PDB-2yns: rImp_alpha_B54NLS

ID or keywords:

Entry

Database: PDB / ID: 2yns

Title

rImp_alpha_B54NLS

Components

B54NLS
IMPORTIN SUBUNIT ALPHA-1A

Keywords

TRANSPORT PROTEIN / NUCLEAR LOCALIZATION SIGNAL

Function / homology

Function and homology information

NLS-bearing protein import into nucleus / nuclear localization sequence binding / nuclear import signal receptor activity / perinuclear region of cytoplasm / nucleus
Similarity search - Function

Biological species

ORYZA SATIVA (Asian cultivated rice)
SYNTHETIC CONSTRUCT (others)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.1 Å

Authors

Chang, C.-W. / Counago, R.L.M. / Williams, S.J. / Boden, M. / Kobe, B.

Citation

Journal: Plant Cell / Year: 2012
Title: Crystal Structure of Rice Importin-Alpha and Structural Basis of its Interaction with Plant-Specific Nuclear Localization Signals.
Authors: Chang, C.-W. / Counago, R.L.M. / Williams, S.J. / Boden, M. / Kobe, B.

History

Deposition	Oct 18, 2012	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jan 9, 2013	Provider: repository / Type: Initial release
Revision 1.1	Feb 20, 2013	Group: Database references
Revision 1.2	Mar 6, 2013	Group: Database references
Revision 1.3	Dec 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	2yns.cif.gz	336.7 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2yns_validation.pdf.gz	450 KB	Display	wwPDB validaton report
Full document	2yns_full_validation.pdf.gz	455.4 KB	Display
Data in XML	2yns_validation.xml.gz	30.5 KB	Display
Data in CIF	2yns_validation.cif.gz	43.6 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/yn/2yns ftp://data.pdbj.org/pub/pdb/validation_reports/yn/2yns	HTTPS FTP

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Related structure data

Related structure data	2ynrC 4b8jC 4b8oC 4b8pSC 4ba3C C: citing same article (ref.) S: Starting model for refinement
Similar structure data	4b8p-1 1bk6-1 4bqk-1 4b8j-d 4b8o-d 4zdu-d 4rxh-d 5oly-d 4xzr-d 4mz5-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) 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	#85 - Jan 2007 Importins similarity (11) #205 - Jan 2017 Nuclear Pore Complex similarity (2) #99 - Mar 2008 Cadherin similarity (4) #88 - Apr 2007 Clathrin similarity (2)

Deposited unit

A: IMPORTIN SUBUNIT ALPHA-1A

B: IMPORTIN SUBUNIT ALPHA-1A

C: B54NLS

D: B54NLS

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

1

A: IMPORTIN SUBUNIT ALPHA-1A

C: B54NLS

defined by author&software
54.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: IMPORTIN SUBUNIT ALPHA-1A

D: B54NLS

defined by author&software
54.4 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	62.242, 141.405, 73.325
Angle α, β, γ (deg.)	90.00, 90.17, 90.00
Int Tables number	4
Space group name H-M	P12₁1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID
1	1
2	1

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details
1	1	1	CHAIN A AND (RESSEQ 73:494 )
2	1	1	CHAIN B AND (RESSEQ 73:494 )

#1: Protein	IMPORTIN SUBUNIT ALPHA-1A Mass: 53026.848 Da / Num. of mol.: 2 / Fragment: NLS BINDING DOMAIN, RESIDUES 73-526 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ORYZA SATIVA (Asian cultivated rice) / Strain: JAPONICA GROUP / Plasmid: PET30A_IMPALPHA_DIBB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q71VM4
#2: Protein/peptide	B54NLS Mass: 1410.753 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SYNTHETIC CONSTRUCT (others) / Plasmid: PGEX2T-B54NLS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 164 / 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: 2.3 Å³/Da / Density % sol: 43 % / Description: NONE
Crystal grow	Details: 0.1 M BIS-TRISPROPANE PH 7.0, 15-17% PEG 3350 AND 0.2 M NAF

