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- PDB-3hu2: Structure of p97 N-D1 R86A mutant in complex with ATPgS -

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Basic information

Entry
Database: PDB / ID: 3hu2
TitleStructure of p97 N-D1 R86A mutant in complex with ATPgS
ComponentsTransitional endoplasmic reticulum ATPase
KeywordsTRANSPORT PROTEIN / p97 / VCP
Function / homology
Function and homology information


positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of oxidative phosphorylation / VCP-NSFL1C complex / protein-DNA covalent cross-linking repair / endosome to lysosome transport via multivesicular body sorting pathway / endoplasmic reticulum stress-induced pre-emptive quality control / cellular response to arsenite ion / BAT3 complex binding / Derlin-1 retrotranslocation complex ...positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of oxidative phosphorylation / VCP-NSFL1C complex / protein-DNA covalent cross-linking repair / endosome to lysosome transport via multivesicular body sorting pathway / endoplasmic reticulum stress-induced pre-emptive quality control / cellular response to arsenite ion / BAT3 complex binding / Derlin-1 retrotranslocation complex / positive regulation of protein K63-linked deubiquitination / deubiquitinase activator activity / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / aggresome assembly / regulation of protein localization to chromatin / NADH metabolic process / vesicle-fusing ATPase / cellular response to misfolded protein / : / positive regulation of mitochondrial membrane potential / stress granule disassembly / ERAD pathway / K48-linked polyubiquitin modification-dependent protein binding / negative regulation of protein localization to chromatin / ubiquitin-modified protein reader activity / retrograde protein transport, ER to cytosol / regulation of aerobic respiration / ATPase complex / regulation of synapse organization / positive regulation of ATP biosynthetic process / ubiquitin-specific protease binding / ubiquitin-like protein ligase binding / autophagosome maturation / RHOH GTPase cycle / polyubiquitin modification-dependent protein binding / HSF1 activation / translesion synthesis / endoplasmic reticulum to Golgi vesicle-mediated transport / MHC class I protein binding / Protein methylation / interstrand cross-link repair / negative regulation of smoothened signaling pathway / Attachment and Entry / ATP metabolic process / : / endoplasmic reticulum unfolded protein response / proteasome complex / lipid droplet / viral genome replication / Josephin domain DUBs / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / ADP binding / proteasomal protein catabolic process / Hh mutants are degraded by ERAD / positive regulation of protein-containing complex assembly / Defective CFTR causes cystic fibrosis / Hedgehog ligand biogenesis / macroautophagy / Translesion Synthesis by POLH / ABC-family proteins mediated transport / establishment of protein localization / autophagy / Aggrephagy / cytoplasmic stress granule / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of canonical Wnt signaling pathway / positive regulation of protein catabolic process / activation of cysteine-type endopeptidase activity involved in apoptotic process / double-strand break repair / KEAP1-NFE2L2 pathway / azurophil granule lumen / Ovarian tumor domain proteases / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / E3 ubiquitin ligases ubiquitinate target proteins / site of double-strand break / cellular response to heat / Neddylation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein phosphatase binding / regulation of apoptotic process / secretory granule lumen / ficolin-1-rich granule lumen / Attachment and Entry / protein ubiquitination / protein domain specific binding / DNA repair / intracellular membrane-bounded organelle / lipid binding / glutamatergic synapse / DNA damage response / ubiquitin protein ligase binding / Neutrophil degranulation / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / protein-containing complex / RNA binding
Similarity search - Function
Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / Barwin-like endoglucanases - #20 / Helicase, Ruva Protein; domain 3 - #60 / AAA ATPase, CDC48 family / Barwin-like endoglucanases / Cell division protein 48 (CDC48), N-terminal domain / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 ...Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / Barwin-like endoglucanases - #20 / Helicase, Ruva Protein; domain 3 - #60 / AAA ATPase, CDC48 family / Barwin-like endoglucanases / Cell division protein 48 (CDC48), N-terminal domain / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Aspartate decarboxylase-like domain superfamily / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / Helicase, Ruva Protein; domain 3 / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Roll / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / Transitional endoplasmic reticulum ATPase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å
AuthorsTang, W.-K.
CitationJournal: Embo J. / Year: 2010
Title: A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants.
Authors: Tang, W.K. / Li, D. / Li, C.C. / Esser, L. / Dai, R. / Guo, L. / Xia, D.
History
DepositionJun 12, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 16, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Feb 15, 2012Group: Non-polymer description
Revision 1.3Feb 26, 2020Group: Data collection / Database references / Category: reflns / struct_ref_seq_dif
Item: _reflns.pdbx_Rmerge_I_obs / _struct_ref_seq_dif.details
Revision 1.4Feb 21, 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_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site
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_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.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 / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transitional endoplasmic reticulum ATPase
B: Transitional endoplasmic reticulum ATPase
C: Transitional endoplasmic reticulum ATPase
D: Transitional endoplasmic reticulum ATPase
E: Transitional endoplasmic reticulum ATPase
F: Transitional endoplasmic reticulum ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)330,25718
Polymers326,9716
Non-polymers3,28512
Water1,67593
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area31560 Å2
ΔGint-159 kcal/mol
Surface area116560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.892, 102.645, 107.182
Angle α, β, γ (deg.)97.52, 90.63, 91.45
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
12A
22B
32C
42D
52E
62F
13A
23B
33C
43D
53E
63F
14A
24B
34C
44D
54E
64F
15A
25B
35C
45D
55E
65F

