PDB-6vzs: Engineered TTLL6 mutant bound to gamma-elongation analog

ID or keywords:

Entry

Database: PDB / ID: 6vzs

Title

Engineered TTLL6 mutant bound to gamma-elongation analog

Components

Tubulin polyglutamylase TTLL6

Keywords

LIGASE / protein engineering / TTLL6 / glutamylation / amino-acid ligase

Function / homology

Function and homology information

positive regulation of cilium movement / protein-glutamic acid ligase activity / tubulin-glutamic acid ligase activity / Carboxyterminal post-translational modifications of tubulin / protein polyglutamylation / 9+0 non-motile cilium / microtubule severing / regulation of cilium beat frequency involved in ciliary motility / Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) / microtubule bundle formation ...
Similarity search - Function

Biological species

Mus musculus (house mouse)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.66 Å

Authors

Mahalingan, K.K. / Keenen, E.K. / Strickland, M. / Li, Y. / Liu, Y. / Ball, H.L. / Tanner, M.E. / Tjandra, N. / Roll-Mecak, A.

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)	ZIA NS 003163	United States
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)	ZIA NS 003122	United States

Citation

Journal: Nat.Struct.Mol.Biol. / Year: 2020
Title: Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes.
Authors: Mahalingan, K.K. / Keith Keenan, E. / Strickland, M. / Li, Y. / Liu, Y. / Ball, H.L. / Tanner, M.E. / Tjandra, N. / Roll-Mecak, A.

History

Deposition	Feb 28, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 12, 2020	Provider: repository / Type: Initial release
Revision 1.1	Feb 10, 2021	Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2	Oct 11, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	6vzs.cif.gz	788.6 KB	Display	PDBx/mmCIF format
PDB format	pdb6vzs.ent.gz	543.9 KB	Display	PDB format
PDBx/mmJSON format	6vzs.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	6vzs_validation.pdf.gz	702.9 KB	Display	wwPDB validaton report
Full document	6vzs_full_validation.pdf.gz	705.8 KB	Display
Data in XML	6vzs_validation.xml.gz	3 KB	Display
Data in CIF	6vzs_validation.cif.gz	19.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/vz/6vzs ftp://data.pdbj.org/pub/pdb/validation_reports/vz/6vzs	HTTPS FTP

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Related structure data

Related structure data	6vzqC 6vzrC 6vztC 6vzuC 6vzvC 6vzwC 4ylrS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6vzr-3 6vzv-2 5kwk-1 5cih-1 6vzr-1 2pcb-1 3int-2 6vzv-3 6vzq-3 3bzn-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) 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

Related structure data

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Tubulin polyglutamylase TTLL6

B: Tubulin polyglutamylase TTLL6

C: Tubulin polyglutamylase TTLL6

D: Tubulin polyglutamylase TTLL6

hetero molecules

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

1

A: Tubulin polyglutamylase TTLL6

hetero molecules

defined by author&software
Evidence: gel filtration
55.2 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Tubulin polyglutamylase TTLL6

hetero molecules

defined by author&software
54.6 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

C: Tubulin polyglutamylase TTLL6

hetero molecules

defined by author&software
55.9 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

D: Tubulin polyglutamylase TTLL6

hetero molecules

defined by author&software
54.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	74.738, 108.648, 170.888
Angle α, β, γ (deg.)	90.000, 90.023, 90.000
Int Tables number	4
Space group name H-M	P12₁1
Space group name Hall	P2yb
Symmetry operation	#1: x,y,z #2: -x,y+1/2,-z

Noncrystallographic symmetry (NCS)

NCS domain:

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

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details	Auth asym-ID	Auth seq-ID
1	1	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	57 - 350
1	2	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	352 - 409
1	3	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	414 - 460
1	4	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	501
1	5	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	601
1	6	1	(chain 'A' and (resid 57 through 111 or (resid 112...	A	701
2	1	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	57 - 350
2	2	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	352 - 409
2	3	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	414 - 460
2	4	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	501
2	5	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	601
2	6	1	(chain 'B' and (resid 57 through 102 or (resid 103...	B	701
3	1	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	57 - 350
3	2	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	352 - 409
3	3	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	414 - 460
3	4	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	501
3	5	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	601
3	6	1	(chain 'C' and (resid 57 through 87 or (resid 88...	C	701
4	1	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	57 - 350
4	2	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	352 - 409
4	3	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	414 - 460
4	4	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	501
4	5	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	601
4	6	1	(chain 'D' and (resid 57 through 98 or (resid 99...	D	701

NCS ensembles :

ID
1
2
3
4

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Tubulin polyglutamylase TTLL6 / Tubulin--tyrosine ligase-like protein 6 Mass: 53345.398 Da / Num. of mol.: 4 / Mutation: C179A, Q180R, H362I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ttll6 / Production host: Escherichia coli (E. coli) / References: UniProt: A4Q9E8, Ligases

