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- PDB-2ve7: Crystal structure of a bonsai version of the human Ndc80 complex -

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Basic information

Entry
Database: PDB / ID: 2ve7
TitleCrystal structure of a bonsai version of the human Ndc80 complex
Components
  • KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
  • KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
KeywordsCELL CYCLE / MITOSIS / CENTROMERE / MICROTUBULE / KINETOCHORE / CELL DIVISION / CALPONIN HOMOLOGY
Function / homology
Function and homology information


G2/MI transition of meiotic cell cycle / kinetochore adaptor activity / skeletal muscle satellite cell proliferation / Ndc80 complex / kinetochore organization / metaphase chromosome alignment / positive regulation of mitotic cell cycle spindle assembly checkpoint / meiotic chromosome segregation / attachment of spindle microtubules to kinetochore / centrosome duplication ...G2/MI transition of meiotic cell cycle / kinetochore adaptor activity / skeletal muscle satellite cell proliferation / Ndc80 complex / kinetochore organization / metaphase chromosome alignment / positive regulation of mitotic cell cycle spindle assembly checkpoint / meiotic chromosome segregation / attachment of spindle microtubules to kinetochore / centrosome duplication / outer kinetochore / attachment of mitotic spindle microtubules to kinetochore / spindle assembly involved in female meiosis I / mitotic spindle assembly checkpoint signaling / establishment of mitotic spindle orientation / mitotic sister chromatid segregation / chromosome, centromeric region / cyclin binding / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / chromosome segregation / RHO GTPases Activate Formins / regulation of protein stability / kinetochore / Separation of Sister Chromatids / mitotic cell cycle / microtubule binding / cell division / centrosome / protein-containing complex binding / nucleolus / nucleoplasm / identical protein binding / membrane / nucleus / cytosol
Similarity search - Function
Ncd80 complex, Nuf2 subunit / Ncd80 complex, Spc24 subunit / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1950 / Ncd80 complex, Ncd80 subunit / Chromosome segregation protein Spc25, C-terminal / Kinetochore protein Spc25 / Chromosome segregation protein Spc25 / Kinetochore protein Nuf2, N-terminal / Nuf2, N-terminal domain superfamily / Nuf2 family ...Ncd80 complex, Nuf2 subunit / Ncd80 complex, Spc24 subunit / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1950 / Ncd80 complex, Ncd80 subunit / Chromosome segregation protein Spc25, C-terminal / Kinetochore protein Spc25 / Chromosome segregation protein Spc25 / Kinetochore protein Nuf2, N-terminal / Nuf2, N-terminal domain superfamily / Nuf2 family / Kinetochore protein Ndc80 / Ndc80 domain superfamily / Domain of unknown function DUF5595 / HEC/Ndc80p family / Domain of unknown function (DUF5595) / Kinetochore-Ndc80 subunit Spc24 / Spc24 subunit of Ndc80 / Actin-binding Protein, T-fimbrin; domain 1 / Double Stranded RNA Binding Domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHENOL / Kinetochore protein NDC80 homolog / Kinetochore protein Spc24 / Kinetochore protein Nuf2 / Kinetochore protein Spc25
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.88 Å
AuthorsCiferri, C. / Pasqualato, S. / Dos Reis, G. / Screpanti, E. / Maiolica, A. / Polka, J. / De Luca, J.G. / De Wulf, P. / Salek, M. / Rappsilber, J. ...Ciferri, C. / Pasqualato, S. / Dos Reis, G. / Screpanti, E. / Maiolica, A. / Polka, J. / De Luca, J.G. / De Wulf, P. / Salek, M. / Rappsilber, J. / Moores, C.A. / Salmon, E.D. / Musacchio, A.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2008
Title: Implications for Kinetochore-Microtubule Attachment from the Structure of an Engineered Ndc80 Complex
Authors: Ciferri, C. / Pasqualato, S. / Screpanti, E. / Varetti, G. / Santaguida, S. / Dos Reis, G. / Maiolica, A. / Polka, J. / De Luca, J.G. / De Wulf, P. / Salek, M. / Rappsilber, J. / Moores, C.A. ...Authors: Ciferri, C. / Pasqualato, S. / Screpanti, E. / Varetti, G. / Santaguida, S. / Dos Reis, G. / Maiolica, A. / Polka, J. / De Luca, J.G. / De Wulf, P. / Salek, M. / Rappsilber, J. / Moores, C.A. / Salmon, E.D. / Musacchio, A.
History
DepositionOct 17, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 13, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Refinement description / Version format compliance
Revision 1.2Jun 21, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3May 4, 2022Group: Advisory / Database references / Category: database_2 / database_PDB_caveat
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Jun 19, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
B: KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
C: KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
D: KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,0628
Polymers130,6894
Non-polymers3724
Water39622
1
A: KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
C: KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,5314
Polymers65,3452
Non-polymers1862
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8840 Å2
ΔGint-82.1 kcal/mol
Surface area32980 Å2
MethodPISA
2
B: KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25
D: KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,5314
Polymers65,3452
Non-polymers1862
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10870 Å2
ΔGint-100.2 kcal/mol
Surface area37280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)157.653, 248.965, 58.250
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D
13A
23B
14A
24B
15C
25D
16C
26D
17A
27B

