PDB-4u0d: Hexameric HIV-1 CA in complex with Nup153 peptide, P212121 crysta...

ID or keywords:

Entry

Database: PDB / ID: 4u0d

Title

Hexameric HIV-1 CA in complex with Nup153 peptide, P212121 crystal form

Components

Gag polyprotein
Nuclear pore complex protein Nup153

Keywords

VIRAL PROTEIN / Capsid

Function / homology

Function and homology information

negative regulation of RNA export from nucleus / nuclear pore complex assembly / 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 ...negative regulation of RNA export from nucleus / nuclear pore complex assembly / 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 / Rev-mediated nuclear export of HIV RNA / structural constituent of nuclear pore / SUMOylation of RNA binding proteins / 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 / RNA export from nucleus / nucleocytoplasmic transport / Viral Messenger RNA Synthesis / nuclear localization sequence binding / SUMOylation of ubiquitinylation proteins / viral budding via host ESCRT complex / Vpr-mediated nuclear import of PICs / SUMOylation of DNA replication proteins / Regulation of HSF1-mediated heat shock response / mRNA transport / SUMOylation of DNA damage response and repair proteins / nuclear pore / protein-membrane adaptor activity / SUMOylation of chromatin organization proteins / nuclear periphery / HCMV Late Events / molecular condensate scaffold activity / Transcriptional regulation by small RNAs / ISG15 antiviral mechanism / host multivesicular body / HCMV Early Events / viral penetration into host nucleus / protein import into nucleus / host cell / nuclear envelope / snRNP Assembly / viral nucleocapsid / nuclear membrane / amyloid fibril formation / symbiont entry into host cell / host cell nucleus / nucleolus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / host cell plasma membrane / structural molecule activity / virion membrane / DNA binding / RNA binding / zinc ion binding / nucleoplasm / identical protein binding / membrane / metal ion binding / cytosol
Similarity search - Function

Biological species

Human immunodeficiency virus type 1 group M subtype B

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 3 Å

Authors

Price, A.J. / Jacques, D.A. / James, L.C.

Citation

Journal: Plos Pathog. / Year: 2014
Title: Host Cofactors and Pharmacologic Ligands Share an Essential Interface in HIV-1 Capsid That Is Lost upon Disassembly.
Authors: Price, A.J. / Jacques, D.A. / McEwan, W.A. / Fletcher, A.J. / Essig, S. / Chin, J.W. / Halambage, U.D. / Aiken, C. / James, L.C.

History

Deposition	Jul 11, 2014	Deposition site: RCSB / Processing site: PDBE
Revision 1.0	Nov 12, 2014	Provider: repository / Type: Initial release
Revision 1.1	Dec 20, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4u0d.cif.gz	955.8 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	4u0d_validation.pdf.gz	505.1 KB	Display	wwPDB validaton report
Full document	4u0d_full_validation.pdf.gz	511.2 KB	Display
Data in XML	4u0d_validation.xml.gz	76.4 KB	Display
Data in CIF	4u0d_validation.cif.gz	102.5 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/u0/4u0d ftp://data.pdbj.org/pub/pdb/validation_reports/u0/4u0d	HTTPS FTP

