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- PDB-4acb: CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METH... -

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Basic information

Entry
Database: PDB / ID: 4acb
TitleCRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS IN COMPLEX WITH THE GTP ANALOGUE GPPNHP
ComponentsTRANSLATION ELONGATION FACTOR SELB
KeywordsTRANSLATION / SELENOCYSTEINE / SECIS ELEMENT / EF-SEC / SEC-TRNA(SEC)
Function / homology
Function and homology information


selenocysteine incorporation / translation elongation factor activity / GTPase activity / GTP binding / RNA binding / cytoplasm
Similarity search - Function
: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Ribosomal protein L35A superfamily / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain ...: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Ribosomal protein L35A superfamily / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Elongation Factor Tu (Ef-tu); domain 3 / Small GTP-binding protein domain / Thrombin, subunit H / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-MONOPHOSPHATE / GUANOSINE-5'-DIPHOSPHATE / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Selenocysteine-specific elongation factor
Similarity search - Component
Biological speciesMETHANOCOCCUS MARIPALUDIS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.34 Å
AuthorsLeibundgut, M. / Frick, C. / Thanbichler, M. / Boeck, A. / Ban, N.
CitationJournal: Embo J. / Year: 2005
Title: Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors.
Authors: Leibundgut, M. / Frick, C. / Thanbichler, M. / Bock, A. / Ban, N.
History
DepositionDec 14, 2011Deposition site: PDBE / Processing site: PDBE
SupersessionNov 7, 2012ID: 1WB3
Revision 1.0Nov 7, 2012Provider: repository / Type: Initial release
Revision 1.1Dec 20, 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_sheet / 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_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_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr2_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_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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_conn.ptnr2_label_seq_id / _struct_sheet.number_strands / _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 "AF" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AF" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -7-STRANDED BARREL THIS IS REPRESENTED BY A -6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -1-STRANDED BARREL THIS IS REPRESENTED BY A 0-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DF" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 0-STRANDED BARREL THIS IS REPRESENTED BY A 1-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: TRANSLATION ELONGATION FACTOR SELB
B: TRANSLATION ELONGATION FACTOR SELB
C: TRANSLATION ELONGATION FACTOR SELB
D: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,28822
Polymers216,5864
Non-polymers4,70218
Water1086
1
A: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,6933
Polymers54,1471
Non-polymers5472
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,5627
Polymers54,1471
Non-polymers1,4156
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: TRANSLATION ELONGATION FACTOR SELB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,88611
Polymers54,1471
Non-polymers2,74010
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: TRANSLATION ELONGATION FACTOR SELB


Theoretical massNumber of molelcules
Total (without water)54,1471
Polymers54,1471
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)146.630, 146.630, 297.220
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number151
Space group name H-MP3112

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
TRANSLATION ELONGATION FACTOR SELB / MJ0495-LIKE PROTEIN


Mass: 54146.504 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) METHANOCOCCUS MARIPALUDIS (archaea) / Strain: JJ / Description: GERMAN COLLECTION OF MICROORGANISMS (DSM 2067) / Plasmid: PT7-7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q8J307

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Non-polymers , 7 types, 24 molecules

#2: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / 5'-Guanylyl imidodiphosphate


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#5: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#6: Chemical
ChemComp-DXC / (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID / DEOXYCHOLIC ACID / Deoxycholic acid


Mass: 392.572 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C24H40O4 / Comment: detergent*YM
#7: Chemical ChemComp-5GP / GUANOSINE-5'-MONOPHOSPHATE / Guanosine monophosphate


Mass: 363.221 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H14N5O8P
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Formula: H2O

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Details

Nonpolymer detailsHEXACOORDINATED MAGNESIUM ION (MG A1470): FOUR WATERS OF THE COORDINATION SPHERE SUBSTITUTED BY OG1 ...HEXACOORDINATED MAGNESIUM ION (MG A1470): FOUR WATERS OF THE COORDINATION SPHERE SUBSTITUTED BY OG1 OF TWO THR AND O2B OR O1G OF GNP, RESPECTIVELY HEXACOORDINATED MAGNESIUM ION (MG B1470): TWO WATERS OF THE COORDINATION SPHERE SUBSTITUTED BY OG1 OF THR AND O2B OF GDP, RESPECTIVELY

