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- PDB-3gzf: Structure of the C-terminal domain of nsp4 from Feline Coronavirus -

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Basic information

Entry
Database: PDB / ID: 3gzf
TitleStructure of the C-terminal domain of nsp4 from Feline Coronavirus
ComponentsReplicase polyprotein 1ab
KeywordsVIRAL PROTEIN / Coronavirus / FCoV / nsp4
Function / homology
Function and homology information


host cell membrane / viral genome replication / Lyases; Phosphorus-oxygen lyases / 5'-3' DNA helicase activity / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-RNA exonuclease activity / host cell endoplasmic reticulum-Golgi intermediate compartment / mRNA guanylyltransferase / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity ...host cell membrane / viral genome replication / Lyases; Phosphorus-oxygen lyases / 5'-3' DNA helicase activity / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-RNA exonuclease activity / host cell endoplasmic reticulum-Golgi intermediate compartment / mRNA guanylyltransferase / omega peptidase activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / methyltransferase cap1 / symbiont-mediated perturbation of host ubiquitin-like protein modification / endonuclease activity / mRNA (nucleoside-2'-O-)-methyltransferase activity / DNA helicase / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / virus-mediated perturbation of host defense response / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
Coronavirus nonstructural protein 4 C-terminus / Alphacoronavirus nsp1 / Replicase polyprotein N-term from Coronavirus nsp1 / Alphacoronavirus nsp1 domain superfamily / : / Nonstructural protein 14, alphacoronavirus / RNA-dependent RNA polymerase, alphacoronavirus / Non-structural protein 5, alphacoronavirus / Non-structural protein 6, alphacoronavirus / Nonstructural protein 2, HCoV-229E-like ...Coronavirus nonstructural protein 4 C-terminus / Alphacoronavirus nsp1 / Replicase polyprotein N-term from Coronavirus nsp1 / Alphacoronavirus nsp1 domain superfamily / : / Nonstructural protein 14, alphacoronavirus / RNA-dependent RNA polymerase, alphacoronavirus / Non-structural protein 5, alphacoronavirus / Non-structural protein 6, alphacoronavirus / Nonstructural protein 2, HCoV-229E-like / AAA domain / DNA polymerase; domain 1 / NSP15, NendoU domain, coronavirus / : / : / Coronavirus Nonstructural protein 13, 1B domain / Coronavirus Non-structural protein 13, zinc-binding domain / Coronavirus Nonstructural protein 13, stalk domain / : / Coronavirus Nsp12 Interface domain profile. / Nonstructural protein 15, middle domain, alpha/betacoronavirus / Nonstructural protein 15, N-terminal domain, alpha/beta-coronavirus / NSP14, guanine-N7-methyltransferase domain, coronavirus / NSP12 RNA-dependent RNA polymerase, coronavirus / Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain profile. / Coronavirus (CoV) Nsp15 N-terminal oligomerization domain profile. / Nidovirus 2-O-methyltransferase / Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain profile. / Nidovirus 3'-5' exoribonuclease domain / Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain profile. / Nidovirus 3'-5' exoribonuclease (ExoN) domain profile. / Nonstructural protein 13, 1B domain, coronavirus / Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain / Non-structural protein NSP15, N-terminal domain superfamily, coronavirus / Non-structural protein NSP15, middle domain superfamily / Coronavirus replicase NSP15, N-terminal oligomerization / Nonstructural protein 15, middle domain, coronavirus / Coronavirus replicase NSP15, middle domain / Coronavirus replicase NSP15, N-terminal oligomerisation / Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain profile. / Non-structural protein NSP16, coronavirus-like / Non-structural protein 14, coronavirus / RNA polymerase, N-terminal, coronavirus / Coronavirus 2'-O-methyltransferase / Coronavirus proofreading exoribonuclease / Coronavirus RNA-dependent RNA polymerase, N-terminal / Nidoviral uridylate-specific endoribonuclease (NendoU) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain / Nonstructural protein 13, zinc-binding domain, coronavirus-like / Coronaviridae zinc-binding (CV ZBD) domain profile. / Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain profile. / Endoribonuclease EndoU-like / NendoU domain, nidovirus / Coronavirus replicase NSP15, uridylate-specific endoribonuclease / DNA2/NAM7 helicase-like, C-terminal / AAA domain / (+) RNA virus helicase core domain / (+)RNA virus helicase core domain profile. / : / Coronavirus 3Ecto domain profile. / Papain-like protease, N-terminal domain superfamily, coronavirus / : / Coronavirus (CoV) Nsp2 middle domain profile. / Coronavirus (CoV) Nsp2 N-terminal domain profile. / Coronavirus (CoV) Nsp2 C-terminal domain profile. / NSP1, globular domain, alpha/betacoronavirus / : / Coronavirus (CoV) Nsp3 Y domain profile. / Coronavirus (CoV) Nsp1 globular domain profile. / Coronavirus replicase NSP2, N-terminal / Nonstructural protein 2, N-terminal domain, coronavirus / Coronavirus replicase NSP2, C-terminal / Non-structural protein 2, C-terminal domain, coronavirus / Coronavirus Nsp3a Ubl domain profile. / Coronavirus Nsp3d Ubl domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain profile. / Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain profile. / Coronavirus Nsp9 single-stranded RNA (ssRNA)-binding domain profile. / Coronavirus (CoV) ExoN/MTase coactivator domain profile. / NSP3, first ubiquitin-like (Ubl) domain, coronavirus / NSP3, second ubiquitin-like (Ubl) domain, coronavirus / Coronavirus Nsp4 C-terminal (Nsp4C) domain profile. / Papain-like protease, thumb domain superfamily, coronavirus / Coronavirus replicase NSP7 / Peptidase family C16 domain profile. / Non-structural protein NSP7, coronavirus / Peptidase C30, coronavirus / Peptidase C16, coronavirus / Non-structural protein NSP9, coronavirus / Non-structural protein NSP8, coronavirus / RNA synthesis protein NSP10, coronavirus / Non-structural protein NSP4, C-terminal, coronavirus / RNA synthesis protein NSP10 superfamily, coronavirus / Non-structural protein NSP9 superfamily, coronavirus / Non-structural protein NSP7 superfamily, coronavirus / Non-structural protein NSP8 superfamily, coronavirus / Non-structural protein NSP4, C-terminal superfamily, coronavirus / Peptidase C30, domain 3, coronavirus / Non-structural protein 6, coronavirus / Coronavirus replicase NSP3, C-terminal
Similarity search - Domain/homology
Replicase polyprotein 1ab
Similarity search - Component
Biological speciesFeline coronavirus
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.756 Å
AuthorsManolaridis, I. / Wojdyla, J.A. / Panjikar, S. / Snijder, E.J. / Gorbalenya, A.E. / Coutard, B. / Tucker, P.A.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2009
Title: Structure of the C-terminal domain of nsp4 from feline coronavirus
Authors: Manolaridis, I. / Wojdyla, J.A. / Panjikar, S. / Snijder, E.J. / Gorbalenya, A.E. / Berglind, H. / Nordlund, P. / Coutard, B. / Tucker, P.A.
History
DepositionApr 7, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Aug 18, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Mar 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _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 / _struct_ref_seq_dif.details / _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: Replicase polyprotein 1ab
B: Replicase polyprotein 1ab
C: Replicase polyprotein 1ab
D: Replicase polyprotein 1ab
E: Replicase polyprotein 1ab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,9827
Polymers53,7905
Non-polymers1922
Water72140
1
A: Replicase polyprotein 1ab
C: Replicase polyprotein 1ab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,6123
Polymers21,5162
Non-polymers961
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint-25 kcal/mol
Surface area10380 Å2
MethodPISA
2
B: Replicase polyprotein 1ab
D: Replicase polyprotein 1ab
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,6123
Polymers21,5162
Non-polymers961
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2110 Å2
ΔGint-24 kcal/mol
Surface area10250 Å2
MethodPISA
3
E: Replicase polyprotein 1ab


