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- PDB-4miv: Crystal Structure of Sulfamidase, Crystal Form L -

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Basic information

Entry
Database: PDB / ID: 4miv
TitleCrystal Structure of Sulfamidase, Crystal Form L
ComponentsN-sulphoglucosamine sulphohydrolase
KeywordsHYDROLASE / sulfatase fold / heparan / heparin / lysosome
Function / homology
Function and homology information


N-sulfoglucosamine sulfohydrolase / N-sulfoglucosamine sulfohydrolase activity / MPS IIIA - Sanfilippo syndrome A / glycosaminoglycan catabolic process / heparan sulfate proteoglycan catabolic process / sulfuric ester hydrolase activity / HS-GAG degradation / motor behavior / lysosomal lumen / determination of adult lifespan ...N-sulfoglucosamine sulfohydrolase / N-sulfoglucosamine sulfohydrolase activity / MPS IIIA - Sanfilippo syndrome A / glycosaminoglycan catabolic process / heparan sulfate proteoglycan catabolic process / sulfuric ester hydrolase activity / HS-GAG degradation / motor behavior / lysosomal lumen / determination of adult lifespan / lysosome / extracellular exosome / metal ion binding
Similarity search - Function
N-sulphoglucosamine sulphohydrolase, C-terminal / N-sulphoglucosamine sulphohydrolase, C-terminal / Sulfatases signature 2. / Sulfatases signature 1. / Sulfatase, conserved site / Sulfatase, N-terminal / Sulfatase / Alkaline Phosphatase, subunit A / Alkaline Phosphatase, subunit A / Alkaline-phosphatase-like, core domain superfamily ...N-sulphoglucosamine sulphohydrolase, C-terminal / N-sulphoglucosamine sulphohydrolase, C-terminal / Sulfatases signature 2. / Sulfatases signature 1. / Sulfatase, conserved site / Sulfatase, N-terminal / Sulfatase / Alkaline Phosphatase, subunit A / Alkaline Phosphatase, subunit A / Alkaline-phosphatase-like, core domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / N-sulphoglucosamine sulphohydrolase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / molecular replacement / Resolution: 2.4 Å
AuthorsSidhu, N.S. / Uson, I. / Schreiber, K. / Proepper, K. / Becker, S. / Sheldrick, G.M. / Gaertner, J. / Kraetzner, R. / Steinfeld, R.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2014
Title: Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIA.
Authors: Sidhu, N.S. / Schreiber, K. / Propper, K. / Becker, S. / Uson, I. / Sheldrick, G.M. / Gartner, J. / Kratzner, R. / Steinfeld, R.
History
DepositionSep 2, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 14, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 9, 2015Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_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_asym_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_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jun 2, 2021Group: Source and taxonomy / Structure summary / Category: chem_comp / entity_src_gen
Item: _chem_comp.pdbx_synonyms / _entity_src_gen.host_org_common_name ..._chem_comp.pdbx_synonyms / _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: N-sulphoglucosamine sulphohydrolase
B: N-sulphoglucosamine sulphohydrolase
C: N-sulphoglucosamine sulphohydrolase
D: N-sulphoglucosamine sulphohydrolase
E: N-sulphoglucosamine sulphohydrolase
F: N-sulphoglucosamine sulphohydrolase
G: N-sulphoglucosamine sulphohydrolase
H: N-sulphoglucosamine sulphohydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)473,85047
Polymers463,2988
Non-polymers10,55239
Water8,557475
1
A: N-sulphoglucosamine sulphohydrolase
B: N-sulphoglucosamine sulphohydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,92913
Polymers115,8242
Non-polymers3,10411
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8470 Å2
ΔGint-26 kcal/mol
Surface area34860 Å2
MethodPISA
2
C: N-sulphoglucosamine sulphohydrolase
D: N-sulphoglucosamine sulphohydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)119,03514
Polymers115,8242
Non-polymers3,21112
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8710 Å2
ΔGint-18 kcal/mol
Surface area34720 Å2
MethodPISA
3
E: N-sulphoglucosamine sulphohydrolase
F: N-sulphoglucosamine sulphohydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,04510
Polymers115,8242
Non-polymers2,2208
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6960 Å2
ΔGint-30 kcal/mol
Surface area34080 Å2
MethodPISA
4
G: N-sulphoglucosamine sulphohydrolase
H: N-sulphoglucosamine sulphohydrolase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,84110
Polymers115,8242
Non-polymers2,0178
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6650 Å2
ΔGint-19 kcal/mol
Surface area34420 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.930, 211.450, 108.350
Angle α, β, γ (deg.)90.000, 102.690, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16A
26G
17A
27H
18A
28B
19A
29C
110A
210D
111A
211E
112A
212F
113A
213G
114A
214H
115B
215C
116B
216D
117B
217E
118B
218F
119B
219G
120B
220H
121B
221C
122B
222D
123B
223E
124B
224F
125B
225G
126B
226H
127C
227D
128C
228E
129C
229F
130C
230G
131C
231H
132C
232D
133C
233E
134C
234F
135C
235G
136C
236H
137D
237E
138D
238F
139D
239G
140D
240H
141D
241E
142D
242F
143D
243G
144D
244H
145E
245F
146E
246G
147E
247H
148E
248F
149E
249G
150E
250H
151F
251G
152F
252H
153F
253G
154F
254H
155G
255H
156G
256H

