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- PDB-4d0z: GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (H... -

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Basic information

Entry
Database: PDB / ID: 4d0z
TitleGalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset)
Components
  • PEPTIDE
  • POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
KeywordsTRANSFERASE/PEPTIDE / TRANSFERASE-PEPTIDE COMPLEX / RETAINING GALNAC-T2 / SUBSTRATE-GUIDED SNI-TYPE REACTION / QM/MM METADYNAMICS / BI-BI KINETIC MECHANISM / SUBSTRATE SPECIFICITY / ACETAMIDO GROUP
Function / homology
Function and homology information


intussusceptive angiogenesis / apoptotic process involved in heart morphogenesis / chorio-allantoic fusion / protein O-linked glycosylation via threonine / protein O-linked glycosylation via serine / polypeptide N-acetylgalactosaminyltransferase / polypeptide N-acetylgalactosaminyltransferase activity / positive regulation of ceramide biosynthetic process / protein O-linked GalNAcylation / chondroblast differentiation ...intussusceptive angiogenesis / apoptotic process involved in heart morphogenesis / chorio-allantoic fusion / protein O-linked glycosylation via threonine / protein O-linked glycosylation via serine / polypeptide N-acetylgalactosaminyltransferase / polypeptide N-acetylgalactosaminyltransferase activity / positive regulation of ceramide biosynthetic process / protein O-linked GalNAcylation / chondroblast differentiation / atrial septum morphogenesis / positive regulation of cartilage development / O-linked glycosylation of mucins / Golgi stack / protein O-linked glycosylation / COPI-independent Golgi-to-ER retrograde traffic / extracellular matrix binding / positive regulation of cell-substrate adhesion / labyrinthine layer blood vessel development / atrioventricular valve morphogenesis / ventricular septum development / Golgi cisterna membrane / positive regulation of immunoglobulin production / growth factor binding / extracellular matrix organization / reactive oxygen species metabolic process / protein maturation / positive regulation of cell differentiation / osteoblast differentiation / integrin binding / manganese ion binding / carbohydrate binding / positive regulation of cell migration / positive regulation of apoptotic process / Golgi membrane / endoplasmic reticulum membrane / negative regulation of apoptotic process / perinuclear region of cytoplasm / Golgi apparatus / signal transduction / extracellular region / membrane
Similarity search - Function
IGFBP-related, CNN / : / CCN, TSP1 domain / CCN3 Nov like TSP1 domain / Insulin-like growth factor binding protein, N-terminal, Cys-rich conserved site / Insulin-like growth factor-binding protein (IGFBP) N-terminal domain signature. / N-acetylgalactosaminyltransferase / Glycoprotein hormone subunit beta / Cystine-knot domain / Insulin-like growth factor binding protein ...IGFBP-related, CNN / : / CCN, TSP1 domain / CCN3 Nov like TSP1 domain / Insulin-like growth factor binding protein, N-terminal, Cys-rich conserved site / Insulin-like growth factor-binding protein (IGFBP) N-terminal domain signature. / N-acetylgalactosaminyltransferase / Glycoprotein hormone subunit beta / Cystine-knot domain / Insulin-like growth factor binding protein / Insulin-like growth factor-binding protein, IGFBP / Insulin-like growth factor-binding protein (IGFBP) N-terminal domain profile. / Insulin growth factor-binding protein homologues / C-terminal cystine knot signature. / C-terminal cystine knot domain profile. / von Willebrand factor type C domain / Cystine knot, C-terminal / C-terminal cystine knot-like domain (CTCK) / Glycosyltransferase 2-like / Glycosyl transferase family 2 / VWFC domain signature. / VWFC domain profile. / von Willebrand factor (vWF) type C domain / VWFC domain / Ricin-type beta-trefoil lectin domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat / Ricin-type beta-trefoil / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Nucleotide-diphospho-sugar transferases / Growth factor receptor cysteine-rich domain superfamily / Alpha-Beta Complex / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Chem-BBK / Chem-HWU / : / Polypeptide N-acetylgalactosaminyltransferase 2 / CCN family member 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsLira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. ...Lira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. / Rovira, C. / Hurtado-Guerrero, R.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Substrate-Guided Front-Face Reaction Revealed by Combined Structural Snapshots and Metadynamics for the Polypeptide N- Acetylgalactosaminyltransferase 2.
Authors: Lira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. / Rovira, C. / Hurtado-Guerrero, R.
History
DepositionApr 30, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 28, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 2, 2014Group: Database references
Revision 1.2Aug 13, 2014Group: Database references
Revision 1.3Jul 29, 2020Group: Advisory / Derived calculations ...Advisory / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _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.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.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_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Dec 20, 2023Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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
Revision 1.5Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
B: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
C: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
D: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
E: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
F: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
X: PEPTIDE
Y: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)397,36161
Polymers390,0458
Non-polymers7,31653
Water11,403633
1
B: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
X: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,78513
Polymers65,3732
Non-polymers1,41211
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3390 Å2
ΔGint18.7 kcal/mol
Surface area21710 Å2
MethodPISA
2
A: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,36114
Polymers64,8251
Non-polymers1,53613
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,5033
Polymers64,8251
Non-polymers6782
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,0519
Polymers64,8251
Non-polymers1,2268
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
F: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,5033
Polymers64,8251
Non-polymers6782
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
E: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
Y: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,15819
Polymers65,3732
Non-polymers1,78517
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3060 Å2
ΔGint13 kcal/mol
Surface area21050 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.485, 121.143, 249.387
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11E
21A
12E
22B
13E
23C
14E
24D
15E
25F
16A
26B
17A
27C
18A
28D
19A
29F
110B
210C
111B
211D
112B
212F
113C
213D
114C
214F
115D
215F