Theoretical massNumber of molelcules
Total (without water)10,7581
Polymers10,7581
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)127.538, 127.538, 42.797
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number78
Space group name H-MP43
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
12B
22A
13C
23D
14A
24B
34E

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLYGLYALAALAAA4 - 425 - 43
211GLYGLYALAALABB4 - 425 - 43
311GLYGLYALAALACC4 - 425 - 43
411GLYGLYALAALADD4 - 425 - 43
511GLYGLYALAALAEE4 - 425 - 43
121SERSERPHEPHEAA44 - 4545 - 46
221SERSERPHEPHEBB44 - 4545 - 46
321SERSERPHEPHECC44 - 4545 - 46
421SERSERPHEPHEDD44 - 4545 - 46
521SERSERPHEPHEEE44 - 4545 - 46
131TYRTYRTYRTYRAA4849
231TYRTYRTYRTYRBB4849
331TYRTYRTYRTYRCC4849
431TYRTYRTYRTYRDD4849
531TYRTYRTYRTYREE4849
141CYSCYSALAALAAA64 - 6665 - 67
241CYSCYSALAALABB64 - 6665 - 67
341CYSCYSALAALACC64 - 6665 - 67
441CYSCYSALAALADD64 - 6665 - 67
541CYSCYSALAALAEE64 - 6665 - 67
151LEULEUPROPROAA68 - 8769 - 88
251LEULEUPROPROBB68 - 8769 - 88
351LEULEUPROPROCC68 - 8769 - 88
451LEULEUPROPRODD68 - 8769 - 88
551LEULEUPROPROEE68 - 8769 - 88
112METMETALAALABB55 - 6356 - 64
212METMETALAALAAA55 - 6356 - 64
122THRTHRLEULEUBB88 - 9589 - 96
222THRTHRLEULEUAA88 - 9589 - 96
113LYSLYSALAALACC49 - 6350 - 64
213LYSLYSALAALADD49 - 6350 - 64
123THRTHRVALVALCC88 - 9189 - 92
223THRTHRVALVALDD88 - 9189 - 92
114GLYGLYALAALAAA56 - 6357 - 64
214GLYGLYALAALABB56 - 6357 - 64
314GLYGLYALAALAEE56 - 6357 - 64
124THRTHRVALVALAA88 - 8989 - 90
224THRTHRVALVALBB88 - 8989 - 90
324THRTHRVALVALEE88 - 8989 - 90

NCS ensembles :
ID
1
2
3
4

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Components

#1: Protein
Replicase polyprotein 1ab / Non-structural protein 4 / nsp4 / Peptide HD2


Mass: 10758.067 Da / Num. of mol.: 5 / Fragment: C-terminal domain of nsp4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Feline coronavirus / Strain: FIPV WSU-79 / Plasmid: pMM8 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q98VG9
#2: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHIS SEQUENCE IS FROM GENBANK DATABASE, AAY32595.

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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: 3.24 Å3/Da / Density % sol: 61.98 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop
Details: PEG 5000, ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
1,21
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONEMBL/DESY, HAMBURG X1210.9777
SYNCHROTRONEMBL/DESY, HAMBURG X1220.978
Detector
TypeIDDetectorDateDetails
MARMOSAIC 225 mm CCD1CCDDec 12, 2008mirrors
MARMOSAIC 225 mm CCD2CCDDec 20, 2008mirrors
Radiation
IDMonochromatorProtocolScattering typeWavelength-ID
1double crystal Si(111)SADx-ray1
2double crystal Si(111)SINGLE WAVELENGTHx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.97771
20.9781
ReflectionResolution: 2.7→20 Å / Num. obs: 18188 / % possible obs: 99.1 % / Observed criterion σ(I): 3 / Redundancy: 6.05 % / Rmerge(I) obs: 0.053 / Net I/σ(I): 23.25
Reflection shellResolution: 2.75→2.92 Å / % possible obs: 96.6 % / Redundancy: 6.36 % / Rmerge(I) obs: 0.441 / Mean I/σ(I) obs: 3.68 / % possible all: 96.6

