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Basic information

Entry
Database: PDB / ID: 4pfq
TitleCrystal structure of hypoxanthine phosphoribosyltransferase from Brachybacterium faecium DSM 4810, NYSGRC Target 029763.
ComponentsHypoxanthine phosphoribosyltransferaseHypoxanthine-guanine phosphoribosyltransferase
KeywordsTRANSFERASE / STRUCTURAL GENOMICS / PROTEIN STRUCTURE INITIATIVE / PSI-Biology / New York Structural Genomics Research Consortium / NYSGRC
Function / homology
Function and homology information


hypoxanthine phosphoribosyltransferase / guanine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase activity / IMP salvage / purine ribonucleoside salvage / nucleotide binding / metal ion binding / cytoplasm
Similarity search - Function
Hypoxanthine phosphoribosyl transferase / Rossmann fold - #2020 / Phosphoribosyl transferase domain / Phosphoribosyltransferase-like / Phosphoribosyltransferase domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Hypoxanthine phosphoribosyltransferase
Similarity search - Component
Biological speciesBrachybacterium faecium (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.1 Å
AuthorsMalashkevich, V.N. / Bhosle, R. / Toro, R. / Hillerich, B. / Gizzi, A. / Garforth, S. / Kar, A. / Chan, M.K. / Lafluer, J. / Patel, H. ...Malashkevich, V.N. / Bhosle, R. / Toro, R. / Hillerich, B. / Gizzi, A. / Garforth, S. / Kar, A. / Chan, M.K. / Lafluer, J. / Patel, H. / Matikainen, B. / Chamala, S. / Lim, S. / Celikgil, A. / Villegas, G. / Evans, B. / Love, J. / Fiser, A. / Seidel, R. / Bonanno, J.B. / Almo, S.C. / New York Structural Genomics Research Consortium (NYSGRC)
CitationJournal: to be published
Title: Crystal structure of hypoxanthine phosphoribosyltransferase from Brachybacterium faecium DSM 4810, NYSGRC Target 0299763.
Authors: Malashkevich, V.N. / Bhosle, R. / Toro, R. / Hillerich, B. / Gizzi, A. / Garforth, S. / Kar, A. / Chan, M.K. / Lafluer, J. / Patel, H. / Matikainen, B. / Chamala, S. / Lim, S. / Celikgil, A. ...Authors: Malashkevich, V.N. / Bhosle, R. / Toro, R. / Hillerich, B. / Gizzi, A. / Garforth, S. / Kar, A. / Chan, M.K. / Lafluer, J. / Patel, H. / Matikainen, B. / Chamala, S. / Lim, S. / Celikgil, A. / Villegas, G. / Evans, B. / Love, J. / Fiser, A. / Seidel, R. / Bonanno, J.B. / Almo, S.C. / New York Structural Genomics Research Consortium (NYSGRC)
History
DepositionApr 30, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 2, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 6, 2014Group: Structure summary
Revision 1.2Nov 22, 2017Group: Derived calculations / Other ...Derived calculations / Other / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_database_status ...entity_src_gen / pdbx_database_status / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.3Dec 27, 2023Group: 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 / pdbx_struct_conn_angle / refine_hist / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr1_symmetry / _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.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_conn.ptnr2_symmetry / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hypoxanthine phosphoribosyltransferase
B: Hypoxanthine phosphoribosyltransferase
C: Hypoxanthine phosphoribosyltransferase
D: Hypoxanthine phosphoribosyltransferase
E: Hypoxanthine phosphoribosyltransferase
F: Hypoxanthine phosphoribosyltransferase
G: Hypoxanthine phosphoribosyltransferase
H: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)187,53620
Polymers187,2458
Non-polymers29212
Water9,782543
1
A: Hypoxanthine phosphoribosyltransferase
D: Hypoxanthine phosphoribosyltransferase
F: Hypoxanthine phosphoribosyltransferase
H: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,76810
Polymers93,6224
Non-polymers1466
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Hypoxanthine phosphoribosyltransferase
C: Hypoxanthine phosphoribosyltransferase
E: Hypoxanthine phosphoribosyltransferase
G: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,76810
Polymers93,6224
Non-polymers1466
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: Hypoxanthine phosphoribosyltransferase
H: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,8845
Polymers46,8112
Non-polymers733
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2470 Å2
ΔGint-13 kcal/mol
Surface area17240 Å2
MethodPISA
4
B: Hypoxanthine phosphoribosyltransferase
C: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,8845
Polymers46,8112
Non-polymers733
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2510 Å2
ΔGint-13 kcal/mol
Surface area17250 Å2
MethodPISA
5
D: Hypoxanthine phosphoribosyltransferase
F: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,8845
Polymers46,8112
Non-polymers733
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2520 Å2
ΔGint-13 kcal/mol
Surface area17180 Å2
MethodPISA
6
E: Hypoxanthine phosphoribosyltransferase
G: Hypoxanthine phosphoribosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,8845
Polymers46,8112
Non-polymers733
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2460 Å2
ΔGint-12 kcal/mol
Surface area17170 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.210, 123.587, 123.285
Angle α, β, γ (deg.)90.00, 90.45, 90.00
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
18B
28C
19B
29D
110B
210E
111B
211F
112B
212G
113B
213H
114C
214D
115C
215E
116C
216F
117C
217G
118C
218H
119D
219E
120D
220F
121D
221G
122D
222H
123E
223F
124E
224G
125E
225H
126F
226G
127F
227H
128G
228H

