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- PDB-2c91: mouse succinic semialdehyde reductase, AKR7A5 -

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Basic information

Entry
Database: PDB / ID: 2c91
Titlemouse succinic semialdehyde reductase, AKR7A5
ComponentsAFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
KeywordsOXIDOREDUCTASE / ALDO/KETO REDUCTASE / AKR / SUCCINIC SEMIALDEHYDE REDUCTASE / TARTRATE / GOLGI STACK / NAD / NADP
Function / homology
Function and homology information


phenanthrene-9,10-epoxide hydrolase activity / : / Aflatoxin activation and detoxification / daunorubicin metabolic process / doxorubicin metabolic process / aldose reductase (NADPH) activity / nuclear envelope / Golgi apparatus / mitochondrion / cytosol / cytoplasm
Similarity search - Function
NADP-dependent oxidoreductase domain / NADP-dependent oxidoreductase domain / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / PHOSPHATE ION / L(+)-TARTARIC ACID / Aflatoxin B1 aldehyde reductase member 2
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsZhu, X. / Ellis, E.M. / Lapthorn, A.J.
Citation
Journal: Biochemistry / Year: 2006
Title: Crystal Structure of Mouse Succinic Semialdehyde Reductase Akr7A5: Structural Basis for Substrate Specificity.
Authors: Zhu, X. / Lapthorn, A.J. / Ellis, E.M.
#1: Journal: FEBS Lett. / Year: 2002
Title: Characterisation of a Novel Mouse Liver Aldo-Keto Reductase Akr7A5
Authors: Hinshelwood, A. / Mcgarvie, G. / Ellis, E.
History
DepositionDec 8, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 15, 2006Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 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 / 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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "GA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "HA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "IA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "JA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
B: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
C: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
D: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
E: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
F: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
G: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
H: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
I: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
J: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)389,08062
Polymers376,67610
Non-polymers12,40352
Water37,9942109
1
A: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8406
Polymers37,6681
Non-polymers1,1735
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,0337
Polymers37,6681
Non-polymers1,3656
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,0337
Polymers37,6681
Non-polymers1,3656
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,0337
Polymers37,6681
Non-polymers1,3656
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
5
E: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8376
Polymers37,6681
Non-polymers1,1705
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
6
F: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,6534
Polymers37,6681
Non-polymers9863
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
7
G: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8376
Polymers37,6681
Non-polymers1,1705
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
8
H: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,7455
Polymers37,6681
Non-polymers1,0784
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
9
I: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9416
Polymers37,6681
Non-polymers1,2735
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
10
J: AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,1288
Polymers37,6681
Non-polymers1,4607
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)98.532, 159.238, 96.698
Angle α, β, γ (deg.)90.02, 119.40, 78.50
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1112A1 - 369
2112B1 - 369
3112C1 - 369
4112D1 - 369
5112E1 - 369
6112F1 - 369
7112G1 - 369
8112H1 - 369
9112I1 - 369
10112J1 - 369

NCS oper:
IDCodeMatrixVector
1given(0.16291, 0.53965, -0.82598), (0.55231, -0.74358, -0.37688), (-0.81757, -0.3948, -0.41919)55.58882, 10.6391, 80.61127
2given(0.202, 0.97799, -0.05225), (0.97739, -0.19791, 0.07438), (0.06241, -0.06609, -0.99586)-65.57173, 11.56627, 65.0894
3given(0.52454, 0.10797, 0.84451), (-0.6601, 0.67805, 0.3233), (-0.53771, -0.72704, 0.42694)-57.87097, -68.84323, 24.44212
4given(-0.99991, -0.01151, -0.00637), (0.00091, -0.54413, 0.839), (-0.01312, 0.83892, 0.5441)12.55283, -45.06129, -64.81061
5given(-0.15571, -0.9874, -0.02815), (-0.55022, 0.11037, -0.82769), (0.82037, -0.11339, -0.56047)33.52959, 63.87856, 34.60317
6given(-0.5183, -0.0982, -0.84954), (-0.09786, -0.98005, 0.17299), (-0.84958, 0.17279, 0.49835)69.26389, 88.61806, 29.04548
7given(0.56444, -0.6878, -0.45644), (0.10672, 0.60911, -0.78588), (0.81855, 0.39487, 0.4172)35.11725, -38.42543, -103.82014
8given(-0.48689, 0.66951, 0.56098), (0.65208, -0.14871, 0.74343), (0.58115, 0.72777, -0.36417)-76.58579, -30.11416, -105.57925
9given(-0.28936, -0.51132, 0.80921), (-0.95516, 0.20971, -0.20904), (-0.06281, -0.83341, -0.54907)54.28667, 21.01304, 120.60841

