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- PDB-7mnz: Crystal Structure of Nup358/RanBP2 Ran-binding domain 4 in comple... -

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Basic information

Entry
Database: PDB / ID: 7mnz
TitleCrystal Structure of Nup358/RanBP2 Ran-binding domain 4 in complex with Ran-GPPNHP
Components
  • E3 SUMO-protein ligase RanBP2
  • GTP-binding nuclear protein Ran
KeywordsTRANSPORT PROTEIN / nuclear pore complex component / nucleocytoplasmic transport / complex (small GTPase-nuclear protein)
Function / homology
Function and homology information


cytoplasmic periphery of the nuclear pore complex / SUMO ligase activity / SUMO ligase complex / annulate lamellae / nuclear pore cytoplasmic filaments / RNA nuclear export complex / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / Nuclear Pore Complex (NPC) Disassembly ...cytoplasmic periphery of the nuclear pore complex / SUMO ligase activity / SUMO ligase complex / annulate lamellae / nuclear pore cytoplasmic filaments / RNA nuclear export complex / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / Nuclear Pore Complex (NPC) Disassembly / manchette / nuclear inclusion body / nuclear pore nuclear basket / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Transport of the SLBP independent Mature mRNA / importin-alpha family protein binding / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / Transferases; Acyltransferases; Aminoacyltransferases / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / nuclear export / Nuclear import of Rev protein / Transport of Mature mRNA derived from an Intron-Containing Transcript / GTP metabolic process / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / SUMO transferase activity / Postmitotic nuclear pore complex (NPC) reformation / MicroRNA (miRNA) biogenesis / nucleocytoplasmic transport / centrosome localization / Viral Messenger RNA Synthesis / NLS-bearing protein import into nucleus / regulation of gluconeogenesis / dynein intermediate chain binding / DNA metabolic process / SUMOylation of ubiquitinylation proteins / ribosomal subunit export from nucleus / Vpr-mediated nuclear import of PICs / spermatid development / mitotic sister chromatid segregation / ribosomal small subunit export from nucleus / SUMOylation of DNA replication proteins / protein sumoylation / ribosomal large subunit export from nucleus / sperm flagellum / Regulation of HSF1-mediated heat shock response / mRNA transport / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / SUMOylation of DNA damage response and repair proteins / nuclear pore / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Signaling by ALK fusions and activated point mutants / Resolution of Sister Chromatid Cohesion / response to amphetamine / centriole / protein export from nucleus / viral process / SUMOylation of chromatin organization proteins / mitotic spindle organization / G protein activity / HCMV Late Events / male germ cell nucleus / RHO GTPases Activate Formins / hippocampus development / Transcriptional regulation by small RNAs / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / recycling endosome / ISG15 antiviral mechanism / small GTPase binding / HCMV Early Events / positive regulation of protein import into nucleus / protein import into nucleus / Separation of Sister Chromatids / GDP binding / melanosome / protein folding / positive regulation of protein binding / mitotic cell cycle / nuclear envelope / snRNP Assembly / midbody / actin cytoskeleton organization / nuclear membrane / cadherin binding / protein heterodimerization activity / protein domain specific binding / cell division / intracellular membrane-bounded organelle / GTPase activity / chromatin binding / chromatin
Similarity search - Function
Nup358/RanBP2 E3 ligase domain / Nup358/RanBP2 E3 ligase domain / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Zinc finger domain ...Nup358/RanBP2 E3 ligase domain / Nup358/RanBP2 E3 ligase domain / Ran binding protein RanBP1-like / Ran binding domain / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Tetratricopeptide-like helical domain superfamily / Small GTP-binding protein domain / PH-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / E3 SUMO-protein ligase RanBP2 / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.35 Å
AuthorsBley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. ...Bley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. / Brown, B. / Tang, A.W. / Rundlet, E.J. / Correia, A.R. / Chen, S. / Regmi, S.G. / Stevens, T.A. / Jette, C.A. / Dasso, M. / Patke, A. / Palazzo, A.F. / Kossiakoff, A.A. / Hoelz, A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM117360 United States
Howard Hughes Medical Institute (HHMI)55108534 United States
Heritage Medical Research Institute United States
CitationJournal: Science / Year: 2022
Title: Architecture of the cytoplasmic face of the nuclear pore.
Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / ...Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / Emily J Rundlet / Ana R Correia / Shane Chen / Saroj G Regmi / Taylor A Stevens / Claudia A Jette / Mary Dasso / Alina Patke / Alexander F Palazzo / Anthony A Kossiakoff / André Hoelz /
Abstract: INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are ...INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are generated by the circumscribed fusion of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) are the sole bidirectional gateways for nucleocytoplasmic transport. The ~110-MDa human NPC is an ~1000-protein assembly that comprises multiple copies of ~34 different proteins, collectively termed nucleoporins. The symmetric core of the NPC is composed of an inner ring encircling the central transport channel and outer rings formed by Y‑shaped coat nucleoporin complexes (CNCs) anchored atop both sides of the nuclear envelope. The outer rings are decorated with compartment‑specific asymmetric nuclear basket and cytoplasmic filament nucleoporins, which establish transport directionality and provide docking sites for transport factors and the small guanosine triphosphatase Ran. The cytoplasmic filament nucleoporins also play an essential role in the irreversible remodeling of messenger ribonucleoprotein particles (mRNPs) as they exit the central transport channel. Unsurprisingly, the NPC's cytoplasmic face represents a hotspot for disease‑associated mutations and is commonly targeted by viral virulence factors. RATIONALE Previous studies established a near-atomic composite structure of the human NPC's symmetric core by combining (i) biochemical reconstitution to elucidate the interaction network between symmetric nucleoporins, (ii) crystal and single-particle cryo-electron microscopy structure determination of nucleoporins and nucleoporin complexes to reveal their three-dimensional shape and the molecular details of their interactions, (iii) quantitative docking in cryo-electron tomography (cryo-ET) maps of the intact human NPC to uncover nucleoporin stoichiometry and positioning, and (iv) cell‑based assays to validate the physiological relevance of the biochemical and structural findings. In this work, we extended our approach to the cytoplasmic filament nucleoporins to reveal the near-atomic architecture of the cytoplasmic face of the human NPC. RESULTS Using biochemical reconstitution, we elucidated the protein-protein and protein-RNA interaction networks of the human and cytoplasmic filament nucleoporins, establishing an evolutionarily conserved heterohexameric cytoplasmic filament nucleoporin complex (CFNC) held together by a central heterotrimeric coiled‑coil hub that tethers two separate mRNP‑remodeling complexes. Further biochemical analysis and determination of a series of crystal structures revealed that the metazoan‑specific cytoplasmic filament nucleoporin NUP358 is composed of 16 distinct domains, including an N‑terminal S‑shaped α‑helical solenoid followed by a coiled‑coil oligomerization element, numerous Ran‑interacting domains, an E3 ligase domain, and a C‑terminal prolyl‑isomerase domain. Physiologically validated quantitative docking into cryo-ET maps of the intact human NPC revealed that pentameric NUP358 bundles, conjoined by the oligomerization element, are anchored through their N‑terminal domains to the central stalk regions of the CNC, projecting flexibly attached domains as far as ~600 Å into the cytoplasm. Using cell‑based assays, we demonstrated that NUP358 is dispensable for the architectural integrity of the assembled interphase NPC and RNA export but is required for efficient translation. After NUP358 assignment, the remaining 4-shaped cryo‑ET density matched the dimensions of the CFNC coiled‑coil hub, in close proximity to an outer-ring NUP93. Whereas the N-terminal NUP93 assembly sensor motif anchors the properly assembled related coiled‑coil channel nucleoporin heterotrimer to the inner ring, biochemical reconstitution confirmed that the NUP93 assembly sensor is reused in anchoring the CFNC to the cytoplasmic face of the human NPC. By contrast, two CFNCs are anchored by a divergent mechanism that involves assembly sensors located in unstructured portions of two CNC nucleoporins. Whereas unassigned cryo‑ET density occupies the NUP358 and CFNC binding sites on the nuclear face, docking of the nuclear basket component ELYS established that the equivalent position on the cytoplasmic face is unoccupied, suggesting that mechanisms other than steric competition promote asymmetric distribution of nucleoporins. CONCLUSION We have substantially advanced the biochemical and structural characterization of the asymmetric nucleoporins' architecture and attachment at the cytoplasmic and nuclear faces of the NPC. Our near‑atomic composite structure of the human NPC's cytoplasmic face provides a biochemical and structural framework for elucidating the molecular basis of mRNP remodeling, viral virulence factor interference with NPC function, and the underlying mechanisms of nucleoporin diseases at the cytoplasmic face of the NPC. [Figure: see text].
