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- PDB-1w2z: PSAO and Xenon -

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Basic information

Entry
Database: PDB / ID: 1w2z
TitlePSAO and Xenon
ComponentsAMINE OXIDASE, COPPER CONTAINING
KeywordsOXIDOREDUCTASE / GLYCOPROTEIN / MANGANESE / METAL-BINDING OXIDASE / PEA SEEDLING / TPQ OXIDOREDUCTASE / COPPER AMINE / OXIDASE / QUINONE / XENON
Function / homology
Function and homology information


diamine oxidase activity / response to chemical / primary-amine oxidase / aliphatic amine oxidase activity / primary methylamine oxidase activity / amine metabolic process / quinone binding / copper ion binding
Similarity search - Function
Copper amine oxidase, N3-terminal / Copper amine oxidase, N2-terminal / Copper amine oxidase, N2 domain / Copper amine oxidase, N3 domain / Copper amine oxidase, catalytic domain / Copper amine oxidase topaquinone signature. / Nuclear Transport Factor 2; Chain: A, - #40 / Copper amine oxidase / Copper amine oxidase, catalytic domain / Copper amine oxidase, N-terminal ...Copper amine oxidase, N3-terminal / Copper amine oxidase, N2-terminal / Copper amine oxidase, N2 domain / Copper amine oxidase, N3 domain / Copper amine oxidase, catalytic domain / Copper amine oxidase topaquinone signature. / Nuclear Transport Factor 2; Chain: A, - #40 / Copper amine oxidase / Copper amine oxidase, catalytic domain / Copper amine oxidase, N-terminal / Copper amine oxidase, catalytic domain superfamily / Copper amine oxidase, enzyme domain / Beta-galactosidase; Chain A, domain 5 / Nuclear Transport Factor 2; Chain: A, / Distorted Sandwich / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
COPPER (II) ION / IODIDE ION / : / XENON / Primary amine oxidase
Similarity search - Component
Biological speciesPISUM SATIVUM (garden pea)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.24 Å
AuthorsDuff, A.P. / Trambaiolo, D.M. / Cohen, A.E. / Ellis, P.J. / Juda, G.A. / Shepard, E.M. / Langley, D.B. / Dooley, D.M. / Freeman, H.C. / Guss, J.M.
CitationJournal: J.Mol.Biol. / Year: 2004
Title: Using Xenon as a Probe for Dioxygen-Binding Sites in Copper Amine Oxidases.
Authors: Duff, A.P. / Trambaiolo, D.M. / Cohen, A.E. / Ellis, P.J. / Juda, G.A. / Shepard, E.M. / Langley, D.B. / Dooley, D.M. / Freeman, H.C. / Guss, J.M.
History
DepositionJul 11, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 17, 2004Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Mar 14, 2012Group: Other
Revision 1.3Mar 6, 2019Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_unobs_or_zero_occ_atoms / struct_conn
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4May 8, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / struct_biol / Item: _exptl_crystal_grow.method
Revision 1.5Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / 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.conn_type_id / _struct_conn.id / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.6Dec 13, 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
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: AMINE OXIDASE, COPPER CONTAINING
B: AMINE OXIDASE, COPPER CONTAINING
C: AMINE OXIDASE, COPPER CONTAINING
D: AMINE OXIDASE, COPPER CONTAINING
hetero molecules


Theoretical massNumber of molelcules
Total (without water)320,827204
Polymers295,1984
Non-polymers25,629200
Water10,539585
1
A: AMINE OXIDASE, COPPER CONTAINING
B: AMINE OXIDASE, COPPER CONTAINING
hetero molecules


Theoretical massNumber of molelcules
Total (without water)161,175108
Polymers147,5992
Non-polymers13,576106
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19300 Å2
ΔGint-62.9 kcal/mol
Surface area53390 Å2
MethodPQS
2
C: AMINE OXIDASE, COPPER CONTAINING
D: AMINE OXIDASE, COPPER CONTAINING
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,65296
Polymers147,5992
Non-polymers12,05394
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19010 Å2
ΔGint-53.1 kcal/mol
Surface area53990 Å2
MethodPQS
Unit cell
Length a, b, c (Å)89.507, 196.268, 89.665
Angle α, β, γ (deg.)90.00, 107.46, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
12A
22C
13B
23D

