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- PDB-3u7u: Crystal structure of extracellular region of human epidermal grow... -

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Basic information

Entry
Database: PDB / ID: 3u7u
TitleCrystal structure of extracellular region of human epidermal growth factor receptor 4 in complex with neuregulin-1 beta
Components
  • Neuregulin 1
  • Receptor tyrosine-protein kinase erbB-4
KeywordsTRANSFERASE/TRANSFERASE REGULATOR / signaling protein / TRANSFERASE-TRANSFERASE REGULATOR COMPLEX / Glycosylation
Function / homology
Function and homology information


ERBB3 signaling pathway / positive regulation of peptidyl-tyrosine autophosphorylation / sequestering of metal ion / establishment of planar polarity involved in nephron morphogenesis / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / olfactory bulb interneuron differentiation / central nervous system morphogenesis / ventricular cardiac muscle cell differentiation / positive regulation of striated muscle cell differentiation ...ERBB3 signaling pathway / positive regulation of peptidyl-tyrosine autophosphorylation / sequestering of metal ion / establishment of planar polarity involved in nephron morphogenesis / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / olfactory bulb interneuron differentiation / central nervous system morphogenesis / ventricular cardiac muscle cell differentiation / positive regulation of striated muscle cell differentiation / neuregulin receptor activity / negative regulation of secretion / cardiac muscle tissue regeneration / animal organ development / endocardial cell differentiation / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / mitochondrial fragmentation involved in apoptotic process / neural crest cell development / cardiac muscle cell myoblast differentiation / cell communication / GABA receptor binding / PI3K events in ERBB4 signaling / cardiac muscle cell differentiation / mammary gland epithelial cell differentiation / embryonic pattern specification / mammary gland development / chemorepellent activity / ventricular trabecula myocardium morphogenesis / positive regulation of protein localization to cell surface / ErbB-3 class receptor binding / regulation of postsynaptic neurotransmitter receptor internalization / neurotransmitter receptor localization to postsynaptic specialization membrane / ERBB signaling pathway / activation of transmembrane receptor protein tyrosine kinase activity / neural crest cell migration / epidermal growth factor receptor activity / negative regulation of cardiac muscle cell apoptotic process / epidermal growth factor receptor binding / ERBB2 Activates PTK6 Signaling / ERBB2-ERBB3 signaling pathway / transmembrane receptor protein tyrosine kinase activator activity / protein tyrosine kinase activator activity / Signaling by ERBB4 / ERBB2 Regulates Cell Motility / cell surface receptor signaling pathway via JAK-STAT / Long-term potentiation / PI3K events in ERBB2 signaling / positive regulation of cell adhesion / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / SHC1 events in ERBB4 signaling / GABA-ergic synapse / mammary gland alveolus development / cell fate commitment / Nuclear signaling by ERBB4 / positive regulation of tyrosine phosphorylation of STAT protein / positive regulation of cardiac muscle cell proliferation / Signaling by ERBB2 / regulation of cell migration / cellular response to epidermal growth factor stimulus / cell surface receptor protein tyrosine kinase signaling pathway / synapse assembly / Downregulation of ERBB4 signaling / lactation / GRB2 events in ERBB2 signaling / Downregulation of ERBB2:ERBB3 signaling / activation of protein kinase B activity / transmembrane receptor protein tyrosine kinase activity / SHC1 events in ERBB2 signaling / neurogenesis / basal plasma membrane / cytokine activity / transcription coregulator activity / postsynaptic density membrane / Signaling by ERBB2 TMD/JMD mutants / positive regulation of receptor signaling pathway via JAK-STAT / growth factor activity / wound healing / positive regulation of protein-containing complex assembly / neuromuscular junction / Signaling by ERBB2 KD Mutants / receptor protein-tyrosine kinase / receptor tyrosine kinase binding / Downregulation of ERBB2 signaling / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / cell migration / integrin binding / PIP3 activates AKT signaling / presynaptic membrane / nervous system development / heart development / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / positive regulation of cell growth / basolateral plasma membrane / postsynaptic membrane / protein tyrosine kinase activity / Estrogen-dependent gene expression / cell population proliferation