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1115A83 - 191
2115B83 - 191
1125C1133 - 1143
2125D1133 - 1143
1225C1180 - 1192
2225D1180 - 1192
1135A1130 - 1144
2135B1130 - 1144
1145A264 - 284
2145B264 - 284
1155C1159 - 1164
2155D1159 - 1164
1254C1171 - 1176
2254D1171 - 1176
1165C9 - 59
2165D9 - 59
1265C88 - 105
2265D88 - 105
1365C113 - 141
2365D113 - 141
1175A1046 - 1068
2175B1046 - 1068
1275A1072 - 1089
2275B1072 - 1089

NCS ensembles :
ID
1
2
3
4
5
6
7

NCS oper:
IDCodeMatrixVector
1given(-0.9911, 0.1294, -0.02977), (-0.1287, -0.9914, -0.02531), (-0.03279, -0.02126, 0.9992)3.241, -115.8, 27.91
2given(-0.6403, 0.639, 0.4263), (-0.6507, -0.1562, -0.7431), (-0.4082, -0.7532, 0.5158)41.92, -145.9, 6.38
3given(-0.7303, 0.6589, 0.1802), (-0.679, -0.6714, -0.2969), (-0.07462, -0.3392, 0.9378)25.94, -101.3, 11.96
4given(-0.8949, 0.4433, 0.05079), (-0.4353, -0.8424, -0.3176), (-0.09801, -0.3063, 0.9469)18.89, -113.5, 13.25
5given(-0.8875, 0.4449, 0.1196), (-0.4595, -0.8358, -0.3006), (-0.03374, -0.3217, 0.9462)22.69, -111.5, 11.09
6given(-0.6702, 0.5898, 0.4505), (-0.6396, -0.1512, -0.7537), (-0.3764, -0.7933, 0.4786)47.64, -147.6, 3.305
7given(-0.6271, 0.6523, 0.4257), (-0.6619, -0.1583, -0.7327), (-0.4105, -0.7413, 0.531)40.18, -144.1, 7.098
8given(-0.6278, 0.653, 0.4236), (-0.6531, -0.1458, -0.7431), (-0.4235, -0.7432, 0.5181)39.91, -145.9, 6.841
9given(-0.9003, 0.4305, 0.06434), (-0.4298, -0.856, -0.2873), (-0.06859, -0.2863, 0.9557)19.37, -112.9, 13.83
10given(-0.9049, 0.4171, 0.08471), (-0.4234, -0.8618, -0.2794), (-0.04356, -0.2887, 0.9564)19.64, -113, 13.05
11given(-0.9035, 0.4226, 0.07101), (-0.4241, -0.858, -0.29), (-0.06162, -0.2921, 0.9544)19.44, -113.2, 13.26
12given(-0.6752, 0.601, 0.4277), (-0.6349, -0.1783, -0.7518), (-0.3755, -0.7791, 0.5019)46.24, -146.2, 3.969

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Components

#1: Protein KINETOCHORE PROTEIN HEC1, KINETOCHORE PROTEIN SPC25 / NDC80-SPC25 CHIMERA / HSHEC1 / KINETOCHORE-ASSOCIATED PROTEIN 2 / HIGHLY EXPRESSED IN CANCER ...NDC80-SPC25 CHIMERA / HSHEC1 / KINETOCHORE-ASSOCIATED PROTEIN 2 / HIGHLY EXPRESSED IN CANCER PROTEIN / RETINOBLASTOMA-ASSOCIATED PROTEIN HEC / HSPC25


