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- PDB-2jfk: Structure of the MAT domain of human FAS with malonyl-CoA -

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Basic information

Entry
Database: PDB / ID: 2jfk
TitleStructure of the MAT domain of human FAS with malonyl-CoA
ComponentsFATTY ACID SYNTHASE
KeywordsTRANSFERASE / OXIDOREDUCTASE / LIPID SYNTHESIS / FATTY ACID BIOSYNTHESIS
Function / homology
Function and homology information


fatty-acid synthase system / (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity / ether lipid biosynthetic process / : / : / (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity / Vitamin B5 (pantothenate) metabolism / neutrophil differentiation / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity ...fatty-acid synthase system / (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity / ether lipid biosynthetic process / : / : / (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity / Vitamin B5 (pantothenate) metabolism / neutrophil differentiation / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity / glandular epithelial cell development / : / glycogen granule / establishment of endothelial intestinal barrier / [acyl-carrier-protein] S-acetyltransferase / [acyl-carrier-protein] S-acetyltransferase activity / Fatty acyl-CoA biosynthesis / oleoyl-[acyl-carrier-protein] hydrolase / (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity / modulation by host of viral process / ChREBP activates metabolic gene expression / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity / fatty acid synthase activity / beta-ketoacyl-[acyl-carrier-protein] synthase I / NR1H2 & NR1H3 regulate gene expression linked to lipogenesis / mammary gland development / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / phosphopantetheine binding / monocyte differentiation / 3-oxoacyl-[acyl-carrier-protein] synthase activity / cellular response to interleukin-4 / Activation of gene expression by SREBF (SREBP) / fatty acid metabolic process / osteoblast differentiation / fatty acid biosynthetic process / melanosome / cadherin binding / inflammatory response / Golgi apparatus / RNA binding / extracellular exosome / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Alpha-Beta Plaits - #3290 / : / Fatty acid synthase, pseudo-KR domain / Malonyl-CoA ACP transacylase, ACP-binding / Malonyl-Coenzyme A Acyl Carrier Protein, domain 2 / Malonyl-Coenzyme A Acyl Carrier Protein; domain 2 / Polyketide and metazoan fatty acid synthase dehydratase (PKS/mFAS DH) domain profile. / Methyltransferase type 12 / Methyltransferase domain / : ...Alpha-Beta Plaits - #3290 / : / Fatty acid synthase, pseudo-KR domain / Malonyl-CoA ACP transacylase, ACP-binding / Malonyl-Coenzyme A Acyl Carrier Protein, domain 2 / Malonyl-Coenzyme A Acyl Carrier Protein; domain 2 / Polyketide and metazoan fatty acid synthase dehydratase (PKS/mFAS DH) domain profile. / Methyltransferase type 12 / Methyltransferase domain / : / Polyketide synthase dehydratase domain / Thioesterase / Thioesterase domain / PKS_DH / Polyketide synthase, dehydratase domain / Polyketide synthase, dehydratase domain superfamily / Polyketide synthase, ketoreductase domain / KR domain / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / Malonyl-CoA ACP transacylase, ACP-binding / PKS_KR / Acyl transferase domain superfamily / Acyl transferase / Acyl transferase domain / Acyl transferase domain in polyketide synthase (PKS) enzymes. / Acyl transferase/acyl hydrolase/lysophospholipase / Alcohol dehydrogenase-like, C-terminal / Zinc-binding dehydrogenase / Polyketide synthase, enoylreductase domain / Enoylreductase / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Beta-ketoacyl synthase / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / GroES-like superfamily / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Thiolase-like / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Alpha/Beta hydrolase fold / Alpha-Beta Plaits / NAD(P)-binding domain superfamily / S-adenosyl-L-methionine-dependent methyltransferase superfamily / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
COENZYME A / Fatty acid synthase
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsBunkoczi, G. / Kavanagh, K. / Hozjan, V. / Rojkova, A. / Watt, S. / Wu, X. / Arrowsmith, C.H. / Edwards, A. / Sundstrom, M. / Weigelt, J. ...Bunkoczi, G. / Kavanagh, K. / Hozjan, V. / Rojkova, A. / Watt, S. / Wu, X. / Arrowsmith, C.H. / Edwards, A. / Sundstrom, M. / Weigelt, J. / Smith, S. / Oppermann, U.
CitationJournal: To be Published
Title: Structure of the MAT Domain of Human Fas with Malonyl-Coa
Authors: Bunkoczi, G. / Kavanagh, K. / Hozjan, V. / Rojkova, A. / Watt, S. / Wu, X. / Arrowsmith, C.H. / Edwards, A. / Sundstrom, M. / Weigelt, J. / Smith, S. / Oppermann, U.
History
DepositionFeb 2, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 13, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Refinement description / Version format compliance
Revision 1.2Feb 28, 2018Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ..._entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
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_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_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _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: FATTY ACID SYNTHASE
B: FATTY ACID SYNTHASE
C: FATTY ACID SYNTHASE
D: FATTY ACID SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)193,6538
Polymers190,5834
Non-polymers3,0704
Water68538
1
A: FATTY ACID SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,4132
Polymers47,6461
Non-polymers7681
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: FATTY ACID SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,4132
Polymers47,6461
Non-polymers7681
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: FATTY ACID SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,4132
Polymers47,6461
Non-polymers7681
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: FATTY ACID SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,4132
Polymers47,6461
Non-polymers7681
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)82.917, 91.410, 261.609
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
12A
22B
32C
42D
13B
23C