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Details: SILICON MIRRORS (ADAPTIVE AND U-BENT)
Radiation	Monochromator: DOUBLE CRYSTAL MONOCHROMATOR (SI111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9537 Å / Relative weight: 1
Reflection twin	Operator: h,-k,-l / Fraction: 0.5
Reflection	Resolution: 2.1→19.95 Å / Num. obs: 73652 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 6.1 % / B_iso Wilson estimate: 32.4 Å² / R_merge(I) obs: 0.11 / Net I/σ(I): 10.8
Reflection shell	Resolution: 2.1→2.21 Å / Redundancy: 5.7 % / R_merge(I) obs: 0.91 / Mean I/σ(I) obs: 2.1 / % possible all: 99.9

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
XDS		data reduction
SCALA		data scaling
MOLREP		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4B8P

4b8p

Resolution: 2.1→19.908 Å / σ(F): 1.34 / Phase error: 20.36 / Stereochemistry target values: TWIN_LSQ_F

	R_factor	Num. reflection	% reflection
R_free	0.1974	3719	5.1 %
R_work	0.1769	-	-
obs	0.1748	73622	99.89 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Displacement parameters

B_iso mean: 50.31 Å²

Refinement step

Cycle: LAST / Resolution: 2.1→19.908 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	6612	0	0	164	6776

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.014	6722
X-RAY DIFFRACTION	f_angle_d	1.681	9142
X-RAY DIFFRACTION	f_dihedral_angle_d	16.447	2482
X-RAY DIFFRACTION	f_chiral_restr	0.065	1092
X-RAY DIFFRACTION	f_plane_restr	0.01	1180

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Type	Rms dev position (Å)
1	1	A	3231	X-RAY DIFFRACTION	POSITIONAL
1	2	B	3231	X-RAY DIFFRACTION	POSITIONAL	0.563

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 (%)
2.1011-2.1373	0.2854	177	0.2726	3505	X-RAY DIFFRACTION	95
2.1373-2.1761	0.2894	193	0.2543	3460	X-RAY DIFFRACTION	95
2.1761-2.2179	0.263	175	0.2463	3527	X-RAY DIFFRACTION	95
2.2179-2.2631	0.244	187	0.2313	3398	X-RAY DIFFRACTION	95
2.2631-2.3122	0.2348	202	0.2296	3522	X-RAY DIFFRACTION	94
2.3122-2.3659	0.2243	182	0.2207	3457	X-RAY DIFFRACTION	95
2.3659-2.425	0.2273	172	0.2141	3484	X-RAY DIFFRACTION	95
2.425-2.4905	0.2604	171	0.1999	3528	X-RAY DIFFRACTION	95
2.4905-2.5636	0.2307	193	0.2046	3449	X-RAY DIFFRACTION	95
2.5636-2.6462	0.2471	182	0.1966	3461	X-RAY DIFFRACTION	95
2.6462-2.7405	0.204	178	0.1814	3528	X-RAY DIFFRACTION	95
2.7405-2.8499	0.2054	180	0.1877	3496	X-RAY DIFFRACTION	95
2.8499-2.9792	0.1952	178	0.1825	3474	X-RAY DIFFRACTION	95
2.9792-3.1357	0.2216	186	0.1797	3509	X-RAY DIFFRACTION	95
3.1357-3.3313	0.1962	162	0.1675	3514	X-RAY DIFFRACTION	96
3.3313-3.5871	0.1977	192	0.1626	3476	X-RAY DIFFRACTION	95
3.5871-3.9455	0.164	203	0.1458	3485	X-RAY DIFFRACTION	94
3.9455-4.5106	0.1526	201	0.1314	3491	X-RAY DIFFRACTION	95
4.5106-5.6609	0.1706	188	0.1499	3529	X-RAY DIFFRACTION	95
5.6609-19.8256	0.1725	210	0.1568	3516	X-RAY DIFFRACTION	94