Similarity search - Function
Neuregulin, C-terminal / Neuregulin-1 / Neuregulin / Neuregulin intracellular region / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment ...Neuregulin, C-terminal / Neuregulin-1 / Neuregulin / Neuregulin intracellular region / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Alpha-Beta Horseshoe / Laminin / Laminin / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / EGF-like domain / Furin-like repeat / Furin-like repeats / Immunoglobulin I-set / Immunoglobulin I-set domain / Epidermal growth factor-like domain. / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Ribbon / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Pro-neuregulin-1, membrane-bound isoform / Receptor tyrosine-protein kinase erbB-4 / Neuregulin 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.03 Å
AuthorsLiu, P. / Cleveland IV, T.E. / Bouyain, S. / Longo, P.A. / Leahy, D.J.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2012
Title: A single ligand is sufficient to activate EGFR dimers.
Authors: Liu, P. / Cleveland, T.E. / Bouyain, S. / Byrne, P.O. / Longo, P.A. / Leahy, D.J.
History
DepositionOct 14, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 29, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 8, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.2Jul 29, 2020Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Sep 13, 2023Group: 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Receptor tyrosine-protein kinase erbB-4
B: Receptor tyrosine-protein kinase erbB-4
C: Receptor tyrosine-protein kinase erbB-4
D: Receptor tyrosine-protein kinase erbB-4
E: Receptor tyrosine-protein kinase erbB-4
F: Receptor tyrosine-protein kinase erbB-4
G: Neuregulin 1
H: Neuregulin 1
I: Neuregulin 1
J: Neuregulin 1
K: Neuregulin 1
L: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)455,34138
Polymers449,59012
Non-polymers5,75126
Water5,242291
1
A: Receptor tyrosine-protein kinase erbB-4
G: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,8166
Polymers74,9322
Non-polymers8854
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4150 Å2
ΔGint4 kcal/mol
Surface area29690 Å2
MethodPISA
2
B: Receptor tyrosine-protein kinase erbB-4
H: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,2598
Polymers74,9322
Non-polymers1,3276
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint12 kcal/mol
Surface area33360 Å2
MethodPISA
3
C: Receptor tyrosine-protein kinase erbB-4
I: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,3744
Polymers74,9322
Non-polymers4422
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3870 Å2
ΔGint1 kcal/mol
Surface area32450 Å2
MethodPISA
4
D: Receptor tyrosine-protein kinase erbB-4
J: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,0387
Polymers74,9322
Non-polymers1,1065
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4610 Å2
ΔGint9 kcal/mol
Surface area32910 Å2
MethodPISA
5
E: Receptor tyrosine-protein kinase erbB-4
K: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,5955
Polymers74,9322
Non-polymers6643
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3950 Å2
ΔGint5 kcal/mol
Surface area32200 Å2
MethodPISA
6
F: Receptor tyrosine-protein kinase erbB-4
L: Neuregulin 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,2598
Polymers74,9322
Non-polymers1,3276
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint13 kcal/mol
Surface area32890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.730, 223.510, 146.920
Angle α, β, γ (deg.)90.00, 99.72, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Receptor tyrosine-protein kinase erbB-4 / Proto-oncogene-like protein c-ErbB-4 / Tyrosine kinase-type cell surface receptor HER4 / p180erbB4 ...Proto-oncogene-like protein c-ErbB-4 / Tyrosine kinase-type cell surface receptor HER4 / p180erbB4 / ERBB4 intracellular domain / 4ICD / E4ICD / s80HER4


Mass: 68735.508 Da / Num. of mol.: 6 / Fragment: Extracellular region (UNP Residues 26-640)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ERBB4, HER4 / Plasmid: pSGHV0 / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): Lec 3.2.8.1
References: UniProt: Q15303, receptor protein-tyrosine kinase
#2: Protein
Neuregulin 1