NCS domain segments:

Component-ID: 0 / Refine code: 0

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PROPROTYRTYRAA29 - 20529 - 205
21PROPROTYRTYRBB29 - 20529 - 205
12PROPROVALVALAA29 - 20429 - 204
22PROPROVALVALCC29 - 20429 - 204
13PROPROVALVALAA29 - 20429 - 204
23PROPROVALVALDD29 - 20429 - 204
14PROPROVALVALAA29 - 20429 - 204
24PROPROVALVALEE29 - 20429 - 204
15PROPROVALVALAA29 - 20429 - 204
25PROPROVALVALFF29 - 20429 - 204
16PROPROTYRTYRAA29 - 20529 - 205
26PROPROTYRTYRGG29 - 20529 - 205
17PROPROVALVALAA29 - 20429 - 204
27PROPROVALVALHH29 - 20429 - 204
18PROPROVALVALBB29 - 20429 - 204
28PROPROVALVALCC29 - 20429 - 204
19PROPROVALVALBB29 - 20429 - 204
29PROPROVALVALDD29 - 20429 - 204
110PROPROVALVALBB29 - 20429 - 204
210PROPROVALVALEE29 - 20429 - 204
111PROPROVALVALBB29 - 20429 - 204
211PROPROVALVALFF29 - 20429 - 204
112PROPROTYRTYRBB29 - 20529 - 205
212PROPROTYRTYRGG29 - 20529 - 205
113PROPROVALVALBB29 - 20429 - 204
213PROPROVALVALHH29 - 20429 - 204
114PROPROTYRTYRCC29 - 20529 - 205
214PROPROTYRTYRDD29 - 20529 - 205
115VALVALASPASPCC24 - 20724 - 207
215VALVALASPASPEE24 - 20724 - 207
116VALVALASPASPCC24 - 20724 - 207
216VALVALASPASPFF24 - 20724 - 207
117PROPROVALVALCC29 - 20429 - 204
217PROPROVALVALGG29 - 20429 - 204
118VALVALASPASPCC24 - 20724 - 207
218VALVALASPASPHH24 - 20724 - 207
119PROPROTYRTYRDD29 - 20529 - 205
219PROPROTYRTYREE29 - 20529 - 205
120PROPROTYRTYRDD29 - 20529 - 205
220PROPROTYRTYRFF29 - 20529 - 205
121PROPROVALVALDD29 - 20429 - 204
221PROPROVALVALGG29 - 20429 - 204
122PROPROTYRTYRDD29 - 20529 - 205
222PROPROTYRTYRHH29 - 20529 - 205
123VALVALASPASPEE24 - 20724 - 207
223VALVALASPASPFF24 - 20724 - 207
124PROPROVALVALEE29 - 20429 - 204
224PROPROVALVALGG29 - 20429 - 204
125VALVALASPASPEE24 - 20724 - 207
225VALVALASPASPHH24 - 20724 - 207
126PROPROVALVALFF29 - 20429 - 204
226PROPROVALVALGG29 - 20429 - 204
127VALVALASPASPFF24 - 20724 - 207
227VALVALASPASPHH24 - 20724 - 207
128PROPROVALVALGG29 - 20429 - 204
228PROPROVALVALHH29 - 20429 - 204