History
DepositionMay 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 15, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2022Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: E3 SUMO-protein ligase RanBP2
C: GTP-binding nuclear protein Ran
D: E3 SUMO-protein ligase RanBP2
E: GTP-binding nuclear protein Ran
F: E3 SUMO-protein ligase RanBP2
G: GTP-binding nuclear protein Ran
H: E3 SUMO-protein ligase RanBP2
I: GTP-binding nuclear protein Ran
J: E3 SUMO-protein ligase RanBP2
K: GTP-binding nuclear protein Ran
L: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)246,99024
Polymers243,71112
Non-polymers3,27912
Water8,521473
1
A: GTP-binding nuclear protein Ran
B: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5590 Å2
ΔGint-36 kcal/mol
Surface area17370 Å2
MethodPISA
2
C: GTP-binding nuclear protein Ran
D: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5780 Å2
ΔGint-33 kcal/mol
Surface area17120 Å2
MethodPISA
3
E: GTP-binding nuclear protein Ran
F: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5830 Å2
ΔGint-35 kcal/mol
Surface area17210 Å2
MethodPISA
4
G: GTP-binding nuclear protein Ran
H: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5830 Å2
ΔGint-36 kcal/mol
Surface area17310 Å2
MethodPISA
5
I: GTP-binding nuclear protein Ran
J: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5600 Å2
ΔGint-36 kcal/mol
Surface area17150 Å2
MethodPISA
6
K: GTP-binding nuclear protein Ran
L: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)41,1654
Polymers40,6182
Non-polymers5472
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5630 Å2
ΔGint-36 kcal/mol
Surface area17280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.690, 142.690, 96.650
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31

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Components

#1: Protein
GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 24430.023 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Production host: Escherichia coli (E. coli) / References: UniProt: P62826
#2: Protein
E3 SUMO-protein ligase RanBP2 / 358 kDa nucleoporin / Nuclear pore complex protein Nup358 / Nucleoporin Nup358 / Ran-binding ...358 kDa nucleoporin / Nuclear pore complex protein Nup358 / Nucleoporin Nup358 / Ran-binding protein 2 / RanBP2 / p270


Mass: 16188.443 Da / Num. of mol.: 6
Fragment: RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969)
Mutation: W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RANBP2, NUP358 / Production host: Escherichia coli (E. coli)
References: UniProt: P49792, Transferases; Acyltransferases; Aminoacyltransferases
#3: Chemical
ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / 5'-Guanylyl imidodiphosphate


Mass: 522.196 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


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


Mass: 18.015 Da / Num. of mol.: 473 / Source method: isolated from a natural source / Formula: H2O
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: 2.33 Å3/Da / Density % sol: 47.23 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 1.03317 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 2, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03317 Å / Relative weight: 1
ReflectionResolution: 2.35→29.36 Å / Num. obs: 91578 / % possible obs: 99.9 % / Redundancy: 10.2 % / Biso Wilson estimate: 47.55 Å2 / Rpim(I) all: 0.048 / Rrim(I) all: 0.154 / Net I/σ(I): 12.4 / Num. measured all: 935004
