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- PDB-6vk8: Crystal Structure of Methylosinus trichosporium OB3b Soluble Meth... -

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Open data

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Basic information

Entry

Database: PDB / ID: 6vk8

Title

Crystal Structure of Methylosinus trichosporium OB3b Soluble Methane Monooxygenase Hydroxylase and Regulatory Component Complex with small organic carboxylate at active center

Components

(Methane monooxygenase ...) x 2
(Methane monooxygenase) x 2

Keywords

OXIDOREDUCTASE / Methane Monooxygenase Hydroxylase

Function / homology

Function and homology information

methane monooxygenase [NAD(P)H] activity / methane metabolic process / methane monooxygenase (soluble) / : / : / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen / : / monooxygenase activity / one-carbon metabolic process / metal ion binding
Similarity search - Function

Biological species

Methylosinus trichosporium OB3b (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

FOURIER SYNTHESIS / Resolution: 2.03 Å

Authors

Jones, J.C. / Banerjee, R. / Shi, K. / Aihara, H. / Lipscomb, J.D.

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	GM118030, GM08347	United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	GM118000, GM118047	United States

Citation

Journal: Biochemistry / Year: 2020
Title: Structural Studies of theMethylosinus trichosporiumOB3b Soluble Methane Monooxygenase Hydroxylase and Regulatory Component Complex Reveal a Transient Substrate Tunnel.
Authors: Jones, J.C. / Banerjee, R. / Shi, K. / Aihara, H. / Lipscomb, J.D.

History

Deposition	Jan 18, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 5, 2020	Provider: repository / Type: Initial release
Revision 1.1	Aug 26, 2020	Group: Database references / Category: citation / citation_author / Item: _citation.title / _citation_author.identifier_ORCID
Revision 1.2	Sep 2, 2020	Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3	Mar 6, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewer	Molecule: MolmilJmol/JSmol

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Downloads & links

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Download

PDBx/mmCIF format	6vk8.cif.gz	1.2 MB	Display	PDBx/mmCIF format
PDB format	pdb6vk8.ent.gz	813 KB	Display	PDB format
PDBx/mmJSON format	6vk8.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	6vk8_validation.pdf.gz	2.3 MB	Display	wwPDB validaton report
Full document	6vk8_full_validation.pdf.gz	2.3 MB	Display
Data in XML	6vk8_validation.xml.gz	95.2 KB	Display
Data in CIF	6vk8_validation.cif.gz	137.9 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/vk/6vk8 ftp://data.pdbj.org/pub/pdb/validation_reports/vk/6vk8	HTTPS FTP

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Related structure data

Related structure data	6vk4C 6vk5C 6vk6C 6vk7C C: citing same article (ref.)
Similar structure data	6vk4-d 4gam-2 6yy3-1 4gam-1 6vk5-d 6ydu-1 6yd0-1 6ydi-1 1yey-d 6ty8-d 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	#238 - Oct 2019 Ribonucleotide Reductase similarity (1)

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Assembly

Deposited unit

A: Methane monooxygenase component A alpha chain

B: Methane monooxygenase

C: Methane monooxygenase

D: Methane monooxygenase regulatory protein B

E: Methane monooxygenase component A alpha chain

F: Methane monooxygenase

G: Methane monooxygenase

H: Methane monooxygenase regulatory protein B

hetero molecules

281 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Idetical with deposited unit
defined by author&software
Evidence: gel filtration

Unit cell

Length a, b, c (Å)	101.866, 105.349, 297.720
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁
Space group name Hall	P2ac2ab
Symmetry operation	#1: x,y,z #2: x+1/2,-y+1/2,-z #3: -x,y+1/2,-z+1/2 #4: -x+1/2,-y,z+1/2

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID
1	1
2	1
1	2
2	2
1	3
2	3
1	4
2	4