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Components

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Protein , 1 types, 10 molecules ABCDEFGHIJ

#1: Protein
AFLATOXIN B1 ALDEHYDE REDUCTASE MEMBER 2 / SUCCINIC SEMIALDEHYDE REDUCTASE


Mass: 37667.613 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Organ: LIVER / Plasmid: PET-15B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): PLYSS / References: UniProt: Q8CG76, Oxidoreductases

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Non-polymers , 6 types, 2161 molecules

#2: Chemical
ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE / Nicotinamide adenine dinucleotide phosphate


Mass: 743.405 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C21H28N7O17P3
#3: Chemical
ChemComp-TLA / L(+)-TARTARIC ACID / Tartaric acid


Mass: 150.087 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C4H6O6
#4: Chemical...
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 25 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#6: Chemical
ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2109 / 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: 3.03 Å3/Da / Density % sol: 59.4 %
Description: STATISTICS ARE GOOD TO 2.5A RESOLUTION RMERGE 0.43 IN FINAL SHELL. HOWEVER WEEK DATA EXTENDS TO 2.3A RESOLUTION AND WAS INCLUDED IN THE REFINEMENT.
Crystal growMethod: vapor diffusion, sitting drop / pH: 6.5
Details: SITTING DROP METHOD EQUILIBRATION OF 15 MG/ML AKR7A5, 20MM TRIS-CL PH7.5, 0.5M DITHITHREITOL, 1MM NADP AGAINST 0.2M SODIUM TARTRATE, 7.5% PEG8000 AND 0.1M MES-NAOH PH6.5, pH 6.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.87
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 24, 2003 / Details: RH COATED SI MIRROR
RadiationMonochromator: SI MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.87 Å / Relative weight: 1
ReflectionResolution: 2.3→42 Å / Num. obs: 630867 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 40.8 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 4.1
Reflection shellResolution: 2.3→2.34 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.89 / Mean I/σ(I) obs: 1 / % possible all: 93.3

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GVE, CHAIN A

1gve


Resolution: 2.3→45 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.935 / SU B: 11.094 / SU ML: 0.144 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.238 / ESU R Free: 0.196 / Stereochemistry target values: MAWIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.208 9982 5 %RANDOM
Rwork0.16 ---
obs0.162 188881 89.8 %-
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: 33.36 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å2-1.22 Å2-0.17 Å2
2---0.99 Å2-0.73 Å2
3---1.33 Å2
Refinement stepCycle: LAST / Resolution: 2.3→45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25471 0 800 2109 28380
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0220.02126969
X-RAY DIFFRACTIONr_bond_other_d0.0030.0223493
X-RAY DIFFRACTIONr_angle_refined_deg1.8891.97936609
X-RAY DIFFRACTIONr_angle_other_deg1.104354690
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.44653242
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.63923.6721258
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.584154293
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.27415183
X-RAY DIFFRACTIONr_chiral_restr0.1040.23861
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0229884
X-RAY DIFFRACTIONr_gen_planes_other0.0030.025519
X-RAY DIFFRACTIONr_nbd_refined0.2130.26025
X-RAY DIFFRACTIONr_nbd_other0.1970.224604
X-RAY DIFFRACTIONr_nbtor_refined0.1840.212865
X-RAY DIFFRACTIONr_nbtor_other0.0930.214644
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_refined0.1690.246
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2370.2195
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2580.245
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1231.520515
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.227225675
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.153312844
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.0424.510929
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

