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- PDB-7mnk: Crystal structure of the tetramerization element of NUP358/RanBP2... -

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Basic information

Entry
Database: PDB / ID: 7mnk
TitleCrystal structure of the tetramerization element of NUP358/RanBP2 (residues 805-832)
ComponentsE3 SUMO-protein ligase RanBP2
KeywordsTRANSPORT PROTEIN / NUCLEAR PORE COMPLEX COMPONENT / NUCLEOCYTOPLASMIC TRANSPORT
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 / Nuclear Pore Complex (NPC) Disassembly / nuclear inclusion body / nuclear pore nuclear basket / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein ...cytoplasmic periphery of the nuclear pore complex / SUMO ligase activity / SUMO ligase complex / annulate lamellae / nuclear pore cytoplasmic filaments / Nuclear Pore Complex (NPC) Disassembly / 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) / Transport of the SLBP independent Mature mRNA / 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 / 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 / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / SUMO transferase activity / nucleocytoplasmic transport / centrosome localization / Viral Messenger RNA Synthesis / regulation of gluconeogenesis / NLS-bearing protein import into nucleus / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / SUMOylation of DNA replication proteins / protein sumoylation / 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 / Resolution of Sister Chromatid Cohesion / response to amphetamine / SUMOylation of chromatin organization proteins / GTPase activator activity / HCMV Late Events / RHO GTPases Activate Formins / Transcriptional regulation by small RNAs / Signaling by ALK fusions and activated point mutants / ISG15 antiviral mechanism / small GTPase binding / HCMV Early Events / Separation of Sister Chromatids / protein folding / nuclear envelope / snRNP Assembly / nuclear membrane / intracellular membrane-bounded organelle / protein-containing complex binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / RNA binding / nucleoplasm / membrane / metal ion binding / cytosol / cytoplasm
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 / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. ...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 / 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 / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / PH-like domain superfamily
Similarity search - Domain/homology
E3 SUMO-protein ligase RanBP2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.1 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.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: E3 SUMO-protein ligase RanBP2
B: E3 SUMO-protein ligase RanBP2
C: E3 SUMO-protein ligase RanBP2
D: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,91313
Polymers14,1844
Non-polymers7299
Water2,378132
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, SEC-MALS
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7280 Å2
ΔGint-118 kcal/mol
Surface area7100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.930, 99.930, 60.160
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number97
Space group name H-MI422
Components on special symmetry positions
IDModelComponents
11A-1008-

HOH

21B-1142-

HOH

31C-1003-

HOH

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Components

#1: Protein/peptide
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: 3546.095 Da / Num. of mol.: 4
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
#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#3: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 132 / 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: 2.65 Å3/Da / Density % sol: 53.53 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 3.5 / Details: 2 M ammonium sulfate; 0.1 M citric acid

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 20, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 1.1→29.14 Å / Num. obs: 61560 / % possible obs: 100 % / Redundancy: 25.3 % / Biso Wilson estimate: 13.79 Å2 / Rpim(I) all: 0.012 / Rrim(I) all: 0.063 / Net I/σ(I): 24.1 / Num. measured all: 1558137
Reflection shell

Diffraction-ID: 1 / % possible all: 99.9

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all
1.1-1.1423.81.114484060770.623.072
2.37-29.1523.983.615390464480.0060.032