Mass: 6196.122 Da / Num. of mol.: 6 / Fragment: EGF-like domain (UNP Residues 230-284)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NRG1 / Plasmid: pET32 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96IB3, UniProt: Q02297*PLUS
#3: 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.: 26
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
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 291 / 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: 3.09 Å3/Da / Density % sol: 60.14 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6
Details: PEG6000, Mg(OAc)2, MES pH6.0, Hampton Silver Bullet, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.98011 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 22, 2010
RadiationMonochromator: Double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98011 Å / Relative weight: 1
ReflectionResolution: 3.03→50 Å / Num. all: 104051 / Num. obs: 104051 / % possible obs: 98.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 93.35 Å2 / Rmerge(I) obs: 0.116 / Net I/σ(I): 8.8
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
3.03-3.082.70.685187
3.08-3.1430.634194.4
3.14-3.23.40.554198
3.2-3.263.60.51199.5
3.26-3.333.80.441199.9
3.33-3.413.80.365199.8
3.41-3.53.80.326199.8
3.5-3.593.90.236199.9
3.59-3.73.80.216199.9
3.7-3.823.90.167199.9
3.82-3.953.80.155199.9
3.95-4.113.90.119199.9
4.11-4.33.90.1031100
4.3-4.533.90.0871100
4.53-4.813.90.0761100
4.81-5.183.90.0731100
5.18-5.73.90.078199.9
5.7-6.523.90.081100
6.52-8.213.90.0661100
8.21-503.80.069199.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
BUSTER-TNTBUSTER 2.8.0refinement
PDB_EXTRACT3.1data extraction
JBluIce-EPICSdata collection
BUSTER2.8.0refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTREIS 1MOX AND 2AHX