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Non-polymers , 5 types, 261 molecules

#2: Chemical	ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE Mass: 427.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₀H₁₅N₅O₁₀P₂ / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
#3: Chemical	ChemComp-S3A / (2~{S})-2-[[[(3~{R})-3-acetamido-4-oxidanyl-4-oxidanylidene-butyl]-phosphonooxy-phosphoryl]methyl]pentanedioic acid Mass: 433.242 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₂H₂₁NO₁₂P₂ / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical	... ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 33 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 212 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.24 Å³/Da / Density % sol: 62.11 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: 100 mM Sodium Citrate, pH 6.2, 200 mM MgCl2, 12 % Peg 20000 PH range: 6.0-6.5

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Data collection

Diffraction	Mean temperature: 100 K / Serial crystal experiment: N
Diffraction source	Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 0.9774 Å
Detector	Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: May 29, 2019
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9774 Å / Relative weight: 1
Reflection	Resolution: 2.66→45.84 Å / Num. obs: 155180 / % possible obs: 99.68 % / Redundancy: 2 % / B_iso Wilson estimate: 50.11 Å² / CC_1/2: 0.998 / CC star: 0.999 / R_merge(I) obs: 0.04598 / R_pim(I) all: 0.045 / R_rim(I) all: 0.06503 / Net I/σ(I): 8.69
Reflection shell	Resolution: 2.66→2.755 Å / Redundancy: 2 % / R_merge(I) obs: 0.3283 / Mean I/σ(I) obs: 2.03 / Num. unique obs: 15165 / CC_1/2: 0.872 / R_pim(I) all: 0.3283 / R_rim(I) all: 0.4643 / % possible all: 98.85

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Processing

Software

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

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4YLR

4ylr

Resolution: 2.66→45.84 Å / SU ML: 0.3735 / Cross valid method: FREE R-VALUE / σ(F): 0.03 / Phase error: 28.5018
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2

	R_factor	Num. reflection	% reflection
R_free	0.2555	7576	4.97 %
R_work	0.2185	144823	-
obs	0.2203	152399	98.64 %

Solvent computation

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

Displacement parameters

B_iso mean: 67.54 Å²

Refinement step

Cycle: LAST / Resolution: 2.66→45.84 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12358	0	422	212	12992

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.0015	13054
X-RAY DIFFRACTION	f_angle_d	0.49	17710
X-RAY DIFFRACTION	f_chiral_restr	0.0386	1932
X-RAY DIFFRACTION	f_plane_restr	0.0025	2233
X-RAY DIFFRACTION	f_dihedral_angle_d	17.7898	4591

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 (%)
2.66-2.69	0.408	225	0.385	4452	X-RAY DIFFRACTION	91.21
2.69-2.72	0.3622	231	0.3131	4823	X-RAY DIFFRACTION	98.5
2.72-2.75	0.3362	231	0.2933	4908	X-RAY DIFFRACTION	98.66
2.75-2.79	0.4383	199	0.2891	4839	X-RAY DIFFRACTION	99.1
2.79-2.83	0.2908	301	0.2809	4803	X-RAY DIFFRACTION	99.18
2.83-2.86	0.3267	261	0.2707	4979	X-RAY DIFFRACTION	99.39
2.86-2.91	0.3298	266	0.2892	4700	X-RAY DIFFRACTION	99.52
2.91-2.95	0.3509	291	0.2793	4878	X-RAY DIFFRACTION	99.38
2.95-3	0.3217	268	0.2677	4935	X-RAY DIFFRACTION	99.07
3-3.04	0.2971	250	0.254	4740	X-RAY DIFFRACTION	98.93
3.04-3.1	0.2988	249	0.2484	4898	X-RAY DIFFRACTION	98.92
3.1-3.15	0.2906	259	0.2489	4791	X-RAY DIFFRACTION	98.12
3.15-3.21	0.3038	270	0.2388	4800	X-RAY DIFFRACTION	97.91
3.21-3.28	0.2443	217	0.222	4844	X-RAY DIFFRACTION	98.41
3.28-3.35	0.2845	237	0.2218	4778	X-RAY DIFFRACTION	98.31
3.35-3.43	0.2633	244	0.2153	4875	X-RAY DIFFRACTION	98.8
3.43-3.51	0.2373	294	0.2292	4760	X-RAY DIFFRACTION	98.94
3.51-3.61	0.2312	311	0.2164	4846	X-RAY DIFFRACTION	99.52
3.61-3.72	0.2659	233	0.216	4871	X-RAY DIFFRACTION	98.72
3.72-3.84	0.252	279	0.1835	4757	X-RAY DIFFRACTION	99.15
3.84-3.97	0.2282	240	0.2072	4946	X-RAY DIFFRACTION	99.22
3.97-4.13	0.2599	222	0.1953	4873	X-RAY DIFFRACTION	98.66
4.13-4.32	0.2533	238	0.1846	4816	X-RAY DIFFRACTION	99
4.32-4.55	0.224	267	0.1793	4824	X-RAY DIFFRACTION	99.03
4.55-4.83	0.2109	290	0.1769	4815	X-RAY DIFFRACTION	99.71
4.83-5.2	0.2409	268	0.1876	4878	X-RAY DIFFRACTION	99.52
5.2-5.73	0.2076	223	0.2129	4942	X-RAY DIFFRACTION	99.37
5.73-6.55	0.2951	211	0.2286	4851	X-RAY DIFFRACTION	98.69
6.55-8.25	0.2505	266	0.2345	4840	X-RAY DIFFRACTION	99.26
8.25-45.84	0.1739	235	0.1858	4761	X-RAY DIFFRACTION	97.18