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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: 4.3 Å3/Da / Density % sol: 71 %
Description: THE INCREASED MERGING R VALUE IN THE HIGHEST RESOLUTION SHELL OF 1.44 IS DUE TO ANISOTROPY OF THE DATA
Crystal growDetails: 10 MM KCL,20 MM TRIS/HCL (PH 7.5), 40 MM MGSO4, 2 MM DTT, 3 MM GDP, 1.8 - 2.0 M AMMONIUM SULFATE, 100 MM SODIUM CITRATE (PH 6.0), 1 MM DEOXYCHOLIC ACID

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Dec 19, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.34→35 Å / Num. obs: 102021 / % possible obs: 98.4 % / Observed criterion σ(I): -3 / Redundancy: 4.6 % / Biso Wilson estimate: 104.37 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.24
Reflection shellResolution: 3.34→3.54 Å / Redundancy: 4.7 % / Rmerge(I) obs: 1.44 / Mean I/σ(I) obs: 1.36 / % possible all: 97.5

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8_1069)refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: SAD
Starting model: PDB ENTRY 4AC9

4ac9


Resolution: 3.34→19.938 Å / SU ML: 0.4 / σ(F): 0.75 / Phase error: 23.98 / Stereochemistry target values: ML
Details: A FOBS OVER SIGMA_FOBS CUTOFF OF 0.75 WAS APPLIED OWING TO ANISOTROPY OF THE DATA. THE MODEL WAS REFINED AGAINST ANOMALOUSLY SCALED DATA
RfactorNum. reflection% reflection
Rfree0.2233 3599 4.2 %
Rwork0.179 --
obs0.1809 85487 82.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 198.98 Å2
Refinement stepCycle: LAST / Resolution: 3.34→19.938 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14305 0 312 6 14623
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00714833
X-RAY DIFFRACTIONf_angle_d1.1520055
X-RAY DIFFRACTIONf_dihedral_angle_d15.695666
X-RAY DIFFRACTIONf_chiral_restr0.0712424
X-RAY DIFFRACTIONf_plane_restr0.0042455
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3401-3.38380.3731050.34582206X-RAY DIFFRACTION59
3.3838-3.42990.3578950.31482250X-RAY DIFFRACTION60
3.4299-3.47870.35371150.3042514X-RAY DIFFRACTION65
3.4787-3.53030.31971140.27892457X-RAY DIFFRACTION66
3.5303-3.58520.30961070.2682517X-RAY DIFFRACTION65
3.5852-3.64360.27471100.24972564X-RAY DIFFRACTION68
3.6436-3.7060.27061160.25262777X-RAY DIFFRACTION74
3.706-3.7730.25521290.22292878X-RAY DIFFRACTION75
3.773-3.84510.25141170.21442860X-RAY DIFFRACTION74
3.8451-3.9230.24431260.20042926X-RAY DIFFRACTION78
3.923-4.00760.22121310.18582984X-RAY DIFFRACTION78
4.0076-4.10.23481360.17793131X-RAY DIFFRACTION81
4.1-4.20160.17911420.16313206X-RAY DIFFRACTION84
4.2016-4.31410.1961460.13713298X-RAY DIFFRACTION87
4.3141-4.43970.17681540.13343420X-RAY DIFFRACTION90
4.4397-4.58140.14511530.12943459X-RAY DIFFRACTION91
4.5814-4.7430.17911610.12573520X-RAY DIFFRACTION92
4.743-4.93010.18691570.13183506X-RAY DIFFRACTION93
4.9301-5.15080.19261570.14023578X-RAY DIFFRACTION94
5.1508-5.41720.23221580.16133618X-RAY DIFFRACTION94
5.4172-5.7490.23171580.17243569X-RAY DIFFRACTION96
5.749-6.18060.27281600.18223690X-RAY DIFFRACTION96
6.1806-6.78020.23841680.18073685X-RAY DIFFRACTION97
6.7802-7.71120.23461670.17023764X-RAY DIFFRACTION98
