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- PDB-5c1a: p97-N750D/R753D/M757D/Q760D in complex with ATP-gamma-S -

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Basic information

Entry
Database: PDB / ID: 5c1a
Titlep97-N750D/R753D/M757D/Q760D in complex with ATP-gamma-S
ComponentsTransitional endoplasmic reticulum ATPase
KeywordsHYDROLASE / AAA ATPase / ERAD / VCP / CDC48
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
Vps4 C terminal oligomerisation domain / AAA ATPase, CDC48 family / 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 ...Vps4 C terminal oligomerisation domain / AAA ATPase, CDC48 family / 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. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
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 / molecular replacement / Resolution: 3.8 Å
AuthorsHaenzelmann, P. / Schindelin, H.
CitationJournal: Structure / Year: 2016
Title: Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
Authors: Hanzelmann, P. / Schindelin, H.
History
DepositionJun 13, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Jan 13, 2016Provider: repository / Type: Initial release
Revision 1.1Jan 20, 2016Group: Database references
Revision 1.2Jan 10, 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 / diffrn_radiation_wavelength / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
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_seq_id / _struct_conn.ptnr2_label_asym_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

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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
G: Transitional endoplasmic reticulum ATPase
H: Transitional endoplasmic reticulum ATPase
I: Transitional endoplasmic reticulum ATPase
J: Transitional endoplasmic reticulum ATPase
K: Transitional endoplasmic reticulum ATPase
L: Transitional endoplasmic reticulum ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,083,96560
Polymers1,070,82412
Non-polymers13,14148
Water0
1
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)541,98330
Polymers535,4126
Non-polymers6,57124
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area56850 Å2
ΔGint-285 kcal/mol
Surface area176690 Å2
MethodPISA
2
G: Transitional endoplasmic reticulum ATPase
H: Transitional endoplasmic reticulum ATPase
I: Transitional endoplasmic reticulum ATPase
J: Transitional endoplasmic reticulum ATPase
K: Transitional endoplasmic reticulum ATPase
L: Transitional endoplasmic reticulum ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)541,98330
Polymers535,4126
Non-polymers6,57124
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area56430 Å2
ΔGint-291 kcal/mol
Surface area175470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)182.669, 145.470, 251.397
Angle α, β, γ (deg.)90.000, 109.770, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B
31chain C
41chain D
51chain E
61chain F
71chain G
81chain H
91chain I
101chain J
111chain K
121chain L

NCS domain segments:

Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ASN / Beg label comp-ID: ASN / End auth comp-ID: MG / End label comp-ID: MG / Auth seq-ID: 21 - 904 / Label seq-ID: 20

Dom-IDSelection detailsAuth asym-IDLabel asym-ID
1chain AAA - P
2chain BBB - T
3chain CCC - X
4chain DDD - BA
5chain EEE - FA
6chain FFF - JA
7chain GGG - NA
8chain HHH - RA
9chain III - VA
10chain JJJ - ZA
11chain KKK - DB
12chain LLL - HB

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Components

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


Mass: 89235.352 Da / Num. of mol.: 12 / Mutation: N750D, R753D, M757D, Q760D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VCP / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P55072, vesicle-fusing ATPase
#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.: 24 / 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.: 24 / Source method: obtained synthetically / Formula: Mg

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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: 2.94 Å3/Da / Density % sol: 58.1 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: 9-9.5% PEG 4000, 0.4-0.5 M magnesium acetate, 0.1 M sodium-citrate pH 5.6

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 7, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 3.8→49.05 Å / Num. obs: 120767 / % possible obs: 98.9 % / Redundancy: 5.8 % / Biso Wilson estimate: 146.75 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.14 / Rpim(I) all: 0.062 / Net I/σ(I): 8 / Num. measured all: 702900
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) all% possible all
3.8-3.8661.8711.13585059700.5010.80899.2
20.81-49.055.40.05929.138517180.9930.02890.5

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
Aimless0.1.27data scaling
MxCuBEdata collection
PHENIXrefinement
PDB_EXTRACT3.15data extraction
PHASERphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3CF3