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1010A22 - 69
2010B22 - 69
1020A22 - 68
2020C22 - 68
1030A22 - 69
2030D22 - 69
1040A22 - 69
2040E22 - 69
1050A22 - 69
2050F22 - 69
1060A22 - 69
2060G22 - 69
1070A22 - 69
2070H22 - 69
1080A71 - 501
2080B71 - 501
1090A71 - 503
2090C71 - 503
10100A71 - 500
20100D71 - 500
10110A71 - 503
20110E71 - 503
10120A71 - 500
20120F71 - 500
10130A71 - 500
20130G71 - 500
10140A71 - 502
20140H71 - 502
10150B22 - 68
20150C22 - 68
10160B22 - 69
20160D22 - 69
10170B22 - 69
20170E22 - 69
10180B22 - 69
20180F22 - 69
10190B22 - 69
20190G22 - 69
10200B22 - 69
20200H22 - 69
10210B71 - 501
20210C71 - 501
10220B71 - 500
20220D71 - 500
10230B71 - 501
20230E71 - 501
10240B71 - 501
20240F71 - 501
10250B71 - 501
20250G71 - 501
10260B71 - 501
20260H71 - 501
10270C22 - 68
20270D22 - 68
10280C22 - 68
20280E22 - 68
10290C22 - 68
20290F22 - 68
10300C22 - 68
20300G22 - 68
10310C22 - 68
20310H22 - 68
10320C71 - 500
20320D71 - 500
10330C71 - 504
20330E71 - 504
10340C71 - 500
20340F71 - 500
10350C71 - 500
20350G71 - 500
10360C71 - 502
20360H71 - 502
10370D22 - 69
20370E22 - 69
10380D22 - 69
20380F22 - 69
10390D22 - 69
20390G22 - 69
10400D22 - 69
20400H22 - 69
10410D71 - 500
20410E71 - 500
10420D71 - 501
20420F71 - 501
10430D71 - 501
20430G71 - 501
10440D71 - 500
20440H71 - 500
10450E22 - 69
20450F22 - 69
10460E22 - 69
20460G22 - 69
10470E22 - 69
20470H22 - 69
10480E71 - 500
20480F71 - 500
10490E71 - 500
20490G71 - 500
10500E71 - 502
20500H71 - 502
10510F22 - 69
20510G22 - 69
10520F22 - 69
20520H22 - 69
10530F71 - 501
20530G71 - 501
10540F71 - 501
20540H71 - 501
10550G22 - 69
20550H22 - 69
10560G71 - 500
20560H71 - 500

