophy in response to stress / positive regulation of osteoclast differentiation / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / dendrite morphogenesis / Calmodulin induced events / regulation of synaptic vesicle endocytosis / Reduction of cytosolic Ca++ levels / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / positive regulation of cyclic-nucleotide phosphodiesterase activity / regulation of synaptic vesicle exocytosis / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / CLEC7A (Dectin-1) induces NFAT activation / cyclosporin A binding / myosin phosphatase activity / extrinsic component of plasma membrane / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / regulation of cardiac muscle cell action potential / Activation of RAC1 downstream of NMDARs / response to corticosterone / protein serine/threonine phosphatase activity / postsynaptic modulation of chemical synaptic transmission / positive regulation of DNA binding / protein-serine/threonine phosphatase / positive regulation of ryanodine-sensitive calcium-release channel activity / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of peptidyl-threonine phosphorylation / Synthesis of IP3 and IP4 in the cytosol / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of activated T cell proliferation / dephosphorylation / Phase 0 - rapid depolarisation / negative regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / RHO GTPases activate PAKs / positive regulation of endocytosis / : / Ion transport by P-type ATPases / Long-term potentiation / Uptake and function of anthrax toxins / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / adenylate cyclase binding / catalytic complex / positive regulation of cell adhesion / DARPP-32 events / detection of calcium ion / regulation of cardiac muscle contraction / regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / epidermis development / cellular response to interferon-beta / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / negative regulation of insulin secretion / positive regulation of osteoblast differentiation / multicellular organismal response to stress / Protein methylation / phosphatidylinositol 3-kinase binding / eNOS activation / skeletal muscle fiber development / enzyme regulator activity / activation of adenylate cyclase activity
Similarity search - Function
PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / : / EF-hand domain pair ...PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair
Similarity search - Domain/homology
Calmodulin-1 / Calmodulin-3 / Protein phosphatase 3 catalytic subunit alpha
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsMajava, V. / Kursula, P.
CitationJournal: Plos One / Year: 2009
Title: Domain Swapping and Different Oligomeric States for the Complex between Calmodulin and the Calmodulin-Binding Domain of Calcineurin A
Authors: Majava, V. / Kursula, P.
History
DepositionDec 19, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 12, 2009Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Advisory / Data collection / Category: diffrn_source / pdbx_unobs_or_zero_occ_atoms / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4May 8, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_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.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_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_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_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: CALMODULIN
B: CALMODULIN
E: CALMODULIN
F: CALMODULIN
K: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
L: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
M: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
O: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,07028
Polymers75,2688
Non-polymers80220
Water6,125340
1
A: CALMODULIN
B: CALMODULIN
K: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
L: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,07515
Polymers37,6344
Non-polymers44111
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6890 Å2
ΔGint-43.9 kcal/mol
Surface area21650 Å2
MethodPQS
2
E: CALMODULIN
F: CALMODULIN
M: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
O: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,99513
Polymers37,6344
Non-polymers3619
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7140 Å2
ΔGint-48.2 kcal/mol
Surface area20830 Å2
MethodPQS
Unit cell
Length a, b, c (Å)65.310, 81.320, 71.190
Angle α, β, γ (deg.)90.00, 111.28, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
CALMODULIN / CAM


Mass: 16852.545 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETCM / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P62158, UniProt: P0DP23*PLUS
#2: Protein/peptide
SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT ALPHA ISOFORM / CALMODULIN-DEPENDENT CALCINEURIN A SUBUNIT ALPHA ISOFORM / CAM-PRP CATALYTIC SUBUNIT


Mass: 1964.449 Da / Num. of mol.: 4 / Fragment: CALMODULIN BINDING DOMAIN, RESIDUES 385-411 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human)
References: UniProt: Q08209, protein-serine/threonine phosphatase
#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: Ca
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 340 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.1 Å3/Da / Density % sol: 40.1 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.45→20 Å / Num. obs: 115319 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 8.9
Reflection shellResolution: 1.45→1.49 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 2.7 / % possible all: 98.7