3cf3


Resolution: 3.8→49.047 Å / SU ML: 0.57 / Cross valid method: NONE / σ(F): 1.34 / Phase error: 29.45 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2536 6032 5 %
Rwork0.1903 114583 -
obs0.1935 120615 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 525.88 Å2 / Biso mean: 199.2002 Å2 / Biso min: 88.03 Å2
Refinement stepCycle: final / Resolution: 3.8→49.047 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms69306 0 1080 0 70386
Biso mean--139.46 --
Num. residues----8829
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00571213
X-RAY DIFFRACTIONf_angle_d1.00496323
X-RAY DIFFRACTIONf_chiral_restr0.03810796
X-RAY DIFFRACTIONf_plane_restr0.00512659
X-RAY DIFFRACTIONf_dihedral_angle_d17.16227696
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A53541X-RAY DIFFRACTION14.46TORSIONAL
12B53541X-RAY DIFFRACTION14.46TORSIONAL
13C53541X-RAY DIFFRACTION14.46TORSIONAL
14D53541X-RAY DIFFRACTION14.46TORSIONAL
15E53541X-RAY DIFFRACTION14.46TORSIONAL
16F53541X-RAY DIFFRACTION14.46TORSIONAL
17G53541X-RAY DIFFRACTION14.46TORSIONAL
18H53541X-RAY DIFFRACTION14.46TORSIONAL
19I53541X-RAY DIFFRACTION14.46TORSIONAL
110J53541X-RAY DIFFRACTION14.46TORSIONAL
111K53541X-RAY DIFFRACTION14.46TORSIONAL
112L53541X-RAY DIFFRACTION14.46TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.8-3.84320.39251940.33243810400499
3.8432-3.88840.38311960.3313828402499
3.8884-3.93580.36632110.31443813402499
3.9358-3.98560.37541900.29273773396399
3.9856-4.0380.36682000.28763851405199
4.038-4.09330.31322240.27273767399199
4.0933-4.15170.27931990.26543841404099
4.1517-4.21370.29171800.24083762394299
4.2137-4.27950.30382090.24413784399398
4.2795-4.34960.31711840.22513684386895
4.3496-4.42450.27811940.21193833402799
4.4245-4.50490.26992210.2063799402099
4.5049-4.59150.26831960.19893855405199
4.5915-4.68520.25682150.19133828404399
4.6852-4.7870.24851890.183800398999
4.787-4.89820.2591850.19373843402899
4.8982-5.02060.25712060.18893840404699
5.0206-5.15620.2622140.18093796401099
5.1562-5.30770.26132190.19353764398398
5.3077-5.47890.27671870.20033766395397
5.4789-5.67440.29982030.20883848405199
5.6744-5.90120.28462080.19353838404699
5.9012-6.16930.28361900.19743867405799
6.1693-6.49390.30572270.21113829405699
6.4939-6.89970.27171960.18833873406999
6.8997-7.43080.22132170.16343751396897
7.4308-8.17550.211940.15523886408099
8.1755-9.35140.18191840.13233900408499
9.3514-11.75490.14861840.12163843402797
11.7549-49.05120.25522160.18843911412797
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)
10.9559-0.68761.00412.9076-0.44383.46750.0809-0.03710.41760.0553-0.1733-0.3907-0.50630.49930.1311.478-0.2637-0.00171.5290.10941.9548207.371342.508672.4768
21.3747-0.69431.80654.4629-0.93654.4766-0.1067-0.0120.37460.3795-0.0827-0.2435-0.28020.09710.21020.9238-0.03080.02951.2092-0.03341.3016195.465516.505872.8478
32.4104-1.2820.4481.6925-0.26731.9164-0.2437-0.15790.31590.32730.11340.1902-0.3864-0.1780.07121.44810.12490.20371.655-0.2531.8189160.573121.668486.8482
41.9802-1.08890.9144.1008-0.12843.4446-0.28080.44080.3447-0.99460.30640.03210.21840.4919-0.06671.53530.1030.26082.2440.29881.2471181.573118.738519.9879
53.0021.66352.03384.05090.21375.2184-0.18310.3640.2094-0.17490.01160.1098-0.05180.00380.12961.020.10940.02341.3462-0.0651.1252181.36162.982543.991
63.09881.3177-0.52573.26011.47992.2639-0.15460.37090.7276-0.2420.0020.6139-0.1539-0.46070.11340.83190.0576-0.03181.4112-0.01791.578146.3677.756258.7944