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
DetailsThe biological unit is a dimer. There are 4 biological units in the asymmetric unit (chains A and B; C and D; E and F; and G and H

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Components

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein
N-sulphoglucosamine sulphohydrolase / Sulfoglucosamine sulfamidase / Sulphamidase


Mass: 57912.199 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SGSH, HSS / Cell line (production host): HEK 293 / Production host: Homo sapiens (human)
References: UniProt: P51688, N-sulfoglucosamine sulfohydrolase

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Sugars , 2 types, 28 molecules

#2: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 19
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 9
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

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Non-polymers , 4 types, 486 molecules

#3: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca
#5: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 475 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsAUTHORS STATE THAT THE CYS->FGP CONFLICT IS DUE TO A NATURAL REACTION THAT FIRST CHANGED CYS TO A ...AUTHORS STATE THAT THE CYS->FGP CONFLICT IS DUE TO A NATURAL REACTION THAT FIRST CHANGED CYS TO A FORMYLGLYCINE RESIDUE. THE LATTER THEN APPARENTLY PICKED UP A PHOSPHATE FROM THE PURIFICATION BUFFER TO BECOME FGP

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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: 2.48 Å3/Da / Density % sol: 50.46 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.1
Details: 13% (w/v) polyethylene glycol (PEG) 8000, 200 mM MgCl2 and 100 mM Bis-Tris buffer, pH 5.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99989 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 23, 2012
RadiationMonochromator: Double-crystal Si(111) monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99989 Å / Relative weight: 1
ReflectionResolution: 2.4→48.9 Å / Num. obs: 333757 / % possible obs: 95.6 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 54.586 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 7.78
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.4-2.460.5611.32439852438994.7
2.46-2.530.4311.72448082460197.5
2.53-2.60.3572.08429892374597.5
2.6-2.680.2962.52414282296196.5
2.68-2.770.2582.95394112224195.9
2.77-2.870.1963.73367902125995.5
2.87-2.980.164.62365412052796
2.98-3.10.1265.65373642033397.9
3.1-3.230.17.06353261932197.3
3.23-3.390.0818.44334061834696.7
3.39-3.580.06410.22307131721095.4
3.58-3.790.05511.7278301606794.4
3.79-4.060.04414.28274671512094.3
4.06-4.380.04115.83259331403594.1
4.38-4.80.03717.09231121275292.8
4.8-5.360.03616.53197861154692.8
5.36-6.190.03616.91183281036894.6
6.19-7.590.03218.7716273878294.9
7.59-10.730.02920.8611540663292.8
10.730.0322.626168352289.7

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.45 Å48.87 Å
Translation2.45 Å48.87 Å

