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- PDB-4d0t: GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese -

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Basic information

Entry
Database: PDB / ID: 4d0t
TitleGalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese
Components
  • PEPTIDE
  • POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
KeywordsTRANSFERASE / RETAINING GALNAC-T2 / SUBSTRATE-GUIDED SNI-TYPE REACTION / QM/MM METADYNAMICS / BI-BI KINETIC MECHANISM / SUBSTRATE SPECIFICITY / PROTEIN X-RAY CRYSTALLOGRAPHY / ACETAMIDO GROUP
Function / homology
Function and homology information


protein O-linked glycosylation via threonine / polypeptide N-acetylgalactosaminyltransferase / polypeptide N-acetylgalactosaminyltransferase activity / protein O-linked glycosylation via serine / O-glycan processing / O-linked glycosylation of mucins / Golgi stack / COPI-independent Golgi-to-ER retrograde traffic / protein O-linked glycosylation / Golgi cisterna membrane ...protein O-linked glycosylation via threonine / polypeptide N-acetylgalactosaminyltransferase / polypeptide N-acetylgalactosaminyltransferase activity / protein O-linked glycosylation via serine / O-glycan processing / O-linked glycosylation of mucins / Golgi stack / COPI-independent Golgi-to-ER retrograde traffic / protein O-linked glycosylation / Golgi cisterna membrane / protein maturation / manganese ion binding / carbohydrate binding / Golgi membrane / endoplasmic reticulum membrane / perinuclear region of cytoplasm / Golgi apparatus / extracellular region / membrane
Similarity search - Function
N-acetylgalactosaminyltransferase / Glycosyltransferase 2-like / Glycosyl transferase family 2 / Ricin-type beta-trefoil lectin domain / Ricin-type beta-trefoil / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A ...N-acetylgalactosaminyltransferase / Glycosyltransferase 2-like / Glycosyl transferase family 2 / Ricin-type beta-trefoil lectin domain / Ricin-type beta-trefoil / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Nucleotide-diphospho-sugar transferases / Alpha-Beta Complex / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
: / 2-acetamido-2-deoxy-beta-D-galactopyranose / URIDINE-DIPHOSPHATE-N-ACETYLGALACTOSAMINE / URIDINE-5'-DIPHOSPHATE / Polypeptide N-acetylgalactosaminyltransferase 2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
SYNTHETIC CONSTRUCT (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 Å
AuthorsLira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. ...Lira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. / Rovira, C. / Hurtado-Guerrero, R.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Substrate-Guided Front-Face Reaction Revealed by Combined Structural Snapshots and Metadynamics for the Polypeptide N-Acetylgalactosaminyltransferase 2.
Authors: Lira-Navarrete, E. / Iglesias-Fernandez, J. / Zandberg, W.F. / Companon, I. / Kong, Y. / Corzana, F. / Pinto, B.M. / Clausen, H. / Peregrina, J.M. / Vocadlo, D. / Rovira, C. / Hurtado-Guerrero, R.
History
DepositionApr 30, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 28, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 2, 2014Group: Database references
Revision 1.2Aug 13, 2014Group: Database references
Revision 1.3Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _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.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.pdbx_role / _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_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _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: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
B: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
C: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
D: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
E: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
F: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
P: PEPTIDE
Z: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)395,13831
Polymers390,5268
Non-polymers4,61223
Water8,449469
1
C: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
F: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
P: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,90510
Polymers130,4383
Non-polymers1,4677
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7590 Å2
ΔGint-29.1 kcal/mol
Surface area39420 Å2
MethodPISA
2
B: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
E: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
Z: PEPTIDE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,01111
Polymers130,4383
Non-polymers1,5738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6850 Å2
ΔGint-20.4 kcal/mol
Surface area39450 Å2
MethodPISA
3
A: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
D: POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,22210
Polymers129,6492
Non-polymers1,5738
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6030 Å2
ΔGint-15.5 kcal/mol
Surface area39960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)117.217, 122.372, 249.724
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
11E
21A
12E
22B
13E
23C
14E
24D
15E
25F
16A
26B
17A
27C
18A
28D
19A
29F
110B
210C
111B
211D
112B
212F
113C
213D
114C
214F
115D
215F

