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Deoxyribonuclease-2-alphaDNASE2Homo sapiens (Human)-Annotation score: -Experimental evidence at protein leveliFunctioniHydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the degradation of nuclear DNA in cellular apoptosis during development. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver, where it degrades nuclear DNA expelled from erythroid precursor cells.MiscellaneousNot required for the generation of the characteristic DNA fragmentation observed in apoptotic cells, but for the degradation of DNA from dying cells.Catalytic activityiEndonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.SitesFeature keyPosition(s)DescriptionActionsGraphical viewLengthActive sitei1GO - Molecular functioniTraceable author statementiGO - Biological processiTraceable author statementiKeywordsiMolecular function, , , Biological processEnzyme and pathway databasesBRENDAi 2681Reactomei Lysosome Vesicle BiogenesisNames & TaxonomyiProtein namesiRecommended name:Deoxyribonuclease-2-alpha (EC:)Alternative name(s):Acid DNaseDeoxyribonuclease II alphaShort name: DNase II alphaLysosomal DNase IIR31240_2Gene namesiName:Synonyms:DNASE2A, DNL2OrganismiTaxonomic identifieri
[]Taxonomic lineagei >
Proteomesi Componenti: Chromosome 19 Organism-specific databasesEuPathDBiHGNCi DNASE2MIMi geneneXtProtiSubcellular locationi
Extracellular region or secreted
Plasma membrane
Cytoskeleton
Peroxisome
Golgi apparatus
Mitochondrion
Manual annotation
Automatic computational assertionGraphics by Christian S Source: Keywords - Cellular componentiPathology & BiotechiMutagenesisOrganism-specific databasesDisGeNETiOpenTargetsiPharmGKBiChemistry databasesChEMBLiPolymorphism and mutation databasesBioMutaiPTM / ProcessingiMolecule processingFeature keyPosition(s)DescriptionActionsGraphical viewLengthSignal peptidei 18ChainiPRO_Deoxyribonuclease-2-alpha 342Amino acid modificationsFeature keyPosition(s)DescriptionActionsGraphical viewLengthDisulfide bondiGlycosylationiN-linked (GlcNAc...) asparagine1GlycosylationiN-linked (GlcNAc...) asparagineManual assertion based on experiment ini"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.", , ,
[] [] []Cited for: GLYCOSYLATION AT ASN-212."Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.", , , , , , ,
[] [] []Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.1GlycosylationiN-linked (GlcNAc...) asparagine1Disulfide bondiGlycosylationiN-linked (GlcNAc...) asparagine1Disulfide bondiPost-translational modificationiGlycosylated. Mutations that eliminate N-glycosylation sites reduce activity, but enzymatic deglycosylation has no effect.Manual assertion based on experiment ini"Revised structure of the active form of human deoxyribonuclease IIalpha.", ,
[] [] []Cited for: LACK OF PROTEOLYTIC PROCESSING, GLYCOSYLATION."Structural requirements of human DNase II alpha for formation of the active enzyme: the role of the signal peptide, N-glycosylation, and disulphide bridging.", ,
[] [] []Cited for: MUTAGENESIS OF CYS-19; ASN-86; CYS-151; CYS-159; ASN-212; ASN-266; CYS-267; ASN-290; CYS-299; CYS-308; CYS-327 AND CYS-347, GLYCOSYLATION, DISULFIDE BONDS."Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.", , ,
[] [] []Cited for: GLYCOSYLATION AT ASN-212."Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.", , , , , , ,
[] [] []Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.Keywords - PTMi, Proteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEiProteomicsDBiPTM databasesiPTMnetiPhosphoSitePlusiExpressioniGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSOrganism-specific databasesHPAiInteractioniProtein-protein interaction databasesBioGridi, 10 interactorsIntActi, 1 interactorSTRINGiChemistry databasesBindingDBiStructurei3D structure databasesProteinModelPortaliSMRiModBaseiMobiDBiFamily & DomainsiSequence similaritiesiBelongs to the .Keywords - DomainiPhylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOGENOMiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiFamily and domain databasesInterProi DNase_IIPANTHERi PTHR10858, 1 hitPfami DNase_II, 1 hitSequences (2)iSequence statusi: Complete.Sequence processingi: The displayed sequence is further processed into a mature form.This entry describes 2 isoformsi produced by alternative splicing.