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: _

Dom-IDEns-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11EE75 - 56975 - 569
21AA75 - 56975 - 569
12EE75 - 56975 - 569
22BB75 - 56975 - 569
13EE75 - 56775 - 567
23CC75 - 56775 - 567
14EE75 - 56975 - 569
24DD75 - 56975 - 569
15EE75 - 56975 - 569
25FF75 - 56975 - 569
16AA75 - 56975 - 569
26BB75 - 56975 - 569
17AA75 - 56775 - 567
27CC75 - 56775 - 567
18AA75 - 56975 - 569
28DD75 - 56975 - 569
19AA75 - 56975 - 569
29FF75 - 56975 - 569
110BB75 - 56775 - 567
210CC75 - 56775 - 567
111BB75 - 56975 - 569
211DD75 - 56975 - 569
112BB75 - 56975 - 569
212FF75 - 56975 - 569
113CC75 - 56775 - 567
213DD75 - 56775 - 567
114CC75 - 56775 - 567
214FF75 - 56775 - 567
115DD75 - 56975 - 569
215FF75 - 56975 - 569

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15

NCS oper: (Code: given
Matrix: (-0.07309, -0.02895, 0.9969), (-0.01826, -0.9994, -0.03036), (0.9972, -0.02042, 0.07252)
Vector: 67.1676, -42.9299, -63.5268)

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Components

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Protein / Protein/peptide / Sugars , 3 types, 12 molecules ABCDEFXY

#1: Protein
POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2 / POLYPEPTIDE GALNAC TRANSFERASE 2 / GALNAC-T2 / PP-GANTASE 2 / PROTEIN-UDP ...POLYPEPTIDE GALNAC TRANSFERASE 2 / GALNAC-T2 / PP-GANTASE 2 / PROTEIN-UDP ACETYLGALACTOSAMINYLTRANSFERASE 2 / UDP-GALNAC\: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2 / POLYPEPTIDE GALNAC-TRANSFERASE T2


Mass: 64824.703 Da / Num. of mol.: 6 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: KOMAGATAELLA PASTORIS (fungus) / Strain (production host): SMD-1168
References: UniProt: Q10471, polypeptide N-acetylgalactosaminyltransferase
#2: Protein/peptide PEPTIDE


Mass: 548.610 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: KOMAGATAELLA PASTORIS (fungus) / Strain (production host): SMD-1168 / References: UniProt: Q6FI18*PLUS
#5: Sugar
ChemComp-BBK / 2-acetamido-2-deoxy-5-thio-alpha-D-galactopyranose / 2-(acetylamino)-2-deoxy-5-thio-alpha-D-galactopyranose / 2-acetamido-2-deoxy-5-thio-alpha-D-galactose / 2-acetamido-2-deoxy-5-thio-D-galactose / 2-acetamido-2-deoxy-5-thio-galactose


Type: D-saccharide, alpha linking / Mass: 237.273 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO5S