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Processing

Software
NameVersionClassification
REFMAC5.4.0077refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.45→10 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.958 / SU B: 4.095 / SU ML: 0.068 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.074 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.217 6070 5 %RANDOM
Rwork0.186 ---
obs0.187 115319 99.3 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 10.28 Å2
Baniso -1Baniso -2Baniso -3
1--1.91 Å20 Å20.55 Å2
2--3.89 Å20 Å2
3----1.58 Å2
Refinement stepCycle: LAST / Resolution: 1.45→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5127 0 20 340 5487
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0225944
X-RAY DIFFRACTIONr_bond_other_d0.0010.024077
X-RAY DIFFRACTIONr_angle_refined_deg1.7991.9617933
X-RAY DIFFRACTIONr_angle_other_deg4.0239989
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.3935785
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.1125.108323
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.147151169
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.6241545
X-RAY DIFFRACTIONr_chiral_restr0.1280.2847
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.026794
X-RAY DIFFRACTIONr_gen_planes_other0.0030.021239
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_it2.3932169
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.5254272
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.7997110
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it6.32810101
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.45→1.49 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.302 436
Rwork0.296 8287
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)
13.5058-1.248-1.68391.90850.55154.47430.03130.2377-0.0962-0.1637-0.0562-0.17160.22210.25890.02490.39760.0189-0.03530.1555-0.0090.3799-10.821-9.12522.55
21.1395-0.31880.11160.9812-0.56111.8894-0.0392-0.1649-0.00680.09780.00920.0135-0.0073-0.0440.030.36530.0162-0.03150.128-0.00170.3412-17.435-0.99334.154
310.90994.8164.26942.26391.95241.7040.1243-0.1183-0.24430.14670.0066-0.18050.07850.1424-0.13090.31830.0038-0.00830.26030.00110.31180.4976.67330.069
47.10941.4903-5.1233.3586-2.10144.4925-0.0561-0.08110.2614-0.1180.1135-0.1497-0.0605-0.3473-0.05740.37430.0197-0.04680.1485-0.06860.351218.42718.77134.894
54.1268-0.8151-2.07354.56780.60124.16010.1822-0.25310.4957-0.123-0.0479-0.0289-0.4029-0.1994-0.13420.41320.0152-0.02340.099-0.06020.4289.13724.33737.026
66.1561-1.538-0.504814.53371.24285.6657-0.05690.1964-0.0610.0147-0.04280.239-0.0318-0.52340.09970.3364-0.0269-0.01230.3605-0.02560.322611.4949.90426.186
713.36350.80455.4352.782-0.18514.5678-0.0548-0.10840.2294-0.1636-0.0270.4334-0.1051-0.56810.08180.34310.0169-0.00110.2776-0.00320.32049.6138.20314.05
83.06560.00260.68291.43240.49351.9034-0.00460.0303-0.0340.02860.0296-0.05540.0345-0.1028-0.0250.3671-0.0071-0.01680.0742-0.0110.357525.0742.7819.746
94.27263.1702-6.91512.4589-5.159911.19980.0770.13820.08650.0660.0581-0.0041-0.249-0.1269-0.1350.3143-0.004-0.01880.22610.00720.32618.324-6.06127.86
