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- PDB-3cos: Crystal structure of human class II alcohol dehydrogenase (ADH4) ... -

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Basic information

Entry
Database: PDB / ID: 3cos
TitleCrystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn
ComponentsAlcohol dehydrogenase 4
KeywordsOXIDOREDUCTASE / medium chain dehydrogenase / alcohol dehydrogenase / Zinc-dependent / Metal-binding / NAD / Structural Genomics / Structural Genomics Consortium / SGC
Function / homology
Function and homology information


benzaldehyde dehydrogenase [NAD(P)+] activity / alcohol catabolic process / quinone metabolic process / ethanol binding / all-trans-retinol dehydrogenase (NAD+) / all-trans retinal binding / S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity / fatty acid omega-oxidation / NADPH:quinone reductase activity / alcohol metabolic process ...benzaldehyde dehydrogenase [NAD(P)+] activity / alcohol catabolic process / quinone metabolic process / ethanol binding / all-trans-retinol dehydrogenase (NAD+) / all-trans retinal binding / S-(hydroxymethyl)glutathione dehydrogenase (NAD(P)+) activity / fatty acid omega-oxidation / NADPH:quinone reductase activity / alcohol metabolic process / formaldehyde catabolic process / cellular aldehyde metabolic process / Ethanol oxidation / alcohol dehydrogenase (NAD+) activity / RA biosynthesis pathway / alcohol dehydrogenase (NAD+) activity, zinc-dependent / : / oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor / all-trans-retinol dehydrogenase (NAD+) activity / aldose reductase (NADPH) activity / retinol metabolic process / retinoid metabolic process / retinol binding / NAD binding / zinc ion binding / nucleoplasm / cytosol
Similarity search - Function
Alcohol dehydrogenase family, zinc-type, class-II subfamily / Alcohol dehydrogenase, zinc-type, conserved site / Zinc-containing alcohol dehydrogenases signature. / Quinone Oxidoreductase; Chain A, domain 1 / Medium-chain alcohol dehydrogenases, catalytic domain / Alcohol dehydrogenase-like, C-terminal / Zinc-binding dehydrogenase / Alcohol dehydrogenase, N-terminal / Alcohol dehydrogenase GroES-like domain / Polyketide synthase, enoylreductase domain ...Alcohol dehydrogenase family, zinc-type, class-II subfamily / Alcohol dehydrogenase, zinc-type, conserved site / Zinc-containing alcohol dehydrogenases signature. / Quinone Oxidoreductase; Chain A, domain 1 / Medium-chain alcohol dehydrogenases, catalytic domain / Alcohol dehydrogenase-like, C-terminal / Zinc-binding dehydrogenase / Alcohol dehydrogenase, N-terminal / Alcohol dehydrogenase GroES-like domain / Polyketide synthase, enoylreductase domain / Enoylreductase / GroES-like superfamily / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Alpha-Beta Complex / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETIC ACID / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / All-trans-retinol dehydrogenase [NAD(+)] ADH4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsKavanagh, K.L. / Shafqat, N. / Yue, W. / von Delft, F. / Bishop, S. / Roos, A. / Murray, J. / Edwards, A.M. / Arrowsmith, C.H. / Bountra, C. ...Kavanagh, K.L. / Shafqat, N. / Yue, W. / von Delft, F. / Bishop, S. / Roos, A. / Murray, J. / Edwards, A.M. / Arrowsmith, C.H. / Bountra, C. / Oppermann, U. / Structural Genomics Consortium (SGC)
CitationJournal: To be Published
Title: Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn.
Authors: Kavanagh, K.L. / Shafqat, N. / Yue, W. / von Delft, F. / Bishop, S. / Roos, A. / Murray, J. / Edwards, A.M. / Arrowsmith, C.H. / Bountra, C. / Oppermann, U.
History