NCS domain segments:

Refine code: 2

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111VALVALSERSERAA6 - 326 - 32
211VALVALSERSERBB6 - 326 - 32
311VALVALSERSERCC6 - 326 - 32
411VALVALSERSERDD6 - 326 - 32
121ASNASNLYSLYSAA34 - 4834 - 48
221ASNASNLYSLYSBB34 - 4834 - 48
321ASNASNLYSLYSCC34 - 4834 - 48
421ASNASNLYSLYSDD34 - 4834 - 48
131HISHISILEILEAA50 - 8650 - 86
231HISHISILEILEBB50 - 8650 - 86
331HISHISILEILECC50 - 8650 - 86
431HISHISILEILEDD50 - 8650 - 86
141SERSERGLYGLYAA88 - 14688 - 146
241SERSERGLYGLYBB88 - 14688 - 146
341SERSERGLYGLYCC88 - 14688 - 146
441SERSERGLYGLYDD88 - 14688 - 146
151LYSLYSGLUGLUAA149 - 201149 - 201
251LYSLYSGLUGLUBB149 - 201149 - 201
351LYSLYSGLUGLUCC149 - 201149 - 201
451LYSLYSGLUGLUDD149 - 201149 - 201
161THRTHRPHEPHEAA203 - 231203 - 231
261THRTHRPHEPHEBB203 - 231203 - 231
361THRTHRPHEPHECC203 - 231203 - 231
461THRTHRPHEPHEDD203 - 231203 - 231
171ILEILETHRTHRAA233 - 468233 - 468
271ILEILETHRTHRBB233 - 468233 - 468
371ILEILETHRTHRCC233 - 468233 - 468
471ILEILETHRTHRDD233 - 468233 - 468
181ARGARGILEILEAA470 - 471470 - 471
281ARGARGILEILEBB470 - 471470 - 471
381ARGARGILEILECC470 - 471470 - 471
481ARGARGILEILEDD470 - 471470 - 471
191SERSERTHRTHRAA475 - 536475 - 536
291SERSERTHRTHRBB475 - 536475 - 536
391SERSERTHRTHRCC475 - 536475 - 536
491SERSERTHRTHRDD475 - 536475 - 536
1101ASPASPSERSERAA538 - 572538 - 572
2101ASPASPSERSERBB538 - 572538 - 572
3101ASPASPSERSERCC538 - 572538 - 572
4101ASPASPSERSERDD538 - 572538 - 572
1111GLYGLYPROPROAA574 - 639574 - 639
2111GLYGLYPROPROBB574 - 639574 - 639
3111GLYGLYPROPROCC574 - 639574 - 639
4111GLYGLYPROPRODD574 - 639574 - 639
112ARGARGCYSCYSAA640 - 647640 - 647
212ARGARGCYSCYSCC640 - 647640 - 647
113ARGARGCYSCYSBB640 - 647640 - 647
213ARGARGCYSCYSDD640 - 647640 - 647

NCS ensembles :
ID
1
2
3

NCS oper: (Code: given
Matrix: (-0.2967, -0.004839, 0.95496), (0.007946, -0.99997, -0.002597), (0.95494, 0.006817, 0.29673)
Vector: -44.54, 48.918, -32.891)

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Components

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Protein / Sugars , 2 types, 12 molecules ABCD

#1: Protein
AMINE OXIDASE, COPPER CONTAINING


Mass: 73799.523 Da / Num. of mol.: 4 / Fragment: HOLOENZYME PLUS XENON, RESIDUES 26-674 / Source method: isolated from a natural source / Details: SEEDLING / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: Q43077, EC: 1.4.3.6
#5: 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.: 8
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 , 5 types, 777 molecules