106.1396-2.09910.91614.6018-0.3370.33440.0179-0.0096-0.0845-0.06460.02630.2966-0.02290.052-0.04410.40510.0058-0.01980.07640.0060.3561-3.215-16.60343.195
112.50710.84340.41152.13180.22620.4123-0.00380.12290.0474-0.1316-0.03210.05830.0167-0.04380.0360.38410.0101-0.02780.07260.01330.36993.559-22.87437.983
126.3002-3.55190.032416.71932.13345.41490.04740.17910.0573-0.20510.0248-0.2317-0.03790.1353-0.07210.26720.0021-0.0150.25290.03620.2621-2.895-9.37630.945
130.78540.00930.64983.07760.83352.6383-0.0347-0.0072-0.01020.1417-0.13480.1114-0.089-0.11030.16950.41520.0281-0.03520.1220.00080.3652-13.21546.3423.213
1414.3638-1.07824.98220.1316-0.40091.74240.0254-0.1548-0.19760.06260.05380.0230.0380.0017-0.07930.3650.005-0.01720.2722-0.00850.33335.91845.6492.313
154.57390.8504-2.26992.99613.37449.7014-0.02860.0376-0.4219-0.04370.4931-0.6260.17241.034-0.46450.40570.0062-0.06610.3352-0.09280.438227.11546.2747.795
167.43393.9537-7.62353.7002-5.64859.40850.3762-0.09640.37-2.1431-0.11970.5154-1.23260.6896-0.25660.6668-0.14230.05040.5013-0.18360.848532.58952.29-1.263
179.09081.69290.50545.89392.35737.83560.0369-0.41110.6325-0.3809-0.15050.0959-0.92830.33850.11360.4874-0.0519-0.05070.0795-0.05390.339719.91856.6878.026
187.09462.87130.162317.4518-1.26997.4107-0.0714-0.0292-0.08140.07870.06120.1290.0313-0.22950.01020.34070.0083-0.01780.2918-0.05350.307916.44442.917-2.149
194.4403-1.97730.94722.9674-0.94572.1138-0.1625-0.24630.19450.05290.0676-0.0271-0.1662-0.15820.09490.39550.0013-0.02060.12960.00250.370416.92141.563-12.514
202.4550.42881.5543.6271-1.00292.31060.1412-0.1572-0.15420.1925-0.1241-0.22110.1958-0.0252-0.01710.4265-0.0054-0.04140.07090.02840.393923.84127.78-6.579
217.0230.5005-8.76530.0442-0.657811.0672-0.0002-0.09870.01770.0730.04040.06090.01510.0469-0.04020.3295-0.0008-0.00450.21750.01120.31337.04331.678-1.681
223.09230.8562-1.69923.7420.3011.6114-0.03960.154-0.0085-0.21160.01930.27090.0756-0.10580.02030.41730.0103-0.02690.11330.02740.3492-13.34327.35414.829
236.4492.476-2.39478.3286-2.52386.6382-0.09730.2676-0.6728-0.309-0.0107-0.28470.4460.21520.1080.44460.03990.00820.00420.01680.4446-4.08619.17811.662
249.52642.90491.139812.57480.79728.67650.06060.2857-0.0197-0.1185-0.0393-0.00420.06890.007-0.02130.34440.0419-0.00280.27910.03880.2876-6.74734.1963.962
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 25
2X-RAY DIFFRACTION2A26 - 68
3X-RAY DIFFRACTION3A69 - 91
4X-RAY DIFFRACTION4A92 - 116
5X-RAY DIFFRACTION5A117 - 147
6X-RAY DIFFRACTION6K395 - 411
7X-RAY DIFFRACTION7B4 - 18
8X-RAY DIFFRACTION8B19 - 68
9X-RAY DIFFRACTION9B69 - 91
10X-RAY DIFFRACTION10B92 - 114
11X-RAY DIFFRACTION11B115 - 147
12X-RAY DIFFRACTION12L395 - 411
13X-RAY DIFFRACTION13E4 - 68
14X-RAY DIFFRACTION14E69 - 91
15X-RAY DIFFRACTION15E92 - 111
16X-RAY DIFFRACTION16E112 - 122
17X-RAY DIFFRACTION17E123 - 147
18X-RAY DIFFRACTION18M395 - 411
19X-RAY DIFFRACTION19F4 - 21
20X-RAY DIFFRACTION20F22 - 64
21X-RAY DIFFRACTION21F65 - 90
22X-RAY DIFFRACTION22F91 - 125
23X-RAY DIFFRACTION23F126 - 147
24X-RAY DIFFRACTION24O395 - 411

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