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- PDB-2w54: Crystal Structure of Xanthine Dehydrogenase from Rhodobacter caps... -

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Basic information

Entry
Database: PDB / ID: 2w54
TitleCrystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus in Complex with Bound Inhibitor Pterin-6-aldehyde
Components(XANTHINE DEHYDROGENASE) x 2
KeywordsOXIDOREDUCTASE / XANTHINE OXIDASE / PURINE CATABOLISM / P6A / IRON / IRON-SULFUR / METAL-BINDING / MOLYBDENUM COFACTOR
Function / homology
Function and homology information


1.1.1.204 / xanthine dehydrogenase activity / molybdenum ion binding / FAD binding / 2 iron, 2 sulfur cluster binding / oxidoreductase activity / iron ion binding
Similarity search - Function
Xanthine dehydrogenase, small subunit, bacteria / Xanthine dehydrogenase, molybdopterin binding subunit / Xanthine dehydrogenase, small subunit / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / CO dehydrogenase flavoprotein, C-terminal domain / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde Oxidoreductase; domain 4 / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain / [2Fe-2S]-binding domain / Molybdopterin dehydrogenase, FAD-binding ...Xanthine dehydrogenase, small subunit, bacteria / Xanthine dehydrogenase, molybdopterin binding subunit / Xanthine dehydrogenase, small subunit / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / CO dehydrogenase flavoprotein, C-terminal domain / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde Oxidoreductase; domain 4 / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain / [2Fe-2S]-binding domain / Molybdopterin dehydrogenase, FAD-binding / CO dehydrogenase flavoprotein, C-terminal / CO dehydrogenase flavoprotein, C-terminal domain superfamily / FAD binding domain in molybdopterin dehydrogenase / CO dehydrogenase flavoprotein C-terminal domain / Aldehyde oxidase/xanthine dehydrogenase / Aldehyde oxidase/xanthine dehydrogenase, second molybdopterin binding domain / Molybdopterin cofactor-binding domain / Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead / [2Fe-2S]-binding / Aldehyde oxidase/xanthine dehydrogenase, first molybdopterin binding domain / Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead superfamily / [2Fe-2S]-binding domain superfamily / Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain superfamily / [2Fe-2S] binding domain / Molybdopterin cofactor-binding domain / Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 - #10 / Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 / FAD-binding, type PCMH, subdomain 1 / Aldehyde Oxidoreductase; domain 3 / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / FAD-binding domain, PCMH-type / PCMH-type FAD-binding domain profile. / 2Fe-2S iron-sulfur cluster binding domain / Beta-grasp domain / FAD-binding, type PCMH, subdomain 2 / FAD-binding, type PCMH-like superfamily / Beta-grasp domain superfamily / Enolase-like; domain 1 / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / Ubiquitin-like (UB roll) / DNA polymerase; domain 1 / Roll / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / 6-HYDROXYMETHYLPTERIN / Chem-XAX / Xanthine dehydrogenase / Xanthine dehydrogenase
Similarity search - Component
Biological speciesRHODOBACTER CAPSULATUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsDoebbler, J.A. / Truglio, J.J. / Leimkuhler, S. / Kisker, C.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: Mechanism of Substrate and Inhibitor Binding of Rhodobacter Capsulatus Xanthine Dehydrogenase.
Authors: Dietzel, U. / Kuper, J. / Doebbler, J.A. / Schulte, A. / Truglio, J.J. / Leimkuhler, S. / Kisker, C.
History
DepositionDec 4, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 23, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Apr 22, 2015Group: Atomic model / Derived calculations ...Atomic model / Derived calculations / Non-polymer description / Other / Structure summary
Revision 1.3May 8, 2019Group: Data collection / Experimental preparation / Other
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_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 / _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_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: XANTHINE DEHYDROGENASE
B: XANTHINE DEHYDROGENASE
C: XANTHINE DEHYDROGENASE
D: XANTHINE DEHYDROGENASE
E: XANTHINE DEHYDROGENASE
F: XANTHINE DEHYDROGENASE
G: XANTHINE DEHYDROGENASE
H: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)537,68232
Polymers529,5948
Non-polymers8,08824
Water0
1
A: XANTHINE DEHYDROGENASE
B: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4218
Polymers132,3992
Non-polymers2,0226
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8100 Å2
ΔGint-31.7 kcal/mol
Surface area49140 Å2
MethodPQS
2
C: XANTHINE DEHYDROGENASE
D: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4218
Polymers132,3992
Non-polymers2,0226
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8110 Å2
ΔGint-30.3 kcal/mol
Surface area49360 Å2
MethodPQS
3
E: XANTHINE DEHYDROGENASE
F: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4218
Polymers132,3992
Non-polymers2,0226
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8100 Å2
ΔGint-29.8 kcal/mol
Surface area49430 Å2
MethodPQS
4
G: XANTHINE DEHYDROGENASE
H: XANTHINE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)134,4218
Polymers132,3992
Non-polymers2,0226
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8080 Å2
ΔGint-31.9 kcal/mol
Surface area49080 Å2
MethodPQS
Unit cell
Length a, b, c (Å)92.571, 140.695, 157.859
Angle α, β, γ (deg.)109.63, 105.83, 101.23
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
12B
22D
32F
42H