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Selection details	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	ASP	ASP	GLY	GLY	(chain 'A' and (resid 12 through 315 or resid 317 through 526 or resid 801 through 802))	A	A	12 - 314	12 - 314
1	2	1	TRP	TRP	PHE	PHE	(chain 'A' and (resid 12 through 315 or resid 317 through 526 or resid 801 through 802))	A	A	317 - 526	317 - 526
2	1	1	ASP	ASP	GLY	GLY	(chain 'E' and (resid 12 through 315 or resid 317 through 526 or resid 801 through 802))	E	E	12 - 314	12 - 314
2	2	1	TRP	TRP	PHE	PHE	(chain 'E' and (resid 12 through 315 or resid 317 through 526 or resid 801 through 802))	E	E	317 - 526	317 - 526
1	1	2	PRO	PRO	LEU	LEU	(chain 'B' and (resid 4 through 320 or resid 322 through 395))	B	B	4 - 320	4 - 320
1	2	2	ALA	ALA	ASN	ASN	(chain 'B' and (resid 4 through 320 or resid 322 through 395))	B	B	322 - 395	322 - 395
2	1	2	PRO	PRO	LEU	LEU	(chain 'F' and (resid 4 through 320 or resid 322 through 395))	F	F	4 - 320	4 - 320
2	2	2	ALA	ALA	ASN	ASN	(chain 'F' and (resid 4 through 320 or resid 322 through 395))	F	F	322 - 395	322 - 395
1	1	3	ALA	ALA	GLN	GLN	chain 'C'	C	C	2 - 168	2 - 168
2	1	3	ALA	ALA	GLN	GLN	chain 'G'	G	G	2 - 168	2 - 168
1	1	4	SER	SER	ARG	ARG	chain 'D'	D	D	2 - 133	2 - 133
2	1	4	SER	SER	ARG	ARG	(chain 'H' and resid 2 through 133)	H	H	2 - 133	2 - 133

NCS ensembles :

ID
1
2
3
4

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Components

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Methane monooxygenase ... , 2 types, 4 molecules AEDH

#1: Protein	Methane monooxygenase component A alpha chain Mass: 60031.293 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Methylosinus trichosporium OB3b (bacteria) References: UniProt: A0A2D2D5X0, UniProt: P27353*PLUS
#4: Protein	Methane monooxygenase regulatory protein B Mass: 14896.885 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Methylosinus trichosporium OB3b (bacteria) References: UniProt: A0A2D2D0T8, UniProt: P27356*PLUS

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Protein , 2 types, 4 molecules BFCG

#2: Protein	Methane monooxygenase Mass: 45295.340 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Methylosinus trichosporium OB3b (bacteria) References: UniProt: A0A2D2D5X7
#3: Protein	Methane monooxygenase Mass: 19444.400 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Methylosinus trichosporium OB3b (bacteria) References: UniProt: A0A2D2D0T0

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Non-polymers , 5 types, 1412 molecules

#5: Chemical	ChemComp-FE / FE (III) ION Mass: 55.845 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical	ChemComp-SIN / SUCCINIC ACID Mass: 118.088 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄H₆O₄
#7: Chemical	... ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C₂H₆O₂
#8: Chemical	ChemComp-BEZ / BENZOIC ACID Mass: 122.121 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₇H₆O₂
#9: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1382 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y

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Experimental details

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.86 Å³/Da / Density % sol: 56.98 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: Tacsimate, PEG3350

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
Detector	Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 7, 2018
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9792 Å / Relative weight: 1
Reflection	Resolution: 2.03→101.87 Å / Num. obs: 203307 / % possible obs: 98.5 % / Redundancy: 4.1 % / B_iso Wilson estimate: 34.52 Å² / CC_1/2: 0.994 / R_merge(I) obs: 0.137 / Net I/σ(I): 7.9
Reflection shell	Resolution: 2.03→2.1 Å / Num. unique obs: 19824 / CC_1/2: 0.387 / R_pim(I) all: 1.105

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Processing

Software

Name	Version	Classification
PHENIX	1.17.1_3660	refinement
XDS		data reduction
PHENIX		phasing
PHENIX		data scaling
PHENIX		data processing

Refinement

Method to determine structure:

FOURIER SYNTHESIS / Resolution: 2.03→85.99 Å / SU ML: 0.2706 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 22.4855

	R_factor	Num. reflection	% reflection
R_free	0.2075	10347	5.11 %
R_work	0.1667	-	-
obs	0.1688	202365	97.85 %

Solvent computation

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

Displacement parameters

B_iso mean: 36.59 Å²

Refinement step

Cycle: LAST / Resolution: 2.03→85.99 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19484	0	117	1382	20983

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.0069	20120
X-RAY DIFFRACTION	f_angle_d	0.8363	27269
X-RAY DIFFRACTION	f_chiral_restr	0.0492	2859
X-RAY DIFFRACTION	f_plane_restr	0.0055	3517
X-RAY DIFFRACTION	f_dihedral_angle_d	16.4998	7217

