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- PDB-6s81: Crystal structure of methionine adenosyltransferase from Pyrococc... -

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Basic information

Entry
Database: PDB / ID: 6s81
TitleCrystal structure of methionine adenosyltransferase from Pyrococcus furiosus
ComponentsS-adenosylmethionine synthase
KeywordsTRANSFERASE / S-adenosyl methionine synthesis / cofactor biosynthesis / cytoplasmic
Function / homology
Function and homology information


methionine adenosyltransferase / methionine adenosyltransferase activity / S-adenosylmethionine biosynthetic process / one-carbon metabolic process / magnesium ion binding / ATP binding
Similarity search - Function
S-adenosylmethionine synthetase, C-terminal domain / S-adenosylmethionine synthetase, N-terminal domain / S-adenosylmethionine synthetase, archaea / S-adenosylmethionine synthase / S-adenosylmethionine synthetase, domain 3 / S-adenosylmethionine synthetase (AdoMet synthetase) / GMP Synthetase; Chain A, domain 3 - #10 / GMP Synthetase; Chain A, domain 3 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
: / S-adenosylmethionine synthase
Similarity search - Component
Biological speciesPyrococcus furiosus (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.784 Å
AuthorsDegano, M. / Minici, C. / Porcelli, M.
Funding support Italy, 1items
OrganizationGrant numberCountry
Italian Association for Cancer Research Italy
CitationJournal: J.Struct.Biol. / Year: 2020
Title: Structures of catalytic cycle intermediates of the Pyrococcus furiosus methionine adenosyltransferase demonstrate negative cooperativity in the archaeal orthologues.
Authors: Minici, C. / Mosca, L. / Ilisso, C.P. / Cacciapuoti, G. / Porcelli, M. / Degano, M.
History
DepositionJul 8, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 5, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 18, 2020Group: Database references / Category: citation / citation_author / Item: _citation.journal_volume / _citation_author.name
Revision 1.2Jan 24, 2024Group: 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 / pdbx_struct_conn_angle / struct_conn
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.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.value / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: S-adenosylmethionine synthase
B: S-adenosylmethionine synthase
C: S-adenosylmethionine synthase
D: S-adenosylmethionine synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)178,10714
Polymers177,3554
Non-polymers75210
Water15,997888
1
A: S-adenosylmethionine synthase
C: S-adenosylmethionine synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,0898
Polymers88,6772
Non-polymers4116
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6290 Å2
ΔGint-56 kcal/mol
Surface area30190 Å2
MethodPISA
2
B: S-adenosylmethionine synthase
D: S-adenosylmethionine synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,0186
Polymers88,6772
Non-polymers3414
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6000 Å2
ΔGint-29 kcal/mol
Surface area30230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.108, 133.900, 213.100
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 2 through 16 or resid 18...
21(chain B and (resid 2 through 16 or resid 18...
31(chain C and (resid 2 through 16 or resid 18...
41(chain D and (resid 2 through 16 or resid 18...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 2 through 16 or resid 18...A2 - 16
121(chain A and (resid 2 through 16 or resid 18...A18 - 109
131(chain A and (resid 2 through 16 or resid 18...A111 - 119
141(chain A and (resid 2 through 16 or resid 18...A121 - 133
151(chain A and (resid 2 through 16 or resid 18...A135 - 136
161(chain A and (resid 2 through 16 or resid 18...A138 - 157
171(chain A and (resid 2 through 16 or resid 18...A159 - 186
181(chain A and (resid 2 through 16 or resid 18...A188 - 2232
191(chain A and (resid 2 through 16 or resid 18...A234232
1101(chain A and (resid 2 through 16 or resid 18...A234 - 248