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	0.0166	0.0194	0.0164	0.0235	0.0213	0.015	-0.0404	0.0049	0.0233	0.0304	-0.0204	0.0124	-0.0719	0.0254	-0.166	0.7002	-0.215	0.0345	0.1536	-0.0848	0.1721	54.5703	34.4747	25.0399
2	0.0039	0.0144	0.0067	0.0443	0.0232	0.0098	0.0103	0.0192	-0.0457	0.0196	0.0009	0.018	-0.0356	-0.008	0.0261	0.8357	-0.1499	0.0014	0.1494	-0.0588	0.2427	47.4941	30.1221	31.5449
3	0.0162	-0.0116	-0.0078	0.009	0.0043	0.0027	0.0417	-0.0136	-0.0658	0.0168	0.005	-0.0904	-0.1498	0.167	0.0011	0.5722	-0.2143	0.0546	0.3662	-0.0229	0.2988	55.2461	22.0046	26.5058
4	0.0063	-0.001	0.0011	0.002	-0.0051	0.0151	0.0134	0.0089	-0.031	-0.0041	0.0244	-0.0049	0.0299	0.0495	0.0536	1.2754	0.4801	0.1638	0.7102	0.0307	0.4952	54.4418	-104.4202	11.8442
5	0.0123	-0.0328	0.0239	0.0882	-0.0616	0.0452	-0.0272	-0.0294	0.0235	0.0257	-0.0485	0.028	0.0468	-0.0397	-0.0634	1.299	0.1824	0.0473	0.3919	-0.1724	0.4152	48.9357	-101.0382	5.4388
6	0.018	0.0097	0.0274	0.0107	0.0088	0.0412	-0.0259	-0.0063	-0.0067	0.1065	-0.0039	0.1323	-0.0315	0.0154	0.0061	0.9493	0.0502	-0.1477	0.172	-0.0775	0.4385	37.9231	-99.9648	10.5143
7	0.0175	0.0185	-0.0132	0.0441	-0.0214	0.0108	-0.0208	0.0364	0.0155	-0.0215	0.0209	0.0876	-0.0009	-0.0295	0.0436	0.4608	-0.1455	0.0793	0.0992	-0.0051	0.2169	40.935	21.4518	27.1222
8	0.0329	0.0146	-0.0377	0.0057	-0.0158	0.0391	0.0327	-0.0728	-0.0323	-0.1105	-0.0006	0.0593	-0.0896	0.1321	0.0073	0.3651	-0.0458	0.0898	0.1894	-0.0095	0.2657	44.0571	16.6514	19.1897
9	0.0413	0.0493	-0.0609	0.0538	-0.0644	0.0736	-0.0141	-0.0021	0.0315	-0.0668	0.1102	-0.0565	-0.0488	0.0249	0.0003	0.2352	-0.0471	0.0338	0.2594	-0.0103	0.2316	44.2074	9.6767	26.5513
10	0.0033	0.0028	0.003	0.0021	0.0017	0.0018	-0.0698	-0.0334	0.0362	-0.048	0.0402	-0.1207	0.0208	0.0085	-0	0.2635	-0.0072	-0.0979	0.4902	0.0235	0.3616	49.824	2.1735	38.1725
11	0.0104	0.0137	-0.012	0.0259	-0.0364	0.0435	0.0176	0.1198	-0.1233	0.1696	0.0487	0.1546	0.0224	0.0036	0.0001	0.2703	-0.034	0.0334	0.1754	0.0039	0.2066	36.8194	5.7594	31.3355
12	0.0051	0.0024	-0.0041	0.0003	-0.0001	0.0052	0.0904	0.0385	-0.0993	-0.2223	-0.143	-0.0912	-0.0263	-0.0376	0	0.2984	0.0391	0.0308	0.3389	-0.0054	0.2538	39.0065	-5.729	25.9999
13	0.0114	-0.0052	-0.0057	0.0131	0.0121	0.0108	-0.0595	0.025	-0.069	0.0966	-0.151	-0.005	-0.1149	0.1945	0	0.2411	-0.0334	0.029	0.2226	0.04	0.1607	34.4232	0.7191	38.826