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
111METMETSERSER2AA421 - 42723 - 29
211METMETSERSER2BB421 - 42723 - 29
311METMETSERSER2CC421 - 42723 - 29
411METMETSERSER2DD421 - 42723 - 29
121GLNGLNPROPRO2AA440 - 48642 - 88
221GLNGLNPROPRO2BB440 - 48642 - 88
321GLNGLNPROPRO2CC440 - 48642 - 88
421GLNGLNPROPRO2DD440 - 48642 - 88
131ARGARGPROPRO2AA490 - 65492 - 256
231ARGARGPROPRO2BB490 - 65492 - 256
331ARGARGPROPRO2CC490 - 65492 - 256
431ARGARGPROPRO2DD490 - 65492 - 256
141GLNGLNTHRTHR5AA655 - 677257 - 279
241GLNGLNTHRTHR5BB655 - 677257 - 279
341GLNGLNTHRTHR5CC655 - 677257 - 279
441GLNGLNTHRTHR5DD655 - 677257 - 279
151GLYGLYGLUGLU2AA678 - 719280 - 321
251GLYGLYGLUGLU2BB678 - 719280 - 321
351GLYGLYGLUGLU2CC678 - 719280 - 321
451GLYGLYGLUGLU2DD678 - 719280 - 321
161SERSERGLYGLY2AA725 - 774327 - 376
261SERSERGLYGLY2BB725 - 774327 - 376
361SERSERGLYGLY2CC725 - 774327 - 376
461SERSERGLYGLY2DD725 - 774327 - 376
171CYSCYSPROPRO2AA779 - 818381 - 420
271CYSCYSPROPRO2BB779 - 818381 - 420
371CYSCYSPROPRO2CC779 - 818381 - 420
471CYSCYSPROPRO2DD779 - 818381 - 420
112GLYGLYGLUGLU5AA428 - 43930 - 41
212GLYGLYGLUGLU5BB428 - 43930 - 41
312GLYGLYGLUGLU5CC428 - 43930 - 41
412GLYGLYGLUGLU5DD428 - 43930 - 41
122ALAALAGLUGLU5AA487 - 48989 - 91
222ALAALAGLUGLU5BB487 - 48989 - 91
322ALAALAGLUGLU5CC487 - 48989 - 91
422ALAALAGLUGLU5DD487 - 48989 - 91
132ALAALASERSER5AA720 - 724322 - 326
232ALAALASERSER5BB720 - 724322 - 326
332ALAALASERSER5CC720 - 724322 - 326
432ALAALASERSER5DD720 - 724322 - 326
142LEULEUSERSER5AA775 - 778377 - 380
242LEULEUSERSER5BB775 - 778377 - 380
342LEULEUSERSER5CC775 - 778377 - 380
442LEULEUSERSER5DD775 - 778377 - 380
113VALVALPROPRO4BB819 - 822421 - 424
213VALVALPROPRO4CC819 - 822421 - 424

NCS ensembles :
ID
1
2
3

NCS oper:
IDCodeMatrixVector
1given(-0.9937, -0.09787, 0.05458), (-0.10417, 0.6273, -0.77178), (0.0413, -0.7726, -0.63355)-38.79674, -36.66288, -70.94931
2given(0.14769, -0.51944, 0.84165), (0.97434, 0.22256, -0.03362), (-0.16985, 0.82502, 0.53898)19.64811, 20.84164, 121.55309
3given(-0.222, -0.97489, -0.01744), (-0.97499, 0.22176, 0.01434), (-0.01011, 0.02019, -0.99974)-27.09086, -14.95972, 55.78765

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Components

#1: Protein
FATTY ACID SYNTHASE /


Mass: 47645.723 Da / Num. of mol.: 4 / Fragment: MAT DOMAIN, RESIDUES 422-831
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): R3 / References: UniProt: P49327, fatty-acid synthase system
#2: Chemical
ChemComp-COA / COENZYME A / Coenzyme A