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Related structure data

Related structure data	4u0aC 4u0bC 4u0cC 4u0eC 4u0fC 3h47S C: citing same article (ref.) S: Starting model for refinement
Similar structure data	3h4e-1 4wym-2 5tsx-1 5tsx-2 6bht-2 6bht-1 4wym-1 5tsv-1 3h4e-2 4qnb-1 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	#205 - Jan 2017 Nuclear Pore Complex similarity (26) #230 - Feb 2019 Initiation Factor eIF4E similarity (3) #234 - Jun 2019 MDM2 and Cancer similarity (6) #163 - Jul 2013 HIV Capsid similarity (4) #85 - Jan 2007 Importins similarity (4) #31 - Jul 2002 p53 Tumor Suppressor similarity (5) #87 - Mar 2007 Zinc Fingers similarity (2) #260 - Aug 2021 Ribonuclease P similarity (1) #73 - Jan 2006 Topoisomerase similarity (1) #150 - Jun 2012 Sliding Clamps similarity (1) #240 - Dec 2019 Hypoxia-Inducible Factors similarity (1) #62 - Feb 2005 Major Histocompatibility Complex similarity (1) #165 - Sep 2013 Designed Protein Cages similarity (1) #33 - Sep 2002 HIV Reverse Transcriptase similarity (1) #6 - Jun 2000 HIV-1 Protease similarity (1) #160 - Apr 2013 Actinomycin similarity (1) #213 - Sep 2017 Sirtuins similarity (1) #55 - Jul 2004 DNA Ligase similarity (1) #98 - Feb 2008 Small Interfering RNA similarity (1) #241 - Jan 2020 Twenty Years of Molecules similarity (3)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#205 - Jan 2017
Nuclear Pore Complex
similarity (26)
#230 - Feb 2019
Initiation Factor eIF4E
similarity (3)
#234 - Jun 2019
MDM2 and Cancer
similarity (6)
#163 - Jul 2013
HIV Capsid
similarity (4)
#85 - Jan 2007
Importins
similarity (4)
#31 - Jul 2002
p53 Tumor Suppressor
similarity (5)
#87 - Mar 2007
Zinc Fingers
similarity (2)
#260 - Aug 2021
Ribonuclease P
similarity (1)
#73 - Jan 2006
Topoisomerase
similarity (1)
#150 - Jun 2012
Sliding Clamps
similarity (1)
#240 - Dec 2019
Hypoxia-Inducible Factors
similarity (1)
#62 - Feb 2005
Major Histocompatibility Complex
similarity (1)
#165 - Sep 2013
Designed Protein Cages
similarity (1)
#33 - Sep 2002
HIV Reverse Transcriptase
similarity (1)
#6 - Jun 2000
HIV-1 Protease
similarity (1)
#160 - Apr 2013
Actinomycin
similarity (1)
#213 - Sep 2017
Sirtuins
similarity (1)
#55 - Jul 2004
DNA Ligase
similarity (1)
#98 - Feb 2008
Small Interfering RNA
similarity (1)
#241 - Jan 2020
Twenty Years of Molecules
similarity (3)

Deposited unit

A: Gag polyprotein

B: Gag polyprotein

C: Gag polyprotein

D: Gag polyprotein

E: Gag polyprotein

F: Gag polyprotein

G: Gag polyprotein

H: Gag polyprotein

I: Gag polyprotein

J: Gag polyprotein

K: Gag polyprotein

L: Gag polyprotein

M: Nuclear pore complex protein Nup153

N: Nuclear pore complex protein Nup153

O: Nuclear pore complex protein Nup153

P: Nuclear pore complex protein Nup153

Q: Nuclear pore complex protein Nup153

R: Nuclear pore complex protein Nup153

hetero molecules

316 kDa, 18 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Gag polyprotein

B: Gag polyprotein

C: Gag polyprotein

D: Gag polyprotein

E: Gag polyprotein

F: Gag polyprotein

M: Nuclear pore complex protein Nup153

O: Nuclear pore complex protein Nup153

P: Nuclear pore complex protein Nup153

hetero molecules

defined by author&software
158 kDa, 9 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

G: Gag polyprotein

H: Gag polyprotein

I: Gag polyprotein

J: Gag polyprotein

K: Gag polyprotein

L: Gag polyprotein

N: Nuclear pore complex protein Nup153

Q: Nuclear pore complex protein Nup153

R: Nuclear pore complex protein Nup153

defined by author&software
158 kDa, 9 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	135.380, 138.060, 211.850
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:
NCS ensembles :

ID
1
2
3

Details

biological unit is the same as asym.

#1: Protein	Gag polyprotein / Pr55Gag Mass: 25461.271 Da / Num. of mol.: 12 / Mutation: yes Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B Strain: isolate NY5 / Gene: gag / Plasmid: pET11a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P12493
#2: Protein/peptide	Nuclear pore complex protein Nup153 / 153 kDa nucleoporin / Nucleoporin Nup153 Mass: 1687.721 Da / Num. of mol.: 6 / Fragment: UNP residues 1407-1423 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P49790
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.14 Å³/Da / Density % sol: 60.78 %
Crystal grow	Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 10% w/v PEG 8K, 0.1M imidazole

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

Diamond

/ Beamline: I04-1 / Wavelength: 0.92 Å

Detector

Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jan 20, 2014

Radiation

Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.92 Å / Relative weight: 1

Reflection

Resolution: 3→46.07 Å / Num. obs: 77432 / Redundancy: 3.2 % / R_merge(I) obs: 0.101 / Net I/σ(I): 8.6

Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Mean I/σ(I) obs	Num. measured all	Num. unique all	CC_1/2	R_pim(I) all	% possible all
3-3.06	3.1	0.664	1.7	13499	4390	0.577	0.436	97.3
15.3-46.07	3.3	0.021	33.8	2154	651	0.999	0.014	95.1

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Phasing

Phasing

Method:

molecular replacement

Phasing MR

Model details: Phaser MODE: MR_AUTO

	Highest resolution	Lowest resolution
Rotation	3 Å	46.07 Å
Translation	3 Å	46.07 Å