1mox

2ahx


Resolution: 3.03→49.63 Å / Cor.coef. Fo:Fc: 0.9316 / Cor.coef. Fo:Fc free: 0.9044 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2272 5198 5 %RANDOM
Rwork0.1895 ---
obs0.1914 103996 --
all-103996 --
Displacement parametersBiso mean: 91 Å2
Baniso -1Baniso -2Baniso -3
1-4.2937 Å20 Å2-3.5897 Å2
2--7.8176 Å20 Å2
3----12.1114 Å2
Refine analyzeLuzzati coordinate error obs: 0.544 Å
Refinement stepCycle: LAST / Resolution: 3.03→49.63 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29872 0 364 291 30527
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0131022HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.2642091HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d10587SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes872HARMONIC2
X-RAY DIFFRACTIONt_gen_planes4525HARMONIC5
X-RAY DIFFRACTIONt_it31022HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.13
X-RAY DIFFRACTIONt_other_torsion19.87
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion4174SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact33541SEMIHARMONIC4
LS refinement shellResolution: 3.03→3.11 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.304 307 4.64 %
Rwork0.2609 6316 -
all0.2629 6623 -
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)
11.36610.9214-0.06061.65080.13051.48490.03880.3127-0.26650.11020.1651-0.19550.44110.0851-0.2039-0.30710.176-0.0966-0.1614-0.1104-0.0688-3.0173-44.03923.261
20.7736-0.24270.31671.0834-0.35870.8593-0.0208-0.01840.07570.1891-0.12220.02-0.0319-0.15950.143-0.211-0.02640.099-0.12330.0095-0.077517.8972-12.974357.6662
30.7610.25830.36531.02840.37331.8413-0.15710.2290.2461-0.2789-0.0650.0704-0.4273-0.22310.2221-0.29430.0395-0.0172-0.06420.1248-0.0512-60.39043.3158-6.4105
40.7128-0.311-0.25770.89620.10451.8764-0.03640.0219-0.1145-0.02480.02530.20880.3670.21060.0111-0.28290.001-0.043-0.19150.0074-0.0411-39.7135-39.85137.4642
50.83821.00330.22831.69480.63651.1464-0.26390.440.2045-0.4110.37720.3125-0.31450.329-0.1133-0.349-0.1033-0.02720.10250.2608-0.0847-12.604517.23388.0565
60.943-0.5392-0.30691.48860.11490.95240.016-0.10140.11950.1867-0.00140.0256-0.17330.2473-0.0147-0.2356-0.0836-0.0118-0.14850.0039-0.0486-32.55097.255652.316
70.20310.97431.75371.99940.90631.6642-0.01080.2832-0.2119-0.17140.1563-0.25650.15020.2899-0.1455-0.1720.18290.0406-0.0788-0.28870.23458.0127-56.06144.4922
80.4362-1.37120.73943.3848-1.21253.33180.0238-0.230.11140.3095-0.05380.2212-0.1843-0.37950.03-0.05980.25430.1203-0.0197-0.16140.02375.221612.279767.188
90.35041.39170.01382.77870.58622.25020.0570.13710.1164-0.1399-0.0489-0.0937-0.46270.1235-0.00810.1922-0.1334-0.1495-0.29730.29050.0467-49.587828.5483-2.6764
101.27120.416-2.04541.1197-2.04642.7880.00410.0078-0.19180.2196-0.09410.2570.4019-0.02910.090.1925-0.10070.2802-0.4444-0.00830.3271-51.3478-60.774224.7167
11-0.6371-0.07431.53194.143-0.41023.825-0.00210.09850.0969-0.2607-0.01610.1156-0.1334-0.00830.0181-0.1007-0.3138-0.30790.24960.2662-0.171-23.296612.4273-17.6639
12-0.139-1.22830.19373.20530.0812.6502-0.0576-0.2790.0770.25950.0021-0.08510.11830.49960.0555-0.09540.0946-0.15890.2506-0.0142-0.2233-20.7346-7.469773.5791
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ A|1 - A|145 A|148 - A|154 A|159 - A|556 A|1001 - A|1004 }A1 - 145
2X-RAY DIFFRACTION1{ A|1 - A|145 A|148 - A|154 A|159 - A|556 A|1001 - A|1004 }A148 - 154
3X-RAY DIFFRACTION1{ A|1 - A|145 A|148 - A|154 A|159 - A|556 A|1001 - A|1004 }A159 - 556