NCS domain segments:

Component-ID: 0 / Beg auth comp-ID: LYS / Beg label comp-ID: LYS / Refine code: 0

Dom-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNEE75 - 56875 - 568
21ASNASNAA75 - 56875 - 568
12LEULEUEE75 - 56975 - 569
22LEULEUBB75 - 56975 - 569
13LEULEUEE75 - 56975 - 569
23LEULEUCC75 - 56975 - 569
14LEULEUEE75 - 56975 - 569
24LEULEUDD75 - 56975 - 569
15PHEPHEEE75 - 56575 - 565
25PHEPHEFF75 - 56575 - 565
16ASNASNAA75 - 56875 - 568
26ASNASNBB75 - 56875 - 568
17ASNASNAA75 - 56875 - 568
27ASNASNCC75 - 56875 - 568
18ASNASNAA75 - 56875 - 568
28ASNASNDD75 - 56875 - 568
19LYSLYSAA75 - 56475 - 564
29LYSLYSFF75 - 56475 - 564
110LEULEUBB75 - 56975 - 569
210LEULEUCC75 - 56975 - 569
111LEULEUBB75 - 56975 - 569
211LEULEUDD75 - 56975 - 569
112PHEPHEBB75 - 56575 - 565
212PHEPHEFF75 - 56575 - 565
113LEULEUCC75 - 56975 - 569
213LEULEUDD75 - 56975 - 569
114PHEPHECC75 - 56575 - 565
214PHEPHEFF75 - 56575 - 565
115PHEPHEDD75 - 56575 - 565
215PHEPHEFF75 - 56575 - 565

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15

NCS oper: (Code: given
Matrix: (-0.07105, -0.02351, 0.9972), (-0.01881, -0.9995, -0.0249), (0.9973, -0.02052, 0.07057)
Vector: 67.3978, -42.3377, -63.8038)

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Components

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Protein / Protein/peptide / Sugars , 3 types, 9 molecules ABCDEFPZ

#1: Protein
POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2 / / POLYPEPTIDE GALNAC TRANSFERASE 2 / GALNAC-T2 / PP-GANTASE 2 / PROTEIN-UDP ...POLYPEPTIDE GALNAC TRANSFERASE 2 / GALNAC-T2 / PP-GANTASE 2 / PROTEIN-UDP ACETYLGALACTOSAMINYLTRANSFERASE 2 / UDP-GALNAC / POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2 / POLYPEPTIDE GALNAC-TRANSFERASE T2


Mass: 64824.703 Da / Num. of mol.: 6 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: KOMAGATAELLA PASTORIS (fungus) / Strain (production host): SMD-1168
References: UniProt: Q10471, polypeptide N-acetylgalactosaminyltransferase
#2: Protein/peptide PEPTIDE /


Mass: 788.800 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) SYNTHETIC CONSTRUCT (others)
#7: Sugar ChemComp-NGA / 2-acetamido-2-deoxy-beta-D-galactopyranose / N-acetyl-beta-D-galactosamine / 2-acetamido-2-deoxy-beta-D-galactose / 2-acetamido-2-deoxy-D-galactose / 2-acetamido-2-deoxy-galactose / N-ACETYL-D-GALACTOSAMINE / N-Acetylgalactosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGalpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-galactopyranosamineCOMMON NAMEGMML 1.0
b-D-GalpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GalNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 5 types, 491 molecules

#3: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-UD2 / URIDINE-DIPHOSPHATE-N-ACETYLGALACTOSAMINE / (2R,3R,4R,5R,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate


Mass: 607.354 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C17H27N3O17P2
#6: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE / Uridine diphosphate


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Comment: UDP*YM
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 469 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 46.36 % / Description: NONE

