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- PDB-6wmn: Human poly-N-acetyl-lactosamine synthase structure demonstrates a... -

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Basic information

Entry
Database: PDB / ID: 6wmn
TitleHuman poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases
ComponentsN-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
KeywordsTRANSFERASE / Glycosyltransferase / GT-A fold / poly LacNAc synthesis
Function / homology
Function and homology information


N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase / : / UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity / poly-N-acetyllactosamine biosynthetic process / keratan sulfate biosynthetic process / Keratan sulfate biosynthesis / O-glycan processing / O-linked glycosylation of mucins / protein O-linked glycosylation ...N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase / : / UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity / poly-N-acetyllactosamine biosynthetic process / keratan sulfate biosynthetic process / Keratan sulfate biosynthesis / O-glycan processing / O-linked glycosylation of mucins / protein O-linked glycosylation / cellular response to leukemia inhibitory factor / axon guidance / sensory perception of smell / Golgi membrane
Similarity search - Function
Glycosyl transferase, family 31 / Galactosyltransferase
Similarity search - Domain/homology
URIDINE-5'-DIPHOSPHATE / N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.04 Å
AuthorsKadirvelraj, R. / Wood, Z.A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)1P01GM107012-02 United States
CitationJournal: J.Biol.Chem. / Year: 2020
Title: Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites.
Authors: Kadirvelraj, R. / Yang, J.Y. / Kim, H.W. / Sanders, J.H. / Moremen, K.W. / Wood, Z.A.
History
DepositionApr 21, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 2, 2020Provider: repository / Type: Initial release
Revision 1.1Dec 9, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed ..._citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Apr 28, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Oct 18, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
B: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
C: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
D: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)174,20924
Polymers168,8814
Non-polymers5,32920
Water5,206289
1
A: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
B: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,13711
Polymers84,4402
Non-polymers2,6979
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6830 Å2
ΔGint-10 kcal/mol
Surface area28460 Å2
MethodPISA
2
C: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
D: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,07213
Polymers84,4402
Non-polymers2,63211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6900 Å2
ΔGint-18 kcal/mol
Surface area28180 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.210, 79.810, 157.790
Angle α, β, γ (deg.)90.000, 97.890, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 57 through 170 or resid 174 through 361 or resid 373 through 387))
21(chain B and (resid 57 through 72 or resid 91...
31(chain C and (resid 57 through 72 or resid 91...
41(chain D and (resid 57 through 72 or resid 91 through 387))

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALAASNASN(chain A and (resid 57 through 170 or resid 174 through 361 or resid 373 through 387))AA57 - 17024 - 137
12GLNGLNLYSLYS(chain A and (resid 57 through 170 or resid 174 through 361 or resid 373 through 387))AA174 - 361141 - 328
13METMETTRPTRP(chain A and (resid 57 through 170 or resid 174 through 361 or resid 373 through 387))AA373 - 387340 - 354
21ALAALAPROPRO(chain B and (resid 57 through 72 or resid 91...BB57 - 7224 - 39
22SERSERASNASN(chain B and (resid 57 through 72 or resid 91...BB91 - 17058 - 137
23GLNGLNLYSLYS(chain B and (resid 57 through 72 or resid 91...BB174 - 361141 - 328
24METMETTRPTRP(chain B and (resid 57 through 72 or resid 91...BB373 - 387340 - 354
31ALAALAPROPRO(chain C and (resid 57 through 72 or resid 91...CC57 - 7224 - 39
32SERSERASNASN(chain C and (resid 57 through 72 or resid 91...CC91 - 17058 - 137
33GLNGLNLYSLYS(chain C and (resid 57 through 72 or resid 91...CC174 - 361141 - 328
34METMETTRPTRP(chain C and (resid 57 through 72 or resid 91...CC373 - 387340 - 354
41ALAALAPROPRO(chain D and (resid 57 through 72 or resid 91 through 387))DD57 - 7224 - 39
42SERSERTRPTRP(chain D and (resid 57 through 72 or resid 91 through 387))DD91 - 38758 - 354