#2: Chemical
ChemComp-CU / COPPER (II) ION


Mass: 63.546 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cu
#3: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mn
#4: Chemical
ChemComp-XE / XENON


Mass: 131.293 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Xe
#6: Chemical...
ChemComp-IOD / IODIDE ION


Mass: 126.904 Da / Num. of mol.: 176 / Source method: obtained synthetically / Formula: I
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 585 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsBINDS 1 COPPER ION, 1 MANGANESE ION AND 1 TOPAQUINONE PER SUBUNIT.
Sequence detailsDATABASE IS SWISS-PROT. THERE IS A 25 AMINO ACID PRECURSOR SEQUENCE

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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: 2.7 Å3/Da / Density % sol: 54 % / Description: NONE
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: HANGING DROP VAPOR DIFFUSION AT 293K. RESERVOIR WAS 20% PEG 3350, 0.28M KI. DROPS WERE 2 MICROL OF PSAO AT 21.58MG/ML IN 0.1M KPO4 PH 7.2, PLUS 1 MICROL OF 0.1M KPO4 PH 7.5, PLUS 1 MICROL OF ...Details: HANGING DROP VAPOR DIFFUSION AT 293K. RESERVOIR WAS 20% PEG 3350, 0.28M KI. DROPS WERE 2 MICROL OF PSAO AT 21.58MG/ML IN 0.1M KPO4 PH 7.2, PLUS 1 MICROL OF 0.1M KPO4 PH 7.5, PLUS 1 MICROL OF RESERVOIR SOLUTION. THE CRYSTAL WAS CRYOPROTECTED BY SOAKING FOR 5 MIN IN 5 MICROL OF 0.2M KI, 25% PEG 3350 AND 15% GLYCEROL UNDER 30MICROL OF PARAFFIN IN A SITTING DROP DEPRESSION. THE CRYSTAL WAS EXPOSED TO XENON GAS FOR 5 MINUTES, INITIALLY AT PRESSURE OF 100 PSI THEN INCREASING TO A FINAL PRESSURE OF 220 PSI, USING A XENON CHAMBER (HAMPTON RESEARCH). AFTER THE XENON WAS RELEASED FROM THE CHAMBER, THE CRYSTAL WAS SNAP-FROZEN IN LIQUID NITROGEN WITHIN 1-3 S.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jan 30, 2004 / Details: OSMIC MIRROR
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.24→29.82 Å / Num. obs: 141039 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 4.75 % / Biso Wilson estimate: 28.5 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 17
Reflection shellResolution: 2.24→2.3 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 7.7 / % possible all: 98.9