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	7.21819820053	2.18085489434	0.942136423283	5.06473288348	-1.75618862403	9.89639756463	0.171853615308	-0.688282165036	0.13249901442	0.841311686813	-0.0671409223074	0.798700092349	-0.499955749329	-0.875342163894	-0.0476964755089	0.367711851147	0.026389996291	0.129959500898	0.371136822834	0.0248943440336	0.612426599373	-1.62930068458	-25.2375284148	21.4379701377
2	2.60055740633	0.912472405193	0.197383299	3.44232176519	-0.467968586692	4.54930515499	0.226673567319	-0.42083476194	0.309127328897	0.575716081977	-0.224101925257	-0.845940286543	-0.127242380279	0.61617903975	0.0210714539201	0.341376818029	-0.0130037685305	-0.164669373274	0.396038456679	-0.0279207781707	0.741192453064	29.395202983	-9.49578038918	16.491871245
3	1.97576366211	-0.131715752432	-0.606781003178	2.17415104286	-0.430982302946	2.63687053092	0.00399442409048	0.0829705726365	-0.16073246019	0.217597169409	0.0127339940045	-0.223718497021	0.0990849561371	0.0404468676989	-0.0395103302955	0.224728577175	0.024765921406	-0.0636279986349	0.24892962531	-0.0301841246769	0.599463924383	19.6428419996	-23.2950330963	8.25833665993
4	2.93841714842	-0.320929668063	-0.722411404463	3.64840456695	-0.863085542589	2.66739708196	-0.165306264328	-0.56199856484	-0.484225616336	0.787208789611	0.00102686790234	0.0179232367485	0.440919306289	0.0235911144711	0.106003976196	0.55553217134	0.0265744102971	-0.0446342763822	0.361672078591	0.0683935811869	0.750997392576	12.1171754525	-33.8982213885	22.0240206731
5	3.46751622394	1.78722290787	2.85920514199	1.49045572341	2.11150785846	7.54389377496	0.104879978038	0.870956272661	0.167932185616	-1.23113788317	-0.210315695104	-0.513539320278	-0.414888102249	0.448863940728	0.195889783556	1.32165204382	0.172522941691	0.12863710306	0.666962322941	-0.0622712623933	0.470199320979	40.0068819485	-46.6343240709	65.0499913908
6	1.82759085992	-0.523631011059	-0.198153849891	2.36570961756	-0.308850750672	0.687154231036	0.121144281164	0.119280159853	-0.0469605933622	-0.457002850349	-0.0476376442883	0.253340859519	0.0800990561281	0.116110369201	-0.0765137859339	1.10142262318	0.00919375869168	-0.104082239316	0.458644766035	-0.042801905572	0.380518493773	16.2077011176	-40.6475920063	74.4008091901
7	0.0104249604182	-0.098160900004	0.00373249025849	0.691437381248	0.00416726104677	-0.00145896039875	-0.159079641194	-0.534033967371	0.369018216367	-0.205077071668	-0.282491419804	0.417383661973	-0.0504901595868	-0.62329599636	0.486115236655	2.13909674604	0.0752691307913	0.228330197059	0.818969242543	-0.556294852845	1.18006198758	31.3059231712	-60.5597308557	43.1287114224
8	2.97610914138	1.32864841052	1.38992637627	1.9272801308	2.97629013703	4.81606444954	0.161724764066	0.262465625697	-1.08239299729	-0.463453943849	0.0029073103232	0.314864228525	0.605133120129	0.113111905951	-0.154671090752	1.36433650083	0.0928744019187	-0.151226909022	0.495783435291	-0.108575398577	0.652491254392	19.1360211127	-60.6140840662	63.2413611478
9	7.72809954951	3.68924422842	-0.855658461813	9.89018817486	2.18554563965	5.58904820142	0.251346651125	-1.10686444861	-0.0663013518102	1.36184049545	-0.381581983269	-0.958124616686	0.163984534625	0.655800085106	0.163673573673	0.532533814391	-0.088053870557	-0.144030764077	0.473411046982	-0.0718847441771	0.670426088244	39.7532279875	22.176709097	20.7062926614