Mass: 36351.297 Da / Num. of mol.: 2
Fragment: CHIMERA OF NDC80 RESIDUES 80-286 WITH SPC25 RESIDUES 118-224
Source method: isolated from a genetically manipulated source
Details: PEPTIDE LINK BETWEEN RESI 286 AND RESI 1118 / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O14777, UniProt: Q9HBM1
#2: Protein KINETOCHORE PROTEIN NUF2, KINETOCHORE PROTEIN SPC24 / NUF2-SPC24 CHIMERA / HNUF2 / HNUF2R / HSNUF2 / CELL DIVISION CYCLE-ASSOCIATED PROTEIN 1 / HSPC24


Mass: 28993.418 Da / Num. of mol.: 2
Fragment: CHIMERA OF NUF2 RESIDUES 1-169 WITH SPC24 RESIDUES 122-197
Mutation: YES
Source method: isolated from a genetically manipulated source
Details: PEPTIDE LINK BETWEEN RESI 169 AND RESI 1122 / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9BZD4, UniProt: Q8NBT2
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-IPH / PHENOL


Mass: 94.111 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H6O
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 22 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN C, GLU 72 TO GLY ENGINEERED RESIDUE IN CHAIN D, GLU 72 TO GLY

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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: 4.62 Å3/Da / Density % sol: 75 % / Description: NONE
Crystal growpH: 7.5
Details: 4.5-6.5 PEG 6000, 1.5-2 MPD, 0.1 M NAHEPES PH 7.5, 16 MM TCEP, 15 MM PHENOL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.954
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 18, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.954 Å / Relative weight: 1
ReflectionResolution: 2.88→50 Å / Num. obs: 52754 / % possible obs: 99.1 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 14.9
Reflection shellResolution: 2.88→3 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 4.2 / % possible all: 99.8