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1KSI

1ksi


Resolution: 2.24→29.88 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.912 / SU B: 5.474 / SU ML: 0.14 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.276 / ESU R Free: 0.205 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS SOME ATOMS WHICH HAVE BEEN REFINED WITH AN OCCUPANCY OF 0.00. ATOMS WITH AN OCCUPANCY OF 0.00 ARE NOT OBSERVED IN ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS SOME ATOMS WHICH HAVE BEEN REFINED WITH AN OCCUPANCY OF 0.00. ATOMS WITH AN OCCUPANCY OF 0.00 ARE NOT OBSERVED IN ELECTRON DENSITY MAPS. OCCUPANCIES OF XENON AND IODIDE ATOMS WERE DETERMINED USING ITERATIVE REFINEMENT OF OCCUPANCY AND B-FACTORS, USING CNS VERSION 1.1 . THE FINAL REFINED COORDINATES OF THE B CONFORMATION OF TPQ A 387 ARE INCLUDED IN THE PDB FILE, BUT ON EXAMINATION WITH THE FOURFOLD NCS AVERAGED OMIT DENSITY, THE AGREEMENT IS POOR. THE FAILURE OF REFINEMENT IS ATTRIBUTED TO THE WEAK ELECTRON DENSITY AND THE FACT THAT THE TWO CONFORMATIONS OF TPQ A 387 OCCUPY THE SAME SPACE. THE INITIAL COORDINATES FOR THE B CONFORMATION, AS OBTAINED BY MODELLING IN FOUR-FOLD AVERAGED OMIT DENSITY, ARE INCLUDED AS THE C CONFORMER.
RfactorNum. reflection% reflectionSelection details
Rfree0.224 7082 5 %RANDOM
Rwork0.179 ---
obs0.181 133957 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 19.5 Å2
Baniso -1Baniso -2Baniso -3
1--0.52 Å20 Å2-1.02 Å2
2--0.06 Å20 Å2
3----0.15 Å2
Refinement stepCycle: LAST / Resolution: 2.24→29.88 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20648 0 304 585 21537
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.02121481
X-RAY DIFFRACTIONr_bond_other_d0.0020.0219073
X-RAY DIFFRACTIONr_angle_refined_deg1.3221.94529284
X-RAY DIFFRACTIONr_angle_other_deg0.806344499
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.21852564
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0830.23266
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0223571
X-RAY DIFFRACTIONr_gen_planes_other0.0020.024292
X-RAY DIFFRACTIONr_nbd_refined0.1880.23674
X-RAY DIFFRACTIONr_nbd_other0.2360.221886
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0820.212967
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1490.2764
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0110.21
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2020.231
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2220.280
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1770.25
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.539212862
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.698321103
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it4.15848619
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it5.97468181
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