7.7112-9.53510.18071600.16323757X-RAY DIFFRACTION99
9.5351-19.93860.23151570.19813754X-RAY DIFFRACTION98
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)
14.6916-0.53850.15355.61730.95386.2583-0.3294-0.8995-0.23720.5150.02610.78920.3375-1.10570.28930.6867-0.14520.04441.7339-0.12660.914628.1802-37.8796-50.2099
26.4735-0.85623.09866.2919-2.96553.0804-0.29960.09450.3716-0.05220.40650.6338-0.5375-0.4259-0.1521.17650.4616-0.02831.0754-0.05320.975644.0224-13.3827-9.7049
35.6969-0.0568-1.66182.8313-0.92177.3375-0.10820.6768-0.1877-0.36140.10730.05210.2902-0.2757-0.03590.69060.047-0.05970.6911-0.03870.619668.9321-49.689924.1196
40.8609-2.8074-0.69728.8753-1.17322.9439-0.38390.26670.9765-0.52610.56621.3609-0.9745-0.9241-0.28942.85140.9024-0.19771.8501-0.17412.634230.803515.7246-17.6783
56.1143-0.1007-2.10357.53024.14433.2184-0.2223-3.1260.73670.7196-0.2484-0.12680.6613-1.29090.12691.4720.3357-0.22343.6159-0.57681.274818.6487-24.6112-27.6717
69.11672.3976-1.35517.7016-0.73117.8467-0.2921-0.94840.10660.70610.2810.1383-0.7192-0.15860.03070.89220.2514-0.07790.8846-0.00460.516458.5145-27.50398.4956
77.544-1.00181.09029.05031.79087.62470.13620.15910.3244-0.79570.0172-0.9053-0.49121.5417-0.2090.6187-0.10090.18820.95760.0670.660992.5303-46.256711.824
84.645-1.08471.57784.82250.53032.5287-0.4278-0.656-0.6991-1.64991.1013-0.4793-1.6247-0.4218-0.39944.74370.7624-0.16811.97970.2282.514839.300432.1704-36.01
98.102-3.9232-0.09257.12780.49111.2399-0.04980.272-0.1605-0.4895-0.42860.89140.1447-1.53940.65531.19060.1628-0.08853.3554-0.49971.68060.4134-27.8644-51.6465
107.44710.1479-5.37659.2452-0.58465.82140.43910.8366-0.6795-1.27330.16761.81090.1798-2.371-0.6171.2089-0.139-0.3181.99710.25021.196930.1913-37.36311.4771
113.329-0.1761-2.00233.4064-1.49216.379-0.0441-0.4229-0.26030.1354-0.2539-0.3284-0.45181.02440.31460.53910.0724-0.08841.23560.02390.808394.3118-53.400341.8289
126.60712.52691.63484.55011.41150.3831-1.00670.58660.8222-0.57050.5253-1.4906-1.61850.2360.63123.1428-0.2013-0.41531.3492-0.19061.97261.423215.3474-25.1932
135.181.0734.21145.90121.08323.37420.084-0.83990.82110.7424-0.696-0.545-1.30950.02250.75931.8859-0.0592-0.27413.76290.07562.2539-24.7568-22.207-76.1033
145.27663.61360.98733.8291-1.27152.7356-0.70581.09233.5966-0.34090.3382.0370.1059-2.49960.43672.1634-0.0508-0.51442.89320.58142.8839-1.7542-50.3357-0.8769
156.6592-0.48786.4436.9997-3.09219.79530.1797-0.0825-0.07370.6533-0.4211-1.24430.48640.570.16371.34270.3011-0.14951.79620.02211.3072111.2807-55.188774.0216
163.00421.1086-1.76217.7027-3.55972.09191.9603-2.18760.37530.2525-1.1298-2.6377-0.1119-0.0035-0.7523.2693-0.80040.08952.4598-0.05123.558195.97457.3887-16.0496
179.95234.66517.15043.69744.17455.5860.0766-1.73740.54161.4875-0.173-1.5918-0.9243.17880.04082.9930.6469-1.76422.2983-0.41744.369630.1397-21.7803-14.9504
184.87054.32990.24284.32941.6844.5209-0.78630.46171.1222-0.34820.37840.4702-0.0931.07540.18612.1445-0.8259-0.89221.90980.76762.07275.5051-25.02534.4711
197.9145-6.3961-4.17017.02925.73065.20751.4158-2.4866-1.58591.0817-1.69671.15281.1991-0.63150.22051.8026-0.36220.511.10240.25731.045870.2126-61.763440.4616