14	0.1274	0.0743	-0.0353	0.0521	0.0022	0.0823	0.0182	0.0064	-0.1421	0.094	-0.0302	-0.0324	-0.0853	-0.0233	0.0107	0.2181	0.0054	0.0015	0.1641	0.006	0.177	24.8595	-8.0464	39.1444
15	0.0014	0.0032	0.0007	0.0038	0.002	0.0004	-0.0469	-0.0154	0.0304	0.0262	0.0117	0.0399	-0.0557	0.0435	-0	0.2317	-0.0057	-0.0195	0.3608	0.1043	0.3875	13.8957	-0.2682	39.0761
16	0.2679	0.0616	-0.0656	0.1534	-0.0611	0.0425	-0.0772	0.031	-0.133	0.1713	0.0063	0.0669	0.0685	-0.0296	-0.011	0.1975	-0.0024	0.014	0.063	0.0648	0.2728	11.0849	-13.4762	40.7505
17	0.0023	0.0014	-0.0007	0.0006	-0.0004	-0.0001	-0.0075	0.0236	-0.0263	0.0444	0.0316	-0.0006	-0.0657	0.0134	0	0.2374	0.042	-0.0276	0.2365	0.0621	0.2938	5.9761	-1.1059	35.8172
18	0.6661	-0.3112	0.1134	0.1463	-0.0392	0.1227	0.1866	0.2382	-0.2518	0.1311	-0.0005	-0.0245	0.1293	-0.0895	0.0832	0.2137	-0.022	-0.0263	0.168	0.0655	0.2831	1.4652	-14.1343	34.7558
19	0.019	-0.004	-0.0161	0.0014	0.0026	0.0117	0.0215	-0.0225	0.0235	-0.0497	0.0119	0.0036	0.0302	-0.0481	0.0235	0.2595	-0.1359	-0.1075	0.1637	0.0788	0.552	-7.4454	-29.6129	36.0652
20	0.0046	-0.0071	0.0077	0.0173	-0.0159	0.0153	0.0505	0.0021	-0.025	-0.0365	0.0665	-0.009	0.0213	-0.0727	0.0082	0.218	-0.0603	0.0133	0.453	0.0926	0.4797	-10.5915	-18.7946	38.9372
21	0.0221	0.0153	0.0195	0.0387	-0.0158	0.064	-0.0233	0.1073	-0.0555	-0.1026	0.0501	0.1163	-0.0035	-0.0091	0.031	0.1732	0.0407	-0.0615	0.4257	0.0631	0.3455	-9.3	-9.1055	25.5207
22	0.0034	0.0051	0.0019	0.0026	0.0015	0.0006	0.1093	0.0848	-0.0508	-0.0936	-0.0949	0.1221	0.0812	-0.0055	-0	0.3689	0.039	-0.1599	0.3501	-0.0001	0.3815	-9.105	-18.8305	23.9964
23	0.0276	0.0192	0.0036	0.0149	-0.0095	0.0664	-0.0008	0.0017	0.0105	-0.0141	-0.0236	-0.0254	0.0553	0.0663	-0.1165	0.8838	0.4645	-0.0194	0.4754	-0.0164	0.2449	54.4068	-92.4351	10.213
24	0.004	-0.0003	0.0058	0.027	-0.0297	0.039	-0.0303	-0.0477	0.0038	0.0504	0.0417	-0.0064	0.0102	-0.0206	0.1084	0.8489	0.1793	-0.1612	0.3447	-0.1873	0.2855	40.1606	-91.8995	9.5912
25	0.005	-0.0054	0.0001	0.0037	-0.0005	-0.0011	0.0778	-0.0698	-0.0329	-0.0139	0.1225	0.049	0.0657	-0.0772	-0	0.453	-0.0214	-0.0831	0.2108	-0.0449	0.3279	40.137	-89.339	19.1437
26	0.0226	-0.0052	-0.0046	0.0413	-0.0043	0.0163	0.0835	-0.0575	-0.1575	-0.1957	-0.0475	0.0208	0.3064	0.2469	0.0203	0.3839	0.0874	-0.0349	0.2466	-0.0117	0.1643	46.6287	-82.7661	7.5659