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

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Components

#1: Protein
Hypoxanthine phosphoribosyltransferase / Hypoxanthine-guanine phosphoribosyltransferase


Mass: 23405.576 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Brachybacterium faecium (bacteria) / Strain: DSM 4810 / Gene: Bfae_12790 / Plasmid: BC-PSGX3(BC) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)CODON+RIL
References: UniProt: C7MC15, hypoxanthine phosphoribosyltransferase
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 543 / Source method: isolated from a natural source / Formula: H2O

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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: 2.11 Å3/Da / Density % sol: 41.67 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.2 M Mg-chloride, 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 31-ID / Wavelength: 0.9791 Å
DetectorType: RAYONIX MX225HE / Detector: CCD / Date: Aug 9, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionRedundancy: 4.7 % / Number: 408245 / Rmerge(I) obs: 0.117 / Χ2: 1.09 / D res high: 2.1 Å / D res low: 50 Å / Num. obs: 86164 / % possible obs: 95.9
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)IDRmerge(I) obsChi squaredRedundancy
5.75010.0861.1255.3
4.525.710.0871.0415.4
3.954.5210.0951.1595.4
3.593.9510.1081.0155.3
3.333.5910.1151.0385.1
3.143.3310.1210.9394.9
2.983.1410.1340.9184.7
2.852.9810.1531.0174.7
2.742.8510.1811.0584.6
2.652.7410.1861.0664.6
2.562.6510.2121.0984.6
2.492.5610.2441.1614.5
2.422.4910.2761.1694.5
2.372.4210.3151.1464.5
2.312.3710.3281.1334.5
2.262.3110.4051.1774.4
2.222.2610.4471.1834.4
2.182.2210.4841.1584.4
2.142.1810.5561.1844.5
2.12.1410.6441.1934.4
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.637
11-h,-k,l20.363
ReflectionResolution: 2.1→50 Å / Num. obs: 86164 / % possible obs: 95.9 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.117 / Χ2: 1.094 / Net I/av σ(I): 10.404 / Net I/σ(I): 12.6 / Num. measured all: 408245
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2% possible all
2.1-2.144.40.64441541.19392.1
2.14-2.184.50.55641601.18493.6
2.18-2.224.40.48441791.15893.1
2.22-2.264.40.44741641.18393.8
2.26-2.314.40.40541871.17792.9
2.31-2.374.50.32841991.13393.7
2.37-2.424.50.31541891.14693.2
2.42-2.494.50.27641591.16993.7
2.49-2.564.50.24442811.16194.4
2.56-2.654.60.21241981.09894.8
2.65-2.744.60.18642781.06695
2.74-2.854.60.18143401.05896
2.85-2.984.70.15343471.01797.4
2.98-3.144.70.13443940.91898.3
3.14-3.334.90.12144300.93998.7
3.33-3.595.10.11544681.03899.4
3.59-3.955.30.10845251.01599.5
3.95-4.525.40.09544381.15999.5
4.52-5.75.40.08745421.04199.5
5.7-505.30.08645321.12598.9