(identifier: O00115-1)
[]This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
50MIPLLLAALL CVPAGALTCY GDSGQPVDWF VVYKLPALRG SGEAAQRGLQ
100YKYLDESSGG WRDGRALINS PEGAVGRSLQ PLYRSNTSQL AFLLYNDQPP
150QPSKAQDSSM RGHTKGVLLL DHDGGFWLVH SVPNFPPPAS SAAYSWPHSA
200CTYGQTLLCV SFPFAQFSKM GKQLTYTYPW VYNYQLEGIF AQEFPDLENV
250VKGHHVSQEP WNSSITLTSQ AGAVFQSFAK FSKFGDDLYS GWLAAALGTN
300LQVQFWHKTV GILPSNCSDI WQVLNVNQIA FPGPAGPSFN STEDHSKWCV
350SPKGPWTCVG DMNRNQGEEQ RGGGTLCAQL PALWKAFQPL VKNYQPCNGM
360ARKPSRAYKI
36039,581July 15, 1998 - v2Checksum:iDF1BBFBA8A9676EABLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutter (identifier: O00115-2)
[]The sequence of this isoform differs from the canonical sequence as follows:
: Missing.Note: No experimental confirmation available.30533,615Checksum:i85A0DD26EC28FE2CBLASTProtParamProtScaleCompute pI/MWPeptideMassPeptideCutterExperimental InfoFeature keyPosition(s)DescriptionActionsGraphical viewLengthSequence conflictiMissing
(PubMed:). 12Natural variantFeature keyPosition(s)DescriptionActionsGraphical viewLengthNatural variantiVAR_048870. Corresponds to variant .1Natural variantiVAR_048871. Corresponds to variant .1Natural variantiVAR_012044. Corresponds to variant .1Alternative sequenceFeature keyPosition(s)DescriptionActionsGraphical viewLengthAlternative sequenceiVSP_056921Missing
in isoform . Manual assertion based on opinion ini"Complete sequencing and characterization of 21,243 full-length human cDNAs.", , , , , , , , , , , , , , , , ,
[] [] []Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 55Sequence databasesSelect the link destinations:EMBLiGenBankiDDBJi Genomic DNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
Genomic DNA No translation available. Genomic DNA Translation:
Genomic DNA Translation:
mRNA Translation:
mRNA Translation: CCDSi []PIRiRefSeqi,
[]UniGeneiGenome annotation databasesEnsembli; ;
[]GeneIDiKEGGiUCSCi human []Keywords - Coding sequence diversityi, Similar proteinsi360404403403367O00115-2218348348305218360404403403367O00115-2218348348305218 Genomic DNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
mRNA Translation:
Genomic DNA No translation available. Genomic DNA Translation:
Genomic DNA Translation:
mRNA Translation:
mRNA Translation: CCDSi []PIRiRefSeqi,
[]UniGenei3D structure databasesProteinModelPortaliSMRiModBaseiMobiDBiProtein-protein interaction databasesBioGridi, 10 interactorsIntActi, 1 interactorSTRINGiChemistry databasesBindingDBiChEMBLiPTM databasesiPTMnetiPhosphoSitePlusiPolymorphism and mutation databasesBioMutaiProteomic databasesEPDiMaxQBiPaxDbiPeptideAtlasiPRIDEiProteomicsDBiProtocols and materials databasesDNASUiStructural Biology KnowledgebaseGenome annotation databasesEnsembli; ;