27	0.0216	-0.0126	0.0233	0.0078	-0.0118	0.0187	-0.0215	0.0441	0.0393	0.0651	-0.0517	-0.1368	-0.0686	-0.0815	-0	0.216	0.0593	-0.0024	0.1546	-0.026	0.171	40.8186	-75.3462	14.4156
28	0.2193	-0.1024	0.0258	0.1897	-0.0496	0.0135	0.1545	0.0071	0.029	-0.116	0.0985	0.0108	0.0313	0.0807	0.0438	0.2615	0.0495	0.0526	0.3796	-0.0632	0.2046	44.379	-76.2763	-2.1423
29	0.0043	-0.0056	0.0063	0.0066	-0.0075	0.0079	0.0313	0.039	0.0078	0.0348	0.089	0.0849	-0.0189	0.0015	0	0.2203	0.0554	0.0239	0.4529	0.032	0.1964	31.6352	-74.0205	10.9383
30	0.0305	-0.0339	0.0352	0.0725	-0.0218	0.0348	-0.0231	-0.0373	-0.0257	0.0509	0.0308	-0.0937	0.1109	0.1664	0	0.1703	0.0343	-0.0062	0.2804	0.0019	0.1919	35.0541	-69.1943	2.024
31	0.1246	-0.0801	-0.0103	0.0937	-0.0609	0.0944	0.0147	-0.1701	0.1477	0.04	-0.0218	0.0246	-0.0516	0.0493	-0.0009	0.1289	0.0237	-0.0029	0.2241	-0.0462	0.1697	24.8418	-61.6347	-1.7772
32	-0.0015	0.0016	0.0009	0.0108	0.0057	0.0019	0.0596	-0.0852	-0.0902	-0.0642	0.0523	0.0784	0.0421	-0.0004	0	0.3543	-0.0207	-0.0193	0.235	-0.0031	0.2389	13.5595	-71.8685	-5.5748
33	0.0941	-0.0688	-0.0291	0.0441	0.0191	0.0687	0.0782	-0.0653	0.2154	-0.0463	-0.0186	0.0171	-0.0025	-0.0397	0.0044	0.1417	0.0296	0.0192	0.2646	0.0052	0.1978	10.2602	-57.1218	-4.0657
34	0.0043	-0.0029	-0.0022	0.0014	0.0016	0.0003	0.03	-0.0404	0.022	-0.0118	0.078	0.0304	0.0956	-0.0231	0	0.231	0.0263	0.0883	0.3562	0.1076	0.3521	5.0972	-69.2944	0.8174
35	0.0729	0.0089	0.0001	0.0826	0.1165	0.1516	0.146	-0.1672	0.2546	0.0366	0.0108	0.1822	-0.1268	-0.3031	0.019	0.1682	0.0401	0.0476	0.3861	0.012	0.2752	0.7603	-56.7209	1.6962
36	0.032	-0.0321	0.0354	0.093	-0.0132	0.0529	0.0193	0.0685	0.0561	0.0359	0.0544	0.0083	-0.0188	-0.0202	0.0382	0.2814	0.1097	0.1628	0.4244	-0.0668	0.56	-4.8369	-43.4001	2.4527
37	0.0077	0.0027	0.0225	0.0113	0.0289	0.1118	0.0333	-0.0653	0.1395	-0.0312	-0.0489	0.0259	-0.0217	-0.2106	0.0105	0.2012	0.098	0.0565	0.6509	0.0943	0.4369	-12.4978	-52.8467	1.3302
38	0.003	-0.0012	-0.0039	0.0051	-0.0016	0.0054	0.0282	-0.0315	-0.022	0.0152	0.0874	-0.0121	-0.0099	-0.0619	0	0.3147	-0.0861	0.0452	0.8567	-0.0199	0.3046	-7.2123	-61.8507	17.5197
39	0.0051	-0.0072	0.0095	0.0071	-0.0114	0.0156	0.0692	-0.0015	0.0392	0.0177	-0.0179	0.027	-0.0867	-0.0204	0.0304	0.3907	0.0291	0.1846	0.464	-0.1798	0.3937	-10.0471	-50.8328	11.9901