NCS domain segments:

Component-ID: 1 / Refine code: 4

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUPROPROAA2 - 4622 - 462
21GLUGLUPROPROCC2 - 4622 - 462
31GLUGLUPROPROEE2 - 4622 - 462
41GLUGLUPROPROGG2 - 4622 - 462
12SERSERALAALABB2 - 7772 - 777
22SERSERALAALADD2 - 7772 - 777
32SERSERALAALAFF2 - 7772 - 777
42SERSERALAALAHH2 - 7772 - 777

NCS ensembles :
ID
1
2

NCS oper:
IDCodeMatrixVector
1given(-0.01083, -0.7912, 0.6114), (-0.7974, -0.3621, -0.4828), (0.6034, -0.4927, -0.627)0.2537, 0.1778, -0.2258
2given(0.3268, -0.7129, -0.6205), (0.8701, -0.02942, 0.492), (-0.369, -0.7007, 0.6107)89.58, -24.19, 10.6
3given(-0.9265, -0.376, -0.01161), (-0.3761, 0.9266, 0.003231), (0.009541, 0.00736, -0.9999)24.01, -67.15, 60.11
4given(-0.02178, -0.791, 0.6114), (-0.789, -0.362, -0.4965), (0.614, -0.4932, -0.6162)0.0713, 0.2571, 0.02035
5given(0.3325, -0.7125, -0.6179), (0.862, -0.03616, 0.5056), (-0.3826, -0.7008, 0.6021)89.27, -24.57, 11.48
6given(-0.9266, -0.3757, -0.01449), (-0.3758, 0.9267, 0.004001), (0.01193, 0.009154, -0.9999)24.03, -67.15, 60.01

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Components

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Protein , 2 types, 8 molecules ACEGBDFH

#1: Protein
XANTHINE DEHYDROGENASE /


Mass: 49420.508 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RHODOBACTER CAPSULATUS (bacteria) / Plasmid: PSL207 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): TP1000 / References: UniProt: O54050, 1.1.1.204
#2: Protein
XANTHINE DEHYDROGENASE /


Mass: 82978.031 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RHODOBACTER CAPSULATUS (bacteria) / Plasmid: PSL207 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): TP1000 / References: UniProt: O54051, 1.1.1.204

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Non-polymers , 5 types, 24 molecules

#3: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Fe2S2
#4: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#5: Chemical
ChemComp-XAX / {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-di(sulfanyl-kappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(hydroxy)oxo(thioxo)molybdenum


Mass: 554.348 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H13MoN5O8PS3
#6: Chemical
ChemComp-BA / BARIUM ION


Mass: 137.327 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ba
#7: Chemical
ChemComp-HHR / 6-HYDROXYMETHYLPTERIN


Mass: 193.163 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H7N5O2

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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: 3.35 Å3/Da / Density % sol: 63.26 % / Description: NONE
Crystal growMethod: vapor diffusion, hanging drop / pH: 8.3
Details: 100 MM TRIS PH 8.3, 6-8 % PEG 8000, 6-8 MM BACL, 5-25 MM DTT, 3-4 % ISOPROPANOL, 10-15 MG/ML PROTEIN, HANGING DROP VAPOR DIFFUSION

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Details: A DOUBLY FOCUSING TOROIDAL MIRROR
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.3→50 Å / Num. obs: 102161 / % possible obs: 99.1 % / Redundancy: 4 % / Rmerge(I) obs: 0.18 / Net I/σ(I): 8.9
Reflection shellResolution: 3.3→3.36 Å / Redundancy: 4 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 2.6 / % possible all: 98.6

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Processing

Software
NameVersionClassification
REFMAC5.5.0055refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1JRO