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 / Beta-1 / 3-N-acetylglucosaminyltransferase 1 / Beta3Gn-T1 / 3-galactosyltransferase 7 / b3Gal-T7 / ...Beta-1 / 3-N-acetylglucosaminyltransferase 1 / Beta3Gn-T1 / 3-galactosyltransferase 7 / b3Gal-T7 / Beta-3-Gx-T7 / UDP-Gal:beta-GlcNAc beta-1 / UDP-GlcNAc:betaGal beta-1 / 3-N-acetylglucosaminyltransferase 2 / Beta3Gn-T2 / UDP-galactose:beta-N-acetylglucosamine beta-1


Mass: 42220.207 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: B3GNT2, B3GALT7, B3GNT1 / Production host: Homo sapiens (human)
References: UniProt: Q9NY97, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase

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Sugars , 3 types, 8 molecules

#2: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 3 / Source method: obtained synthetically
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#3: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1 / Source method: obtained synthetically
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 5 types, 301 molecules

#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: Mg
#5: Chemical
ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C9H14N2O12P2 / Comment: UDP*YM
#7: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 289 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.48 Å3/Da / Density % sol: 50.5 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 11% PEG3350, 12% Ethylene glycol, 100 mM Hepes pH 7.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Apr 27, 2016
RadiationMonochromator: Rosenbaum-Rock double monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.04→44.07 Å / Num. obs: 105155 / % possible obs: 99.8 % / Redundancy: 7.515 % / Biso Wilson estimate: 42.17 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.088 / Rrim(I) all: 0.095 / Χ2: 0.996 / Net I/σ(I): 13.89 / Num. measured all: 790241 / Scaling rejects: 86
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique obsCC1/2% possible allRmerge(I) obsRrim(I) all
2.04-2.097.290.9977230.51199.4
2.09-2.157.3771.3474740.60599.5
2.15-2.217.3621.8373590.76399.6
2.21-2.287.322.2571080.82999.6
2.28-2.367.5083.0368900.91499.6
2.36-2.447.5913.5766830.92799.80.62
2.44-2.537.6794.8264410.95899.8
2.53-2.637.7026.2162310.97199.9
2.63-2.757.6518.1160100.98499.9
2.75-2.887.69810.8456970.993100
2.88-3.047.69313.8754470.995100
3.04-3.237.68617.8851670.99799.9
3.23-3.457.62924.1848320.998100
3.45-3.727.59932.0345470.999100
3.72-4.087.53637.8641360.999100
4.08-4.567.52742.3137800.999100
4.56-5.277.46244.4633560.99999.9
5.27-6.457.39543.9528200.999100
6.45-9.127.17647.6522190.999100
9.12-44.076.77351.212350.99797.90.038

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Processing

Software
NameVersionClassification
PHENIX1.12_2829refinement
XDSdata reduction
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6WMM