NCS domain segments:

Refine code: 1

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111LEULEUVALVALAA12 - 16612 - 166
211LEULEUVALVALBB12 - 16612 - 166
311LEULEUVALVALCC12 - 16612 - 166
411LEULEUVALVALDD12 - 16612 - 166
511LEULEUVALVALEE12 - 16612 - 166
611LEULEUVALVALFF12 - 16612 - 166
121THRTHRILEILEAA168 - 189168 - 189
221THRTHRILEILEBB168 - 189168 - 189
321THRTHRILEILECC168 - 189168 - 189
421THRTHRILEILEDD168 - 189168 - 189
521THRTHRILEILEEE168 - 189168 - 189
621THRTHRILEILEFF168 - 189168 - 189
112LYSLYSVALVALAA190 - 201190 - 201
212LYSLYSVALVALBB190 - 201190 - 201
312LYSLYSVALVALCC190 - 201190 - 201
412LYSLYSVALVALDD190 - 201190 - 201
512LYSLYSVALVALEE190 - 201190 - 201
612LYSLYSVALVALFF190 - 201190 - 201
113GLYGLYILEILEAA202 - 371202 - 371
213GLYGLYILEILEBB202 - 371202 - 371
313GLYGLYILEILECC202 - 371202 - 371
413GLYGLYILEILEDD202 - 371202 - 371
513GLYGLYILEILEEE202 - 371202 - 371
613GLYGLYILEILEFF202 - 371202 - 371
114PROPROTHRTHRAA372 - 403372 - 403
214PROPROTHRTHRBB372 - 403372 - 403
314PROPROTHRTHRCC372 - 403372 - 403
414PROPROTHRTHRDD372 - 403372 - 403
514PROPROTHRTHREE372 - 403372 - 403
614PROPROTHRTHRFF372 - 403372 - 403
124GLYGLYSERSERAA405 - 462405 - 462
224GLYGLYSERSERBB405 - 462405 - 462
324GLYGLYSERSERCC405 - 462405 - 462
424GLYGLYSERSERDD405 - 462405 - 462
524GLYGLYSERSEREE405 - 462405 - 462
624GLYGLYSERSERFF405 - 462405 - 462
115AGSAGSMGMGAG - H800 - 801
215AGSAGSMGMGBI - J800 - 801
315AGSAGSMGMGCK - L800 - 801
415AGSAGSMGMGDM - N800 - 801
515AGSAGSMGMGEO - P800 - 801
615AGSAGSMGMGFQ - R800 - 801

NCS ensembles :
ID
1
2
3
4
5

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Components

#1: Protein
Transitional endoplasmic reticulum ATPase / TER ATPase / 15S Mg(2+)-ATPase p97 subunit / Valosin-containing protein / VCP


Mass: 54495.199 Da / Num. of mol.: 6 / Fragment: residues 1-481 / Mutation: R86G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: Human / Gene: P97, VCP / Plasmid: pQE60 / Production host: Escherichia coli (E. coli) / Strain (production host): M15 / References: UniProt: P55072
#2: Chemical
ChemComp-AGS / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-GAMMA-S / ADENOSINE 5'-(3-THIOTRIPHOSPHATE) / ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE) / ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE


Mass: 523.247 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H16N5O12P3S / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 93 / Source method: isolated from a natural source / Formula: H2O

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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: 3.03 Å3/Da / Density % sol: 59.41 %
Crystal growTemperature: 288 K / Method: vapor diffusion, hanging drop / pH: 5.8
Details: 100mM NaCl, 4% benzamidine, 100mM citrate, pH 5.8, 16.5% PEG3350 and 20% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 288K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.85→40 Å / Num. obs: 85163 / Rmerge(I) obs: 0.049 / Net I/σ(I): 13.8

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.85→40 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.902 / SU B: 41.334 / SU ML: 0.385 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.449 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.29027 4194 5 %RANDOM
Rwork0.25773 ---
obs0.25936 79168 93.01 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 70.682 Å2
Baniso -1Baniso -2Baniso -3
1-3.47 Å2-0.14 Å20.9 Å2
2---0.62 Å2-2.48 Å2
3----3.49 Å2
Refinement stepCycle: LAST / Resolution: 2.85→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21168 0 192 93 21453
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.02221690
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.521.99729358
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.07452706
X-RAY DIFFRACTIONr_dihedral_angle_2_deg40.29824.303990
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.527153972
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.89115192
X-RAY DIFFRACTIONr_chiral_restr0.1270.23360
X-RAY DIFFRACTIONr_gen_planes_refined0.0150.0216182
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1610.29474
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2640.214525
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1070.2599
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.2110.212
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2220.279
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3250.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4331.514042
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.65221906
X-RAY DIFFRACTIONr_scbond_it1.12438567
X-RAY DIFFRACTIONr_scangle_it1.6464.57452
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
11A1399tight positional0.080.05
12B1399tight positional0.10.05
13C1399tight positional0.090.05
14D1399tight positional0.070.05
15E1399tight positional0.080.05
16F1399tight positional0.070.05
21A102tight positional0.070.05
22B102tight positional0.070.05
23C102tight positional0.060.05
24D102tight positional0.050.05
25E102tight positional0.060.05
26F102tight positional0.050.05
31A1318tight positional0.080.05
32B1318tight positional0.080.05
33C1318tight positional0.080.05
34D1318tight positional0.080.05
35E1318tight positional0.080.05
36F1318tight positional0.080.05
41A685tight positional0.080.05
42B685tight positional0.080.05
43C685tight positional0.080.05
44D685tight positional0.070.05
45E685tight positional0.080.05
46F685tight positional0.090.05
51A32tight positional0.080.05
52B32tight positional0.050.05
53C32tight positional0.080.05
54D32tight positional0.050.05
55E32tight positional0.060.05
56F32tight positional0.060.05
11A1399tight thermal0.150.5