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 (%)
2.03-2.05	0.3704	339	0.3313	6035	X-RAY DIFFRACTION	93.6
2.05-2.08	0.352	304	0.3241	6215	X-RAY DIFFRACTION	95.17
2.08-2.1	0.3133	376	0.2936	6247	X-RAY DIFFRACTION	97.3
2.1-2.13	0.3457	325	0.2999	6348	X-RAY DIFFRACTION	97.99
2.13-2.16	0.3226	364	0.2794	6373	X-RAY DIFFRACTION	98.35
2.16-2.19	0.3254	326	0.2731	6403	X-RAY DIFFRACTION	98.43
2.19-2.22	0.3155	336	0.2601	6358	X-RAY DIFFRACTION	98.48
2.22-2.25	0.3114	367	0.262	6359	X-RAY DIFFRACTION	97.83
2.25-2.29	0.2964	339	0.2408	6342	X-RAY DIFFRACTION	98.03
2.29-2.32	0.2752	340	0.2351	6335	X-RAY DIFFRACTION	97.18
2.32-2.36	0.2597	347	0.2205	6139	X-RAY DIFFRACTION	94.85
2.36-2.41	0.2452	346	0.206	6368	X-RAY DIFFRACTION	98.37
2.41-2.45	0.2488	352	0.1928	6400	X-RAY DIFFRACTION	98.93
2.45-2.5	0.2653	353	0.195	6411	X-RAY DIFFRACTION	98.87
2.5-2.56	0.2466	353	0.1769	6463	X-RAY DIFFRACTION	99
2.56-2.62	0.2358	310	0.1783	6502	X-RAY DIFFRACTION	98.95
2.62-2.68	0.2436	363	0.1676	6390	X-RAY DIFFRACTION	98.83
2.68-2.76	0.2043	358	0.161	6448	X-RAY DIFFRACTION	99.07
2.76-2.84	0.2001	354	0.1557	6477	X-RAY DIFFRACTION	98.96
2.84-2.93	0.1932	350	0.1624	6384	X-RAY DIFFRACTION	98.11
2.93-3.03	0.2203	341	0.1632	6262	X-RAY DIFFRACTION	96.03
3.03-3.15	0.2105	370	0.165	6300	X-RAY DIFFRACTION	96.91
3.15-3.3	0.2128	382	0.1636	6533	X-RAY DIFFRACTION	99.53
3.3-3.47	0.1986	323	0.1581	6499	X-RAY DIFFRACTION	99.01
3.47-3.69	0.2056	304	0.1502	6560	X-RAY DIFFRACTION	98.95
3.69-3.97	0.1627	301	0.1356	6518	X-RAY DIFFRACTION	98.24
3.97-4.37	0.1547	350	0.1204	6517	X-RAY DIFFRACTION	98.09
4.37-5.01	0.1466	332	0.1149	6454	X-RAY DIFFRACTION	96.75
5.01-6.31	0.1656	350	0.1287	6645	X-RAY DIFFRACTION	98.9
6.31-85.99	0.1492	392	0.1432	6733	X-RAY DIFFRACTION	96.78