6wmm


Resolution: 2.04→44.07 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 28.87
RfactorNum. reflection% reflection
Rfree0.2321 5213 4.96 %
Rwork0.218 --
obs0.2187 105083 99.73 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 144.97 Å2 / Biso mean: 58.866 Å2 / Biso min: 28.91 Å2
Refinement stepCycle: final / Resolution: 2.04→44.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10513 0 340 289 11142
Biso mean--51.67 50.7 -
Num. residues----1273
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00411178
X-RAY DIFFRACTIONf_angle_d0.56415167
X-RAY DIFFRACTIONf_chiral_restr0.0411659
X-RAY DIFFRACTIONf_plane_restr0.0031901
X-RAY DIFFRACTIONf_dihedral_angle_d10.2286643
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6053X-RAY DIFFRACTION8.569TORSIONAL
12B6053X-RAY DIFFRACTION8.569TORSIONAL
13C6053X-RAY DIFFRACTION8.569TORSIONAL
14D6053X-RAY DIFFRACTION8.569TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.04-2.06310.41041580.404326299
2.0631-2.08740.3771820.3824332599
2.0874-2.11280.38511490.3626329499
2.1128-2.13960.31961980.34423271100
2.1396-2.16770.35531740.3269336299
2.1677-2.19740.31611760.30573245100
2.1974-2.22880.32451850.2971330299
2.2288-2.26210.32981660.30313312100
2.2621-2.29740.32891670.2777329899
2.2974-2.33510.26391720.27173321100
2.3351-2.37540.29191610.26733314100
2.3754-2.41860.29061700.273330100
2.4186-2.46510.3151490.26193310100
2.4651-2.51540.29491720.25223338100
2.5154-2.57010.30931840.24523337100
2.5701-2.62990.28371690.24033293100
2.6299-2.69560.26011900.24473344100
2.6956-2.76850.26941730.23673306100
2.7685-2.84990.24991640.22933352100
2.8499-2.94190.23551790.2293324100
2.9419-3.0470.24981910.23063344100
3.047-3.1690.2411760.23463337100
3.169-3.31320.20841670.22563320100
3.3132-3.48780.24451820.20363358100
3.4878-3.70620.19011700.19043346100
3.7062-3.99220.19361770.1883366100
3.9922-4.39360.18481800.17093348100
4.3936-5.02860.19931760.16853360100
5.0286-6.33250.19641740.19753392100
6.3325-44.070.20121820.19973459100
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)
12.7829-0.6907-1.33282.91070.51078.4359-0.0729-0.25510.18970.4117-0.07050.87370.461-1.66980.09430.5745-0.01670.17730.92130.10710.8199-31.6549.66824.5641
24.3245-1.3195-3.88943.73482.0155.73260.60160.54830.2081-0.62-0.251.0591-0.4952-1.5033-0.31670.40650.02260.02530.89670.15310.7085-30.272812.9802-7.4959
32.27040.2449-1.25962.5617-1.9284.356-0.082-0.6822-0.21410.0041-0.0171-0.12720.57161.00920.01790.46170.0864-0.02260.54540.02750.3418-1.96610.5202-8.6381
42.7388-0.6298-0.75233.1081-1.04686.3085-0.1807-0.3730.31690.05020.04110.01210.1607-0.2617-0.09130.3826-0.05240.01060.37280.02980.3265-9.43932.1697-13.017
53.7319-0.3176-1.95592.3047-0.97855.6446-0.0756-0.373-0.12270.0310.10670.16940.5353-0.0637-0.09160.388-0.048-0.01620.44140.04410.3501-11.06671.047-7.7496
63.2394-0.30790.11182.5412-0.17625.40280.0736-0.9383-0.22480.44440.1643-0.17270.49841.3344-0.23090.49820.00460.00081.0797-0.11460.45143.35578.04495.2586
73.8616-1.3558-1.26832.43070.17284.77470.2277-0.79870.5060.4620.22850.2299-0.49740.1917-0.41860.4832-0.09670.1610.6492-0.0780.5048-15.998215.79063.2381