72.63880.07470.25245.02470.47782.11730.02051.043-0.3448-0.7786-0.2270.09080.2299-0.40770.12621.72880.0521-0.13971.9558-0.53191.4431168.4685-42.925116.8937
82.90842.27680.82764.90810.49432.97650.08780.0146-0.3104-0.0027-0.14090.35440.1552-0.29130.11281.0108-0.0203-0.04881.6091-0.30471.3122173.9878-31.181542.4374
90.9673-0.34620.05763.5528-0.22171.60320.18310.0975-0.44420.28070.05610.82140.3344-0.0822-0.21921.031-0.12890.10051.7625-0.25061.995140.7415-26.200557.1387
101.7017-1.55650.12842.4417-2.01152.1199-0.03040.1299-0.2411-0.338-0.31670.03180.5866-0.58850.2312.3565-0.16370.00721.6796-0.36961.9501181.2494-80.769165.0992
111.19020.06280.70762.8623-1.15314.95610.03680.157-0.219-0.18560.20690.56830.3978-0.2519-0.17971.2651-0.11380.07291.4443-0.32911.4571181.9841-52.398469.4498
121.8912-0.31710.55841.2404-0.74252.94740.0291-0.3826-0.5230.30010.23870.23470.4864-0.4736-0.31021.3539-0.22910.36411.54930.07481.9877148.5473-45.944684.2952
135.42080.71120.95873.17980.90995.0864-0.23860.0777-0.05820.225-0.0723-0.07050.38720.03920.32341.55380.1101-0.05951.17980.13711.2803209.6979-57.0886116.177
140.9292-0.34011.16143.19090.06795.7985-0.0779-0.1947-0.0092-0.00340.18020.14220.1977-0.2245-0.08351.03560.01190.10441.3330.01261.3416197.2693-39.052697.7213
151.4008-0.4382-0.31241.53270.97341.2205-0.0346-0.4991-0.02280.6842-0.02940.26930.3448-0.04550.08731.723-0.15310.41711.97120.0811.5335162.3322-31.9948112.3954
163.47560.96260.42894.2575-0.92054.3027-0.31860.10690.1086-0.04380.03530.0654-0.153-0.1750.32191.5512-0.0068-0.21541.2886-0.24621.3088220.65174.8417120.7649
172.00270.24750.38485.51590.08732.04780.03410.05090.2795-0.0194-0.03420.0959-0.1541-0.0325-0.00321.21860.015-0.00641.2163-0.07681.0581203.2404-4.61999.9633
181.1975-0.34870.28783.1446-1.27140.5651-0.1297-0.23560.18410.87060.11690.4416-0.52040.10280.04951.82810.05350.44491.8296-0.22981.4946168.72731.8363113.7587
192.5483-0.02140.44052.31632.10051.75970.2326-0.3489-0.14960.38350.1808-0.12880.7774-0.5048-0.39981.5921-0.31080.00481.55950.47671.6403230.4749-70.409779.685
202.05920.02431.68692.9160.0833.67460.1823-0.0438-0.12340.2596-0.0147-0.1279-0.00330.0675-0.19331.2183-0.06610.30011.21860.02541.3122232.8868-47.453262.7128
211.98810.54850.50872.55771.1342.69030.21750.4481-0.40960.03340.1482-0.25350.91860.4129-0.35431.50330.2520.20691.4939-0.08561.5191266.4871-52.678347.225
222.33040.19830.31341.150.37324.31350.0135-0.0702-0.12220.0134-0.34260.94640.18510.07680.26181.9307-0.114-0.2951.4166-0.00262.0937203.9059-70.271922.6065
231.00430.60711.85083.0740.3593.92490.29040.3543-0.3975-0.23460.04260.31920.17920.1188-0.22131.14270.03730.15741.4824-0.10991.4337218.601-47.224931.0903
241.85830.17780.95210.4461-1.15163.1650.07910.3929-0.0396-0.29250.0314-0.30560.44290.5157-0.14361.46230.25580.4281.7468-0.32761.3175252.8129-52.4515.8047
252.6417-0.7472-0.59564.1311-0.43450.95-0.17860.71860.3916-0.60870.23290.4855-0.4493-0.3868-0.02381.7710.0839-0.37122.1196-0.01541.6648199.5983-17.0144-10.8526
263.05760.61141.53473.2562-0.19833.23260.17650.47160.03-0.0175-0.23840.267-0.1420.12350.12511.30850.02070.07741.3966-0.10591.2844216.3413-17.696312.5571
271.42320.27390.04653.0662-0.48341.2803-0.50420.5523-0.0785-0.50660.3328-0.3153-0.20560.17670.20471.5125-0.05170.33252.0823-0.12961.183250.5447-22.5685-1.3911
281.98170.34630.88712.39731.68952.0508-0.12710.38410.1686-0.1186-0.24420.3419-0.63640.19990.45112.11840.191-0.42171.42740.13482.1068218.351836.875115.1799
