PDB-5zq5: SidE-Ubi

ID or keywords:

Entry

Database: PDB / ID: 5zq5

Title

SidE-Ubi

Components

SidE
Ubiquitin

Keywords

CELL INVASION / ubiquitination

Function / homology

Function and homology information

NAD+-protein-arginine ADP-ribosyltransferase activity / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis ...NAD+-protein-arginine ADP-ribosyltransferase activity / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Pexophagy / Regulation of innate immune responses to cytosolic DNA / InlA-mediated entry of Listeria monocytogenes into host cells / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLK / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Josephin domain DUBs / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / AUF1 (hnRNP D0) binds and destabilizes mRNA / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / Regulation of NF-kappa B signaling / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Hh mutants are degraded by ERAD / Recognition of DNA damage by PCNA-containing replication complex / Peroxisomal protein import / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Regulation of TNFR1 signaling / Negative regulation of FGFR2 signaling / Termination of translesion DNA synthesis / Negative regulation of FGFR4 signaling / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Stabilization of p53 / EGFR downregulation / Negative regulation of NOTCH4 signaling / Negative regulation of FGFR1 signaling / Iron uptake and transport / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
Similarity search - Function

Biological species

Legionella pneumophila (bacteria)

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

SAD / Resolution: 2.487 Å

Authors

Wang, Y. / Gao, A. / Gao, P.

Funding support

China, 4items

Citation

Journal: Cell / Year: 2018
Title: Structural Insights into Non-canonical Ubiquitination Catalyzed by SidE.
Authors: Wang, Y. / Shi, M. / Feng, H. / Zhu, Y. / Liu, S. / Gao, A. / Gao, P.

History

Deposition	Apr 17, 2018	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	May 23, 2018	Provider: repository / Type: Initial release
Revision 1.1	May 30, 2018	Group: Data collection / Database references / Category: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	5zq5.cif.gz	733.8 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	5zq5_validation.pdf.gz	464.6 KB	Display	wwPDB validaton report
Full document	5zq5_full_validation.pdf.gz	502.3 KB	Display
Data in XML	5zq5_validation.xml.gz	65.1 KB	Display
Data in CIF	5zq5_validation.cif.gz	89.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/zq/5zq5 ftp://data.pdbj.org/pub/pdb/validation_reports/zq/5zq5	HTTPS FTP

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Related structure data

Related structure data	5zq2C 5zq3C 5zq4C 5zq6C 5zq7C C: citing same article (ref.)
Similar structure data	5zq6-d 5zq7-d 2304 3dhw-d 1yfj-d 4lgv-2 Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#60 - Dec 2004 Ubiquitin similarity (67) #234 - Jun 2019 MDM2 and Cancer similarity (66) #122 - Feb 2010 Enhanceosome similarity (6) #88 - Apr 2007 Clathrin similarity (1) #150 - Jun 2012 Sliding Clamps similarity (5) #172 - Apr 2014 RecA and Rad51 similarity (8) #68 - Aug 2005 Neurotrophins similarity (3) #143 - Nov 2011 Toll-like Receptors similarity (4) #56 - Aug 2004 Caspases similarity (3) #255 - Mar 2021 Cisplatin and DNA similarity (2) #126 - Jun 2010 Epidermal Growth Factor similarity (1) #43 - Jul 2003 Src Tyrosine Kinase similarity (2) #195 - Mar 2016 RAF Protein Kinases similarity (1) #205 - Jan 2017 Nuclear Pore Complex similarity (1) #163 - Jul 2013 HIV Capsid similarity (1) #266 - Feb 2022 Oligosaccharyltransferase similarity (1) #112 - Apr 2009 Oct and Sox Transcription Factors similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

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Deposited unit

A: SidE

B: Ubiquitin

D: Ubiquitin

C: SidE

211 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	92.672, 129.084, 191.507
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

#1: Protein	SidE Mass: 96813.352 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Legionella pneumophila (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: Q6RCR1, UniProt: Q6BBR6*PLUS
#2: Protein	Ubiquitin Mass: 8691.896 Da / Num. of mol.: 2 / Mutation: R42A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 250 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.73 Å³/Da / Density % sol: 55.03 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: PEG 3350, Tacsimate