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Processing

Software

Name	Version	Classification
Aimless	0.2.7	data scaling
PDB_EXTRACT	3.14	data extraction
PHASER		phasing
iMOSFLM		data reduction
REFMAC	5.8.0073	refinement

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 3H47

3h47

Resolution: 3→115.67 Å / Cor.coef. F_o:F_c: 0.911 / Cor.coef. F_o:F_c free: 0.901 / WR_factor R_free: 0.2402 / WR_factor R_work: 0.2209 / FOM work R set: 0.7754 / SU B: 46.735 / SU ML: 0.376 / SU R Cruickshank DPI: 0.3986 / SU R_free: 0.4221 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.422 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.267	3884	5 %	RANDOM
R_work	0.2457	73490	-	-
obs	0.2468	77374	96.6 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK

Displacement parameters

B_iso max: 209.14 Å² / B_iso mean: 77.183 Å² / B_iso min: 33.36 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-0.02 Å²	0 Å²	0 Å²
2-	-	1.14 Å²	-0 Å²
3-	-	-	-1.12 Å²

Refinement step

Cycle: final / Resolution: 3→115.67 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19254	0	1	0	19255
B_iso mean	-	-	58.41	-	-
Num. residues	-	-	-	-	2512

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.004	0.019	19708
X-RAY DIFFRACTION	r_bond_other_d	0.001	0.02	18755
X-RAY DIFFRACTION	r_angle_refined_deg	0.651	1.959	26808
X-RAY DIFFRACTION	r_angle_other_deg	0.656	3	43214
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	4.526	5.016	2480
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	26.511	24.901	812
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	10.163	15	3266
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	8.949	15	103
X-RAY DIFFRACTION	r_chiral_restr	0.036	0.2	3059
X-RAY DIFFRACTION	r_gen_planes_refined	0.003	0.021	22048
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	4179
X-RAY DIFFRACTION	r_mcbond_it	1.286	6.12	10012
X-RAY DIFFRACTION	r_mcbond_other	1.285	6.12	10011
X-RAY DIFFRACTION	r_mcangle_it	2.263	10.306	12440