1111(chain A and (resid 2 through 16 or resid 18...A250 - 274
1121(chain A and (resid 2 through 16 or resid 18...A276 - 289
1131(chain A and (resid 2 through 16 or resid 18...A291 - 319
1141(chain A and (resid 2 through 16 or resid 18...A321 - 327
1151(chain A and (resid 2 through 16 or resid 18...A329 - 3369
1161(chain A and (resid 2 through 16 or resid 18...A371369
1171(chain A and (resid 2 through 16 or resid 18...A371 - 380
1181(chain A and (resid 2 through 16 or resid 18...A382 - 401
211(chain B and (resid 2 through 16 or resid 18...B2 - 16
221(chain B and (resid 2 through 16 or resid 18...B18 - 109
231(chain B and (resid 2 through 16 or resid 18...B111 - 19
241(chain B and (resid 2 through 16 or resid 18...B2 - 401
251(chain B and (resid 2 through 16 or resid 18...B135 - 136
261(chain B and (resid 2 through 16 or resid 18...B138 - 157
271(chain B and (resid 2 through 16 or resid 18...B159 - 186
281(chain B and (resid 2 through 16 or resid 18...B188 - 2232
291(chain B and (resid 2 through 16 or resid 18...B234232
2101(chain B and (resid 2 through 16 or resid 18...B234 - 248
2111(chain B and (resid 2 through 16 or resid 18...B250 - 274
2121(chain B and (resid 2 through 16 or resid 18...B276 - 289
2131(chain B and (resid 2 through 16 or resid 18...B291 - 319
2141(chain B and (resid 2 through 16 or resid 18...B321 - 327
2151(chain B and (resid 2 through 16 or resid 18...B329 - 3369
2161(chain B and (resid 2 through 16 or resid 18...B371369
2171(chain B and (resid 2 through 16 or resid 18...B371 - 380
2181(chain B and (resid 2 through 16 or resid 18...B382 - 401
311(chain C and (resid 2 through 16 or resid 18...C2 - 16
321(chain C and (resid 2 through 16 or resid 18...C18 - 109
331(chain C and (resid 2 through 16 or resid 18...C111 - 119
341(chain C and (resid 2 through 16 or resid 18...C121 - 133
351(chain C and (resid 2 through 16 or resid 18...C135 - 136
361(chain C and (resid 2 through 16 or resid 18...C138 - 142
371(chain C and (resid 2 through 16 or resid 18...C154 - 157
381(chain C and (resid 2 through 16 or resid 18...C159 - 1212
391(chain C and (resid 2 through 16 or resid 18...C214212
3101(chain C and (resid 2 through 16 or resid 18...C214 - 232
3111(chain C and (resid 2 through 16 or resid 18...C234 - 248
3121(chain C and (resid 2 through 16 or resid 18...C250 - 274
3131(chain C and (resid 2 through 16 or resid 18...C276 - 289
3141(chain C and (resid 2 through 16 or resid 18...C291 - 319
3151(chain C and (resid 2 through 16 or resid 18...C321 - 3335
3161(chain C and (resid 2 through 16 or resid 18...C337335
3171(chain C and (resid 2 through 16 or resid 18...C337 - 369
3181(chain C and (resid 2 through 16 or resid 18...C371 - 380
3191(chain C and (resid 2 through 16 or resid 18...C382 - 401
411(chain D and (resid 2 through 16 or resid 18...D2 - 16
421(chain D and (resid 2 through 16 or resid 18...D18 - 109
431(chain D and (resid 2 through 16 or resid 18...D111 - 119
441(chain D and (resid 2 through 16 or resid 18...D121 - 133
451(chain D and (resid 2 through 16 or resid 18...D135 - 136
461(chain D and (resid 2 through 16 or resid 18...D138 - 142
471(chain D and (resid 2 through 16 or resid 18...D154 - 157
481(chain D and (resid 2 through 16 or resid 18...D159 - 1212
491(chain D and (resid 2 through 16 or resid 18...D214212
4101(chain D and (resid 2 through 16 or resid 18...D214 - 232
4111(chain D and (resid 2 through 16 or resid 18...D234 - 248
4121(chain D and (resid 2 through 16 or resid 18...D250 - 274
4131(chain D and (resid 2 through 16 or resid 18...D276 - 289
4141(chain D and (resid 2 through 16 or resid 18...D291 - 319
4151(chain D and (resid 2 through 16 or resid 18...D321 - 3335
4161(chain D and (resid 2 through 16 or resid 18...D337335
4171(chain D and (resid 2 through 16 or resid 18...D337 - 369
4181(chain D and (resid 2 through 16 or resid 18...D371 - 380
4191(chain D and (resid 2 through 16 or resid 18...D382 - 401

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Components

#1: Protein
S-adenosylmethionine synthase / AdoMet synthase / Methionine adenosyltransferase