84.04541.6701-1.56242.45730.42562.31180.1175-0.25720.2956-0.1530.2602-0.3522-0.79960.6637-0.47310.6888-0.26190.15511.1103-0.31610.65584.083420.8933-0.9443
93.3695-0.71652.63586.07921.84243.51160.4031-1.03220.3530.0062-0.0622-0.7518-0.25271.3147-0.33850.4118-0.14450.07930.9386-0.14550.47058.04213.9187-9.1887
102.96411.3953-0.9782.7265-0.60463.34550.1187-0.14-0.0229-0.0907-0.2001-0.52880.03260.65680.08130.34020.07580.06320.5509-0.0130.426816.168418.6848-42.5448
112.9155-0.6594-0.65072.2707-0.76447.11680.00690.4202-0.4014-0.32660.14660.17940.4318-0.0614-0.19950.399-0.0143-0.03110.2599-0.01640.2974-5.06857.8864-34.7214
124.14531.7672-0.95421.2791-0.59613.88110.00370.0872-0.4117-0.3072-0.03630.00460.48560.03270.07440.42750.0672-0.01930.2874-0.03010.34432.73376.9579-37.5599
133.765-1.1719-1.47362.516-0.19664.5468-0.03050.9512-0.1138-0.16280.05940.42030.3278-1.0562-0.07390.4853-0.0404-0.0520.6390.09150.4022-12.281815.0153-46.2262
145.49071.79091.46191.71320.3874.0990.01160.41660.5566-0.52970.24040.1281-0.8137-0.4066-0.15710.61910.14830.13940.54350.17650.5966-2.564728.1485-46.4467
153.9787-0.337-2.35951.6041-1.25652.72570.6003-0.31981.2882-0.10760.06840.8087-0.92480.211-0.58730.6395-0.08310.20090.2736-0.1020.59969.263232.1368-37.3292
164.48611.1014-0.21251.8003-0.02571.89650.16970.47770.1963-0.16410.0709-0.05890.0727-0.0244-0.22340.57030.07810.06290.50170.08130.40024.100820.9971-48.6988
176.8487-0.7063-4.55692.36961.18156.24120.56780.61430.77380.2679-0.19040.2833-0.8968-1.0154-0.32450.60180.10480.06020.58230.21950.7634-14.249328.2126-39.7174
186.3037-0.51023.70196.9844-0.39945.03420.22560.77050.3382-0.1516-0.07140.9252-0.0211-0.9113-0.07720.36740.09060.03590.76830.1420.5157-21.977918.4329-35.0324
195.48950.2077-0.31343.8822-1.74454.2453-0.1022-0.09230.1710.32780.03890.6031-0.1503-0.83270.07140.37030.08490.06820.7052-0.06220.6686-45.29-20.025-31.6806
204.2398-0.0082-1.38831.30390.82922.0735-0.26150.3736-0.34770.01080.00780.22410.3041-0.41590.18730.3483-0.06750.05530.3009-0.03680.3693-25.3209-31.0009-41.4816
216.1179-0.5331-0.76282.2679-0.36235.3089-0.35530.5572-0.8432-0.09760.00570.11160.6984-0.34480.21110.4614-0.07630.07670.4087-0.09340.5772-20.9762-34.7395-46.2575
224.6501-0.0206-0.36031.2339-0.21742.6379-0.1756-0.51220.21690.27710.0509-0.0150.01430.07710.14190.39480.02170.03640.3928-0.04510.4198-23.505-22.8803-30.9564
239.65836.6844-6.95387.1086-4.95086.6753-0.0841-0.81710.2210.1364-0.297-0.5339-0.97470.30930.19980.40450.0351-0.05110.533-0.13740.4775-11.3662-14.7811-31.8912
244.23530.20252.89524.25781.20046.2571-0.01640.05070.1252-0.12420.0291-0.4063-0.27280.9306-0.00610.3437-0.05740.03270.5020.00390.4857-1.287-21.3329-41.537
251.859-0.6603-0.37412.3943-1.7732.51950.2627-0.3403-0.06860.0427-0.2697-0.3799-0.6881.5870.12910.643-0.07950.13830.9381-0.09960.53499.3691-16.4532-81.8282
261.2406-0.7438-2.18732.3521-0.68875.41930.0787-0.3645-0.18010.1627-0.4302-0.35530.05670.69030.09130.4142-0.03960.05150.772-0.13330.41580.8081-22.5191-71.7355
270.357-0.42861.09991.5361-1.31756.8857-0.25480.6709-0.5868-0.17250.08910.15180.6158-0.8445-0.07870.4261-0.1210.00360.912-0.23560.4579-17.1281-28.453-67.4031
284.041.5552-3.26882.4204-1.86936.2162-0.38420.3106-0.5778-0.2688-0.1777-0.18340.7426-0.42590.55530.4702-0.06190.05310.6459-0.19090.5219-9.6572-30.3527-70.4964