[]GeneIDiKEGGiUCSCi human []Organism-specific databasesCTDiDisGeNETiEuPathDBiGeneCardsiHGNCi DNASE2HPAiMIMi geneneXtProtiOpenTargetsiPharmGKBiGenAtlasiPhylogenomic databaseseggNOGi Eukaryota LUCAGeneTreeiHOGENOMiHOVERGENiInParanoidiKOiOMAiOrthoDBiPhylomeDBiTreeFamiEnzyme and pathway databasesBRENDAi 2681Reactomei Lysosome Vesicle BiogenesisMiscellaneous databasesChiTaRSi humanGenomeRNAiiPROiSOURCEiGene expression databasesBgeeiCleanExiExpressionAtlasi baseline and differentialGenevisiblei HSFamily and domain databasesInterProi DNase_IIPANTHERi PTHR10858, 1 hitPfami DNase_II, 1 hitProtoNetiMiscellaneousiKeywords - Technical termi, DocumentsHuman chromosome 19: entries, gene names and cross-references to MIMList of human entries with polymorphisms or disease mutationsIndex of human polymorphisms and disease mutationsOnline Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-ProtIndex of protein domains and familiesWe'd like to inform you that we have updated our
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南京雨润食品5亿元的短融债危机解除日 11:11每日经济新闻手机客户端 |扫码下载中金网APP摘要：困扰着南京雨润食品的短期融资债务危机终于得到化解。3月30日，雨润食品通过上海清算所发布公告称，经过公司积极努力筹措资金，定于日兑付剩余应付本金2.8亿元。【免责声明】此文章内容来源为每日经济新闻，中金网发布此信息目的在于传播更多信息，与本网站立场无关。中金网不保证该信息的准确性、真实性、完整性、有效性等。相关信息并未经过本网站证实，不构成任何投资建议，据此操作，风险自担。
　　3月31日消息，困扰着南京雨润食品的短期融资债务危机终于得到化解。　　3月30日，雨润食品通过上海清算所发布公告称，经过公司积极努力筹措资金，定于日兑付剩余应付本金2.8亿元。　　事实上，就在3月17日，雨润食品曾发布公告称，该公司发行的2015年度第一期短期融资券(简称：15雨润CP001)应于日兑付本息。截至到期兑付日日终，公司未能按照约定筹措足额偿债资金，15雨润CP001不能按期足额偿付，已构成实质性违约。　　然而，仅仅4天之后，雨润食品就对外宣布，确定于3月21日兑付15雨润CP001全部应付利息和部分应付本金，共计约2.52亿元，而随着此次余下的2.8亿元本金得以兑付，15雨润CP001本息全部兑付完毕。　　据记者了解，本期短融规模为5亿元，期限为1年，利率为6.45%，到期应偿还的本息为53225万元，而在此前的3月9日，南京雨润就发布公告称，对于15雨润CP001兑付存在不确定性。　　在3月15日，新世纪评级也将南京雨润食品的主体信用等级由BB直接下调为CCC，并列入负面观察名单，将15雨润CP001的债项信用等级由B级下调为C级。　　对于15雨润CP001发生的实质性违约，南京雨润食品于3月17日表示，公司目前正通过多途径努力筹措偿债资金，并积极通过外部渠道筹措资金等方式，力争尽快完成15雨润CP001本息资金的兑付，以及努力保障后续债务融资工具到期偿付。　　然而，仅仅在宣布发生实质性违约4天之后，南京雨润食品就在3月21日宣布，公司确定于3月21日兑付15雨润CP001全部应付利息和部分应付本金，共计约2.52亿元人民币。据记者了解，当时本金5亿元只兑付了45%。　　对于上述的兑付方案，投资者蒋诚对记者说，“ 3月17日宣布违约，我们在此前已经开了投资者的会议，突然在4天之后宣布将兑付利息和45%的本金，这种方案投资者是可以接受的，但是余下的本金何时偿还，公司要给投资者一个说法。”　　随后，就在投资者认为余下的本金需要等待一段时间才有结果时，3月30日，南京雨润食品通过上海清算所发布公告称，经过公司经积极努力筹措资金，定于日兑付剩余应付本金2.8亿元。　　随着余下的2.8亿元本金全部兑付，这也就意味着15雨润CP001短期融资债务本息得以全部兑付。　　事实上，除了已经兑付的5亿元的15雨润CP001外，南京雨润发行额度为10亿元的中期票据13雨润MTN1也将于今年5月13日到期，到期之后如何解决，也成为投资者关注的焦点。　　对此，上述投资者蒋诚对记者说，“15雨润CP001短期融资债务，公司在违约仅仅不到半个月时间就全部兑付了本息，这也让投资者对5月份即将到期的短期融资债务充满期待。”关注（http://m.cngold.com.cn），掌握最新财经要闻。
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2-Hydrazinyl-4-methyl-1,3-benzothia-zole.
MedLine Citation:
PubMed-not-MEDLINE
Abstract/OtherAbstract:
The title compound, C(8)H(9)N(3)S, is almost planar (r.m.s. deviation = 0.019 ?) apart from the terminal -NH(2) grouping [deviation of the N atom = 0.286 (2) ?]. In the crystal, mol-ecules are linked by N-H?N hydrogen bonds, generating (001) sheets.