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.92
DetectorDate: Oct 5, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 2.45→80 Å / Num. obs: 131982 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 5.7 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.3
Reflection shellResolution: 2.45→2.58 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.8 / Mean I/σ(I) obs: 2.3 / % possible all: 99.9

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
XDSdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2FFV

2ffv


Resolution: 2.45→249.72 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.921 / SU B: 20.017 / SU ML: 0.219 / Cross valid method: THROUGHOUT / ESU R: 0.475 / ESU R Free: 0.261 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.24116 3670 2.8 %RANDOM
Rwork0.21351 ---
obs0.21429 128239 99.68 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 45.822 Å2
Baniso -1Baniso -2Baniso -3
1-0.5 Å20 Å20 Å2
2--0.36 Å20 Å2
3----0.86 Å2
Refinement stepCycle: LAST / Resolution: 2.45→249.72 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23723 0 280 469 24472
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01924587
X-RAY DIFFRACTIONr_bond_other_d0.0070.0223116
X-RAY DIFFRACTIONr_angle_refined_deg1.7141.95633316
X-RAY DIFFRACTIONr_angle_other_deg1.338353023
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.68552974
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.85123.2891204
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.492154144
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.1615230
X-RAY DIFFRACTIONr_chiral_restr0.1010.23532
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.02127869
X-RAY DIFFRACTIONr_gen_planes_other0.0070.025943
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
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_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.0072.49611899
X-RAY DIFFRACTIONr_mcbond_other1.9962.49611898
X-RAY DIFFRACTIONr_mcangle_it3.2533.73714860
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.3782.75512688
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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 / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11E306910.06
12A306910.06
21E305440.07
22B305440.07
31E305030.07
32C305030.07
41E306450.08
42D306450.08
51E301230.07
52F301230.07
61A302820.07
62B302820.07
71A302870.07
72C302870.07
81A305440.08
82D305440.08
91A299200.07
92F299200.07
101B304900.07
102C304900.07
111B303760.08
112D303760.08
121B299370.08
122F299370.08
131C303910.09
132D303910.09
141C297850.08
142F297850.08
151D301070.08
152F301070.08
LS refinement shellResolution: 2.45→2.514 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.363 320 -
Rwork0.324 9342 -
obs--99.92 %
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)
10.18250.20890.06120.56650.37660.3908-0.0254-0.0065-0.0409-0.034-0.01280.0878-0.08830.04530.03830.2542-0.02670.01770.17390.01490.169710.157-39.8311-37.9862
20.2803-0.22830.02290.4798-0.08250.13090.0353-0.0862-0.0112-0.108-0.0323-0.0321-0.0389-0.0241-0.0030.214-0.03640.03520.15480.03450.207229.7797-1.7587-55.3302
30.2747-0.2264-0.5220.3890.44071.0473-0.0564-0.01570.01620.11740.09380.00420.05740.1239-0.03740.21280.0395-0.00050.24870.00390.132822.0287-32.30791.1086
40.29350.1265-0.30780.5784-0.90891.5286-0.10910.0183-0.14250.05980.08660.0156-0.1369-0.13110.02250.2188-0.00540.06040.08350.05130.2607-15.28328.9294-19.3163
51.3686-0.6566-0.2150.37460.25880.46180.2422-0.160.2522-0.11090.0346-0.22220.0666-0.0729-0.27680.3591-0.06230.1610.04140.01780.272467.9849-9.7666-42.9636
60.1139-0.22180.25240.4454-0.48891.1037-0.07-0.02540.04860.13350.0139-0.1127-0.32170.0690.05610.3077-0.08-0.00340.1493-0.01830.2194-4.120921.782419.7883
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1E75 - 600
2X-RAY DIFFRACTION2A75 - 600
3X-RAY DIFFRACTION3B75 - 600
4X-RAY DIFFRACTION4C75 - 601
5X-RAY DIFFRACTION5D75 - 600
6X-RAY DIFFRACTION6F75 - 600

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Jul 12, 2017. Major update of PDB

Major update of PDB

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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