DepositionMar 29, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 15, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Aug 30, 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_initial_refinement_model / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ref_seq_dif.details / _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: Alcohol dehydrogenase 4
B: Alcohol dehydrogenase 4
C: Alcohol dehydrogenase 4
D: Alcohol dehydrogenase 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)165,33528
Polymers161,4234
Non-polymers3,91224
Water13,151730
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A: Alcohol dehydrogenase 4
B: Alcohol dehydrogenase 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)82,72815
Polymers80,7112
Non-polymers2,01713
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3140 Å2
ΔGint-26.8 kcal/mol
Surface area28550 Å2
MethodPISA
2
C: Alcohol dehydrogenase 4
D: Alcohol dehydrogenase 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)82,60613
Polymers80,7112
Non-polymers1,89511
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3030 Å2
ΔGint-26.5 kcal/mol
Surface area28600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.299, 160.919, 88.739
Angle α, β, γ (deg.)90.00, 111.64, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51A
61B
71C
81D
91A
101B
111C
121D
131A
141B
151C
161D
171A
181B
191C
201D
211A
221B
231C
241D
251A
261B
271C
281D
291A
301B
311C
321D
331A
341B
351C
361D
12A
22B
32C
42D
52A
62B
72C
82D
92A
102B
112C
122D
132A
142B
152C
162D
172A
182B
192C
202D
212A
222B
232C
242D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111THRTHRVALVAL2AA3 - 824 - 83
211THRTHRVALVAL2BB3 - 824 - 83
311THRTHRVALVAL2CC3 - 824 - 83
411THRTHRVALVAL2DD3 - 824 - 83
521ASNASNCYSCYS2AA84 - 9985 - 100
621ASNASNCYSCYS2BB84 - 9985 - 100
721ASNASNCYSCYS2CC84 - 9985 - 100
821ASNASNCYSCYS2DD84 - 9985 - 100
931PHEPHEMETMET2AA104 - 129105 - 130
1031PHEPHEMETMET2BB104 - 129105 - 130
1131PHEPHEMETMET2CC104 - 129105 - 130
1231PHEPHEMETMET2DD104 - 129105 - 130
1341THRTHRLEULEU2AA133 - 172134 - 173
1441THRTHRLEULEU2BB133 - 172134 - 173
1541THRTHRLEULEU2CC133 - 172134 - 173
1641THRTHRLEULEU2DD133 - 172134 - 173
1751ARGARGASNASN2AA174 - 231175 - 232
1851ARGARGASNASN2BB174 - 231175 - 232
1951ARGARGASNASN2CC174 - 231175 - 232
2051ARGARGASNASN2DD174 - 231175 - 232
2161LEULEUSERSER2AA241 - 304242 - 305
2261LEULEUSERSER2BB241 - 304242 - 305
2361LEULEUSERSER2CC241 - 304242 - 305
2461LEULEUSERSER2DD241 - 304242 - 305
2571PROPROHISHIS2AA311 - 354312 - 355
2671PROPROHISHIS2BB311 - 354312 - 355
2771PROPROHISHIS2CC311 - 354312 - 355
2871PROPROHISHIS2DD311 - 354312 - 355
2981ILEILEMETMET2AA361 - 368362 - 369
3081ILEILEMETMET2BB361 - 368362 - 369
3181ILEILEMETMET2CC361 - 368362 - 369
3281ILEILEMETMET2DD361 - 368362 - 369
3391SERSERPHEPHE2AA373 - 380374 - 381
3491SERSERPHEPHE2BB373 - 380374 - 381
3591SERSERPHEPHE2CC373 - 380374 - 381
3691SERSERPHEPHE2DD373 - 380374 - 381
112ARGARGLYSLYS5AA100 - 103101 - 104
212ARGARGLYSLYS5BB100 - 103101 - 104
312ARGARGLYSLYS5CC100 - 103101 - 104
412ARGARGLYSLYS5DD100 - 103101 - 104
522GLUGLULYSLYS5AA130 - 132131 - 133
622GLUGLULYSLYS5BB130 - 132131 - 133
722GLUGLULYSLYS5CC130 - 132131 - 133
822GLUGLULYSLYS5DD130 - 132131 - 133
932SERSERALAALA5AA232 - 240233 - 241
1032SERSERALAALA5BB232 - 240233 - 241
1132SERSERALAALA5CC232 - 240233 - 241
1232SERSERALAALA5DD232 - 240233 - 241
1342LYSLYSPHEPHE5AA305 - 310306 - 311
1442LYSLYSPHEPHE5BB305 - 310306 - 311
1542LYSLYSPHEPHE5CC305 - 310306 - 311
1642LYSLYSPHEPHE5DD305 - 310306 - 311
1752THRTHRLYSLYS5AA355 - 360356 - 361
1852THRTHRLYSLYS5BB355 - 360356 - 361
1952THRTHRLYSLYS5CC355 - 360356 - 361
2052THRTHRLYSLYS5DD355 - 360356 - 361
2162ASNASNLYSLYS5AA369 - 372370 - 373
2262ASNASNLYSLYS5BB369 - 372370 - 373
2362ASNASNLYSLYS5CC369 - 372370 - 373
2462ASNASNLYSLYS5DD369 - 372370 - 373