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
SHELXDphasing
SHARPphasing
piratephasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 2.88→50 Å / Cor.coef. Fo:Fc: 0.9 / Cor.coef. Fo:Fc free: 0.88 / SU B: 24.976 / SU ML: 0.225 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.479 / ESU R Free: 0.312 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS CHAIN A AND B ARE CHIMERAS OF NDC80 (RESIDUES 80-286) AND SPC25 (RESIDUES 118-224). FOR CLARITY SPC25 RESIDUES ARE NUMBERED 1118-1224. ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS CHAIN A AND B ARE CHIMERAS OF NDC80 (RESIDUES 80-286) AND SPC25 (RESIDUES 118-224). FOR CLARITY SPC25 RESIDUES ARE NUMBERED 1118-1224. RESIDUE 286 IS FUSED TO RESIDUE 1118 CHAIN C AND D ARE CHIMERAS OF NUF2 (RESIDUES 1- 169) AND SPC24 (RESIDUES 122-197). FOR CLARITY SPC24 RESIDUES ARE NUMBERED 1122-1197. RESIDUE 169 IS FUSED TO RESIDUE 1122 RESIDUES MET 79A, LYS 1122A, ILE 1161A, TRP 211B, ARG 1202B HAVE BEEN BUILT AS ALANINES BECAUSE THERE WAS NO ELECTRON DENSITY FOR THEIR SIDE CHAINS (SEE REMARK 470)
RfactorNum. reflection% reflectionSelection details
Rfree0.261 2647 5 %RANDOM
Rwork0.232 ---
obs0.234 49837 99.1 %-
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: 65.6 Å2
Baniso -1Baniso -2Baniso -3
1-2.95 Å20 Å20 Å2
2---1.26 Å20 Å2
3----1.7 Å2
Refinement stepCycle: LAST / Resolution: 2.88→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8210 0 26 22 8258
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0228428
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3921.9611373
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg11.465998
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.58924.212406
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.519151501
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3621544
X-RAY DIFFRACTIONr_chiral_restr0.2090.21232
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.026351
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2350.23829
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3160.25718
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1620.2221
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2940.2122
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1350.213
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.4491.55051
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.77328161
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.15633377
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.9994.53212
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
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A436medium positional0.161
2C128medium positional0.361
3A60medium positional0.121
4A84medium positional0.261
5C74medium positional0.441
6C392medium positional0.161
7A164medium positional0.211
1A448loose positional0.415
2C145loose positional0.545
3A64loose positional0.655
4A87loose positional0.745
5C22loose positional0.535
6C416loose positional0.455
7A178loose positional0.475
1A436medium thermal0.865
2C128medium thermal1.25
3A60medium thermal1.295
4A84medium thermal0.645
5C74medium thermal1.595
6C392medium thermal1.235
7A164medium thermal0.95
1A448loose thermal1.2210
2C145loose thermal1.5310
3A64loose thermal1.2310
4A87loose thermal1.0310
5C22loose thermal1.4210
6C416loose thermal1.6210
7A178loose thermal1.1610
LS refinement shellResolution: 2.88→2.96 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.407 197 -
Rwork0.328 3548 -
obs--99.26 %
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)
122.409414.11315.506132.93910.691313.4829-0.5592-1.1384-1.4311-1.12350.95820.71030.694-1.8759-0.399-0.065-0.10130.00430.12140.1705-0.086-6.67-75.92418.141
239.35084.23210.807820.0391-6.57213.024-0.3272-2.11271.6878-0.67360.0558-1.6494-1.36591.64140.27150.2544-0.14560.1628-0.0068-0.19840.13575.583-40.735-10.487
34.1488-2.1906-0.824211.91480.77744.5862-0.7811-0.25960.78610.6870.6955-1.2858-0.72620.1540.08560.4550.0415-0.11960.1612-0.4641.0724-2.9491-141.0387
45.62321.1343-0.82186.45480.41073.2618-0.08710.0482-1.1496-0.05820.20440.46250.1721-0.2065-0.1173-0.2987-0.052-0.0399-0.46590.0120.156762.11839.54-74.17
51.60650.71381.73070.42250.59672.5719-0.0240.1771-0.3161-0.04170.2128-0.2353-0.05570.3796-0.1888-0.1254-0.0144-0.02490.0364-0.06870.0936-24.736-75.962-16.148
62.6969-0.4584-1.11960.78840.09071.90630.0810.110.33810.14250.09290.2483-0.2282-0.0631-0.1739-0.1116-0.05620.0886-0.14240.07720.161525.558-43.147-41.752
713.1802-0.4956-5.960760.63131.06735.37891.30920.686-0.5815-1.3421-1.48160.1465-1.385-1.42340.1725-0.03730.15530.1117-0.1126-0.2061-0.0705-18.5231-106.2051
810.51188.8751-4.461624.2302-5.71044.8471-0.3338-0.01660.65580.14450.93091.20750.2383-0.2129-0.5970.0464-0.1524-0.077-0.40370.19830.628940.0742.59-68.496
92.49250.36410.57022.9672-0.21065.655-0.07330.06170.1596-0.1762-0.03240.2091-0.2649-0.16140.1058-0.1496-0.0104-0.01-0.03580.0128-0.1056-4.703-61.10810.06
102.76030.2952-1.13713.3863-0.15386.73520.00670.07120.07760.1702-0.0724-0.0950.1386-0.13270.0657-0.10980.00460.0246-0.0536-0.0106-0.10921.512-54.822-18.839
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A79 - 86
2X-RAY DIFFRACTION2B79 - 86
3X-RAY DIFFRACTION3C1134 - 1193
4X-RAY DIFFRACTION3A1130 - 1147
5X-RAY DIFFRACTION3A1158 - 1161
6X-RAY DIFFRACTION3A1165 - 1170
7X-RAY DIFFRACTION3A1215 - 1221
8X-RAY DIFFRACTION4B1125 - 1188
9X-RAY DIFFRACTION4B1193 - 1224
10X-RAY DIFFRACTION4D1130 - 1197
11X-RAY DIFFRACTION5C4 - 159
12X-RAY DIFFRACTION5A212 - 265
13X-RAY DIFFRACTION6D4 - 152
14X-RAY DIFFRACTION6B213 - 265
15X-RAY DIFFRACTION7A266 - 286
16X-RAY DIFFRACTION8B266 - 286
17X-RAY DIFFRACTION8D153 - 169
18X-RAY DIFFRACTION9A87 - 201
19X-RAY DIFFRACTION10B87 - 202

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