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassification
REFMAC5.8.0069refinement
SCALEPACKdata scaling
PDB_EXTRACT3.14data extraction
PHENIXmodel building
SHELXphasing
SHELXDphasing
RefinementMethod to determine structure: SAD / Resolution: 2.1→33.31 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.949 / SU B: 6.336 / SU ML: 0.095 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.047 / ESU R Free: 0.037 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.213 4349 5 %RANDOM
Rwork0.173 ---
obs0.176 86139 93.8 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.11 Å2
Baniso -1Baniso -2Baniso -3
1--8.39 Å20 Å2-1.06 Å2
2--4.02 Å20 Å2
3---4.37 Å2
Refinement stepCycle: final / Resolution: 2.1→33.31 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11272 0 12 543 11827
Biso mean--43.09 39.3 -
Num. residues----1445
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.01911465
X-RAY DIFFRACTIONr_bond_other_d0.0130.0211234
X-RAY DIFFRACTIONr_angle_refined_deg1.8871.99915571
X-RAY DIFFRACTIONr_angle_other_deg1.872325802
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.60351439
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.38123.813514
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.37151901
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.27215105
X-RAY DIFFRACTIONr_chiral_restr0.1070.21806
X-RAY DIFFRACTIONr_gen_planes_refined0.0130.02112863
X-RAY DIFFRACTIONr_gen_planes_other0.010.022410
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_it3.912.7435774
X-RAY DIFFRACTIONr_mcbond_other3.912.7435773
X-RAY DIFFRACTIONr_mcangle_it5.1124.0977204
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
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)
11A112840.06
12B112840.06
21A106260.09
22C106260.09
31A112650.05
32D112650.05
41A104500.1
42E104500.1
51A104980.11
52F104980.11
61A113130.06
62G113130.06
71A106970.09
72H106970.09
81B105840.1
82C105840.1
91B112250.06
92D112250.06
101B104150.11
102E104150.11
111B104720.11
112F104720.11
121B112480.05
122G112480.05
131B106620.09
132H106620.09
141C106830.1
142D106830.1
151C109270.1
152E109270.1
161C108930.1
162F108930.1
171C105700.1
172G105700.1
181C109940.1
182H109940.1
191D103860.11
192E103860.11
201D104550.11
202F104550.11
211D112320.06
212G112320.06
221D107410.09
222H107410.09
231E111080.09
232F111080.09
241E104220.11
242G104220.11
251E108290.11
252H108290.11
261F104570.11
262G104570.11
271F110160.1
272H110160.1
281G106610.09
282H106610.09
LS refinement shellResolution: 2.1→2.14 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.244 216 -
Rwork0.194 4211 -
obs--65.02 %
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)
10.4759-0.25830.17081.2291-0.75991.4540.07940.11260.0242-0.2294-0.03980.0245-0.01930.0575-0.03960.1391-0.0261-0.0270.08470.00120.02958.35867.20427.483
20.57940.498-0.40611.3885-0.66281.19530.1138-0.1405-0.01020.2726-0.0770.0729-0.01940.0846-0.03680.1550.01990.00330.094-0.00530.03998.54411.23933.882
30.89330.3381-0.36170.3424-0.34470.932-0.010.0982-0.0374-0.06610.06110.19410.1436-0.2054-0.05110.21430.0041-0.07680.1023-0.02740.2429-1.671.35515.575
40.8483-0.2440.04261.0421-0.42531.4793-0-0.0246-0.1603-0.0364-0.01630.07850.33260.07840.01640.14660.00990.01720.0329-0.01590.057417.04539.5851.822
51.26230.416-0.25840.7748-0.15440.0746-0.03440.01-0.0461-0.17110.0165-0.14120.04220.04680.01790.21570.0373-0.04210.1864-0.02640.095927.32121.857-2.507
60.6339-0.44580.07550.6615-0.10910.0359-0.0468-0.04420.05870.1150.0296-0.0816-0.03640.05220.01720.1994-0.02330.00480.199-0.00430.04626.90456.47464.129
70.79420.20120.00711.4672-0.58571.22190.0683-0.00450.19190.1072-0.00850.1275-0.30140.1068-0.05980.15790.0003-0.02430.0446-0.03510.094217.69738.7059.885
81.2824-0.10130.48670.2819-0.10320.7543-0.038-0.06910.10450.08460.04430.2169-0.1457-0.137-0.00630.2099-0.00840.04360.08590.01320.2019-1.84277.11945.681
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A29 - 205
2X-RAY DIFFRACTION2B29 - 205
3X-RAY DIFFRACTION3C24 - 207
4X-RAY DIFFRACTION4D29 - 206
5X-RAY DIFFRACTION5E24 - 207
6X-RAY DIFFRACTION6F24 - 207
7X-RAY DIFFRACTION7G29 - 205
8X-RAY DIFFRACTION8H24 - 207

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