Xu-Feng L Xiao-Yong Yu; Shao-Liang Jiang
Related Documents
- 9241136 -
- 6314846 -
Publication Detail:
Journal Article
Journal Detail:
Acta crystallographica. Section E, Structure reports online
ISO Abbreviation:
Acta Crystallogr Sect E Struct Rep Online
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Date Detail:
Created Date:
Completed Date:
Revised Date:
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Nlm Unique ID:
Medline TA:
Acta Crystallogr Sect E Struct Rep Online
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From MEDLINE(R)/PubMed(R), a database of the U.S. National Library of Medicine
Journal Information
Journal ID (nlm-ta): Acta Crystallogr Sect E Struct Rep Online
Journal ID (publisher-id): Acta Cryst. E
Publisher: International Union of Crystallography
Article Information
A full version of this article is available from Crystallography Journals Online.(C) Liu et al. 2011
open-access:
Received Day: 24 Month: 5 Year: 2011
Accepted Day: 26 Month: 5 Year: 2011
collection publication date: Day: 01 Month: 7 Year: 2011
Electronic publication date: Day: 11 Month: 6 Year: 2011
pmc-release publication date: Day: 11 Month: 6 Year: 2011
Volume: 67 Issue: Pt 7
First Page: o1641 Last Page: o1641
ID: 3152062
PubMed Id:
Publisher Id: hb5894
Coden: ACSEBH
Publisher Item Identifier: S0149
2-Hydrazinyl-4-methyl-1,3-benzothia-zole
Alternate Title:C8H9N3S
Xu-Feng Liu
Xiao-Yong Yu
Shao-Liang Jiang*
aDepartment of Chemical Engineering, Ningbo University of Technology, Ningbo 315016, People’s Republic of China
bCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou 310014, People’s Republic of China
Correspondence: Correspondence e-mail:
Related literature
For related structures and their biactivity, see Sun & Cui (2008); Liu & Liu (2011); Liuet al. (2011a,b). For the synthesis, see: Patel et al. (2010).[Chemical Structure ID: scheme1]
Experimental
Crystal data
Mr = 179.24
Monoclinic,
a = 3.893 (2) ?
b = 7.312 (4) ?
c = 14.137 (8) ?
β = 93.416 (13)°
V = 401.7 (4) ?3
Mo Kα radiation
μ = 0.34 mm-1
0.28 × 0.18 × 0.10 mm
Data collection
Rigaku Saturn CCD area-detector diffractometer
Absorption correction: multi-scan (CrystalClear; Rigaku/MSC, 2005) Tmin = 0.910, Tmax = 0.967
4186 measured reflections
1864 independent reflections
1614 reflections with I & 2σ(I)
Rint = 0.043
Refinement
R[F2 & 2σ(F2)] = 0.028
wR(F2) = 0.057
1864 reflections
122 parameters
5 restraints
H atoms treated by a mixture of independent and constrained refinement
Δρmax = 0.28 e ?-3
Δρmin = -0.20 e ?-3
Absolute structure: Flack (1983), 836 Friedel pairs
Flack parameter: -0.09 (6)
Data collection: CrystalClear (Rigaku/MSC, 2005); cell refinement: CrystalClear; data reduction: CrystalClear; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: SHELXTL (Sheldrick, 2008); software used to prepare material for publication: SHELXTL.
Supplementary Material
Crystal structure: contains datablock(s) global, I. DOI: 10./hb5894sup1.cif
Structure factors: contains datablock(s) I. DOI: 10./hb5894Isup2.hkl
Supplementary material file. DOI: 10./hb5894Isup3.cml
Additional supplementary materials:
crystall 3D checkCIF report
fnu1Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: HB5894).
We thank the Social Practice of the Excellent Engineer Programs of Ningbo University of Technology.
supplementary crystallographic
information
Experimental
The title compound was prepared according to the literature procedures
(Patel et al., (2010). Colourless prisms of (I)
were grown by the slow evaporation of an
ethanol solution at room temperature.
Refinement
All the H atoms were positioned geometrically (C—H = 0.93–0.97 ?) and
refined as riding with Uiso(H) = 1.2Ueq(C) or
1.5Ueq(methyl C).
Crystal data
Data collection
Refinement
Special details
Fractional atomic coordinates and isotropic or equivalent isotropic displacement parameters (?2)
Atomic displacement parameters (?2)
Geometric parameters (?, °)
Hydrogen-bond geometry (?, °)
Symmetry codes: (i) -x+2, y+1/2, -z+1; (ii) -x+1, y-1/2, -z+1.
References
Flack, H. D. (1983). Acta Cryst. A39, 876–881.
Liu, X.-F. & Liu, X.-H. (2011). Acta Cryst. E67, o202.
Liu, X. H., Tan, C. X. & Weng, J. Q. (2011a). Phosphorus Sulfur Silicon Relat. Elem.186, 552–557.