12B1399tight thermal0.190.5
13C1399tight thermal0.140.5
14D1399tight thermal0.120.5
15E1399tight thermal0.130.5
16F1399tight thermal0.130.5
21A102tight thermal0.110.5
22B102tight thermal0.150.5
23C102tight thermal0.090.5
24D102tight thermal0.090.5
25E102tight thermal0.110.5
26F102tight thermal0.10.5
31A1318tight thermal0.20.5
32B1318tight thermal0.20.5
33C1318tight thermal0.20.5
34D1318tight thermal0.190.5
35E1318tight thermal0.20.5
36F1318tight thermal0.210.5
41A685tight thermal0.190.5
42B685tight thermal0.170.5
43C685tight thermal0.160.5
44D685tight thermal0.150.5
45E685tight thermal0.170.5
46F685tight thermal0.190.5
51A32tight thermal0.240.5
52B32tight thermal0.230.5
53C32tight thermal0.280.5
54D32tight thermal0.330.5
55E32tight thermal0.360.5
56F32tight thermal0.250.5
LS refinement shellResolution: 2.85→2.924 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.392 267 -
Rwork0.347 4484 -
obs--71.64 %
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)
12.3962-0.96370.72996.5255-1.05917.82410.3508-0.43190.75110.7907-0.0471-0.0048-0.8546-0.6454-0.30370.13860.12540.256-0.06270.0560.2883-10.246281.34630.9905
27.8999-1.0197-0.550410.56611.447411.4952-0.00530.51780.2675-0.22490.0870.2586-0.69510.4597-0.0817-0.19260.07960.1591-0.10070.24590.1232-0.895682.986-19.3136
33.1607-7.662512.597518.5763-30.540250.2094-0.3443-0.9054-0.8342-0.22340.4316-0.42151.1316-2.581-0.08740.0821-0.20280.01330.11280.21260.6206-5.547364.7642-15.965
43.8250.5651-0.40584.2091.53454.12750.1280.03110.07450.2720.0001-0.2984-0.02530.3047-0.1281-0.25250.0459-0.0255-0.25610.0784-0.21448.412150.94483.0607
54.2106-0.3821.1534.42350.16112.1778-0.1091-0.04010.3602-0.39710.1470.3931-0.3519-1.104-0.038-0.44680.0524-0.00720.06670.03610.1655-22.813650.665-13.1368
64.5219-0.6216-3.1046.7922-1.067910.564-0.00640.77020.00040.4840.13591.0047-0.5305-1.6929-0.1296-0.35590.1098-0.11380.4190.05150.0819-22.15749.807-52.414
78.4848-1.3827-0.81659.48551.81611.06990.02290.2015-0.02-0.62420.1414-0.47130.2256-0.0112-0.1643-0.3752-0.088-0.0366-0.04310.1044-0.2474-2.54449.6926-63.1953
820.98234.2881-28.15060.8763-5.75337.7678-0.3677-0.3021-1.9398-0.35360.0656-0.04430.63830.61930.30210.3026-0.1940.03420.20840.18880.073-2.998935.2223-50.4037
94.42450.10620.16765.13710.66233.4581-0.0835-0.10780.17270.35750.1622-0.0243-0.1631-0.0609-0.0786-0.23930.04140.0273-0.26230.0946-0.2803-2.675440.8699-23.6824
105.1732-2.4122-3.326.38893.90318.3245-0.27960.9038-0.6085-0.2699-0.40580.72580.4998-0.60570.6854-0.2718-0.1676-0.11410.0993-0.00910.2306-13.598615.3582-45.291
119.3139-0.617-0.54163.9641.60096.853-0.05250.6232-0.4534-0.3180.16230.3681-0.3478-0.6218-0.10980.1528-0.04670.001-0.1212-0.05080.006813.6992-0.8073-68.324
128.7146-1.02681.34096.2466-2.47917.4293-0.03480.59120.0507-0.3108-0.0206-0.7372-0.28221.1290.05540.3651-0.2870.1829-0.0472-0.15650.171434.67696.9431-66.6921
1361.5612-10.9931-20.89691.96313.73167.09340.4763-1.8199-1.3759-0.3130.6166-0.6459-0.6074-0.7035-1.09290.59110.0256-0.14670.621-0.15780.551228.77271.0122-49.3516
143.3027-0.13150.44355.5814-0.44414.1117-0.13930.04140.1933-0.02930.08090.0395-0.2633-0.25120.0584-0.27090.06470.002-0.28010.0296-0.21499.879516.4375-37.3151
157.4313-3.25861.40175.8741.2354.5344-0.21110.2681-0.79990.17120.2660.03820.56110.5122-0.05490.0424-0.05750.0579-0.1833-0.01560.003322.3028-16.4433-36.269