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASER2.5.1phasing
DMphasing
REFMACrefinement
PDB_EXTRACT3.11data extraction
DA+data collection
XDSdata reduction
RefinementResolution: 2.4→48.85 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.919 / WRfactor Rfree: 0.247 / WRfactor Rwork: 0.212 / Occupancy max: 1 / Occupancy min: 0.25 / FOM work R set: 0.7789 / SU B: 21.746 / SU ML: 0.244 / SU R Cruickshank DPI: 0.4565 / SU Rfree: 0.259 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.456 / ESU R Free: 0.259 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2447 8462 4.8 %RANDOM
Rwork0.2157 166273 --
obs0.2173 174735 99.34 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 177.76 Å2 / Biso mean: 64.5717 Å2 / Biso min: 15.07 Å2
Baniso -1Baniso -2Baniso -3
1-2.39 Å20 Å20.57 Å2
2--0.36 Å2-0 Å2
3----2.61 Å2
Refinement stepCycle: LAST / Resolution: 2.4→48.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29985 0 662 475 31122
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0030.01931707
X-RAY DIFFRACTIONr_bond_other_d0.0010.0228097
X-RAY DIFFRACTIONr_angle_refined_deg0.6831.96943459
X-RAY DIFFRACTIONr_angle_other_deg0.5533.00164240
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.39653837
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.81223.2431446
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.552154357
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.43315197
X-RAY DIFFRACTIONr_chiral_restr0.0420.24723
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02136187
X-RAY DIFFRACTIONr_gen_planes_other0.0030.027717
X-RAY DIFFRACTIONr_mcbond_it2.2121.6215411
X-RAY DIFFRACTIONr_mcbond_other2.2121.6215410
X-RAY DIFFRACTIONr_mcangle_it3.3022.42819206
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A19720.11
12B19720.11
21A19860.07
22C19860.07
31A19940.09
32D19940.09
41A15510.1
42E15510.1
51A19170.06
52F19170.06
61A19660.1
62G19660.1
71A14600.11
72H14600.11
81A253500.08
82B253500.08
91A261220.06
92C261220.06
101A252340.09
102D252340.09
111A219030.07
112E219030.07
121A233130.09
122F233130.09
131A232420.08
132G232420.08
141A220060.1
142H220060.1
151B19650.11
152C19650.11
161B20130.11
162D20130.11
171B15590.1
172E15590.1
181B18990.09
182F18990.09
191B19990.1
192G19990.1
201B14210.15
202H14210.15
211B254630.09
212C254630.09
221B257580.07
222D257580.07
231B213650.1
232E213650.1
241B235780.08
242F235780.08
251B231030.09
252G231030.09
261B221570.09
262H221570.09
271C20030.07
272D20030.07
281C15120.1
282E15120.1
291C18980.04
292F18980.04
301C19620.09
302G19620.09
311C14210.11
312H14210.11
321C251960.09
322D251960.09
331C219300.08
332E219300.08
341C232640.09
342F232640.09
351C233380.08
352G233380.08
361C220360.1
362H220360.1
371D15720.09
372E15720.09
381D19360.06
382F19360.06
391D20330.09
392G20330.09
401D14500.12
402H14500.12
411D210840.1
412E210840.1
421D233070.09
422F233070.09
431D229440.09
432G229440.09
441D218870.09
442H218870.09
451E15650.09
452F15650.09
461E15590.1
462G15590.1
471E12170.13
472H12170.13
481E201950.1
482F201950.1
491E202720.09
492G202720.09
501E194580.1
502H194580.1
511F18970.07
512G18970.07
521F14440.12
522H14440.12
531F217890.09
532G217890.09
541F208040.09