Liu, X. H., Tan, C. X. & Weng, J. Q. (2011b). Phosphorus Sulfur Silicon Relat. Elem.186, 558–564.
Patel, N. B., Khan, I. H. & Rajani, A. D. (2010). Eur. J. Med. Chem.45, .
Rigaku/MSC (2005). CrystalClear Rigaku/MSC Inc. The Woodlands, Texas, USA.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112–122.
Sun, Y.-F. & Cui, Y.-P. (2008). Acta Cryst. E64, o690.
[Figure ID: Fap1]
The molecular structure of (I). Displacement ellipsoids are drawn at the 30% probability level and H atoms are shown as small spheres of arbitrary radii.
[Figure ID: Fap2]
The crystal packing for (I).
[TableWrap ID: d1e118]
F(000) = 188
Mr = 179.24
Dx = 1.482 Mg m-3
Monoclinic, P21
Mo Kα radiation, λ = 0.71073 ?
a = 3.893 (2) ?
Cell parameters from 1356 reflections
b = 7.312 (4) ?
θ = 2.9–27.9°
c = 14.137 (8) ?
u = 0.34 mm-1
β = 93.416 (13)°
V = 401.7 (4)
Prism, colorless
0.28 × 0.18 × 0.10 mm
[TableWrap ID: d1e239]
Rigaku Saturn CCD area-detector diffractometer
1864 independent reflections
Radiation source: rotating anode
1614 reflections with I & 2σ(I)
multilayer
Rint = 0.043
Detector resolution: 14.63 pixels mm-1
θmax = 27.9°, θmin = 1.4°
ω and φ scans
Absorption correction: multi-scan (CrystalClear; Rigaku/MSC, 2005)
Tmin = 0.910, Tmax = 0.967
l = -18→18
4186 measured reflections
[TableWrap ID: d1e362]
Refinement on F2
Secondary atom site location: difference Fourier map
Least-squares matrix: full
Hydrogen site location: inferred from neighbouring sites
R[F2 & 2σ(F2)] = 0.028
H atoms treated by a mixture of independent and constrained refinement
wR(F2) = 0.057
w = 1/[σ2(Fo2) + (0.006P)2]
where P = (Fo2 + 2Fc2)/3
(Δ/σ)max & 0.001
1864 reflections
Δρmax = 0.28 e ?-3
122 parameters
Δρmin = -0.20 e ?-3
5 restraints
Absolute structure:
Flack (1983), 836 Friedel pairs
Primary atom site location: structure-invariant direct methods
Flack parameter: -0.09 (6)
[TableWrap ID: d1e524]
Geometry. All e.s.d.'s (except the e.s.d. in the dihedral angle between two l.s. planes)
are estimated using the full covariance matrix. The cell e.s.d.'s are taken
into account individually in the estimation of e.s.d.'s in distances, angles
correlations between e.s.d.'s in cell parameters are only
used when they are defined by crystal symmetry. An approximate (isotropic)
treatment of cell e.s.d.'s is used for estimating e.s.d.'s involving l.s.
Refinement. Refinement of F2 against ALL reflections. The weighted R-factor
wR and goodness of fit S are based on F2, conventional
R-factors R are based on F, with F set to zero for
negative F2. The threshold expression of F2 &
σ(F2) is used only for calculating R-factors(gt) etc.
and is not relevant to the choice of reflections for refinement.
R-factors based on F2 are statistically about twice as large
as those based on F, and R- factors based on ALL data will be
even larger.