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
2.35-2.439.51.88681091700.5911.83599.8
5.06-29.369.930.39064491620.0190.06199.9

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.19.1refinement
PDB_EXTRACT3.27data extraction
Cootmodel building
PHASERphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1RRP

1rrp


Resolution: 2.35→29.36 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 27.08 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2252 4426 4.84 %
Rwork0.1833 87089 -
obs0.1854 91515 99.87 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 179.4 Å2 / Biso mean: 66.4518 Å2 / Biso min: 26.12 Å2
Refinement stepCycle: final / Resolution: 2.35→29.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16634 0 270 473 17377
Biso mean--44.78 50.65 -
Num. residues----2060
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.35-2.380.40881000.330729793079100
2.38-2.40.3191140.285929053019100
2.4-2.430.3351800.280228963076100
2.43-2.460.28451320.268429313063100
2.46-2.50.26781280.258129253053100
2.5-2.530.30731350.238429423077100
2.53-2.570.31141300.233328512981100
2.57-2.610.26191640.232829383102100
2.61-2.650.27411780.240628613039100
2.65-2.690.27611240.227929503074100
2.69-2.740.28181320.232529263058100
2.74-2.790.2711620.246728613023100
2.79-2.840.30521420.249628562998100
2.84-2.90.31521280.241629123040100
2.9-2.960.27021480.214129293077100
2.96-3.030.26311980.221828813079100
3.03-3.10.27191480.204828833031100
3.11-3.190.23951380.201229433081100
3.19-3.280.27111320.197628983030100
3.28-3.390.23391500.196429073057100
3.39-3.510.24381960.184628463042100
3.51-3.650.22911680.173328863054100
3.65-3.810.21620.159328973059100
3.82-4.020.20121470.15229093056100
4.02-4.270.17321940.137128022996100
4.27-4.590.17381070.128829753082100
4.6-5.050.19091560.132229023058100
5.06-5.780.17061020.162329553057100
5.78-7.270.20061520.185128823034100
7.27-29.360.18661790.15972861304099
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)
12.50560.08570.51752.24561.17751.8013-0.0729-0.1613-0.10970.0415-0.0707-0.0380.23620.1155-00.3323-0.06950.03710.4864-0.06730.3992-28.8623-6.64376.2297
23.49090.2219-0.09312.2860.56743.2053-0.0880.1290.6601-0.3186-0.01140.0926-0.5005-0.0691-00.4252-0.0409-0.01610.4746-0.04990.4994-29.86885.0472-0.8998
30.6484-0.35120.5310.1717-0.20160.832-1.8487-0.17191.36460.09670.58540.3804-1.11180.3283-0.10251.3734-0.241-0.00850.8503-0.15451.1505-20.155215.07612.27
41.2178-1.1014-0.30522.08610.26692.2992-0.1511-0.5060.04830.4066-0.0668-0.2721-0.07180.5978-0.00280.3321-0.0401-0.0070.63-0.1430.4488-21.3059-2.499414.1497
5-0.00050.0131-0.0406-0.0271-0.02710.05530.0491-0.5708-0.7924-0.0079-0.2240.4411.5275-0.25660.00051.1739-0.26630.09110.9611-0.09171.0923-24.1552-36.94514.017
61.4941-0.94930.65350.6038-0.43820.3321-0.5328-0.4282-1.1083-0.75420.8702-0.41960.42530.34690.05870.76340.09630.17510.48640.01220.4734-12.8475-24.9609-4.6321
71.3963-1.9916-0.05658.1066-1.42154.1451-0.26510.39740.31880.0937-0.6031-0.5465-0.5071-0.247-0.26930.5211-0.0612-0.0871.1845-0.29770.5737-31.99917.222523.1851
83.1856-1.1197-0.87145.0017-0.2252.1737-0.3031-0.5234-0.13710.52460.2625-0.30060.1854-0.09040.00010.4575-0.00380.06910.6079-0.02110.4855-14.9792-22.174613.7881