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Phasing

PhasingMethod: SAD
Phasing MADD res high: 3.28 Å / D res low: 19.95 Å / FOM : 0.331 / FOM acentric: 0.355 / FOM centric: 0.327 / Reflection: 6945 / Reflection acentric: 860 / Reflection centric: 6085
Phasing MAD set

Reflection: 6945 / Reflection acentric: 6085 / Reflection centric: 860

IDR cullisR cullis acentricR cullis centricR krautR kraut acentricR kraut centricHighest resolution (Å)Lowest resolution (Å)Power (kW)Power acentricPower centric
NATIVE0000.1640.1280.423.2819.95000
PEAK0.8380.8360.8520.1470.1440.1683.819.981.091.1310.804
Phasing MAD set shell
IDResolution (Å)R cullisR cullis acentricR cullis centricR krautR kraut acentricR kraut centricPower (kW)Power acentricPower centricReflectionReflection acentricReflection centric
NATIVE6.97-19.950000.1930.1380.420001174944230
NATIVE5.08-6.970000.160.1250.400018631627236
NATIVE4.2-5.080000.1620.1310.44600023282097231
NATIVE3.65-4.20000.1520.1220.41200015801417163
NATIVE3.28-3.6500000000000
PEAK7.94-19.980.7680.740.8640.0890.0830.1111.4981.6281.041763594169
PEAK5.85-7.940.7490.7430.7810.1250.1220.1441.5311.6231.0031154983171
PEAK4.85-5.850.7980.7990.7960.1460.1410.1771.1891.230.88814681294174
PEAK4.23-4.850.8790.8780.8810.150.1480.1640.8960.9270.62916701497173
PEAK3.8-4.230.9150.9130.9350.1830.1770.2430.7510.780.46518901717173
Phasing MAD set site
IDAtom type symbolB isoFract xFract yFract zOccupancy
1SE40-0.695-0.618-0.1410.191
2SE40-0.733-0.5940.0210.176
3SE40-0.976-0.7760.0140.154
4SE40-1.109-0.7070.220.113
5SE40-0.745-0.527-0.1110.134
6SE40-0.769-0.690.1110.181
7SE40-0.885-0.509-0.0680.126
8SE40-1.181-0.7310.020.134
9SE40-0.81-0.4010.1070.164
10SE40-0.769-0.3310.3080.134
11SE40-0.883-0.375-0.0750.164
12SE40-1.11-0.8430.0720.117
13SE40-0.933-0.7620.1840.12
14SE40-0.687-0.4430.1780.126
15SE40-0.672-0.5720.0680.1
16SE40-0.954-0.8220.2490.141
17SE40-0.988-0.6660.2670.074
18SE40-0.634-0.539-0.3590.037
19SE40-0.989-0.476-0.3240.076
20SE40-0.618-0.585-0.1050.091
Phasing MAD shell
Resolution (Å)FOM FOM acentricFOM centricReflectionReflection acentricReflection centric
6.97-19.950.4190.4180.4191174230944
5.08-6.970.3850.4150.3818632361627
4.2-5.080.3030.3140.30123282312097
3.65-4.20.2430.240.24415801631417
3.28-3.6500000
Phasing dmFOM : 0.65 / FOM acentric: 0.64 / FOM centric: 0.75 / Reflection: 11105 / Reflection acentric: 9950 / Reflection centric: 1155
Phasing dm shell
Resolution (Å)FOM FOM acentricFOM centricReflectionReflection acentricReflection centric
9.4-19.9520.920.930.91466350116
5.9-9.40.830.830.8415111289222
4.7-5.90.780.780.7818771663214
4.1-4.70.750.750.8118861705181
3.5-4.10.580.580.6733293055274
3.3-3.50.360.350.4920361888148