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Data collection

Diffraction	Mean temperature: 193 K
Diffraction source	Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9785 Å
Detector	Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 5, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9785 Å / Relative weight: 1
Reflection	Resolution: 2.48→50 Å / Num. obs: 80934 / % possible obs: 100 % / Redundancy: 9 % / R_merge(I) obs: 0.127 / R_pim(I) all: 0.044 / R_rim(I) all: 0.134 / Net I/σ(I): 13.8
Reflection shell	Resolution: 2.49→2.56 Å / CC_1/2: 0.769 / R_pim(I) all: 0.35

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Processing

Software

Name	Version	Classification
PHENIX	1.11.1_2575	refinement
Coot		model building
HKL-3000		data scaling
PHENIX		phasing

Refinement

Method to determine structure:

SAD / Resolution: 2.487→48.688 Å / SU ML: 0.3 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 24.2

	R_factor	Num. reflection	% reflection
R_free	0.2329	4060	5.02 %
R_work	0.1895	-	-
obs	0.1917	80934	99.53 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Refinement step

Cycle: LAST / Resolution: 2.487→48.688 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	14374	0	0	250	14624

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.005	14646
X-RAY DIFFRACTION	f_angle_d	0.711	19783
X-RAY DIFFRACTION	f_dihedral_angle_d	7.736	8953
X-RAY DIFFRACTION	f_chiral_restr	0.044	2197
X-RAY DIFFRACTION	f_plane_restr	0.006	2592

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.4874-2.5167	0.3298	124	0.2809	2284	X-RAY DIFFRACTION	87
2.5167-2.5473	0.3138	159	0.2713	2562	X-RAY DIFFRACTION	100
2.5473-2.5796	0.3403	142	0.2682	2655	X-RAY DIFFRACTION	100
2.5796-2.6135	0.3178	139	0.2629	2622	X-RAY DIFFRACTION	100
2.6135-2.6493	0.3137	141	0.2545	2657	X-RAY DIFFRACTION	100
2.6493-2.6872	0.3111	136	0.2451	2629	X-RAY DIFFRACTION	100
2.6872-2.7273	0.3243	154	0.2405	2627	X-RAY DIFFRACTION	100
2.7273-2.7699	0.2829	131	0.2249	2624	X-RAY DIFFRACTION	100
2.7699-2.8153	0.3127	122	0.2321	2665	X-RAY DIFFRACTION	100
2.8153-2.8638	0.2458	137	0.2307	2626	X-RAY DIFFRACTION	100
2.8638-2.9159	0.2781	122	0.2294	2644	X-RAY DIFFRACTION	100
2.9159-2.972	0.3239	139	0.2385	2634	X-RAY DIFFRACTION	100
2.972-3.0326	0.2649	132	0.2352	2666	X-RAY DIFFRACTION	100
3.0326-3.0986	0.2631	131	0.2362	2658	X-RAY DIFFRACTION	100
3.0986-3.1706	0.2697	131	0.2306	2650	X-RAY DIFFRACTION	100
3.1706-3.2499	0.2957	171	0.2197	2624	X-RAY DIFFRACTION	100
3.2499-3.3378	0.2432	117	0.2161	2669	X-RAY DIFFRACTION	100
3.3378-3.436	0.2572	138	0.203	2664	X-RAY DIFFRACTION	100
3.436-3.5468	0.2594	123	0.2008	2684	X-RAY DIFFRACTION	100
3.5468-3.6736	0.2253	162	0.181	2628	X-RAY DIFFRACTION	100
3.6736-3.8206	0.2201	145	0.1822	2652	X-RAY DIFFRACTION	100
3.8206-3.9944	0.2153	145	0.1614	2658	X-RAY DIFFRACTION	100
3.9944-4.2049	0.1917	150	0.1461	2679	X-RAY DIFFRACTION	100
4.2049-4.4682	0.1996	145	0.1444	2685	X-RAY DIFFRACTION	100
4.4682-4.8129	0.1793	147	0.1421	2694	X-RAY DIFFRACTION	100
4.8129-5.2967	0.1889	139	0.1522	2702	X-RAY DIFFRACTION	100
5.2967-6.0619	0.2154	150	0.1757	2710	X-RAY DIFFRACTION	100
6.0619-7.6326	0.235	129	0.1868	2775	X-RAY DIFFRACTION	100
7.6326-48.697	0.1688	159	0.1611	2847	X-RAY DIFFRACTION	99