93.20880.25441.1770.80520.89792.0333-0.1124-0.4339-0.10990.6375-0.0311-0.44330.5634-0.3095-0.00020.6161-0.03280.10150.6981-0.04120.5261-16.4177-24.21815.8783
101.7468-0.62762.42792.8356-0.09823.99190.04180.04060.0217-0.254-0.0488-0.14060.8-0.0192-00.5994-0.03240.09560.5568-0.02230.6235-14.8466-26.77936.1259
110.9469-0.30920.58610.42590.12160.6499-0.1484-0.6443-0.65290.1269-0.0762-1.02940.57310.56860.00060.74020.07930.09580.67360.04140.9752-4.0319-31.383813.7373
120.05010.02110.01040.0405-0.04020.08521.0236-0.84871.07570.2730.28430.3883-0.6761-1.1098-0.00080.95370.0397-0.01270.6397-0.11280.8311-59.056-5.454717.6246
133.15040.44570.35951.04990.45060.7066-0.15040.4226-0.0565-0.00340.21590.0574-0.1576-0.04190.00080.3129-0.02360.01360.3657-0.03720.3364-63.0165-13.74221.7175
142.98960.82260.6983.16390.55120.9553-0.18390.6837-0.4877-0.19710.3241-0.38350.10850.35110.00140.3401-0.04810.0530.5642-0.1330.4689-52.1052-17.563-2.3062
15-0.01730.0562-0.02690.183-0.21340.20770.5906-0.0298-1.467-1.133-0.56290.68620.6269-0.1413-0.00130.92440.14620.00991.3119-0.27891.4065-46.8412-30.68361.0265
161.55660.48780.51320.8068-0.05872.1314-0.2454-0.3059-0.33130.36940.06130.00160.32-0.1017-0.00970.3955-0.00330.01890.35410.01220.4652-62.3611-21.159512.2321
172.04681.3725-0.04151.399-0.35252.1326-0.3970.33680.5740.15060.29481.034-0.823-0.5435-0.00040.62830.1477-0.00330.66680.04510.6721-89.99-6.8192-0.5659
180.8123-0.48860.91240.2849-0.53510.9491-0.37770.8752-0.8767-0.3092-0.0443-0.24460.296-0.0743-0.00010.7945-0.05680.04930.6345-0.06420.6744-47.2221-16.372620.1771
195.1901-0.80210.30132.57621.01412.2978-0.0544-0.4216-0.37880.37330.06080.1587-0.01530.1881-0.00010.4323-0.02650.04760.3670.00190.516-81.3318-17.435510.0755
202.8521.18331.17752.62770.23723.0957-0.3605-0.6892-0.26560.54030.23170.1322-0.0738-0.5128-0.00020.43630.04970.04150.5030.03540.4428-84.5472-15.033616.1722
212.3671-0.8254-1.04131.4839-1.23452.8494-0.08730.52950.1610.2655-0.09370.31080.0063-0.3998-0.00010.3352-0.05550.06310.5001-0.06030.5554-87.8188-14.58134.323
222.5602-1.99550.60242.28250.39092.1333-0.12740.1308-1.03120.0786-0.32630.66590.1034-0.6853-0.00870.5021-0.13360.14350.5327-0.07870.6571-92.3222-20.3399.385
230.0653-0.0116-0.04460.0258-0.03180.07220.16120.2891-0.3693-0.0689-0.47070.06440.1926-1.8126-0.00021.0799-0.29540.13841.0344-0.34580.9068-13.8925-33.6024-43.4384
241.4648-0.1027-1.58481.0851-0.18053.4044-0.42490.0783-0.22410.2323-0.16190.21870.8288-0.3787-0.00790.7278-0.06360.19980.4566-0.06690.4799-10.0079-28.2223-25.5104
253.44860.279-1.60932.6047-0.33646.3701-0.1927-0.5149-0.18640.6718-0.1425-0.66630.61181.10830.00790.75840.09470.02720.62740.08710.54753.2219-26.2598-21.5194
260.3162-0.7120.50961.4393-1.37541.19-0.10110.2870.2773-0.2701-0.1969-0.13330.1293-0.0588-0.00030.5683-0.0120.12590.4947-0.140.5031-10.5086-22.2872-39.7128
270.06110.03620.0740.06780.02580.06540.6674-0.1041-0.74860.13480.2271-0.2625-0.01190.229-0.00051.07180.01350.27321.412-0.32451.5596-42.9769-17.8735-25.8407
281.0039-0.49730.43651.32340.01631.18990.10761.3740.32280.5025-0.43080.45951.1231-0.4047-0.01780.5019-0.11420.09350.7001-0.15910.5199-30.2166-10.8354-17.2562
291.7812-0.0231-2.03911.17260.27812.19550.04940.4874-0.0096-0.3131-0.41560.09470.4841-0.1564-0.00640.7733-0.02050.05920.5114-0.09220.4531-9.1657-22.9686-45.4976
302.4253-1.10291.32652.36670.90161.94920.1421-0.3073-0.06680.084-0.1830.23550.70920.1511-00.5115-0.03960.06730.5064-0.12640.4619-23.7908-14.3757-23.973