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Processing

Software
NameVersionClassification
PDB_EXTRACT3.27data extraction
PHENIX1.18.2refinement
Cootmodel building
xia2data reduction
AutoSolphasing
XDSdata processing
XSCALEdata scaling
RefinementMethod to determine structure: SAD / Resolution: 1.1→29.14 Å / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 17.75 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1669 2090 3.4 %
Rwork0.1546 59451 -
obs0.155 61541 99.93 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 123.95 Å2 / Biso mean: 25.1171 Å2 / Biso min: 10.01 Å2
Refinement stepCycle: final / Resolution: 1.1→29.14 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms980 0 85 138 1203
Biso mean--57.11 36.71 -
Num. residues----120
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 15 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
1.1-1.130.31531400.299839084048
1.13-1.150.2961530.259538824035
1.15-1.180.24491450.242639044049
1.18-1.220.22941380.23839504088
1.22-1.260.20941350.198439114046
1.26-1.30.20151390.197239154054
1.3-1.360.19961420.184439284070
1.36-1.420.20941260.175139494075
1.42-1.490.17321370.15739524089
1.49-1.590.15771510.144339454096
1.59-1.710.17921280.141439714099
1.71-1.880.15241430.139139924135
1.88-2.150.13741300.130939984128
2.15-2.710.15291470.13540324179
2.71-29.140.15921360.153542144350
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)
10.22090.09740.14380.12650.00740.1183-0.0012-0.33720.09310.38170.0576-0.17540.1246-0.250900.19880.0056-0.02660.22560.00640.188852.566521.644925.6655
20.25160.07050.07810.09720.04530.1144-0.0790.1143-0.17260.00270.1517-0.25880.04230.168800.1282-0.0033-0.00880.1437-0.00120.134848.878818.980120.9446
30.43790.35990.27740.42270.07880.2440.04880.05170.0269-0.02750.1011-0.2408-0.11830.27770.00040.1372-0.01440.00130.1622-0.0160.137943.092615.112316.0324
40.43450.388-0.09630.313-0.09740.3260.08040.0288-0.0501-0.010.0707-0.1642-0.05470.1300.12970.00160.00390.1365-0.00390.13139.492113.211310.2748
50.3840.21950.27080.2987-0.0990.511-0.00870.1461-0.0003-0.065-0.09170.06390.2460.1454-0.00010.1622-0.00040.00980.1388-0.01550.132333.22669.42255.6749
60.0560.00840.12420.30120.20920.3695-0.0666-0.0059-0.1433-0.0034-0.13020.01430.4756-0.3346-00.1903-0.02410.01060.2017-0.04350.157528.70537.9417-0.1049
72.64341.22281.56614.13321.5113.9546-0.0753-0.76640.54660.564-0.80881.3532-0.3658-0.7247-0.27450.22680.0376-0.02640.2866-0.13660.349824.298713.844-6.687
80.06790.10950.01680.16510.01680.1437-0.03720.1943-0.0015-0.1007-0.06890.218-0.06320.0363-0.00030.1550.019-0.01250.1768-0.0280.161933.158514.7187-7.6732
90.3963-0.09440.08430.16090.15660.2113-0.01930.369-0.0901-0.301-0.0414-0.1006-0.24720.0979-0.00020.12730.00180.0010.1628-0.01630.136737.702215.1773-4.2495
100.48610.1796-0.17530.37950.13970.2974-0.00350.2323-0.3863-0.144-0.0085-0.06080.12610.049300.1240.0094-0.00340.1727-0.00930.156742.281513.84410.473
110.20160.14590.02980.1293-0.00640.16240.1498-0.2864-0.33060.1366-0.0884-0.04210.10610.005700.1456-0.0068-0.02020.19910.0170.18848.068913.39215.5597
120.94530.0510.11390.35350.38410.44760.39390.0136-0.1504-0.02040.1325-0.24010.60710.09780.08340.1874-0.0143-0.03110.24610.01570.173150.70416.21648.5045
130.1354-0.06970.2070.1386-0.04890.25310.10.3315-0.0683-0.025-0.0127-0.22280.07740.18470.00020.18150.0012-0.02040.233-0.01190.189957.249319.953115.7933