Mass: 767.534 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H36N7O16P3S
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 38 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsRESIDUES 399-421 CONSTITUTE A HIS-TAG THAT WAS NOT CLEAVED DURING PURIFICATION

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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: 55 %
Crystal growpH: 8.5 / Details: 16% PEG10K 0.16M MGCL2 0.08 M TRIS PH=8.5, pH 8.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9795
DetectorType: MARRESEARCH / Detector: CCD / Date: Oct 19, 2006
RadiationMonochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.4→41 Å / Num. obs: 78546 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 7.22 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 17.3
Reflection shellResolution: 2.4→2.5 Å / Redundancy: 6.13 % / Rmerge(I) obs: 0.61 / Mean I/σ(I) obs: 2.62 / % possible all: 92.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2JFD

2jfd


Resolution: 2.4→40.96 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.927 / SU B: 32.806 / SU ML: 0.318 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.371 / ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.271 3902 5 %RANDOM
Rwork0.222 ---
obs0.224 74428 99.6 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 26.16 Å2
Baniso -1Baniso -2Baniso -3
1-4.12 Å20 Å20 Å2
2--0.83 Å20 Å2
3----4.95 Å2
Refinement stepCycle: LAST / Resolution: 2.4→40.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12036 0 36 38 12110
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.02212400
X-RAY DIFFRACTIONr_bond_other_d0.0020.028251
X-RAY DIFFRACTIONr_angle_refined_deg1.4151.97116902
X-RAY DIFFRACTIONr_angle_other_deg1.3853.00120130
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.29351616
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.37723.333468
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.845151864
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.3051575
X-RAY DIFFRACTIONr_chiral_restr0.0710.21922
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0213961
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022439
X-RAY DIFFRACTIONr_nbd_refined0.2260.23027
X-RAY DIFFRACTIONr_nbd_other0.190.28554
X-RAY DIFFRACTIONr_nbtor_refined0.180.26160
X-RAY DIFFRACTIONr_nbtor_other0.0960.26570
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1540.2269
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1310.218
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2390.267
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1850.25
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.96738251
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it4.384512928
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it8.6884643
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it10.193113974
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
11A2051tight positional0.050.05
12B2051tight positional0.040.05
13C2051tight positional0.050.05
14D2051tight positional0.040.05
11A2218medium positional0.420.5
12B2218medium positional0.380.5
13C2218medium positional0.390.5
14D2218medium positional0.380.5
21A140medium positional0.680.5
22B140medium positional0.350.5
23C140medium positional0.420.5
24D140medium positional0.390.5
31B59medium positional0.340.5
32C59medium positional0.340.5
11A115loose positional1.075
12B115loose positional0.975
13C115loose positional0.915
14D115loose positional0.895
21A136loose positional1.175
22B136loose positional1.285
23C136loose positional0.975
24D136loose positional1.015
11A2051tight thermal1.212
12B2051tight thermal1.32
13C2051tight thermal1.682
14D2051tight thermal0.962
11A2218medium thermal4.095
12B2218medium thermal3.215
13C2218medium thermal4.185
14D2218medium thermal2.635
21A140medium thermal2.475
22B140medium thermal2.15
23C140medium thermal1.665
24D140medium thermal2.095
31B59medium thermal1.965
32C59medium thermal1.965
11A115loose thermal5.5810
12B115loose thermal3.4810
13C115loose thermal3.5210
14D115loose thermal4.4910
21A136loose thermal3.6410
22B136loose thermal3.5110
23C136loose thermal4.1310