311.4002-0.3294-0.90572.5999-0.48762.9894-0.01560.14790.1767-0.1863-0.09150.0519-0.1332-0.25200.4671-0.06320.02210.5321-0.14040.4985-26.7669-10.4859-36.0193
321.2365-0.8064-0.26450.7577-0.54042.26060.0046-0.2792-0.26180.5481-0.3765-0.25950.5471-0.28390.00010.4971-0.10280.10260.6096-0.19020.5834-28.5955-14.3327-29.8307
330.61880.0235-0.20170.3075-0.09720.3497-0.09860.17520.9993-0.4462-0.314-0.0796-0.6449-0.57050.00030.5930.0413-0.09210.6067-0.18180.7831-31.9071-0.0358-35.1067
344.76210.93240.60797.82093.90561.9637-0.22291.0659-0.1907-1.4508-0.5186-0.013-0.0121-0.2709-0.19650.40770.03070.2690.7616-0.02470.6333-34.2429-33.089621.993
351.20260.24350.55292.7003-0.09982.05840.1521-0.10210.06970.2048-0.1199-0.01950.14520.036600.3131-0.00820.03310.3211-0.00550.3481-43.0985-36.2537.4043
363.46470.58570.20722.94460.20322.5657-0.0154-0.21830.51510.3103-0.07870.1689-0.32590.0062-00.4461-0.0286-0.00720.3369-0.02950.4782-45.9107-25.023841.5104
370.3819-0.10860.43660.016-0.15990.4983-0.3103-0.09531.61-0.15830.69061.2297-0.8894-0.7826-0.00071.01640.1769-0.04460.7267-0.09831.2907-58.6524-18.768737.7728
381.1485-0.1125-0.30592.00420.36291.88870.05080.1278-0.0947-0.4171-0.24290.099-0.0705-0.31550.00010.36580.0141-0.00630.35290.02070.408-50.0735-35.640426.6641
391.69592.0159-0.22352.37940.09562.2848-0.15750.1282-0.28720.8451-0.0261-1.00480.84370.8775-0.00020.81320.1869-0.12870.65750.03250.6872-39.8696-63.863740.4574
400.4838-0.70760.47150.7466-0.53990.517-0.1011-0.40940.3309-0.1194-0.0677-0.2812-0.46070.13080.00020.8489-0.09950.03770.65240.04340.7457-43.8104-20.256519.1387
412.0195-0.1742-2.29413.48480.63632.5617-0.02790.4048-0.1638-0.11420.12740.1759-0.2467-0.13410.00010.4107-0.0363-0.02670.3813-0.03360.4699-48.6472-53.666229.4464
420.77150.7535-0.11260.7476-0.13720.4628-0.24440.819-0.6423-0.6675-0.03740.2680.30570.1190.00050.5748-0.03590.0420.6264-0.140.5783-48.4295-61.899615.3779
431.30540.9777-0.89482.0255-0.434.1439-0.04370.06690.01940.3938-0.05370.05010.29550.020700.4364-0.00460.00140.3976-0.010.481-47.0631-57.869330.031
442.1278-2.37240.6612.5514-0.70112.2783-0.3579-0.1426-0.39550.1921-0.06620.90520.7436-0.2001-0.00030.6109-0.12880.14030.4884-0.06720.6194-52.7048-64.372129.519
450.6427-0.39690.43881.7423-0.80211.26810.0178-0.02520.09150.1677-0.1422-0.1533-0.49850.601900.5118-0.1389-0.03470.52570.01120.4279-41.67442.2357-25.9485
460.8202-0.27480.95011.32580.49581.5663-0.3545-0.32540.45010.4302-0.1021-0.455-0.81410.5576-0.00910.7992-0.2254-0.11550.66340.06130.6254-39.320751.6342-18.9655
473.1213-1.32111.73452.6517-0.29432.1016-0.4639-0.25410.9423-0.05490.1334-0.0294-0.8054-0.25700.6638-0.0001-0.08240.6104-0.090.5941-51.694455.0045-21.3599
480.4191-0.29430.29130.2946-0.31250.2106-0.16820.1746-0.0097-0.6576-0.14720.1755-0.2777-0.3737-0.00010.7336-0.111-0.070.5125-0.01180.5232-48.639749.0289-37.5207
490.2007-0.39130.27550.3872-0.22280.4579-0.36020.50250.1556-0.70090.6466-0.40260.07740.6503-0.01060.6771-0.16880.14590.6485-0.20470.7509-42.926526.7881-41.0103
501.28110.49250.63270.69990.68961.5511-0.0981-0.1685-0.18950.40420.4804-0.62950.69491.01890.00130.73540.1013-0.04910.6652-0.06560.6763-42.572614.374-20.2643
510.3781-0.0924-0.44090.27820.00130.41270.1657-0.47190.10131.0067-0.62390.57690.4667-0.7487-00.8033-0.11710.08710.7912-0.03760.7553-41.631357.6926-42.3901