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	1.86608035862	-0.270524195362	-1.17475353681	0.780064421259	0.18929694173	1.83272298892	-0.0862901565338	-0.269729585734	-0.3441907967	-0.0559524333318	0.000379801120201	0.01172076846	0.2591855483	0.196713705042	0.0810563060823	0.291449386183	0.0265417303083	-0.0445040008584	0.228843848266	0.055032567267	0.297209705795	-0.423060483051	-5.67764071287	37.2631343069
2	0.668956449997	0.146933919861	-0.411410660244	0.0613122036912	0.00554779506204	0.936019525339	-0.0224259740421	-0.00671653235359	-0.0970357800406	0.147091367538	0.00961080434125	0.0257771456342	0.175835820989	-0.00125770644098	-0.00389077506764	0.24366387718	0.0306316485421	-0.0275754811984	0.23288357479	-0.00281696527804	0.222346383489	10.9491794055	15.5435710422	31.2563817259
3	0.314963120797	0.335019889322	-0.0279785658041	0.35464121933	0.00261689501961	0.528777578527	0.0169541797522	0.00681320478757	-0.0766547133144	-0.00599326046885	0.00744523723315	-0.0597978297704	0.0820905830898	0.0540294990886	-0.0220760818633	0.232732899295	0.0317081357961	0.00142462355249	0.247320152004	-0.0176998101908	0.218882555809	17.5769611876	18.902864127	21.2296722439
4	0.971306263499	-0.797147463316	-0.197415175156	2.67051175352	-0.439239563976	0.916745702352	-0.0823978356156	0.00241850890805	-0.243184813132	-0.0784112197817	0.0219643084544	0.1174112828	0.343672900674	0.129891529799	0.0489508443294	0.320190667968	0.00150451237076	-0.00744064038274	0.368076316521	-0.0413121571903	0.298919764089	19.3267982402	9.96672497467	31.3132180413
5	0.603436973333	-0.0151625048801	0.170788869451	3.19752826756	-0.255543947081	0.454988718422	0.151109900468	0.0484913144988	-0.256217315638	-0.0576071488753	-0.313706856793	0.250992383387	0.159159348524	0.256425016402	0.145845664463	0.273974731814	0.0596172838738	0.0358136081615	0.293253442927	-0.0068320078742	0.316914942711	31.9123168005	12.1003952229	20.3276838869
6	0.412693559522	0.282306020963	-0.407332120271	0.630011387908	0.0130627944346	0.968509898992	0.0468886121688	-0.0681353028388	-0.138106586617	0.0518305708091	-0.0860141276148	-0.124328430611	0.166830999257	0.218963480716	0.0638025496654	0.248757401813	0.044400141942	0.00166738323146	0.292311535505	0.00794605346995	0.2717883605	36.2397487116	18.2176281446	26.4996975389
7	0.834651133829	0.0530470468741	0.105853379491	0.591233343565	-0.188913611631	1.23896767579	-0.0163407351377	0.0254283835878	0.0359344138425	0.0188412351232	0.00434535480563	-0.049267984874	-0.153937693876	0.153513922543	6.02160649555E-5	0.243085947377	0.0154515576094	0.0207167914461	0.255682673151	-0.0202256158888	0.23932125079	36.3983843528	38.4784365403	14.3434412252
8	0.419944651825	0.080687316936	-0.136316947936	0.529770616382	0.17565677681	0.119880815388	-0.00968411670733	0.106812267086	-0.0625932126269	0.00428064119296	0.0130396719502	-0.0200942275295	0.0368026378618	-0.00858488982351	-0.00616989893604	0.246945791791	0.0160076017312	0.0283549777557	0.258085582308	-0.0219028797411	0.245253445602	34.1527591239	18.540904673	2.71796484545
9	1.48888792297	-0.431991752399	-0.76521864205	0.877944781856	-0.183006028003	0.933290036373	0.0573269839779	0.248724078078	0.0066242440063	0.0185365189142	-0.0403526761975	-0.0637874670576	-0.235149375014	-0.00857297583994	-0.0100563214686	0.238689774814	-0.01834405911	0.00953814718236	0.278358095625	-0.000312041136495	0.223166438365	24.7633160967	37.3665492189	2.45759693723
10	0.957499378011	0.41436988678	-0.321206633607	1.33982232517	0.506767746951	0.925428078062	0.146608519297	-0.0443424038464	-0.0034095024346	0.084865155833	-0.0186330391226	-0.0280992513751	0.0103290737237	0.135132251644	-0.0798967186157	0.241188233471	0.0145465067827	7.91815463381E-5	0.21960231989	-0.0181776235398	0.228509755223	21.9985541272	41.1109096947	29.7597420437
11	0.270080182282	0.0289581726964	-0.131138130867	0.306034335183	-0.0843231888171	0.459788318322	-0.0160093733346	0.0337740170163	-0.079598570529	-0.0326384706196	0.0242451749682	0.00864103252101	0.122356243209	-0.0369938106198	-0.00854188053155	0.233868674904	0.00399508215761	-0.0176951714454	0.202420820564	-0.0131744502288	0.2246132931	-3.22399679413	4.3373229576	22.1167635414
12	0.828764839162	0.587351753768	-1.01807373202	0.750674364842	-0.829248832753	1.34577719441	0.00330052788976	0.195609269362	-0.112785532941	0.0135275039842	0.0796784180929	0.112396412269	0.107017777035	-0.269193528846	-0.0279296842747	0.31875192867	-0.0677975285391	-0.0256164948351	0.271831402131	-0.00999118920065	0.290742403245	-10.7512907186	-7.35456942409	11.051195075
13	0.96077407683	0.190678988189	-0.43585565517	1.01207186726	-0.317375970265	0.602370257391	-0.230810628016	0.323148403928	-0.203663115138	-0.185920223373	0.150494836119	0.0669668374507	0.249372250564	-0.52671576935	0.0629571424072	0.33638585563	-0.075347348531	-0.0228911142802	0.343043215303	-0.0174105946135	0.34069155534	-22.3380751172	-6.88086109629	15.6767139593
14	4.93497900698	-0.257088812727	-0.520432321268	3.8260441636	0.319932550983	3.44203122703	-0.0839053201199	0.32223786313	0.117309944691	-0.597321590263	0.0741462782896	0.092276925602	-0.289415375272	0.406938773392	-0.00123402226837	0.327317552457	-0.00667424277147	0.0300715807735	0.360405747041	-0.0054015173943	0.211612514116	19.3703668274	23.5778789343	-9.5664921895
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50	3.51989710986	-1.22348506159	-1.03913037546	4.74892428836	2.46608931416	3.7860007407	-0.0931976071088	0.499135836385	-0.474329769737	-0.608778763057	-0.234828058209	0.122891518924	-0.0224331962633	-0.409563638828	0.319596712485	0.373357938239	0.0200065128264	0.0168444368531	0.455681660525	-0.0439912982413	0.381487976812	-10.4504431274	39.4825501866	21.6464481592
51	0.776604957633	-0.574547439703	-0.844471595913	1.07149241195	0.569957257219	0.972346949555	-0.171844675974	0.054827124533	-0.391000226134	0.263276843224	-0.174144716665	0.410096834804	0.193126364081	-0.220036413534	0.339109853969	0.327576616835	-0.00943326740245	0.0449368364022	0.355419888866	-0.103585542752	0.406153193639	-13.6420764885	39.3794803971	30.3379693741
52	1.10470828784	0.671454064814	1.73102126864	0.566502401859	0.595911616563	4.00343700415	-0.17890842791	0.300002275475	-0.258141493823	-0.648947362034	-0.00963038988679	0.283693255954	-0.0075117771509	-0.789543366032	0.176586376903	0.586227537415	-0.0488460251179	-0.0741202755501	0.888085797159	-0.123304646529	0.571053938874	-30.2756079334	51.6551310757	28.9329714347