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Processing

Software
NameVersionClassificationNB
SCALA3.2.25data scaling
BP3phasing
RESOLVE2.11phasing
REFMACrefinement
PDB_EXTRACT3.005data extraction
XDSdata reduction
RefinementMethod to determine structure: SAD / Resolution: 2.756→19.95 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.893 / WRfactor Rfree: 0.293 / WRfactor Rwork: 0.239 / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.746 / SU B: 31.264 / SU ML: 0.354 / SU R Cruickshank DPI: 0.804 / SU Rfree: 0.394 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.778 / ESU R Free: 0.386 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.3 927 5.1 %RANDOM
Rwork0.24 ---
obs0.243 18174 99.84 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 126.7 Å2 / Biso mean: 68.225 Å2 / Biso min: 20 Å2
Baniso -1Baniso -2Baniso -3
1--0.01 Å20 Å20 Å2
2---0.01 Å20 Å2
3---0.02 Å2
Refinement stepCycle: LAST / Resolution: 2.756→19.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3581 0 10 40 3631
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0223663
X-RAY DIFFRACTIONr_angle_refined_deg1.6131.9634928
X-RAY DIFFRACTIONr_dihedral_angle_1_deg15.9835449
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.16923.19163
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.91415618
X-RAY DIFFRACTIONr_dihedral_angle_4_deg26.8611520
X-RAY DIFFRACTIONr_chiral_restr0.0910.2524
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.022757
X-RAY DIFFRACTIONr_mcbond_it0.2671.52250
X-RAY DIFFRACTIONr_mcangle_it0.50723592
X-RAY DIFFRACTIONr_scbond_it0.89931413
X-RAY DIFFRACTIONr_scangle_it1.3794.51336
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A510TIGHT POSITIONAL0.040.05
1B510TIGHT POSITIONAL0.040.05
1C510TIGHT POSITIONAL0.040.05
1D510TIGHT POSITIONAL0.040.05
1E510TIGHT POSITIONAL0.040.05
1A510TIGHT THERMAL0.060.5
1B510TIGHT THERMAL0.060.5
1C510TIGHT THERMAL0.060.5
1D510TIGHT THERMAL0.080.5
1E510TIGHT THERMAL0.070.5
2A126TIGHT POSITIONAL0.060.05
2A126TIGHT THERMAL0.060.5
3C147TIGHT POSITIONAL0.050.05
3C147TIGHT THERMAL0.070.5
4A76TIGHT POSITIONAL0.030.05
4B76TIGHT POSITIONAL0.030.05
4E76TIGHT POSITIONAL0.040.05
4A76TIGHT THERMAL0.060.5
4B76TIGHT THERMAL0.040.5
4E76TIGHT THERMAL0.060.5
LS refinement shellResolution: 2.756→2.827 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.395 62 -
Rwork0.365 1231 -
all-1293 -
obs--97.81 %
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)
16.4854.99581.65556.48261.40321.6667-0.0040.028-0.7534-0.59210.4738-1.54990.50530.2228-0.4697-0.04340.06190.05690.04190.0083-0.1055-17.132419.65585.0484
29.4663-0.7279-2.40091.5047-0.53031.87820.12930.41341.0947-0.06880.17090.0539-0.51560.1332-0.30010.0624-0.0320.0241-0.0202-0.0512-0.0679-69.306438.1736-1.0479
36.65533.6863-0.32349.4773-2.2652.2236-0.11730.13370.7177-0.12860.28910.6977-0.1494-0.2678-0.1719-0.08080.0085-0.0083-0.15240.0045-0.2258-40.24791.70765.1113
49.7702-0.59821.41422.49010.79722.52140.09770.3088-0.2957-0.1040.03350.24330.1845-0.1749-0.1311-0.0614-0.05440.0331-0.1190.0182-0.31-40.904630.8742-2.1329
56.7732-2.11480.77169.3720.92524.0440.46320.43320.5819-0.477-0.21570.9135-0.3706-0.7872-0.2475-0.04630.01950.04730.10120.1018-0.0792-62.1983-13.327713.6781
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A0 - 95
2X-RAY DIFFRACTION2B0 - 95
3X-RAY DIFFRACTION3C0 - 91
4X-RAY DIFFRACTION4D1 - 91
5X-RAY DIFFRACTION5E0 - 89

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