291.83531.60131.2255.34580.97361.497-0.1075-0.03340.4322-0.1906-0.26180.3986-0.32110.13060.39351.30420.0661-0.03671.38080.04671.485226.880712.494127.2834
302.37761.45281.13553.08430.96032.4218-0.31990.76070.3671-0.51850.21640.0206-0.3720.60820.10641.0711-0.25120.27821.88550.37131.0509261.3087.188613.6848
312.3119-0.2270.35140.7445-0.58542.32990.13110.26720.52790.448-0.39810.3552-0.4186-0.46710.33152.19620.0802-0.0561.5825-0.36731.7547243.194137.497973.3642
323.5434-0.33391.9613.7622-0.18492.96480.0518-0.13670.19510.1554-0.37490.0198-0.1930.12750.22421.27420.0130.24041.4473-0.04121.2287240.426212.601159.3811
333.3025-0.19750.33812.7183-0.99114.66430.00180.32160.68530.0865-0.1697-0.5291-0.18060.61020.11080.7171-0.03280.21581.27010.12021.2704275.1936.536646.3819
342.0786-0.54110.90093.2995-1.10190.219-0.1845-0.48860.06260.31590.3787-0.2160.3499-0.1434-0.26692.1796-0.15040.22481.7167-0.08631.2227250.9732-16.709104.7441
352.6224-0.91872.48015.0421-0.29413.46640.0798-0.11310.02660.2943-0.2857-0.1179-0.09740.1560.10141.2105-0.23760.35291.3357-0.00131.1001244.2688-17.501476.9455
362.3219-0.15790.40394.444-0.31481.15780.2865-0.3131-0.26360.2897-0.1818-0.98580.3068-0.0004-0.08691.001-0.01370.08461.42350.19861.3677277.4102-23.456261.8767
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 21 through 200 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 201 through 460 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 461 through 770 )A0
4X-RAY DIFFRACTION4chain 'B' and (resid 21 through 200 )B0
5X-RAY DIFFRACTION5chain 'B' and (resid 201 through 460 )B0
6X-RAY DIFFRACTION6chain 'B' and (resid 461 through 770 )B0
7X-RAY DIFFRACTION7chain 'C' and (resid 21 through 200 )C0
8X-RAY DIFFRACTION8chain 'C' and (resid 201 through 460 )C0
9X-RAY DIFFRACTION9chain 'C' and (resid 461 through 770 )C0
10X-RAY DIFFRACTION10chain 'D' and (resid 21 through 200 )D0
11X-RAY DIFFRACTION11chain 'D' and (resid 201 through 460 )D0
12X-RAY DIFFRACTION12chain 'D' and (resid 461 through 770 )D0
13X-RAY DIFFRACTION13chain 'E' and (resid 21 through 200 )E0
14X-RAY DIFFRACTION14chain 'E' and (resid 201 through 460 )E0
15X-RAY DIFFRACTION15chain 'E' and (resid 461 through 770 )E0
16X-RAY DIFFRACTION16chain 'F' and (resid 21 through 200 )F0
17X-RAY DIFFRACTION17chain 'F' and (resid 201 through 460 )F0
18X-RAY DIFFRACTION18chain 'F' and (resid 461 through 770 )F0
19X-RAY DIFFRACTION19chain 'G' and (resid 21 through 200 )G0
20X-RAY DIFFRACTION20chain 'G' and (resid 201 through 460 )G0
21X-RAY DIFFRACTION21chain 'G' and (resid 461 through 770 )G0
22X-RAY DIFFRACTION22chain 'H' and (resid 21 through 200 )H0
23X-RAY DIFFRACTION23chain 'H' and (resid 201 through 460 )H0
24X-RAY DIFFRACTION24chain 'H' and (resid 461 through 770 )H0
25X-RAY DIFFRACTION25chain 'I' and (resid 21 through 200 )I0
26X-RAY DIFFRACTION26chain 'I' and (resid 201 through 460 )I0
27X-RAY DIFFRACTION27chain 'I' and (resid 461 through 770 )I0
28X-RAY DIFFRACTION28chain 'J' and (resid 21 through 200 )J0
29X-RAY DIFFRACTION29chain 'J' and (resid 201 through 460 )J0
30X-RAY DIFFRACTION30chain 'J' and (resid 461 through 770 )J0
31X-RAY DIFFRACTION31chain 'K' and (resid 21 through 200 )K0
32X-RAY DIFFRACTION32chain 'K' and (resid 201 through 460 )K0
33X-RAY DIFFRACTION33chain 'K' and (resid 461 through 770 )K0
34X-RAY DIFFRACTION34chain 'L' and (resid 21 through 200 )L0
35X-RAY DIFFRACTION35chain 'L' and (resid 201 through 460 )L0
36X-RAY DIFFRACTION36chain 'L' and (resid 461 through 770 )L0

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