NCS ensembles :
ID
1
2

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Alcohol dehydrogenase 4 / / Alcohol dehydrogenase class II pi chain


Mass: 40355.730 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ADH4 / Plasmid: pNIC28-Bsa4 (pET derivative) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P08319, alcohol dehydrogenase

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Non-polymers , 5 types, 754 molecules

#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-NAD / NICOTINAMIDE-ADENINE-DINUCLEOTIDE / Nicotinamide adenine dinucleotide


Mass: 663.425 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H27N7O14P2 / Comment: NAD*YM
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-ACY / ACETIC ACID / Acetic acid


Mass: 60.052 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H4O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 730 / 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: 2.77 Å3/Da / Density % sol: 55.55 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 25% PEG 3350, 0.2 M Ammonium acetate, 0.1 M Bis-tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9919 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 9, 2008
RadiationMonochromator: Si III / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9919 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. all: 97589 / Num. obs: 97589 / % possible obs: 96 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 23 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 7.2
Reflection shellResolution: 2.1→2.21 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 2 / Num. unique all: 13182 / % possible all: 89

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MAR345CCDdata collection
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1EE2

1ee2


Resolution: 2.1→49.39 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.942 / SU B: 7.691 / SU ML: 0.113 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.183 / ESU R Free: 0.157 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20626 1674 1.7 %RANDOM
Rwork0.16893 ---
all0.16958 95873 --
obs0.16958 95873 95.65 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.963 Å2
Baniso -1Baniso -2Baniso -3
1-0.08 Å20 Å20.15 Å2
2--0.72 Å20 Å2
3----0.69 Å2
Refinement stepCycle: LAST / Resolution: 2.1→49.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11167 0 232 730 12129
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02211613
X-RAY DIFFRACTIONr_bond_other_d0.0040.027749
X-RAY DIFFRACTIONr_angle_refined_deg1.211.99615745
X-RAY DIFFRACTIONr_angle_other_deg0.9053.00119009
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.66851518
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.76424.907377
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.099151935
X-RAY DIFFRACTIONr_dihedral_angle_4_deg8.1411532
X-RAY DIFFRACTIONr_chiral_restr0.0680.21864
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0212768
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022140
X-RAY DIFFRACTIONr_nbd_refined0.1790.21996
X-RAY DIFFRACTIONr_nbd_other0.180.27795
X-RAY DIFFRACTIONr_nbtor_refined0.1660.25574
X-RAY DIFFRACTIONr_nbtor_other0.0810.25766
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.130.2611
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0150.21
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1180.211
X-RAY DIFFRACTIONr_symmetry_vdw_other0.140.221
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2290.29
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.46338143
X-RAY DIFFRACTIONr_mcbond_other0.24233122
X-RAY DIFFRACTIONr_mcangle_it2512084
X-RAY DIFFRACTIONr_scbond_it3.78874479
X-RAY DIFFRACTIONr_scangle_it4.842113659
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
11A2010tight positional0.030.05
12B2010tight positional0.030.05
13C2010tight positional0.030.05
14D2010tight positional0.030.05
11A2139medium positional0.160.5
12B2139medium positional0.20.5
13C2139medium positional0.160.5
14D2139medium positional0.170.5
21A189medium positional0.130.5