143.46150.98121.22940.30980.50561.3041-0.1122-0.55031.1321-0.03780.8031-1.2451-0.24761.2630.64020.1906-0.0595-0.00720.4365-0.16230.424561.100124.995710.4919
152.7729-0.45861.80741.7596-0.77746.5945-0.44690.09350.8766-0.03080.2374-0.2843-1.03590.4954-0.10880.1804-0.0677-0.02130.24010.00550.196354.678525.91267.2962
160.3033-0.02440.2650.164-0.06630.2315-0.22970.30350.1424-0.23050.1493-0.2299-0.16180.5272-0.00020.1965-0.0392-0.01640.2460.01470.161848.857525.13.6864
170.30350.26120.09990.2316-0.01830.3292-0.12880.15280.2990.0842-0.0335-0.1022-0.29980.2196-0.00010.1494-0.0067-0.02120.15570.0140.142641.633623.96172.7919
180.1826-0.09750.01820.24560.05090.18870.05410.25790.27470.0603-0.2826-0.0513-0.02450.340300.13310.0123-0.00520.13170.01130.141233.925823.8588-0.8798
190.0641-0.1127-0.01730.167-0.00760.12170.10220.3458-0.46730.0298-0.10010.76020.1889-0.2089-00.14220.0240.00790.1525-0.04210.227525.873721.5051-3.5333
200.3266-0.0902-1.00220.41570.57123.38080.5094-0.2039-1.2154-0.38550.44541.0572-0.0001-1.11170.18190.2828-0.0698-0.03780.49640.04760.625220.908313.12433.7808
211.4436-0.06021.15290.9266-0.14133.3240.2441-0.9354-0.16030.2227-0.09490.5663-0.1748-1.01390.05770.1272-0.00090.03780.2658-0.0130.239926.313317.44648.272
220.67550.35840.36530.4976-0.0060.3077-0.0699-0.36460.3580.3829-0.190.4599-0.2177-0.547-0.01430.21220.00090.02440.1848-0.03550.188833.529121.74099.828
230.0115-0.0325-0.00420.0907-0.01390.1074-0.16650.25490.47960.1904-0.1444-0.2088-0.3540.09460.00020.2003-0.0138-0.03140.16540.02840.199439.956326.48511.7332
240.3097-0.0055-0.02830.10920.08050.0549-0.32130.40740.6826-0.14170.1344-0.2576-0.0942-0.0344-00.1932-0.0159-0.0450.16190.02640.290644.894926.78715.229
250.25610.12320.0670.2519-0.05630.10750.0710.30980.54890.1723-0.2182-0.1374-0.01470.66950.01680.23570.0415-0.05280.21350.01090.210854.267526.367418.4717
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resid 803:806A803 - 806
2X-RAY DIFFRACTION2chain A and resid 807:812A807 - 812
3X-RAY DIFFRACTION3chain A and resid 813:816A813 - 816
4X-RAY DIFFRACTION4chain A and resid 817:822A817 - 822
5X-RAY DIFFRACTION5chain A and resid 823:827A823 - 827
6X-RAY DIFFRACTION6chain A and resid 828:832A828 - 832
7X-RAY DIFFRACTION7chain B and resid 803:806B803 - 806
8X-RAY DIFFRACTION8chain B and resid 807:810B807 - 810
9X-RAY DIFFRACTION9chain B and resid 811:814B811 - 814
10X-RAY DIFFRACTION10chain B and resid 815:819B815 - 819
11X-RAY DIFFRACTION11chain B and resid 820:823B820 - 823
12X-RAY DIFFRACTION12chain B and resid 824:827B824 - 827
13X-RAY DIFFRACTION13chain B and resid 828:832B828 - 832
14X-RAY DIFFRACTION14chain C and resid 803:807C803 - 807
15X-RAY DIFFRACTION15chain C and resid 808:812C808 - 812
16X-RAY DIFFRACTION16chain C and resid 813:816C813 - 816
17X-RAY DIFFRACTION17chain C and resid 817:822C817 - 822
18X-RAY DIFFRACTION18chain C and resid 823:827C823 - 827
19X-RAY DIFFRACTION19chain C and resid 828:832C828 - 832
20X-RAY DIFFRACTION20chain D and resid 803:807D803 - 807
21X-RAY DIFFRACTION21chain D and resid 808:813D808 - 813
22X-RAY DIFFRACTION22chain D and resid 814:819D814 - 819
23X-RAY DIFFRACTION23chain D and resid 820:823D820 - 823
24X-RAY DIFFRACTION24chain D and resid 824:827D824 - 827
25X-RAY DIFFRACTION25chain D and resid 828:832D828 - 832

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