521.18140.4729-0.35760.8944-0.60190.32420.07940.96390.2798-1.04620.30060.4871-0.2933-0.6980.00020.9359-0.1153-0.04160.6707-0.05470.6656-53.625325.3275-42.8665
532.2278-0.2684-0.38144.3601-0.08942.46560.01790.2689-0.0343-0.55110.1234-0.0657-0.02250.237900.4986-0.02990.02880.4951-0.0420.5331-48.671322.5549-32.7808
541.5449-0.66871.18082.40451.12263.5254-0.1422-0.11030.0840.12140.21990.1230.52010.1698-00.4646-0.0022-0.0280.4998-0.04510.6192-49.821818.7007-26.5168
550.6328-0.33920.02020.949-0.49720.4820.03190.5518-0.8773-0.26180.01131.46870.738-0.1693-0.0020.6795-0.1288-0.08310.5138-0.0730.9428-58.882511.7808-34.1317
568.08061.5798-8.37980.3266-1.73199.32081.1144-1.3462-0.01440.88880.2005-0.6108-1.26890.39630.68170.6960.1629-0.24160.85090.31580.8951-51.146410.200920.8076
571.56490.7354-0.35631.21320.05451.4276-0.1826-0.01790.1157-0.02380.06890.0827-0.2540.0204-0.00010.49650.0837-0.01890.26840.03450.408-54.775417.42015.7613
580.70030.4604-0.54322.36010.56981.193-0.24550.3629-0.1324-0.34730.32510.33280.2114-0.2881-0.00010.5689-0.0058-0.02930.44420.03830.529-62.378310.3441-1.5946
592.7536-0.71250.00053.0447-0.5273.0450.01150.0993-0.0317-0.15090.20521.4776-0.3144-0.7161-0.00220.52390.0969-0.06770.54270.08280.7458-70.310116.92862.7904
600.63350.9183-0.10330.9128-0.16731.9217-0.0523-0.95250.65680.5769-0.21260.3983-0.4143-0.1486-0.00620.69490.10610.01650.50960.04520.4737-57.808521.35419.469
610.12870.48840.04672.0818-0.05311.803-0.1526-0.3898-0.28990.02920.0625-0.59990.26251.27900.73260.0225-0.03141.00660.06910.7798-32.827634.1161.5524
621.4337-0.4443-0.80110.8321-0.51661.2664-0.5235-0.0708-0.1563-0.85260.18770.4358-0.665-0.09370.00020.95260.06470.05790.58590.08150.5895-63.715410.868924.5954
633.60971.16080.57552.452-1.67872.92310.1272-0.25140.42560.545-0.14580.1960.24850.082-0.00020.62390.0647-0.0330.3991-0.04360.5236-44.405736.456115.1638
640.6368-0.9208-0.17841.76450.71122.228-0.0625-0.00660.26040.45250.16470.18690.16090.26850.00010.5480.084-0.02810.44380.05040.4835-43.099735.3414.2142
652.41270.5829-0.81211.63191.94113.326-0.148-0.00210.1366-0.3481-0.02890.37690.38640.533700.56670.0827-0.04670.46640.0370.5082-40.984836.85587.076
660.56080.176-0.38740.92520.00680.8349-0.64870.41441.78820.732-0.01830.6054-0.79190.38170.00040.7633-0.0255-0.06950.52550.06860.9974-41.72349.171514.3859
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 61 )A6 - 61
2X-RAY DIFFRACTION2chain 'A' and (resid 62 through 130 )A62 - 130
3X-RAY DIFFRACTION3chain 'A' and (resid 131 through 144 )A131 - 144
4X-RAY DIFFRACTION4chain 'A' and (resid 145 through 185 )A145 - 185
5X-RAY DIFFRACTION5chain 'A' and (resid 186 through 203 )A186 - 203
6X-RAY DIFFRACTION6chain 'A' and (resid 204 through 211 )A204 - 211
7X-RAY DIFFRACTION7chain 'B' and (resid 2907 through 2922 )B0
8X-RAY DIFFRACTION8chain 'B' and (resid 2923 through 2966 )B0
9X-RAY DIFFRACTION9chain 'B' and (resid 2967 through 2992 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 2993 through 3025 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 3026 through 3044 )B0
12X-RAY DIFFRACTION12chain 'C' and (resid 7 through 10 )C7 - 10
13X-RAY DIFFRACTION13chain 'C' and (resid 11 through 58 )C11 - 58
14X-RAY DIFFRACTION14chain 'C' and (resid 59 through 131 )C59 - 131
15X-RAY DIFFRACTION15chain 'C' and (resid 132 through 144 )C132 - 144
16X-RAY DIFFRACTION16chain 'C' and (resid 145 through 185 )C145 - 185