542H208040.09
551G14250.14
552H14250.14
561G203270.1
562H203270.1
LS refinement shellResolution: 2.399→2.461 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree1.26 1 -
Rwork0.397 12653 -
all-12654 -
obs--97.92 %
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)
11.36380.00840.13560.4968-0.30951.54860.0176-0.1621-0.06680.12190.0990.33010.0618-0.3911-0.11650.19520.03970.10550.41910.07180.411319.9673130.149153.1102
25.2213-1.39421.88482.4998-0.84813.52030.0180.00780.56610.20030.11840.063-0.6338-0.2116-0.13640.38540.12690.15320.3162-0.01760.430627.7022149.82953.7096
31.9210.2590.78311.70170.14461.3960.01860.04250.0521-0.11210.08250.3428-0.1164-0.1748-0.10110.14380.02420.03280.27030.04920.29231.2769135.162731.6529
49.6951.6116-5.01582.6695-0.96277.36320.02780.08340.819-0.2938-0.18270.2044-1.13510.01560.15490.34230.0338-0.06020.17470.05610.35649.8326145.830335.501
51.4206-0.08130.15630.9853-0.33052.7605-0.0533-0.22940.20170.2762-0.0425-0.2551-0.32590.4410.09580.1999-0.0233-0.02550.30980.00690.26270.0903130.254753.7551
69.7336-3.5318-3.10522.13510.48323.20770.17750.0925-0.5673-0.0182-0.08280.08120.42490.0062-0.09480.33140.0114-0.00960.22210.0350.263462.2297110.54754.1072
71.27670.156-0.29512.6699-0.40481.83860.0377-0.01820.0101-0.2655-0.0126-0.05780.1150.1222-0.02520.1020.00760.01210.18990.02050.155459.4067125.404331.8801
812.37513.66486.52874.92553.11333.81180.67060.063-0.7885-0.0419-0.3248-0.07170.3103-0.0735-0.34580.2652-0.01760.01880.2527-0.00450.262240.7328114.834235.7293
91.3216-0.21120.07340.8278-0.082.00580.08410.1593-0.0479-0.1447-0.0821-0.32160.07990.3256-0.00210.16450.0390.10620.37050.03840.373697.9199130.134293.4268
105.38212.862.43043.05170.45422.61630.33050.08530.6288-0.0293-0.20380.0281-0.32850.1439-0.12670.46490.04320.29620.30910.0810.570690.2304149.700993.1103
111.3249-0.2410.5381.7989-0.46971.48830.0509-0.02610.04170.19260.0065-0.2654-0.15650.1313-0.05740.13590.01050.04180.26420.01680.31287.1002134.8645115.3558
129.7976-3.8252-5.65925.12516.01717.70190.869-0.28130.5158-0.1103-0.6473-0.2916-0.8218-0.3482-0.22170.8408-0.2882-0.17380.35790.14790.40468.5939145.4207111.8182
131.4053-0.2539-0.35021.0944-0.05641.41270.07910.41550.1356-0.2209-0.02560.2633-0.1265-0.362-0.05350.18960.0594-0.01250.41730.04540.282847.7098129.808794.5121
144.75991.6662-3.36372.7405-0.13423.1037-0.09620.2498-0.3097-0.03590.0177-0.02150.3096-0.14070.07850.3420.0385-0.0980.3158-0.03830.316555.9005110.192894.1039
151.759-0.4649-0.9061.96710.55681.36780.06820.0531-0.05850.1489-0.016-0.00350.0601-0.0191-0.05220.10910.0269-0.00140.21020.01780.178559.1879125.0783115.8008
167.6295-1.10074.55035.7846-1.9313.02360.23530.2892-0.60020.11460.00250.00770.13620.1743-0.23790.17610.0340.08830.31430.00650.371977.9988114.1896110.7326
173.19881.0956-1.62621.5995-0.24891.8695-0.21980.5299-0.02140.0479-0.02210.2416-0.3542-0.82430.24190.96950.0065-0.13120.6132-0.13440.430822.027475.4247103.1248
1811.0778-0.82624.44672.34850.51016.23710.01560.71331.127-0.06260.04870.1873-0.6818-0.5359-0.06421.2560.0819-0.15130.45930.14920.684728.842395.423597.8541
192.3761-0.2002-1.54013.2405-0.00792.7942-0.32481.1296-0.1499-0.37160.01170.1482-0.313-0.94390.31320.9137-0.1939-0.11730.9491-0.13220.3833.377774.366281.3518