207.59031.2501-5.39115.50760.57436.603-0.48990.5346-0.6547-0.4331.1235-0.02791.5758-1.4917-0.31961.2619-0.3826-0.57191.4657-0.18431.157548.4485-56.823727.147
215.13233.385-1.39344.21332.576.5222-0.02751.98460.3767-0.5003-0.6571.3796-0.4714-1.61830.48340.47280.09420.09211.7889-0.05210.812249.1086-49.794430.6364
229.64375.09393.24986.44010.07461.8066-0.0757-0.4724-1.42690.5453-0.8544-0.46310.9308-0.11870.6761.44450.16610.11460.8432-0.00480.408579.5748-58.568853.7061
23222222.00016.8943-10.92115.599123.6516-2.982-3.8514-5.3587-39.453-3.94962.8997-0.47870.16274.1744-0.90421.620348.9828-35.9443-10.5015
241.9999-3.1919-7.96593.12164.19076.74324.1933-56.2226-5.47297.33216.708642.56112.1671-33.4043-10.92152.36240.22230.25323.32940.47742.893972.6827-37.9025.1068
253.3533.35522.00963.35891.97871.9759-1.868-7.87516.50563.82911.38527.7226-8.2021-28.74210.45381.8588-0.3268-0.53722.39350.19961.302679.5308-49.421743.6132
2625.88342.0001222-2.204312.66910.046431.48825.3002-12.49465.39460.22-3.12282.1244-0.034-0.26532.26350.55331.60475.8303-45.373847.1238
2722224.14876.25542.8443-1.8573-19.69938.4588-4.7516-21.776711.5258-7.81191.86661.22110.148-0.02672.1458-0.381.621113.28-54.509557.617
281.9999221.999921.9999-0.071310.2881-6.4012-12.4744-1.00172.7868-17.06545.96621.07111.33910.39780.45871.35030.88771.900989.619-65.839354.9117
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1((CHAIN A AND RESID 0:179) OR (CHAIN A AND RESID 1469:1470) OR (CHAIN A AND RESID 2002:2004))
2X-RAY DIFFRACTION2((CHAIN B AND RESID 1:179) OR (CHAIN B AND RESID 1469:1470) OR (CHAIN B AND RESID 2001:2004))
3X-RAY DIFFRACTION3((CHAIN C AND RESID -2:179))
4X-RAY DIFFRACTION4(CHAIN D AND RESID 2:179)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 180:270)
6X-RAY DIFFRACTION6((CHAIN B AND RESID 180:270) OR (CHAIN B AND RESID 1473))
7X-RAY DIFFRACTION7((CHAIN C AND RESID 180:270) OR (CHAIN C AND RESID 1475))
8X-RAY DIFFRACTION8(CHAIN D AND RESID 180:270)
9X-RAY DIFFRACTION9(CHAIN A AND RESID 271:388)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 271:388)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 271:388)
12X-RAY DIFFRACTION12(CHAIN D AND RESID 271:388)
13X-RAY DIFFRACTION13(CHAIN A AND RESID 389:468)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 389:468)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 389:468)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 389:468)
17X-RAY DIFFRACTION17(CHAIN B AND RESID 1474)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 1476)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 1477)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 1478)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 1479)
22X-RAY DIFFRACTION22(CHAIN C AND RESID 1480)
23X-RAY DIFFRACTION23(CHAIN B AND RESID 1471)
24X-RAY DIFFRACTION24(CHAIN B AND RESID 1472)
25X-RAY DIFFRACTION25(CHAIN C AND RESID 1471)
26X-RAY DIFFRACTION26(CHAIN C AND RESID 1472)
27X-RAY DIFFRACTION27(CHAIN C AND RESID 1473)
28X-RAY DIFFRACTION28(CHAIN C AND RESID 1481)

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