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN A AND (RESID 73 THROUGH 88 )
2	X-RAY DIFFRACTION	2	CHAIN A AND (RESID 89 THROUGH 102 )
3	X-RAY DIFFRACTION	3	CHAIN A AND (RESID 118 THROUGH 135 )
4	X-RAY DIFFRACTION	4	CHAIN B AND (RESID 74 THROUGH 88 )
5	X-RAY DIFFRACTION	5	CHAIN B AND (RESID 89 THROUGH 99 )
6	X-RAY DIFFRACTION	6	CHAIN B AND (RESID 100 THROUGH 117 )
7	X-RAY DIFFRACTION	7	CHAIN A AND (RESID 136 THROUGH 148 )
8	X-RAY DIFFRACTION	8	CHAIN A AND (RESID 149 THROUGH 165 )
9	X-RAY DIFFRACTION	9	CHAIN A AND (RESID 166 THROUGH 204 )
10	X-RAY DIFFRACTION	10	CHAIN A AND (RESID 205 THROUGH 214 )
11	X-RAY DIFFRACTION	11	CHAIN A AND (RESID 215 THROUGH 235 )
12	X-RAY DIFFRACTION	12	CHAIN A AND (RESID 236 THROUGH 246 )
13	X-RAY DIFFRACTION	13	CHAIN A AND (RESID 247 THROUGH 269 )
14	X-RAY DIFFRACTION	14	CHAIN A AND (RESID 270 THROUGH 340 )
15	X-RAY DIFFRACTION	15	CHAIN A AND (RESID 341 THROUGH 348 )
16	X-RAY DIFFRACTION	16	CHAIN A AND (RESID 349 THROUGH 381 )
17	X-RAY DIFFRACTION	17	CHAIN A AND (RESID 382 THROUGH 389 )
18	X-RAY DIFFRACTION	18	CHAIN A AND (RESID 390 THROUGH 439 )
19	X-RAY DIFFRACTION	19	CHAIN A AND (RESID 440 THROUGH 455 )
20	X-RAY DIFFRACTION	20	CHAIN A AND (RESID 456 THROUGH 463 )
21	X-RAY DIFFRACTION	21	CHAIN A AND (RESID 464 THROUGH 481 )
22	X-RAY DIFFRACTION	22	CHAIN A AND (RESID 482 THROUGH 494 )
23	X-RAY DIFFRACTION	23	CHAIN B AND (RESID 118 THROUGH 135 )
24	X-RAY DIFFRACTION	24	CHAIN B AND (RESID 136 THROUGH 148 )
25	X-RAY DIFFRACTION	25	CHAIN B AND (RESID 149 THROUGH 160 )
26	X-RAY DIFFRACTION	26	CHAIN B AND (RESID 161 THROUGH 188 )
27	X-RAY DIFFRACTION	27	CHAIN B AND (RESID 189 THROUGH 207 )
28	X-RAY DIFFRACTION	28	CHAIN B AND (RESID 208 THROUGH 224 )
29	X-RAY DIFFRACTION	29	CHAIN B AND (RESID 225 THROUGH 234 )
30	X-RAY DIFFRACTION	30	CHAIN B AND (RESID 235 THROUGH 268 )
31	X-RAY DIFFRACTION	31	CHAIN B AND (RESID 269 THROUGH 336 )
32	X-RAY DIFFRACTION	32	CHAIN B AND (RESID 337 THROUGH 347 )
33	X-RAY DIFFRACTION	33	CHAIN B AND (RESID 348 THROUGH 381 )
34	X-RAY DIFFRACTION	34	CHAIN B AND (RESID 382 THROUGH 389 )
35	X-RAY DIFFRACTION	35	CHAIN B AND (RESID 390 THROUGH 436 )
36	X-RAY DIFFRACTION	36	CHAIN B AND (RESID 437 THROUGH 449 )
37	X-RAY DIFFRACTION	37	CHAIN B AND (RESID 450 THROUGH 473 )
38	X-RAY DIFFRACTION	38	CHAIN B AND (RESID 474 THROUGH 482 )
39	X-RAY DIFFRACTION	39	CHAIN B AND (RESID 483 THROUGH 494 )

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