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A3653tight positional0.040.05
12B3653tight positional0.030.05
13C3653tight positional0.030.05
14D3653tight positional0.040.05
21A46tight positional0.020.05
31B46tight positional0.020.05
11A5958medium positional0.220.5
12B5958medium positional0.190.5
13C5958medium positional0.190.5
14D5958medium positional0.20.5
21A71medium positional0.120.5
31B71medium positional0.280.5
11A3653tight thermal0.130.5
12B3653tight thermal0.130.5
13C3653tight thermal0.120.5
14D3653tight thermal0.130.5
21A46tight thermal0.110.5
31B46tight thermal0.060.5
11A5958medium thermal0.732
12B5958medium thermal0.712
13C5958medium thermal0.722
14D5958medium thermal0.722
21A71medium thermal0.572
31B71medium thermal0.572
LS refinement shellResolution: 2.24→2.3 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.252 545
Rwork0.192 9845
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)
10.79310.65330.48350.847-0.01130.318-0.12430.24080.0597-0.14450.10360.07720.01830.0450.02080.1786-0.0480.00110.1939-0.00180.05067.41982.6528-36.5658
20.6632-0.2536-0.2060.33550.35510.5541-0.07980.1032-0.048-0.0428-0.0230.27850.051-0.25640.10280.0981-0.0172-0.02980.2379-0.0470.1902-21.0018-7.1368-18.9427
32.0365-0.4255-0.01780.95320.47240.87550.0104-0.16790.3463-0.0035-0.08660.2837-0.1266-0.15950.07630.12890.0045-0.01510.125-0.00790.1254-4.904219.97950.3993
40.27540.03470.15910.31440.05920.3343-0.01590.05310.0137-0.03-0.00930.03220.0085-0.03160.02520.1336-0.01410.01980.1312-0.00170.128111.2588-2.2772-9.1552
530.3214-8.7797-0.115614.3838-0.95193.70730.2783-0.03592.534-0.0015-0.3935-1.2512-0.06520.09360.11520.1242-0.0008-0.00120.1240.00010.12515.286530.9082.7774
61.2873-0.3727-0.10880.89910.1770.6097-0.0161-0.16960.07680.16970.0055-0.03840.0277-0.06540.01060.1839-0.00740.03230.1423-0.03210.03112.93315.460341.2067
70.94570.4112-0.45050.3644-0.15621.10170.0187-0.1412-0.02570.1775-0.0366-0.157-0.05390.20260.01790.1343-0.0178-0.04680.12540.01380.100342.86330.841723.9062
81.6462-0.08310.41370.2792-0.1052-0.1572-0.12280.15590.18510.1169-0.01440.053-0.15620.01750.13710.1425-0.0272-0.0360.12990.01220.125721.526522.85253.1917
90.29960.00020.12570.31440.0110.4083-0.0022-0.03430.01940.0709-0.01780.06480.0086-0.07310.02010.1459-0.0080.03270.1199-0.0180.13110.3137-1.699414.1308
1029.432624.502-5.283655.2877-7.69497.38160.2671.23271.7763-0.5225-0.04851.29680.19910.0696-0.21850.1240-0.00070.1239-0.00040.12440.551629.9645-1.0881
110.3369-0.0117-0.16410.29770.01420.7882-0.03730.06780.0897-0.12650.07350.15850.0876-0.2096-0.03620.1012-0.0801-0.07580.25740.08220.2394-18.699246.687548.1862
120.7190.0555-0.06380.5015-0.0061.1591-0.06730.2898-0.0059-0.30640.08610.1040.0343-0.1135-0.01880.2625-0.0788-0.0620.20770.04880.1046.624756.139226.2211
130.83450.2763-0.36631.28450.67850.883-0.00060.1371-0.2287-0.2341-0.0001-0.12980.13530.07220.00070.13490.0224-0.0420.1304-0.02140.142520.207329.155447.5277
140.29410.12410.0510.422-0.07370.444-0.02360.02950.0284-0.05850.03880.06860.016-0.0921-0.01520.1323-0.0125-0.00190.13360.02070.15796.361351.570759.9682
152.5944-4.135-8.628213.29095.798826.9504-0.4880.145-0.06020.7316-0.37180.21721.7365-0.24210.85970.1252-0.0002-0.00050.12380.00090.12416.384618.347467.6044
160.919-0.1086-0.20520.65910.31161.23310.01870.0018-0.09910.0832-0.0092-0.18890.10560.1719-0.00940.04240.0295-0.02720.1560.00870.24753.808643.739476.6397
171.17220.5195-0.43820.6679-0.2530.70190.1164-0.2714-0.10230.2625-0.1008-0.1247-0.01590.0922-0.01560.1691-0.0484-0.04770.16310.04240.094828.513148.675699.9834
18-0.49510.3338-0.47490.6305-0.00122.80050.0046-0.0627-0.13250.00260.0181-0.25220.3982-0.0308-0.02270.1366-0.0155-0.04990.12640.01150.140814.906726.523673.6502
190.31470.10650.08560.4193-0.03890.47260.00490.0244-0.0364-0.04430.0028-0.08160.01190.0706-0.00770.12050.00130.01720.11210.00930.154228.862850.886165.9971
2013.171317.8678-14.133360.4107-25.889431.321-0.50910.33960.3321-0.44310.22130.60211.4597-0.73020.28780.1246-0.0001-0.00080.12410.00010.124116.990119.241252.3609
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A6 - 102
2X-RAY DIFFRACTION2A103 - 204
3X-RAY DIFFRACTION3A205 - 230
4X-RAY DIFFRACTION4A231 - 638
5X-RAY DIFFRACTION5A639 - 647
6X-RAY DIFFRACTION6B6 - 102
7X-RAY DIFFRACTION7B103 - 204
8X-RAY DIFFRACTION8B205 - 230
9X-RAY DIFFRACTION9B231 - 638
10X-RAY DIFFRACTION10B639 - 647
11X-RAY DIFFRACTION11C6 - 102
12X-RAY DIFFRACTION12C103 - 204
13X-RAY DIFFRACTION13C205 - 230
14X-RAY DIFFRACTION14C231 - 638
15X-RAY DIFFRACTION15C639 - 647
16X-RAY DIFFRACTION16D6 - 102
17X-RAY DIFFRACTION17D103 - 204
18X-RAY DIFFRACTION18D205 - 230
19X-RAY DIFFRACTION19D231 - 638
20X-RAY DIFFRACTION20D639 - 647

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