Mass: 44338.660 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (archaea)
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / Gene: mat, PF1866 / Plasmid: pET22b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q8TZW1, methionine adenosyltransferase
#2: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mn
#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 888 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 2.46 Å3/Da / Density % sol: 49.96 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 0.1 M MES pH 5.5, 0.05 M Mn(HCOO)2, 30% v/v PEG MME 550

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 30, 2010 / Details: Mirrors
RadiationMonochromator: Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 1.78→133.9 Å / Num. obs: 166737 / % possible obs: 99.9 % / Redundancy: 13.2 % / Biso Wilson estimate: 25.96 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.257 / Rpim(I) all: 0.073 / Rrim(I) all: 0.267 / Net I/σ(I): 8.2 / Num. measured all: 2208219 / Scaling rejects: 28
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.78-1.8812.35.085294645239460.4741.4885.3050.699.4
5.64-133.912.60.0557203257110.9990.0160.05730.499.9

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Processing

Software
NameVersionClassification
XDSdata reduction
Aimless0.7.1data scaling
PHENIXrefinement
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1p7l, 1rg9, 3iml, 1qm4

1p7l

1rg9

3iml

1qm4


Resolution: 1.784→106.55 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 28.16
RfactorNum. reflection% reflection
Rfree0.2311 8245 4.98 %
Rwork0.2095 --
obs0.2106 165455 99.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 102.47 Å2 / Biso mean: 35.1319 Å2 / Biso min: 16.92 Å2
Refinement stepCycle: final / Resolution: 1.784→106.55 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12260 0 32 888 13180
Biso mean--38.01 37.28 -
Num. residues----1578
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00512639
X-RAY DIFFRACTIONf_angle_d0.71717158
X-RAY DIFFRACTIONf_chiral_restr0.0531998
X-RAY DIFFRACTIONf_plane_restr0.0052233
X-RAY DIFFRACTIONf_dihedral_angle_d11.8427854
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A8817X-RAY DIFFRACTION8.871TORSIONAL
12B8817X-RAY DIFFRACTION8.871TORSIONAL
13C8817X-RAY DIFFRACTION8.871TORSIONAL
14D8817X-RAY DIFFRACTION8.871TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.784-1.80430.43382460.4284479091
1.8043-1.82550.4522470.4243488694
1.8255-1.84780.37532580.3949522199
1.8478-1.87120.38882780.3737516199
1.8712-1.89580.33262420.3344523799
1.8958-1.92180.31572670.3167523699
1.9218-1.94920.36252590.30995207100
1.9492-1.97830.33332780.2936521499
1.9783-2.00920.32162900.2732518799
2.0092-2.04220.27222970.2663520699
2.0422-2.07740.25232800.2631515199
2.0774-2.11520.27123030.25635239100
2.1152-2.15580.28012540.22825199100
2.1558-2.19990.23352680.21415270100
2.1999-2.24770.20492950.19765196100
2.2477-2.30.24122790.19685241100
2.3-2.35750.23372800.18785255100
2.3575-2.42130.23312590.19145235100
2.4213-2.49250.23982860.18675256100
2.4925-2.5730.21242610.17895286100
2.573-2.66490.21312940.18245257100
2.6649-2.77160.22592740.19645267100
2.7716-2.89780.2352880.19215278100
2.8978-3.05060.21843050.19725282100
3.0506-3.24170.20852620.20065322100
3.2417-3.4920.22872770.19295306100