1jro


Resolution: 3.3→50 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.877 / SU B: 43.602 / SU ML: 0.33 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.466 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.224 5185 5.1 %RANDOM
Rwork0.186 ---
obs0.188 96884 99.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 23.23 Å2
Baniso -1Baniso -2Baniso -3
1-1.22 Å2-0.28 Å2-0.5 Å2
2---2.26 Å2-1.87 Å2
3----0.6 Å2
Refinement stepCycle: LAST / Resolution: 3.3→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms36372 0 416 0 36788
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.02237584
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.9921.9751080
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.7954824
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.29922.5931620
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.858155780
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.66415368
X-RAY DIFFRACTIONr_chiral_restr0.0640.25652
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02128944
X-RAY DIFFRACTIONr_gen_planes_other
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_it0.0981.523996
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.204238116
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.378313588
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.684.512948
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
11A3368medium positional0.210.5
12C3368medium positional0.220.5
13E3368medium positional0.230.5
14G3368medium positional0.210.5
21B5717medium positional0.190.5
22D5717medium positional0.190.5
23F5717medium positional0.190.5
24H5717medium positional0.210.5
11A3368medium thermal0.12
12C3368medium thermal0.172
13E3368medium thermal0.12
14G3368medium thermal0.12
21B5717medium thermal0.112
22D5717medium thermal0.152
23F5717medium thermal0.122
24H5717medium thermal0.122
LS refinement shellResolution: 3.3→3.38 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.315 409 -
Rwork0.266 7113 -
obs--98.68 %
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)
13.7175-1.03191.20783.5777-0.4132.615-0.07980.51030.3261-0.43870.05150.1829-0.57330.08210.02830.2419-0.0636-0.03790.14310.08130.128910.091526.5074-9.4881
21.4240.40260.40751.8780.36322.1331-0.0190.06880.5075-0.1470.0250.3738-0.7597-0.053-0.0060.67470.04170.02430.15720.07510.56435.566952.71823.0476
30.6470.12530.1121.2420.31550.78720.0423-0.16020.14980.25680.0224-0.1364-0.23660.1698-0.06470.189-0.0794-0.00930.1676-0.01760.102417.94315.850318.9294
43.5984-1.50441.75853.038-0.75692.25290.0216-0.07440.22810.1022-0.15950.5063-0.1705-0.3910.13790.0280.03590.02470.1103-0.05970.1656-26.7363-12.7622-0.9315
51.6373-0.43930.29572.95741.31282.5837-0.03980.24380.0385-0.231-0.0920.3389-0.0478-0.32350.13170.0276-0.0138-0.04090.3332-0.0070.0696-39.9629-24.8548-24.1429
60.76780.31780.39931.21950.44730.98730.02860.1527-0.1890.0360.0006-0.11010.12760.1282-0.02920.01840.02310.00530.1233-0.01240.0595-1.0803-29.1066-8.4701
72.46080.58920.28664.00160.51041.94650.3190.05380.7025-0.3952-0.0823-0.6082-0.56110.5094-0.23670.336-0.06790.29250.25750.01070.405525.59869.240762.0093
81.1931-0.36470.34092.2558-0.49741.64430.0679-0.33210.5695-0.05470.2133-0.7329-0.23690.6327-0.28120.1171-0.18640.13860.7416-0.3530.663342.240362.934985.3296
90.9053-0.330.35530.468-0.10231.04780.154-0.0797-0.1044-0.15650.00880.01470.17910.1146-0.16280.2029-0.00660.00830.12640.0130.04768.27444.137168.9903
102.50530.98711.14313.20591.05013.31620.0281-0.51550.40440.5212-0.0232-0.09-0.3947-0.22-0.00490.41680.07250.18810.197-0.02920.2908-23.002191.491270.0634
111.514-0.50740.98481.8511-0.09182.1159-0.1696-0.12260.53260.06240.0852-0.0355-0.5624-0.08440.08440.6780.12170.22740.20920.00650.7479-28.564117.581757.6562
120.9061-0.24280.47850.9367-0.29630.73660.08570.14070.1885-0.07870.03740.1948-0.0476-0.1355-0.12320.28040.06690.13920.17250.12470.2128-26.046478.827741.4899
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 166
2X-RAY DIFFRACTION2A179 - 462
3X-RAY DIFFRACTION3B2 - 777
4X-RAY DIFFRACTION4C1 - 166
5X-RAY DIFFRACTION5C179 - 462
6X-RAY DIFFRACTION6D2 - 777
7X-RAY DIFFRACTION7E1 - 166
8X-RAY DIFFRACTION8E179 - 462
9X-RAY DIFFRACTION9F2 - 777
10X-RAY DIFFRACTION10G1 - 166
11X-RAY DIFFRACTION11G179 - 462
12X-RAY DIFFRACTION12H2 - 777

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