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 12 through 45 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 46 through 96 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 97 through 230 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 231 through 260 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 261 through 292 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 293 through 352 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 353 through 403 )
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 404 through 484 )
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 485 through 526 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 4 through 36 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 37 through 312 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 313 through 344 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 345 through 395 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 2 through 10 )
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 11 through 25 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 26 through 40 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 41 through 53 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 54 through 72 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 73 through 87 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 88 through 125 )
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 126 through 144 )
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 145 through 152 )
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 153 through 169 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 2 through 36 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 37 through 82 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 83 through 133 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 12 through 45 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 46 through 96 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 97 through 260 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 261 through 331 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 332 through 382 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 383 through 441 )
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 442 through 526 )
34	X-RAY DIFFRACTION	34	chain 'F' and (resid 4 through 36 )
35	X-RAY DIFFRACTION	35	chain 'F' and (resid 37 through 66 )
36	X-RAY DIFFRACTION	36	chain 'F' and (resid 67 through 312 )
37	X-RAY DIFFRACTION	37	chain 'F' and (resid 313 through 344 )
38	X-RAY DIFFRACTION	38	chain 'F' and (resid 345 through 395 )
39	X-RAY DIFFRACTION	39	chain 'G' and (resid 2 through 10 )
40	X-RAY DIFFRACTION	40	chain 'G' and (resid 11 through 25 )
41	X-RAY DIFFRACTION	41	chain 'G' and (resid 26 through 87 )
42	X-RAY DIFFRACTION	42	chain 'G' and (resid 88 through 125 )
43	X-RAY DIFFRACTION	43	chain 'G' and (resid 126 through 152 )
44	X-RAY DIFFRACTION	44	chain 'G' and (resid 153 through 169 )
45	X-RAY DIFFRACTION	45	chain 'H' and (resid 2 through 10 )
46	X-RAY DIFFRACTION	46	chain 'H' and (resid 11 through 36 )
47	X-RAY DIFFRACTION	47	chain 'H' and (resid 37 through 45 )
48	X-RAY DIFFRACTION	48	chain 'H' and (resid 46 through 63 )
49	X-RAY DIFFRACTION	49	chain 'H' and (resid 64 through 82 )
50	X-RAY DIFFRACTION	50	chain 'H' and (resid 83 through 95 )
51	X-RAY DIFFRACTION	51	chain 'H' and (resid 96 through 125 )
52	X-RAY DIFFRACTION	52	chain 'H' and (resid 126 through 138 )

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