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°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)
1	2.0705	0.1367	-0.2131	2.2201	0.8795	2.0764	-0.0017	-0.0181	0.1325	-0.0047	0.1058	-0.3503	-0.1452	0.2573	-0.0721	0.2607	-0.0007	0.0336	0.2807	-0.0214	0.3659	79.0072	98.5492	125.8214
2	1.1012	0.7951	0.1407	2.194	-0.2639	1.1943	0.1883	-0.2283	-0.0802	0.4276	-0.1443	-0.2232	0.097	0.0188	-0.0205	0.326	-0.0514	-0.0165	0.3392	-0.0161	0.3391	74.5114	84.8543	135.4508
3	0.7549	-0.0106	-0.2266	0.7807	0.5039	3.2346	0.0525	0.0792	0.0249	-0.0916	-0.136	0.1041	0.0267	-0.4141	0.0798	0.239	-0.008	-0.0146	0.281	-0.01	0.3086	59.9556	75.519	89.5987
4	1.9652	0.9305	0.9237	2.1549	1.1773	3.711	-0.0499	-0.1771	-0.084	0.1637	-0.0146	-0.1035	0.4455	-0.0743	0.0071	0.6333	-0.1175	-0.0116	0.5853	0.0433	0.5302	46.5454	15.2545	57.0996
5	3.6031	0.314	-0.0745	4.6516	-1.4439	4.7334	-0.2477	-0.1469	1.1676	-0.6139	0.0127	-0.31	-1.0236	0.238	0.1882	0.8126	0.0258	0.0121	0.5646	0.0842	0.8144	71.8339	106.8793	81.8386
6	8.2542	-1.6102	2.3417	0.9882	0.8187	6.8111	0.0216	0.878	1.2695	-1.1001	-0.262	0.4356	-1.6441	0.1775	0.356	1.0533	0.0884	-0.1721	0.4216	0.1038	1.0534	62.7571	108.5546	70.6433
7	5.5385	-1.2602	-2.2669	7.9236	-1.6327	3.6465	-0.0453	0.6812	0.9185	-0.8267	0.0446	-0.4627	-1.2931	0.7806	0.4087	0.8924	-0.1522	-0.026	0.6708	0.1797	0.7273	72.3822	102.342	72.2484
8	3.9055	0.9825	1.237	7.6179	-0.7734	5.4428	0.0774	0.5145	-0.1645	-0.5653	-0.2004	-0.3064	-0.1011	0.4762	-0.205	0.6966	-0.0182	0.045	0.6309	0.0446	0.6687	72.434	95.3801	75.8831
9	1.0263	-1.3472	-0.678	2.2204	1.0215	3.5232	0.0432	0.2259	-0.2917	0.3519	-0.1547	0.9292	-0.1609	-0.5265	0.119	0.7309	0.1833	0.0294	0.6228	0.12	0.8968	60.137	97.6406	82.9245
10	2.131	1.8278	0.9021	1.5703	0.7001	3.5879	0.1425	0.0784	-0.6912	-0.231	0.0021	0.5638	-0.0487	-0.0922	-0.0552	0.8765	0.1004	0.0389	0.78	-0.0686	0.857	59.9774	96.7988	72.7596
11	1.6633	-0.5674	0.3845	2.6659	1.2638	3.8672	-0.2441	0.1683	0.6689	0.1341	-0.6081	0.1545	-0.3806	-0.0722	0.8218	0.8442	0.0664	0.0666	0.6201	-0.0401	0.974	58.8627	107.4026	77.9868
12	2.3131	0.1254	0.0325	3.3414	0.4318	3.8415	0.0592	-0.2307	0.052	0.3088	0.1086	-0.2271	-0.3929	0.1407	-0.197	0.5204	-0.0928	0.1578	0.5137	-0.0446	0.4767	70.9662	92.8175	80.6518
13	1.2291	0.4914	0.2933	2.1435	-0.2461	2.3324	-0.0246	0.1511	-0.3041	-0.0728	0.0922	0.6329	0.4087	-0.7025	0.1157	0.3666	-0.0981	-0.0355	0.5388	-0.015	0.6993	-15.9647	-9.7248	19.0089
14	1.1439	0.1991	0.0275	2.5062	0.2119	2.7533	-0.2024	0.6449	-0.4386	-0.6295	0.2768	0.3064	0.1492	-0.1436	0.285	0.4324	-0.1123	-0.0924	0.5563	-0.0911	0.4502	-4.6496	-4.9322	7.5785
15	1.124	0.0096	0.2905	1.5305	1.0243	2.9568	-0.0365	0.5784	-0.4369	-0.3614	0.1795	-0.0265	0.1226	0.2867	0.1581	0.4585	-0.0592	-0.0077	0.5484	-0.1266	0.4699	4.7887	-8.4864	9.6124
16	1.3038	-0.1689	0.777	0.9495	-0.0876	2.7272	-0.2238	-0.2691	0.1446	0.2639	0.1609	0.0548	-0.3607	-0.1267	0.0027	0.3787	0.1071	0.0067	0.2898	0.0038	0.3406	8.7158	11.4625	53.8208
17	1.5301	-0.6663	1.1139	0.6326	-0.4299	2.0163	-0.262	-0.372	0.0516	0.1439	-0.0754	-0.3924	-0.4501	-0.0956	-0.3703	1.0263	-0.2988	-0.0731	0.7873	0.0029	0.8405	60.5027	44.3986	94.314
18	1.4632	0.502	0.9838	1.5002	0.1393	4.2751	-0.147	0.4483	0.0874	0.2806	0.0312	-0.0535	-0.6908	0.4594	-0.0779	0.9335	-0.2538	0.0174	0.7652	-0.0155	0.7342	61.8681	34.1791	84.374