2010.74071.7165-5.99530.2802-0.83659.9128-0.68891.5591.2823-0.09390.21770.2456-0.83420.39310.47121.4253-0.3455-0.33030.74240.22570.517251.142686.420580.9099
212.95540.1323-0.00141.04550.22770.8561-0.4439-0.02940.23440.17770.0918-0.2595-0.24620.33290.35211.0223-0.1566-0.18980.42870.06450.459571.613478.9025103.3684
229.7146-2.5508-2.72491.98060.19243.01-0.1825-0.0958-1.21430.15820.06430.07970.06760.19930.11821.0093-0.0551-0.00140.35660.08080.561864.738659.7516109.5144
232.5858-0.1941-0.26722.6065-1.38551.7933-0.30070.5457-0.2616-0.0145-0.0191-0.2133-0.13950.27790.31980.8423-0.2231-0.01680.5164-0.09550.413961.687667.191184.4056
2410.22657.80860.44576.74032.92498.7424-0.34750.237-1.53240.0357-0.0155-0.96870.8037-0.49320.3630.826-0.14420.1770.3998-0.19230.786143.410156.80991.8213
251.87320.08980.77581.2649-0.26712.92870.3278-0.1689-0.4515-0.1407-0.10680.19751.3891-0.5775-0.2211.2778-0.1477-0.15370.37520.01650.441849.197377.927243.6366
263.99-4.0063.68754.2826-4.40556.3789-0.3108-0.25760.74440.24810.0922-0.5339-0.0159-0.32690.21860.7299-0.0327-0.0570.4231-0.13690.393854.983296.710451.0529
272.0934-0.18780.97823.20310.43052.93620.30930.4167-0.0815-0.4557-0.2227-0.03811.02160.4351-0.08650.98770.3173-0.01420.41830.00110.316466.875787.244129.5743
286.60674.0171-2.30167.7522-2.73651.16670.1599-0.14970.8981-0.2711-0.2219-0.1660.1750.22720.0620.81390.40290.08110.60770.15240.57881.966896.220842.7426
291.1874-0.12190.3710.9235-0.16612.35270.32620.00040.0968-0.0947-0.3256-0.18160.76140.8971-0.00061.06350.49-0.04580.74260.07580.514494.393477.018462.7613
303.083-2.8969-1.44743.2518-0.5677.80470.5751-0.3235-0.176-0.79210.09430.37031.43911.3719-0.66942.24280.6286-0.26550.5876-0.22020.67988.634357.266956.1921
311.82750.04280.15022.89640.61591.85980.19350.3534-0.0947-0.3773-0.1106-0.37440.98810.983-0.08291.35630.7389-0.01970.95360.01830.44693.211777.552838.1308
322.8154-2.4543.81694.7448-3.06055.52940.62680.7373-0.57280.77490.0377-0.03350.97020.674-0.66452.04820.6641-0.39540.9029-0.30530.717675.8766.130732.0079
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A21 - 327
2X-RAY DIFFRACTION2A328 - 358
3X-RAY DIFFRACTION3A359 - 477
4X-RAY DIFFRACTION4A478 - 505
5X-RAY DIFFRACTION5B22 - 327
6X-RAY DIFFRACTION6B328 - 358
7X-RAY DIFFRACTION7B359 - 477
8X-RAY DIFFRACTION8B478 - 502
9X-RAY DIFFRACTION9C21 - 327
10X-RAY DIFFRACTION10C328 - 358
11X-RAY DIFFRACTION11C359 - 477
12X-RAY DIFFRACTION12C478 - 504
13X-RAY DIFFRACTION13D21 - 327
14X-RAY DIFFRACTION14D328 - 358
15X-RAY DIFFRACTION15D359 - 477
16X-RAY DIFFRACTION16D478 - 501
17X-RAY DIFFRACTION17E22 - 327
18X-RAY DIFFRACTION18E328 - 358
19X-RAY DIFFRACTION19E359 - 477
20X-RAY DIFFRACTION20E478 - 504
21X-RAY DIFFRACTION21F22 - 327
22X-RAY DIFFRACTION22F328 - 358
23X-RAY DIFFRACTION23F359 - 477
24X-RAY DIFFRACTION24F478 - 502
25X-RAY DIFFRACTION25G22 - 327
26X-RAY DIFFRACTION26G328 - 358
27X-RAY DIFFRACTION27G359 - 477
28X-RAY DIFFRACTION28G478 - 501
29X-RAY DIFFRACTION29H22 - 327
30X-RAY DIFFRACTION30H328 - 358
31X-RAY DIFFRACTION31H359 - 477
32X-RAY DIFFRACTION32H478 - 503

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