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Non-polymers , 4 types, 682 molecules

#3: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#4: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 37 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical
ChemComp-HWU / (2R,3R,4R,5R,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-thiopyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate / URIDINE DIPHOSPHO-5-THIO-N-ACETYLGALACTOSAMINE


Mass: 623.419 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C17H27N3O16P2S
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 633 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.26 Å3/Da / Density % sol: 45.47 % / Description: NONE

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.92
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 2.2→20 Å / Num. obs: 178474 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 8.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.5
Reflection shellResolution: 2.2→2.32 Å / Redundancy: 8.7 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 2.6 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
XDSdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2FFV

2ffv


Resolution: 2.2→249.39 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.938 / SU B: 13.345 / SU ML: 0.167 / Cross valid method: THROUGHOUT / ESU R: 0.251 / ESU R Free: 0.196 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.23377 4936 2.8 %RANDOM
Rwork0.19641 ---
obs0.19743 173416 99.67 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 54.284 Å2
Baniso -1Baniso -2Baniso -3
1-0.89 Å20 Å20 Å2
2---0.41 Å20 Å2
3----0.48 Å2
Refinement stepCycle: LAST / Resolution: 2.2→249.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23684 0 448 633 24765
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.01924545
X-RAY DIFFRACTIONr_bond_other_d0.0080.0223134
X-RAY DIFFRACTIONr_angle_refined_deg1.8841.96133199
X-RAY DIFFRACTIONr_angle_other_deg1.416353057
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.23452948
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.42923.3221192
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.883154117
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.17615226
X-RAY DIFFRACTIONr_chiral_restr0.1510.23530
X-RAY DIFFRACTIONr_gen_planes_refined0.010.02127668
X-RAY DIFFRACTIONr_gen_planes_other0.0070.025886
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.0583.44811821
X-RAY DIFFRACTIONr_mcbond_other3.0573.44811822
X-RAY DIFFRACTIONr_mcangle_it4.6475.15514759
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.0253.94212724
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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

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

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11E309030.06
12A309030.06
21E307800.06
22B307800.06
31E294540.06
32C294540.06
41E306830.07
42D306830.07
51E304820.06
52F304820.06
61A307290.06
62B307290.06
71A295560.06
72C295560.06
81A304680.07
82D304680.07
91A306330.06
92F306330.06
101B294160.07
102C294160.07
111B305920.07
112D305920.07
121B305640.06
122F305640.06
131C293100.07
132D293100.07
141C291290.07
142F291290.07
151D302330.07
152F302330.07
LS refinement shellResolution: 2.2→2.257 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.323 386 -
Rwork0.275 12679 -
obs--99.85 %
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)
10.06250.1346-0.05940.86930.16210.2415-0.00490.0281-0.00730.0046-0.01220.0781-0.0002-0.03910.0170.18930.00150.01310.1479-0.01080.055710.1018-39.4319-37.884
20.3055-0.42440.00691.15360.02710.03160.08980.03230.0601-0.2129-0.096-0.1666-0.0197-0.03610.00620.23340.02940.08110.10960.0540.08829.6809-2.3603-55.1407
30.1985-0.1296-0.37430.46410.32160.75870.01530.0418-0.00460.1895-0.0198-0.04830.0106-0.00690.00440.29650.0001-0.02430.14150.0110.008422.1901-32.11011.1109
40.72060.9529-0.39181.8879-1.11640.8901-0.5370.1366-0.3562-0.40770.2999-0.58220.125-0.30530.23710.5654-0.12020.17280.1522-0.07110.208953.8183-82.3863-19.254
50.626-0.2283-0.24830.34560.2710.2756-0.0227-0.08690.094-0.11460.1065-0.0604-0.00550.043-0.08380.3172-0.05160.01420.08670.0090.041167.5469-9.781-42.765
60.4835-0.1290.3170.4729-0.71751.1689-0.14940.0810.0603-0.01460.1351-0.03470.0716-0.13120.01420.22780.0447-0.10620.1222-0.02880.081141.9618-88.764919.1201
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1E75 - 569
2X-RAY DIFFRACTION2A75 - 600
3X-RAY DIFFRACTION3B75 - 569
4X-RAY DIFFRACTION4C75 - 568
5X-RAY DIFFRACTION5D75 - 600
6X-RAY DIFFRACTION6F75 - 600

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