17X-RAY DIFFRACTION17chain 'C' and (resid 186 through 211 )C186 - 211
18X-RAY DIFFRACTION18chain 'D' and (resid 2907 through 2921 )D0
19X-RAY DIFFRACTION19chain 'D' and (resid 2922 through 2960 )D0
20X-RAY DIFFRACTION20chain 'D' and (resid 2961 through 2992 )D0
21X-RAY DIFFRACTION21chain 'D' and (resid 2993 through 3015 )D0
22X-RAY DIFFRACTION22chain 'D' and (resid 3016 through 3044 )D0
23X-RAY DIFFRACTION23chain 'E' and (resid 6 through 9 )E6 - 9
24X-RAY DIFFRACTION24chain 'E' and (resid 10 through 69 )E10 - 69
25X-RAY DIFFRACTION25chain 'E' and (resid 70 through 156 )E70 - 156
26X-RAY DIFFRACTION26chain 'E' and (resid 157 through 188 )E157 - 188
27X-RAY DIFFRACTION27chain 'E' and (resid 189 through 199 )E189 - 199
28X-RAY DIFFRACTION28chain 'E' and (resid 200 through 211 )E200 - 211
29X-RAY DIFFRACTION29chain 'F' and (resid 2907 through 2934 )F0
30X-RAY DIFFRACTION30chain 'F' and (resid 2935 through 2954 )F0
31X-RAY DIFFRACTION31chain 'F' and (resid 2955 through 3001 )F0
32X-RAY DIFFRACTION32chain 'F' and (resid 3002 through 3025 )F0
33X-RAY DIFFRACTION33chain 'F' and (resid 3026 through 3044 )F0
34X-RAY DIFFRACTION34chain 'G' and (resid 7 through 10 )G7 - 10
35X-RAY DIFFRACTION35chain 'G' and (resid 11 through 58 )G11 - 58
36X-RAY DIFFRACTION36chain 'G' and (resid 59 through 131 )G59 - 131
37X-RAY DIFFRACTION37chain 'G' and (resid 132 through 144 )G132 - 144
38X-RAY DIFFRACTION38chain 'G' and (resid 145 through 186 )G145 - 186
39X-RAY DIFFRACTION39chain 'G' and (resid 187 through 211 )G187 - 211
40X-RAY DIFFRACTION40chain 'H' and (resid 2907 through 2921 )H0
41X-RAY DIFFRACTION41chain 'H' and (resid 2922 through 2957 )H0
42X-RAY DIFFRACTION42chain 'H' and (resid 2958 through 2968 )H0
43X-RAY DIFFRACTION43chain 'H' and (resid 2969 through 3014 )H0
44X-RAY DIFFRACTION44chain 'H' and (resid 3015 through 3044 )H0
45X-RAY DIFFRACTION45chain 'I' and (resid 8 through 62 )I8 - 62
46X-RAY DIFFRACTION46chain 'I' and (resid 63 through 94 )I63 - 94
47X-RAY DIFFRACTION47chain 'I' and (resid 95 through 156 )I95 - 156
48X-RAY DIFFRACTION48chain 'I' and (resid 157 through 175 )I157 - 175
49X-RAY DIFFRACTION49chain 'I' and (resid 176 through 187 )I176 - 187
50X-RAY DIFFRACTION50chain 'I' and (resid 188 through 211 )I188 - 211
51X-RAY DIFFRACTION51chain 'J' and (resid 2907 through 2921 )J0
52X-RAY DIFFRACTION52chain 'J' and (resid 2922 through 2939 )J0
53X-RAY DIFFRACTION53chain 'J' and (resid 2940 through 2991 )J0
54X-RAY DIFFRACTION54chain 'J' and (resid 2992 through 3025 )J0
55X-RAY DIFFRACTION55chain 'J' and (resid 3026 through 3044 )J0
56X-RAY DIFFRACTION56chain 'K' and (resid 7 through 10 )K7 - 10
57X-RAY DIFFRACTION57chain 'K' and (resid 11 through 63 )K11 - 63
58X-RAY DIFFRACTION58chain 'K' and (resid 64 through 99 )K64 - 99
59X-RAY DIFFRACTION59chain 'K' and (resid 100 through 156 )K100 - 156
60X-RAY DIFFRACTION60chain 'K' and (resid 157 through 186 )K157 - 186
61X-RAY DIFFRACTION61chain 'K' and (resid 187 through 211 )K187 - 211
62X-RAY DIFFRACTION62chain 'L' and (resid 2907 through 2924 )L0
63X-RAY DIFFRACTION63chain 'L' and (resid 2925 through 2973 )L0
64X-RAY DIFFRACTION64chain 'L' and (resid 2974 through 2994 )L0
65X-RAY DIFFRACTION65chain 'L' and (resid 2995 through 3024 )L0
66X-RAY DIFFRACTION66chain 'L' and (resid 3025 through 3044 )L0

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