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1871tight positional0.070.05
2B1871tight positional0.050.05
3C1871tight positional0.060.05
4D1871tight positional0.060.05
5E1871tight positional0.060.05
6F1871tight positional0.060.05
7G1871tight positional0.070.05
8H1871tight positional0.050.05
9I1871tight positional0.070.05
10J1871tight positional0.070.05
1A2902medium positional0.440.5
2B2902medium positional0.40.5
3C2902medium positional0.420.5
4D2902medium positional0.360.5
5E2902medium positional0.330.5
6F2902medium positional0.430.5
7G2902medium positional0.410.5
8H2902medium positional0.40.5
9I2902medium positional0.390.5
10J2902medium positional0.370.5
1A1871tight thermal0.180.5
2B1871tight thermal0.140.5
3C1871tight thermal0.170.5
4D1871tight thermal0.190.5
5E1871tight thermal0.190.5
6F1871tight thermal0.160.5
7G1871tight thermal0.180.5
8H1871tight thermal0.150.5
9I1871tight thermal0.160.5
10J1871tight thermal0.150.5
1A2902medium thermal0.882
2B2902medium thermal0.872
3C2902medium thermal0.792
4D2902medium thermal0.972
5E2902medium thermal0.872
6F2902medium thermal0.782
7G2902medium thermal0.932
8H2902medium thermal0.912
9I2902medium thermal0.782
10J2902medium thermal0.772
LS refinement shellResolution: 2.3→2.38 Å / Total num. of bins used: 15 /
RfactorNum. reflection
Rfree0.339 812
Rwork0.265 14808
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)
11.01370.0828-0.11460.8082-0.39820.69320.0091-0.0757-0.10570.09960.00490.11420.0355-0.1184-0.014-0.06980.0079-0.0022-0.0901-0.0005-0.13086.84219.203515.4009
21.58570.11110.19880.85340.05821.23120.17720.2324-0.4551-0.0555-0.0261-0.04450.19410.1242-0.15110.01370.061-0.1091-0.0015-0.16760.112244.57290.525568.1492
31.19760.2973-0.27270.7428-0.06460.8827-0.02480.01280.0022-0.0155-0.0319-0.10830.01310.10040.0567-0.1162-0.00280.05260.04650.0485-0.06959.210674.560845.5317
40.32710.18640.23450.97080.22110.5344-0.05470.07490.0480.01540.04370.09610.0325-0.00440.0109-0.11630.01480.0467-0.11520.0284-0.1247-12.702266.47976.0073
50.75950.35170.00310.9599-0.02510.12920.03560.0391-0.04040.10570.0197-0.0495-0.01060.0386-0.0553-0.05790.02440.0187-0.1169-0.0072-0.16784.723137.81989.1994
60.7542-0.0055-0.10590.9350.41181.13930.07920.0902-0.0692-0.1048-0.03730.0366-0.0256-0.0469-0.0419-0.02440.0447-0.01510.029-0.0599-0.150718.483722.504356.7719
70.5892-0.2030.09730.87670.31840.9403-0.0569-0.12130.09360.13910.01840.0378-0.0990.01230.0384-0.11360.01130.0158-0.09130.0075-0.079351.722881.606832.496
81.5405-0.00650.43260.71430.12731.2176-0.15830.29770.3637-0.0857-0.0195-0.0691-0.20910.2120.1778-0.0214-0.1179-0.05360.06440.1650.079486.666695.566225.3083
90.93830.1058-0.09711.43390.02281.04420.0391-0.11590.00040.3008-0.0577-0.1422-0.0142-0.00170.01850.0221-0.0095-0.0697-0.11640.0427-0.035155.3402138.047131.9675
100.88920.1019-0.13491.49990.00910.99130.0124-0.06030.07650.039-0.00780.3508-0.0016-0.0863-0.0046-0.08660.0243-0.0153-0.11650.00920.078331.6269109.49121.8375
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A4 - 327
2X-RAY DIFFRACTION2B4 - 327
3X-RAY DIFFRACTION3C4 - 327
4X-RAY DIFFRACTION4D4 - 327
5X-RAY DIFFRACTION5E4 - 327
6X-RAY DIFFRACTION6F4 - 327
7X-RAY DIFFRACTION7G4 - 327
8X-RAY DIFFRACTION8H4 - 327
9X-RAY DIFFRACTION9I4 - 327
10X-RAY DIFFRACTION10J4 - 327

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