3.492-3.84350.19422630.17895379100
3.8435-4.39960.17352770.1645386100
4.3996-5.54310.18152820.16365441100
5.5431-106.550.21952960.2208561999
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)
10.0773-0.0408-0.34540.6006-0.03511.2375-0.0023-0.07180.0615-0.00610.0706-0.0734-0.05520.0932-0.08210.18130.00280.00350.2811-0.02170.2587-29.886113.6292-9.6368
21.17580.0168-0.02930.4131-0.39762.2997-0.0713-0.0564-0.1072-0.14160.14730.19840.20320.1539-0.09850.22330.0040.03570.2815-0.03640.2122-24.67674.9258-28.8623
32.5132-1.267-0.28556.5423-2.20743.16780.10330.01560.3417-0.30670.0361-0.2558-0.38020.1384-0.06970.3364-0.03710.06190.2645-0.03030.2867-21.385520.3666-31.0189
40.5118-0.0685-0.01910.5116-0.09071.7713-0.06350.16490.0801-0.1444-0.0031-0.132-0.24660.05690.06370.2535-0.0371-0.01360.27540.02090.261-27.545915.5099-21.9444
53.0659-0.9146-1.46941.41620.4442.51060.01230.05030.2118-0.0498-0.0256-0.28060.02120.4046-0.00250.21350.0493-0.00030.3670.00290.3123-18.01850.6365-5.7478
60.52510.3123-0.48820.3451-0.13132.372-0.0803-0.088-0.0868-0.03810.0157-0.11360.35880.28080.0690.25770.05930.01480.2823-0.00940.2621-24.34-4.5969-10.7756
71.4463-0.34660.4691.7527-0.45482.3657-0.1012-0.12940.1850.10170.1198-0.1286-0.37870.03430.02110.2670.0032-0.03230.2841-0.04340.2956-31.733622.50280.2501
80.2239-0.1524-0.19610.73040.16440.8078-0.01990.05480.07350.04490.07090.0419-0.0741-0.0282-0.07230.18620.00790.00190.23820.02370.2489-31.005713.16-71.6206
90.91750.08080.0920.12840.37491.9975-0.0451-0.0164-0.1170.1250.065-0.1280.1519-0.0537-0.02740.24030.03250.04540.23330.0180.2215-36.34024.7553-52.2891
102.32251.96980.31977.27962.71333.57990.1625-0.24020.14070.3926-0.13270.1009-0.2376-0.21320.02650.30090.06780.04260.25680.04430.2502-39.279520.2863-50.3698
110.50560.0746-0.14680.4972-0.00061.8183-0.05690.0614-0.00440.03370.03610.09310.1392-0.2050.02870.1933-0.00350.00680.22320.01690.2539-36.71440.3713-68.4392
121.68480.24650.26561.54440.40732.1057-0.07450.1540.2297-0.11280.05410.0685-0.3124-0.03340.01590.2515-0.0084-0.02520.24660.05240.3103-29.120221.8191-81.6492
130.2451-0.1584-0.36020.4809-0.22081.4648-0.0169-0.0386-0.0113-0.03150.02410.05490.1321-0.2674-0.02140.2368-0.0120.00530.33570.00930.2426-48.02722.3454-15.9993
141.4013-0.1852-0.26080.38580.22211.40230.01890.12480.087-0.1169-0.061-0.2531-0.0893-0.04130.00970.2682-0.00470.01850.28740.00410.2242-41.915810.9812-34.3326
152.1117-2.1901-0.59366.51490.27872.84220.0630.0823-0.154-0.7006-0.0201-0.09590.4460.05020.00670.3776-0.02770.01570.32080.03320.24-43.3358-4.7171-37.8702
161.06520.07040.21442.1578-0.24331.7174-0.12720.0285-0.2045-0.11590.18770.09250.1447-0.1766-0.04430.3033-0.05250.02430.292-0.00960.2201-42.35122.6354-37.679
171.3286-0.1917-0.31971.47440.2021.6004-0.07480.2224-0.3018-0.25650.1025-0.17260.56150.024-0.0130.452-0.01460.04890.3695-0.05880.3056-43.146-12.3925-16.1529
182.16480.24593.08081.89020.54977.41540.0430.2937-0.1047-0.00060.0920.27270.1778-0.702-0.14630.17830.03020.02450.49270.02260.3119-60.688614.9559-19.3477
190.6004-0.14990.0150.9178-0.8663.66710.0215-0.01250.19210.11230.11610.1675-0.6251-0.6589-0.12870.37190.1370.03560.39040.02570.332-57.289626.3552-19.3728
200.10950.2093-0.04010.7292-0.77691.5353-0.03210.01710.0182-0.08150.0514-0.01110.0932-0.1687-0.01780.23050.00470.01270.3008-0.00920.2488-46.45292.5694-13.9812