19	1.524	-0.6538	-0.9395	1.1117	2.2864	5.796	-0.1797	-0.7775	0.1982	0.1173	0.0367	1.163	-0.6136	-1.4695	-0.2757	0.8331	0.1872	0.1996	1.8368	0.0429	1.3472	-23.0954	1.9339	63.1737
20	3.6152	2.028	0.8214	4.7974	-1.1288	3.0366	0.1925	-0.1102	-0.489	0.1352	-0.1632	0.1832	-0.1494	-1.4707	-0.0445	0.8715	0.0862	0.1466	1.2915	-0.1494	1.4445	-20.3452	-3.7224	62.8179
21	0.6938	-0.6517	-1.0047	0.6639	1.0222	1.5732	0.0683	-0.3512	-0.0253	0.4543	0.2812	0.143	-0.2184	-0.0486	-0.5224	1.5773	0.2657	0.1606	3.2279	0.3233	1.4811	-23.5857	9.516	73.2631
22	6.0271	4.3871	-0.2136	4.7257	-1.5353	1.4297	0.023	-0.391	-0.5989	0.6437	-0.1363	0.5489	0.1986	-1.4653	-0.4105	1.0537	0.2206	0.271	2.0717	0.2815	1.0602	-16.8773	-0.6926	72.6864
23	9.8795	0.5086	0.0608	4.5003	1.6244	6.5986	0.0088	-1.1454	-0.5934	0.5064	0.0738	0.5945	0.1934	-1.5962	-1.2674	0.747	0.0446	0.0654	1.3485	0.1131	0.8922	-10.8658	0.8876	67.782
24	3.3491	-2.2702	-0.2669	1.6642	0.3246	0.8022	0.0445	-0.4871	-0.1644	0.143	0.2777	0.0379	-0.1494	-0.5383	-0.5413	0.6692	0.4026	-0.1065	1.2553	-0.126	1.1718	-11.5079	10.7756	61.9227
25	3.1999	-1.1208	-0.4992	1.0121	0.6137	0.4237	0.0212	-0.6195	0.025	0.3335	0.1824	0.6158	-0.243	-0.6485	-0.3175	1.1872	0.4779	0.1569	2.3554	-0.1724	1.3902	-19.1132	12.2475	67.2635
26	2.2678	0.5305	0.253	2.4132	-1.5974	6.3596	-0.1789	-0.1881	-0.1827	0.1716	0.2881	0.7655	0.1101	-1.1404	0.0441	0.5993	0.0548	0.1565	1.0096	0.2852	0.6539	-7.5075	0.3697	63.7742

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 222 through 365 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 366 through 584 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 585 through 919 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 920 through 1058 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 1 through 16 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 17 through 22 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 23 through 34 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 35 through 44 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 45 through 49 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 50 through 54 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 55 through 65 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 66 through 76 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 223 through 372 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 373 through 480 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 481 through 584 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 585 through 919 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 920 through 978 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 979 through 1058 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 1 through 7 )
20	X-RAY DIFFRACTION	20	chain 'D' and (resid 8 through 16 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 17 through 22 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 23 through 34 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 35 through 45 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 46 through 50 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 51 through 65 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 66 through 76 )

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