10	1.88000408754	-0.204825189979	-0.288398705207	1.97909081553	-0.436638285028	3.18147924468	0.184233994049	-0.345932179696	0.00379303643584	0.595657886771	0.00564527853807	0.961051285073	0.00427293964313	-0.518875299373	-0.143236198587	0.400001503058	-0.0122211920636	0.220964377641	0.376031766989	-0.0133220763403	0.748695432429	8.59479877073	7.1886608466	16.0996254169
11	2.36993996608	0.1943390919	0.639925597297	2.74894519868	0.191179325361	1.96944655134	0.0623983920259	-0.0122950666044	0.254298372526	0.359064828165	-0.0648928783027	0.114427390303	-0.120724088534	0.0426672269794	-0.00524330854435	0.268191478013	-0.00841290601571	0.108993567528	0.231653115754	-0.021896173499	0.568193307664	20.8137246655	21.4135954365	9.52528480014
12	2.21000989305	0.828181241956	-0.0500904654457	1.70345427913	1.42467663292	1.50865884046	0.362037423639	-0.588730825446	0.720185446211	1.17729751874	-0.334865613961	0.284039623525	-0.422182650652	-0.144749854973	-0.183850551502	1.03229918705	-0.0701801086593	0.124895800184	0.518854428217	-0.261308002949	0.940005145353	20.6244878722	36.3074827556	27.8884274502
13	2.06509570865	-2.85613703177	-6.13184938314	6.54696097389	0.61016742678	8.62791001904	-0.0589883652628	0.743391030473	-0.29215692601	-0.585004702439	-0.105782984842	0.495226505797	0.502399267162	-0.685516932705	0.127261673049	0.872461994947	-0.0681375393308	-0.129098419672	0.702782792713	0.0315270568001	0.458059205472	-1.60864715606	0.796255374644	63.7707552584
14	5.49371089971	-1.38383808486	-1.35987618201	2.18670598165	-0.118934554029	4.74409000206	0.149591832244	0.717995050579	-0.417090135803	-0.704330638471	-0.215213558952	-0.204544609762	0.287152229709	0.220623849972	0.0671086996314	1.04193609857	-0.0164918852266	0.119980792954	0.481073732619	-0.0811543672563	0.463972579916	29.0598371591	-14.5731267238	69.4213624176
15	2.8662978415	-0.119104443744	0.280377096592	2.73244673408	0.120339070094	0.969920952472	-0.0311167263786	0.107051580852	-0.0361325851397	-0.193473842089	0.057309695727	-0.175724480527	-0.0826857428845	-0.0736124051496	-0.030940731922	0.919536993177	0.00191874872684	0.0549556654862	0.40055799236	-0.0306117825826	0.357695440614	18.3643249009	-1.16009284534	77.0545551343
16	2.77793004799	1.39343777661	-1.75248733765	3.77181908078	-3.4606711896	3.26176872438	-0.0236207786953	0.431875985386	0.176312569052	-0.581876802077	0.161082059404	-0.0301011214863	-0.210900887724	-0.130608961396	-0.0964343470111	1.08068446509	-0.0573201038414	0.0931377578012	0.520325657557	-0.0436083910297	0.54588703896	11.7072521343	13.9653913862	57.8681130486

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	(chain A and resid 57:117)
2	X-RAY DIFFRACTION	2	(chain A and resid 118:208)
3	X-RAY DIFFRACTION	3	(chain A and resid 209:353)
4	X-RAY DIFFRACTION	4	(chain A and resid 354:460)
5	X-RAY DIFFRACTION	5	(chain B and resid 57:112)
6	X-RAY DIFFRACTION	6	(chain B and resid 113:394)
7	X-RAY DIFFRACTION	7	(chain B and resid 395:420)
8	X-RAY DIFFRACTION	8	(chain B and resid 421:460)
9	X-RAY DIFFRACTION	9	(chain C and resid 57:114)
10	X-RAY DIFFRACTION	10	(chain C and resid 115:210)
11	X-RAY DIFFRACTION	11	(chain C and resid 211:406)
12	X-RAY DIFFRACTION	12	(chain C and resid 407:460)
13	X-RAY DIFFRACTION	13	(chain D and resid 58:117)
14	X-RAY DIFFRACTION	14	(chain D and resid 118:210)
15	X-RAY DIFFRACTION	15	(chain D and resid 211:379)
16	X-RAY DIFFRACTION	16	(chain D and resid 380:460)

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