[TableWrap ID: d1e623]
0.74281 (13)
0.41481 (6)
0.33097 (3)
0.01462 (12)
0.2809 (5)
0.8047 (3)
0.18122 (14)
0.0144 (5)
0.9465 (5)
0.4807 (2)
0.52579 (12)
0.0163 (4)
0.5274 (5)
0.4513 (3)
0.13713 (13)
0.0163 (5)
0.4899 (4)
0.7443 (2)
0.34709 (11)
0.0136 (4)
0.2524 (5)
0.7352 (3)
0.08962 (14)
0.0158 (5)
0.4388 (5)
0.6942 (3)
0.25178 (13)
0.0127 (4)
0.6412 (5)
0.6127 (3)
0.39382 (13)
0.0130 (4)
0.7110 (4)
0.6159 (2)
0.49033 (12)
0.0150 (4)
0.3711 (5)
0.5633 (3)
0.06809 (13)
0.0185 (5)
0.5572 (5)
0.5186 (3)
0.22906 (13)
0.0124 (4)
0.1482 (5)
0.9932 (3)
0.20484 (14)
0.0182 (5)
0.7236 (19)
0.5172 (16)
0.060 (10)*
0.5774 (10)
0.043 (7)*
0.5428 (12)
0.038 (8)*
[TableWrap ID: d1e914]
0.0167 (3)
0.0120 (2)
0.0151 (2)
0.0012 (3)
0.00115 (18)
0.0003 (2)
0.0078 (11)
0.0166 (11)
0.0191 (11)
-0.0007 (10)
0.0026 (9)
0.0030 (9)
0.0141 (11)
0.0180 (10)
0.0163 (9)
0.0006 (8)
-0.0015 (7)
0.0049 (8)
0.0142 (11)
0.0169 (14)
0.0180 (10)
-0.0005 (9)
0.0029 (8)
-0.0029 (9)
0.0139 (10)
0.0126 (9)
0.0142 (9)
0.0000 (7)
0.0007 (7)
0.0017 (7)
0.0124 (12)
0.0188 (11)
0.0163 (11)
-0.0008 (9)
0.0004 (8)
0.0044 (9)
0.0091 (10)
0.0132 (10)
0.0160 (10)
-0.0037 (9)
0.0032 (8)
0.0004 (9)
0.0125 (11)
0.0137 (10)
0.0133 (10)
-0.0043 (9)
0.0033 (9)
-0.0010 (9)
0.0186 (11)
0.0117 (9)
0.0145 (9)
0.0011 (8)
-0.0009 (7)
0.0004 (8)
0.0189 (13)
0.0231 (12)
0.0133 (10)
-0.0065 (9)
0.0009 (9)
-0.0015 (10)
0.0113 (11)
0.0129 (11)
0.0129 (10)
0.0004 (9)
0.0005 (8)
0.0027 (8)
0.0167 (13)
0.0162 (10)
0.0215 (11)
0.0010 (10)
-0.0008 (9)
0.0034 (9)
[TableWrap ID: d1e1164]
C1—S1—C7
87.97 (10)
N1—C7—S1
117.74 (15)
C4—C5—C6
117.47 (18)
N2—C7—S1
118.61 (15)
C4—C5—C8
121.90 (18)
C7—N2—N3
115.08 (15)
C6—C5—C8
120.64 (17)
C7—N2—H2
117.6 (16)
N2—N3—H3A
110.0 (13)
N3—N2—H2
110.2 (17)
N2—N3—H3B
110.7 (14)
C4—C3—C2
121.44 (19)
H3A—N3—H3B
109.6 (12)
C4—C3—H3
C3—C2—C1
117.26 (17)
C2—C3—H3
C3—C2—H2A
C2—C1—C6
121.80 (18)
C1—C2—H2A
C2—C1—S1
128.72 (15)
C7—N1—C6
109.43 (16)
C6—C1—S1
109.47 (14)
C3—C4—C5
121.98 (19)
C5—C8—H8A
C3—C4—H4
C5—C8—H8B
C5—C4—H4
H8A—C8—H8B
C5—C6—N1
124.57 (18)
C5—C8—H8C
C5—C6—C1
120.04 (17)
H8A—C8—H8C
N1—C6—C1
115.39 (17)
H8B—C8—H8C
N1—C7—N2
123.57 (18)
C6—C5—C4—C3
N1—C7—N2—N3
-165.94 (18)
C8—C5—C4—C3
-179.61 (17)
S1—C7—N2—N3
C4—C5—C6—N1
179.46 (18)
C5—C4—C3—C2
C8—C5—C6—N1
C1—C2—C3—C4
C4—C5—C6—C1
C3—C2—C1—C6
C8—C5—C6—C1
179.27 (16)
C3—C2—C1—S1
-179.19 (14)
C7—N1—C6—C5
179.87 (19)
C5—C6—C1—C2
C7—N1—C6—C1
N1—C6—C1—C2
-179.26 (17)
C6—N1—C7—N2
-176.41 (18)
C5—C6—C1—S1
179.73 (15)
C6—N1—C7—S1
N1—C6—C1—S1
C1—S1—C7—N1
-0.54 (17)
C7—S1—C1—C2
179.11 (18)
C1—S1—C7—N2
176.31 (16)
C7—S1—C1—C6
[TableWrap ID: d1e1582]
D—H···A
D—H···A
N2—H2···N3i
N3—H3A···N1ii
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