24D136loose thermal3.6810
LS refinement shellResolution: 2.4→2.46 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.412 275 -
Rwork0.373 5233 -
obs--96.26 %
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)
12.48220.2432-1.11757.65350.83627.1667-0.1301-0.12680.0769-0.06980.1437-0.4007-0.49180.4826-0.01360.1273-0.1705-0.0105-0.1321-0.1257-0.2806-24.0271-24.1353-41.4781
20.64630.1845-0.70773.11362.19443.29590.09530.3718-0.088-0.18250.5812-0.708-0.42081.4299-0.6765-0.1435-0.0898-0.03110.6214-0.24940.1597-11.2761-38.6523-64.1896
33.935-1.2943-2.26071.1251.79418.64360.03580.28890.43480.01220.2971-0.13370.38640.5103-0.3329-0.11090.0648-0.0921-0.2435-0.227-0.0941-28.2669-56.8216-74.5158
41.43522.71930.50245.48992.38026.21630.06080.9306-0.5334-0.12410.7767-0.69090.38251.5198-0.8375-0.1920.1627-0.01230.5931-0.44290.148-11.3601-54.25-74.146
50.85980.4341-0.10433.07052.35954.37040.10660.2906-0.26940.620.469-0.6280.42761.1079-0.5756-0.08560.1384-0.18160.179-0.2102-0.0051-18.1838-45.6991-55.3029
64.7962-1.79370.75452.62630.1227.67650.23551.3368-0.4091-0.39870.0255-0.30880.13551.1904-0.2610.08520.033-0.0640.2964-0.1551-0.121-15.124-17.2979-27.112
73.04040.52731.21132.28940.56614.50180.078-0.3634-0.03850.1292-0.14440.18720.0007-0.21260.0664-0.0169-0.0469-0.0823-0.4795-0.0212-0.3062-27.399-10.3955-0.9474
86.02041.60312.78813.50330.86193.60390.6534-1.4306-0.28160.4606-0.2839-0.78650.25460.2842-0.36950.2237-0.1219-0.14260.40920.1255-0.1517-9.5101-11.85619.223
917.16953.72970.65683.89541.07210.30510.0786-1.75840.35080.1052-0.20830.10630.1803-0.39930.12970.2725-0.229-0.03820.34140.0504-0.3178-26.1825-11.975317.7616
104.35430.13192.04231.10580.05955.62130.3162-0.1547-0.70090.12960.0954-0.06050.45630.2848-0.41160.07920.0275-0.1275-0.4690.023-0.1711-19.8426-20.2242-2.4716
110.3892-1.4847-1.41928.28121.019612.55380.112-0.7376-0.11030.4353-0.081-0.37870.73270.478-0.031-0.0377-0.14490.0002-0.18730.0371-0.2702-6.822-6.3683.3938
121.40510.187-0.96762.1854-0.122111.35350.38440.08640.025-0.2606-0.29670.5187-1.7264-1.5921-0.08770.03570.3067-0.0285-0.1977-0.0397-0.1159-15.51993.638557.0059
131.10942.14580.60064.22331.94078.6460.07020.3040.0075-0.4433-0.28590.18291.5569-2.14860.21580.2585-0.2517-0.07510.3559-0.011-0.2429-17.7632-16.409939.1241
141.91762.8842-0.24514.36320.06217.45030.02570.24650.1801-0.4450.02460.5574-1.1861-1.8459-0.05030.26220.3402-0.140.13760.1112-0.1642-16.42910.198238.4307
150.44550.081-0.60461.91831.731110.25050.1893-0.1307-0.0834-0.1077-0.19580.119-0.32570.04180.0065-0.23680.0738-0.0158-0.40720.0343-0.2679-5.8787-4.25657.9517
161.4159-0.6927-1.79033.3033-1.58488.75840.0581-0.32740.10110.2176-0.0111-0.1232-0.0059-0.092-0.0469-0.0068-0.01010.0205-0.1418-0.0478-0.23690.89771.80698.7332
173.0282-1.8542.21972.6584-1.55794.07120.1023-0.2947-0.11360.2087-0.0627-0.22760.0797-0.3449-0.03960.1709-0.1437-0.0801-0.19150.0726-0.003614.1066-13.7199119.3072
182.84012.06261.26924.87531.63870.71940.21640.2231-0.2177-0.06820.0987-0.9140.38920.1049-0.31510.4829-0.2208-0.2470.27480.20080.409736.2318-1.8354129.6625
193.81192.8847-2.120813.8332-0.22341.604-0.0125-0.5047-0.24140.9571-0.2014-0.64940.32170.79840.21380.3671-0.1203-0.3596-0.11060.18270.187828.6925-18.5653128.489
203.5763-1.07023.08751.6135-1.28364.67990.28470.26830.14820.0462-0.4661-0.54730.24220.81050.18140.1261-0.01890.0014-0.12130.13560.114722.1485-8.4242110.2806
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A419 - 489
2X-RAY DIFFRACTION2A490 - 606
3X-RAY DIFFRACTION3A607 - 673
4X-RAY DIFFRACTION4A674 - 703
5X-RAY DIFFRACTION5A704 - 819
6X-RAY DIFFRACTION6B419 - 489
7X-RAY DIFFRACTION7B490 - 606
8X-RAY DIFFRACTION8B607 - 673
9X-RAY DIFFRACTION9B674 - 703
10X-RAY DIFFRACTION10B704 - 822
11X-RAY DIFFRACTION11C419 - 489
12X-RAY DIFFRACTION12C490 - 606
13X-RAY DIFFRACTION13C607 - 673
14X-RAY DIFFRACTION14C674 - 703
15X-RAY DIFFRACTION15C704 - 823
16X-RAY DIFFRACTION16D411 - 489
17X-RAY DIFFRACTION17D490 - 606
18X-RAY DIFFRACTION18D607 - 673
19X-RAY DIFFRACTION19D674 - 703
20X-RAY DIFFRACTION20D704 - 820

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