168.67451.0723-0.10317.80463.30238.37740.19770.8492-1.258-0.2034-0.3266-0.34890.5962-0.35880.1289-0.04720.1725-0.00440.06980.00210.344960.5329-21.2114-29.0058
178.312-1.51811.65266.94973.230713.16710.04190.4080.6644-0.43170.1861-1.5156-1.93311.0001-0.22790.4425-0.05040.21250.13740.31240.665773.7991-3.3564-26.1325
1824.28791.24630.06370.0640.00330.00021.9328-0.95980.4121.0375-1.2714-0.5258-0.6531-0.1909-0.66140.3783-0.1974-0.03430.66820.23420.421758.683-2.2834-14.031
192.54690.3415-0.15443.4162-0.00075.05980.02060.4448-0.0761-0.06-0.07330.065-0.0371-0.02130.0528-0.25850.1011-0.052-0.15610.009-0.142733.41751.8838-23.9337
209.0090.45553.0833.6691.40177.66750.0959-0.6636-0.17540.15590.0791-0.19120.67960.5082-0.1750.05740.1320.0097-0.16210.1598-0.007749.2276-12.22714.0568
217.5286-0.21443.65758.07580.28162.73620.19610.4553-0.91051.1510.0806-0.94840.77590.4222-0.27660.130.0054-0.21810.2862-0.07680.309172.409510.964225.8271
228.2768-1.5859-1.066714.60743.58068.29750.0970.35550.2298-1.00590.3292-0.9208-1.1340.8376-0.42620.0138-0.2631-0.13960.50550.10690.019175.591632.409620.2041
2320.704921.07556.980121.45287.1052.3531-0.51670.23080.75221.57841.0682.2946-2.4714-0.5496-0.55130.6017-0.33020.00610.57960.26440.318656.77128.91821.1929
243.5738-0.5871-1.32683.6740.23624.42050.18130.4531-0.223-0.2925-0.145-0.07920.00410.2251-0.0363-0.37490.0155-0.06-0.18690.0196-0.170644.658812.04822.8313
254.6499-1.1931-0.550711.00691.43764.8682-0.0916-0.65440.57190.8253-0.0691-0.16110.00280.18740.1607-0.15180.014-0.1319-0.04590.0241-0.147340.179323.712835.8067
264.0424-0.63822.67848.9255-2.20056.68150.1399-0.3874-0.09781.02450.2559-0.7785-0.53820.2598-0.39580.1021-0.0487-0.00860.034-0.21990.163236.774562.528540.9934
2713.0223-4.71034.06867.7723-2.138610.94530.11970.44081.1365-0.7076-0.0435-1.2921-1.21320.3435-0.07620.5531-0.32980.4810.0252-0.10520.501338.036176.352423.395
280.92377.3945-4.293559.1956-34.371519.9576-0.32571.6172-0.988-1.74571.0540.5384-0.3149-1.4521-0.72830.7502-0.11960.18770.2384-0.20690.4524.580462.806319.9039
294.61960.0801-0.20313.69620.05234.25650.19470.1947-0.0946-0.0996-0.0668-0.51390.04620.3047-0.1278-0.36520.0187-0.0189-0.29440.0123-0.126832.123636.679716.3968
305.5176-3.2576-0.06036.5538-0.80463.1754-0.022-0.04010.36050.01620.10760.2797-0.634-0.2091-0.0856-0.1072-0.0470.033-0.1605-0.0375-0.14974.332555.293527.0031
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A16 - 107
2X-RAY DIFFRACTION2A108 - 189
3X-RAY DIFFRACTION3A190 - 201
4X-RAY DIFFRACTION4A202 - 371
5X-RAY DIFFRACTION5A372 - 460
6X-RAY DIFFRACTION6B16 - 107
7X-RAY DIFFRACTION7B108 - 189
8X-RAY DIFFRACTION8B190 - 201
9X-RAY DIFFRACTION9B202 - 371
10X-RAY DIFFRACTION10B372 - 460
11X-RAY DIFFRACTION11C16 - 107
12X-RAY DIFFRACTION12C108 - 189
13X-RAY DIFFRACTION13C190 - 201
14X-RAY DIFFRACTION14C202 - 371
15X-RAY DIFFRACTION15C372 - 460
16X-RAY DIFFRACTION16D16 - 107
17X-RAY DIFFRACTION17D108 - 189
18X-RAY DIFFRACTION18D190 - 201
19X-RAY DIFFRACTION19D202 - 371
20X-RAY DIFFRACTION20D372 - 460
21X-RAY DIFFRACTION21E16 - 107
22X-RAY DIFFRACTION22E108 - 189
23X-RAY DIFFRACTION23E190 - 201
24X-RAY DIFFRACTION24E202 - 371
25X-RAY DIFFRACTION25E372 - 460
26X-RAY DIFFRACTION26F16 - 107
27X-RAY DIFFRACTION27F108 - 189
28X-RAY DIFFRACTION28F190 - 201
29X-RAY DIFFRACTION29F202 - 371
30X-RAY DIFFRACTION30F372 - 460

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