294.30360.32552.63991.3496-0.24331.7361-0.23330.8811-0.3174-0.35530.04780.33930.2397-1.7344-0.15720.5161-0.0017-0.07871.4546-0.12650.4589-23.8957-21.3348-79.8829
305.06453.67585.36883.78033.42275.95460.15690.69710.4584-0.7349-0.0745-0.0762-1.8948-1.13620.32280.80030.21370.05961.1277-0.06750.5011-13.2473-9.1056-80.7461
313.3242-0.5765-1.87843.5461-2.90954.16150.7279-0.17660.42150.1792-0.15710.7394-1.4390.3732-0.55280.9648-0.16520.16170.6537-0.1710.5248-1.3862-5.6214-71.7154
324.70070.54381.06842.8843-1.28153.32560.16160.66010.1313-0.314-0.061-0.0049-0.4777-0.6836-0.07810.57830.09380.05340.8837-0.03360.3128-9.0717-15.619-82.7353
332.02610.1918-0.81060.0582-0.27953.92720.52590.88720.4155-0.1949-0.04960.1935-1.354-1.64660.31330.70060.36420.09481.36580.10650.4175-27.3008-13.7775-66.8588
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 57 through 99 )A57 - 99
2X-RAY DIFFRACTION2chain 'A' and (resid 100 through 131 )A100 - 131
3X-RAY DIFFRACTION3chain 'A' and (resid 132 through 170 )A132 - 170
4X-RAY DIFFRACTION4chain 'A' and (resid 171 through 194 )A171 - 194
5X-RAY DIFFRACTION5chain 'A' and (resid 195 through 245 )A195 - 245
6X-RAY DIFFRACTION6chain 'A' and (resid 246 through 270 )A246 - 270
7X-RAY DIFFRACTION7chain 'A' and (resid 271 through 343 )A271 - 343
8X-RAY DIFFRACTION8chain 'A' and (resid 344 through 368 )A344 - 368
9X-RAY DIFFRACTION9chain 'A' and (resid 369 through 392 )A369 - 392
10X-RAY DIFFRACTION10chain 'B' and (resid 56 through 143 )B56 - 143
11X-RAY DIFFRACTION11chain 'B' and (resid 144 through 194 )B144 - 194
12X-RAY DIFFRACTION12chain 'B' and (resid 195 through 234 )B195 - 234
13X-RAY DIFFRACTION13chain 'B' and (resid 235 through 261 )B235 - 261
14X-RAY DIFFRACTION14chain 'B' and (resid 262 through 286 )B262 - 286
15X-RAY DIFFRACTION15chain 'B' and (resid 287 through 302 )B287 - 302
16X-RAY DIFFRACTION16chain 'B' and (resid 303 through 343 )B303 - 343
17X-RAY DIFFRACTION17chain 'B' and (resid 344 through 364 )B344 - 364
18X-RAY DIFFRACTION18chain 'B' and (resid 365 through 397 )B365 - 397
19X-RAY DIFFRACTION19chain 'C' and (resid 57 through 113 )C57 - 113
20X-RAY DIFFRACTION20chain 'C' and (resid 114 through 163 )C114 - 163
21X-RAY DIFFRACTION21chain 'C' and (resid 164 through 216 )C164 - 216
22X-RAY DIFFRACTION22chain 'C' and (resid 217 through 342 )C217 - 342
23X-RAY DIFFRACTION23chain 'C' and (resid 343 through 362 )C343 - 362
24X-RAY DIFFRACTION24chain 'C' and (resid 363 through 397 )C363 - 397
25X-RAY DIFFRACTION25chain 'D' and (resid 57 through 99 )D57 - 99
26X-RAY DIFFRACTION26chain 'D' and (resid 100 through 143 )D100 - 143
27X-RAY DIFFRACTION27chain 'D' and (resid 144 through 194 )D144 - 194
28X-RAY DIFFRACTION28chain 'D' and (resid 195 through 234 )D195 - 234
29X-RAY DIFFRACTION29chain 'D' and (resid 235 through 261 )D235 - 261
30X-RAY DIFFRACTION30chain 'D' and (resid 262 through 286 )D262 - 286
31X-RAY DIFFRACTION31chain 'D' and (resid 287 through 302 )D287 - 302
32X-RAY DIFFRACTION32chain 'D' and (resid 303 through 352 )D303 - 352
33X-RAY DIFFRACTION33chain 'D' and (resid 353 through 387 )D353 - 387

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