211.3101-0.0524-0.93071.202-0.33320.7797-0.05780.0773-0.0676-0.12150.04920.04280.1316-0.36310.03020.2193-0.04090.00580.3226-0.00740.2417-53.4234-6.9506-5.5111
220.23860.1513-0.32750.54540.03051.5378-0.01990.0244-0.03090.0708-0.0019-0.09010.12170.30520.0310.21470.04190.00160.3001-0.00180.2396-12.96241.8165-65.0952
231.48790.2012-0.480.3939-0.05521.5492-0.0641-0.0860.11530.0482-0.01050.2003-0.09940.16930.06080.25590.0264-0.00940.24930.00770.1912-19.005910.7155-46.8554
242.32492.5149-0.49127.2388-0.45332.68230.1231-0.2358-0.14520.798-0.17930.07860.32790.0250.0830.37680.06550.03160.3149-0.00290.2551-17.7145-4.9408-43.1024
250.4827-0.3313-0.14840.2281-0.06871.6325-0.1182-0.0832-0.12530.12080.04840.0490.29670.13470.07590.3090.0360.05050.29560.03980.262-18.3017-5.347-54.24
260.7501-0.0691-0.39340.96190.79443.4063-0.0803-0.06270.08150.04560.0642-0.1842-0.28920.67580.02520.2522-0.0793-0.03510.41240.02520.324-1.762721.4059-61.3007
270.5756-0.0239-0.07230.59840.03941.9394-0.0646-0.01220.11890.07980.0232-0.0476-0.18420.17420.03250.2382-0.0258-0.02210.24940.01690.2708-11.561520.9562-61.417
281.3048-0.019-0.35621.01690.21652.1051-0.0917-0.1243-0.10290.07490.0529-0.01860.2550.24360.03440.20460.05320.01650.2580.02260.2029-11.3559-6.3507-73.2223
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 54 )A2 - 54
2X-RAY DIFFRACTION2chain 'A' and (resid 55 through 91 )A55 - 91
3X-RAY DIFFRACTION3chain 'A' and (resid 92 through 119 )A92 - 119
4X-RAY DIFFRACTION4chain 'A' and (resid 120 through 170 )A120 - 170
5X-RAY DIFFRACTION5chain 'A' and (resid 171 through 191 )A171 - 191
6X-RAY DIFFRACTION6chain 'A' and (resid 192 through 313 )A192 - 313
7X-RAY DIFFRACTION7chain 'A' and (resid 314 through 401 )A314 - 401
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 54 )B2 - 54
9X-RAY DIFFRACTION9chain 'B' and (resid 55 through 91 )B55 - 91
10X-RAY DIFFRACTION10chain 'B' and (resid 92 through 119 )B92 - 119
11X-RAY DIFFRACTION11chain 'B' and (resid 120 through 313 )B120 - 313
12X-RAY DIFFRACTION12chain 'B' and (resid 314 through 401 )B314 - 401
13X-RAY DIFFRACTION13chain 'C' and (resid 2 through 54 )C2 - 54
14X-RAY DIFFRACTION14chain 'C' and (resid 55 through 91 )C55 - 91
15X-RAY DIFFRACTION15chain 'C' and (resid 92 through 119 )C92 - 119
16X-RAY DIFFRACTION16chain 'C' and (resid 120 through 143 )C120 - 143
17X-RAY DIFFRACTION17chain 'C' and (resid 144 through 170 )C144 - 170
18X-RAY DIFFRACTION18chain 'C' and (resid 171 through 191 )C171 - 191
19X-RAY DIFFRACTION19chain 'C' and (resid 192 through 266 )C192 - 266
20X-RAY DIFFRACTION20chain 'C' and (resid 267 through 354 )C267 - 354
21X-RAY DIFFRACTION21chain 'C' and (resid 355 through 401 )C355 - 401
22X-RAY DIFFRACTION22chain 'D' and (resid 2 through 54 )D2 - 54
23X-RAY DIFFRACTION23chain 'D' and (resid 55 through 91 )D55 - 91
24X-RAY DIFFRACTION24chain 'D' and (resid 92 through 119 )D92 - 119
25X-RAY DIFFRACTION25chain 'D' and (resid 120 through 170 )D120 - 170
26X-RAY DIFFRACTION26chain 'D' and (resid 171 through 247 )D171 - 247
27X-RAY DIFFRACTION27chain 'D' and (resid 248 through 298 )D248 - 298
28X-RAY DIFFRACTION28chain 'D' and (resid 299 through 401 )D299 - 401

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