22B189medium positional0.150.5
23C189medium positional0.190.5
24D189medium positional0.210.5
21A256loose positional0.595
22B256loose positional0.585
23C256loose positional0.655
24D256loose positional0.545
11A2010tight thermal0.090.5
12B2010tight thermal0.090.5
13C2010tight thermal0.10.5
14D2010tight thermal0.090.5
11A2139medium thermal0.632
12B2139medium thermal0.622
13C2139medium thermal0.652
14D2139medium thermal0.632
21A189medium thermal0.592
22B189medium thermal0.562
23C189medium thermal0.62
24D189medium thermal0.632
21A256loose thermal1.9110
22B256loose thermal1.6810
23C256loose thermal1.7310
24D256loose thermal1.6910
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.312 115 -
Rwork0.238 6487 -
obs--88.01 %
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)
10.9668-0.0379-0.25931.0830.18981.9458-0.00740.11930.0909-0.06540.00840.017-0.2989-0.1734-0.001-0.05050.0401-0.00550.00410.0002-0.1002-6.613786.790647.0542
20.76880.218-0.23280.7677-0.29911.3544-0.00580.1126-0.0221-0.0572-0.0282-0.04720.0088-0.08250.034-0.07890.0129-0.0062-0.0026-0.0299-0.1047-2.976.982750.3101
30.7174-0.22650.46341.292-0.80381.229-0.0403-0.0558-0.06880.15350.02730.05990.0185-0.25760.0131-0.0499-0.02330.0203-0.0047-0.0326-0.078-11.611366.744873.2061
41.4531-0.7337-0.86973.5925-0.1532.042-0.02290.16690.00610.01230.1260.0723-0.012-0.4369-0.1032-0.11910.0103-0.03640.0888-0.0313-0.0858-19.106777.0754.0302
51.38950.48760.05532.1628-0.01291.47980.0513-0.159-0.15270.4048-0.1137-0.28150.17640.01570.06240.1178-0.0538-0.0668-0.03850.04890.020912.38647.0053101.2316
61.42180.39330.24210.9213-0.08441.37880.0426-0.1041-0.14410.2105-0.1175-0.01430.083-0.07230.07480.0619-0.065-0.0372-0.09150.01070.04025.149447.131194.5207
70.9884-0.36190.32170.7664-0.44441.7986-0.01990.0738-0.0619-0.0291-0.079-0.25240.03930.18130.0989-0.0435-0.00010.0055-0.07810.00650.017918.711861.034973.5525
80.5883-0.0980.23991.0685-0.77731.468-0.0061-0.0281-0.16060.0626-0.1114-0.26270.10360.1120.1175-0.0004-0.0009-0.0143-0.08910.00480.068518.069252.192183.855
91.1464-0.0507-0.17322.4677-0.1131.54840.04130.11540.0534-0.4869-0.0842-0.2851-0.14390.0050.04290.00750.03020.0625-0.0710.0057-0.029820.3305104.093861.5233
100.8583-0.2389-0.18291.3422-0.38241.54180.06840.08580.0844-0.1453-0.0556-0.1042-0.2479-0.0032-0.0128-0.03890.01740.0124-0.1005-0.0032-0.026215.7336106.446369.9957
111.5268-0.0123-0.64961.4051-0.48281.4686-0.0008-0.1276-0.06560.0998-0.0947-0.2376-0.01040.14510.0955-0.147-0.0069-0.0466-0.06710.0129-0.027322.925287.915891.6557
120.73170.2346-0.59051.317-0.68041.32440.0306-0.11020.0299-0.067-0.1037-0.2595-0.08320.12910.073-0.1333-0.0269-0.0144-0.0616-0.0111-0.020323.0496.553579.2823
131.07890.38210.12332.2281.00192.4976-0.0402-0.1483-0.25350.3656-0.024-0.01010.5385-0.09620.06420.02270.00820.03220.0050.0241-0.0533-9.514371.7643115.9725
141.19010.2751-0.17970.87250.13941.2276-0.0032-0.1675-0.16190.1555-0.0307-0.11880.23140.08950.0339-0.0320.0351-0.0237-0.0036-0.0073-0.076-3.2879.5206112.7395
150.94150.4308-0.79110.8081-0.371.93080.01650.13120.1002-0.07070.01820.0339-0.1112-0.3152-0.0347-0.13640.0418-0.029-0.0086-0.0182-0.0931-10.444792.693588.895
160.84960.218-0.92330.3769-0.62022.2441-0.1325-0.0202-0.0480.01520.052-0.04550.084-0.20930.0805-0.10740.02690.0027-0.0469-0.0592-0.092-12.250986.3799103.8941
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA2 - 913 - 92
2X-RAY DIFFRACTION2AA92 - 19493 - 195
3X-RAY DIFFRACTION3AA195 - 330196 - 331
4X-RAY DIFFRACTION4AA331 - 380332 - 381
5X-RAY DIFFRACTION5BB2 - 903 - 91
6X-RAY DIFFRACTION6BB91 - 17292 - 173
7X-RAY DIFFRACTION7BB173 - 309174 - 310
8X-RAY DIFFRACTION8BB310 - 380311 - 381
9X-RAY DIFFRACTION9CC2 - 883 - 89
10X-RAY DIFFRACTION10CC89 - 18590 - 186
11X-RAY DIFFRACTION11CC186 - 297187 - 298
12X-RAY DIFFRACTION12CC298 - 380299 - 381
13X-RAY DIFFRACTION13DD1 - 912 - 92
14X-RAY DIFFRACTION14DD92 - 19293 - 193
15X-RAY DIFFRACTION15DD193 - 309194 - 310
16X-RAY DIFFRACTION16DD310 - 380311 - 381

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