4X-RAY DIFFRACTION1{ A|1 - A|145 A|148 - A|154 A|159 - A|556 A|1001 - A|1004 }A1001 - 1004
5X-RAY DIFFRACTION2{ B|1 - B|145 B|148 - B|154 B|159 - B|572 B|578 - B|612 B|1001 - B|1006 }B1 - 145
6X-RAY DIFFRACTION2{ B|1 - B|145 B|148 - B|154 B|159 - B|572 B|578 - B|612 B|1001 - B|1006 }B148 - 154
7X-RAY DIFFRACTION2{ B|1 - B|145 B|148 - B|154 B|159 - B|572 B|578 - B|612 B|1001 - B|1006 }B159 - 572
8X-RAY DIFFRACTION2{ B|1 - B|145 B|148 - B|154 B|159 - B|572 B|578 - B|612 B|1001 - B|1006 }B578 - 612
9X-RAY DIFFRACTION2{ B|1 - B|145 B|148 - B|154 B|159 - B|572 B|578 - B|612 B|1001 - B|1006 }B1001 - 1006
10X-RAY DIFFRACTION3{ C|1 - C|145 C|148 - C|154 C|158 - C|572 C|579 - C|609 C|1001 - C|1002 }C1 - 145
11X-RAY DIFFRACTION3{ C|1 - C|145 C|148 - C|154 C|158 - C|572 C|579 - C|609 C|1001 - C|1002 }C148 - 154
12X-RAY DIFFRACTION3{ C|1 - C|145 C|148 - C|154 C|158 - C|572 C|579 - C|609 C|1001 - C|1002 }C158 - 572
13X-RAY DIFFRACTION3{ C|1 - C|145 C|148 - C|154 C|158 - C|572 C|579 - C|609 C|1001 - C|1002 }C579 - 609
14X-RAY DIFFRACTION3{ C|1 - C|145 C|148 - C|154 C|158 - C|572 C|579 - C|609 C|1001 - C|1002 }C1001 - 1002
15X-RAY DIFFRACTION4{ D|1 - D|145 D|148 - D|154 D|159 - D|570 D|579 - D|614 D|1001 - D|1005 }D1 - 145
16X-RAY DIFFRACTION4{ D|1 - D|145 D|148 - D|154 D|159 - D|570 D|579 - D|614 D|1001 - D|1005 }D148 - 154
17X-RAY DIFFRACTION4{ D|1 - D|145 D|148 - D|154 D|159 - D|570 D|579 - D|614 D|1001 - D|1005 }D159 - 570
18X-RAY DIFFRACTION4{ D|1 - D|145 D|148 - D|154 D|159 - D|570 D|579 - D|614 D|1001 - D|1005 }D579 - 614
19X-RAY DIFFRACTION4{ D|1 - D|145 D|148 - D|154 D|159 - D|570 D|579 - D|614 D|1001 - D|1005 }D1001 - 1005
20X-RAY DIFFRACTION5{ E|1 - E|145 E|148 - E|154 E|159 - E|570 E|580 - E|608 E|1001 - E|1003 }E1 - 145
21X-RAY DIFFRACTION5{ E|1 - E|145 E|148 - E|154 E|159 - E|570 E|580 - E|608 E|1001 - E|1003 }E148 - 154
22X-RAY DIFFRACTION5{ E|1 - E|145 E|148 - E|154 E|159 - E|570 E|580 - E|608 E|1001 - E|1003 }E159 - 570
23X-RAY DIFFRACTION5{ E|1 - E|145 E|148 - E|154 E|159 - E|570 E|580 - E|608 E|1001 - E|1003 }E580 - 608
24X-RAY DIFFRACTION5{ E|1 - E|145 E|148 - E|154 E|159 - E|570 E|580 - E|608 E|1001 - E|1003 }E1001 - 1003
25X-RAY DIFFRACTION6{ F|1 - F|144 F|147 - F|154 F|159 - F|569 F|583 - F|610 F|1001 - F|1006 }F1 - 144
26X-RAY DIFFRACTION6{ F|1 - F|144 F|147 - F|154 F|159 - F|569 F|583 - F|610 F|1001 - F|1006 }F147 - 154
27X-RAY DIFFRACTION6{ F|1 - F|144 F|147 - F|154 F|159 - F|569 F|583 - F|610 F|1001 - F|1006 }F159 - 569
28X-RAY DIFFRACTION6{ F|1 - F|144 F|147 - F|154 F|159 - F|569 F|583 - F|610 F|1001 - F|1006 }F583 - 610
29X-RAY DIFFRACTION6{ F|1 - F|144 F|147 - F|154 F|159 - F|569 F|583 - F|610 F|1001 - F|1006 }F1001 - 1006
30X-RAY DIFFRACTION7{ G|3 - G|28 G|31 - G|54 }G3 - 28
31X-RAY DIFFRACTION7{ G|3 - G|28 G|31 - G|54 }G31 - 54
32X-RAY DIFFRACTION8{ H|2 - H|28 H|31 - H|54 }H2 - 28
33X-RAY DIFFRACTION8{ H|2 - H|28 H|31 - H|54 }H31 - 54
34X-RAY DIFFRACTION9{ I|3 - I|28 I|31 - I|54 }I3 - 28
35X-RAY DIFFRACTION9{ I|3 - I|28 I|31 - I|54 }I31 - 54
36X-RAY DIFFRACTION10{ J|2 - J|28 J|31 - J|54 }J2 - 28
37X-RAY DIFFRACTION10{ J|2 - J|28 J|31 - J|54 }J31 - 54
38X-RAY DIFFRACTION11{ K|3 - K|28 K|31 - K|53 }K3 - 28
39X-RAY DIFFRACTION11{ K|3 - K|28 K|31 - K|53 }K31 - 53
40X-RAY DIFFRACTION12{ L|2 - L|28 L|31 - L|54 }L2 - 28
41X-RAY DIFFRACTION12{ L|2 - L|28 L|31 - L|54 }L31 - 54

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