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	1180	MEDIUM POSITIONAL	0.12	0.5
1	2	B	1180	MEDIUM POSITIONAL	0.1	0.5
1	3	C	1180	MEDIUM POSITIONAL	0.07	0.5
1	4	D	1180	MEDIUM POSITIONAL	0.08	0.5
1	5	E	1180	MEDIUM POSITIONAL	0.24	0.5
1	6	F	1180	MEDIUM POSITIONAL	0.08	0.5
1	7	G	1180	MEDIUM POSITIONAL	0.14	0.5
1	8	H	1180	MEDIUM POSITIONAL	0.12	0.5
1	9	I	1180	MEDIUM POSITIONAL	0.07	0.5
1	10		1180	MEDIUM POSITIONAL	0.08	0.5
1	11	A	1180	MEDIUM POSITIONAL	0.07	0.5
1	12	B	1180	MEDIUM POSITIONAL	0.07	0.5
1	1	A	1180	MEDIUM THERMAL	7.42	2
1	2	B	1180	MEDIUM THERMAL	6.78	2
1	3	C	1180	MEDIUM THERMAL	6.02	2
1	4	D	1180	MEDIUM THERMAL	5.42	2
1	5	E	1180	MEDIUM THERMAL	6.47	2
1	6	F	1180	MEDIUM THERMAL	5.09	2
1	7	G	1180	MEDIUM THERMAL	5.24	2
1	8	H	1180	MEDIUM THERMAL	8.1	2
1	9	I	1180	MEDIUM THERMAL	6.98	2
1	10		1180	MEDIUM THERMAL	5.58	2
1	11	A	1180	MEDIUM THERMAL	14.5	2
1	12	B	1180	MEDIUM THERMAL	11.4	2
2	1	A	871	LOOSE POSITIONAL	0.31	5
2	2	B	871	LOOSE POSITIONAL	0.35	5
2	3	C	871	LOOSE POSITIONAL	0.32	5
2	4	D	871	LOOSE POSITIONAL	0.33	5
2	5	E	871	LOOSE POSITIONAL	0.54	5
2	6	F	871	LOOSE POSITIONAL	0.57	5
2	7	G	871	LOOSE POSITIONAL	0.65	5
2	8	H	871	LOOSE POSITIONAL	0.35	5
2	9	I	871	LOOSE POSITIONAL	0.22	5
2	10		871	LOOSE POSITIONAL	0.22	5
2	11	A	871	LOOSE POSITIONAL	0.28	5
2	12	B	871	LOOSE POSITIONAL	0.43	5
2	1	A	871	LOOSE THERMAL	6.56	10
2	2	B	871	LOOSE THERMAL	10.86	10
2	3	C	871	LOOSE THERMAL	3.01	10
2	4	D	871	LOOSE THERMAL	10.28	10
2	5	E	871	LOOSE THERMAL	11.47	10
2	6	F	871	LOOSE THERMAL	10.54	10
2	7	G	871	LOOSE THERMAL	14.49	10
2	8	H	871	LOOSE THERMAL	5.81	10
2	9	I	871	LOOSE THERMAL	6.58	10
2	10		871	LOOSE THERMAL	14.97	10
2	11	A	871	LOOSE THERMAL	22.25	10
2	12	B	871	LOOSE THERMAL	8.81	10
3	1	A	681	MEDIUM POSITIONAL	0.09	0.5
3	2	B	681	MEDIUM POSITIONAL	0.06	0.5
3	3	C	681	MEDIUM POSITIONAL	0.08	0.5
3	4	D	681	MEDIUM POSITIONAL	0.08	0.5
3	5	E	681	MEDIUM POSITIONAL	0.1	0.5
3	6	F	681	MEDIUM POSITIONAL	0.1	0.5
3	7	G	681	MEDIUM POSITIONAL	0.1	0.5
3	8	H	681	MEDIUM POSITIONAL	0.09	0.5
3	9	I	681	MEDIUM POSITIONAL	0.07	0.5
3	10		681	MEDIUM POSITIONAL	0.06	0.5
3	11	A	681	MEDIUM POSITIONAL	0.08	0.5
3	12	B	681	MEDIUM POSITIONAL	0.09	0.5
3	1	A	681	MEDIUM THERMAL	10.44	2
3	2	B	681	MEDIUM THERMAL	5.42	2
3	3	C	681	MEDIUM THERMAL	4.83	2
3	4	D	681	MEDIUM THERMAL	3.47	2
3	5	E	681	MEDIUM THERMAL	8.36	2
3	6	F	681	MEDIUM THERMAL	4.46	2
3	7	G	681	MEDIUM THERMAL	5.6	2
3	8	H	681	MEDIUM THERMAL	11.75	2
3	9	I	681	MEDIUM THERMAL	4.6	2
3	10		681	MEDIUM THERMAL	6.02	2
3	11	A	681	MEDIUM THERMAL	14.32	2
3	12	B	681	MEDIUM THERMAL	13.65	2

LS refinement shell

Resolution: 3→3.078 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.39	252	-
R_work	0.365	5439	-
all	-	5691	-
obs	-	-	96.93 %

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	1.0213	0.0293	-0.352	2.9373	0.5315	3.5548	-0.0033	0.0324	0.2198	-0.0293	0.0135	-0.4005	-0.4745	0.249	-0.0103	0.1635	-0.051	-0.1089	0.1382	0.0553	0.2033	-35.5389	-30.8352	9.5396
2	2.5381	-0.456	-2.0783	2.1314	0.9484	3.6231	-0.1492	-0.429	0.2477	0.1814	0.1522	-0.0874	-0.0774	0.3179	-0.0031	0.2128	0.0862	-0.172	0.1042	-0.0814	0.1518	-40.4188	-29.4798	37.4783
3	2.4769	0.8769	0.1193	1.9104	0.6104	1.9651	-0.1349	-0.524	0.2929	0.2162	0.0683	0.1049	-0.0932	-0.396	0.0666	0.1633	0.1852	0.0201	0.3321	-0.0209	0.0973	-56.7586	-47.1484	48.9212
4	2.2574	-0.0218	0.8246	0.5525	-0.3166	3.5812	-0.0968	0.0255	-0.2473	-0.0227	0.1636	0.0459	0.3288	-1.0155	-0.0668	0.0529	-0.0937	0.0224	0.3792	0.0106	0.0526	-71.0031	-64.7469	33.7449
5	0.9775	-0.4784	0.5773	0.8523	-1.0501	6.3262	0.0612	0.0273	-0.0983	-0.0401	0.0898	0.0939	0.8407	-0.5008	-0.1509	0.1522	-0.1132	-0.0122	0.1824	0.0337	0.0494	-67.8825	-64.5145	6.1992
6	1.0993	0.9055	0.5861	4.0687	-0.2168	1.8734	-0.0687	0.1269	-0.0693	-0.2503	-0.0176	-0.0529	-0.0794	0.0319	0.0863	0.0289	-0.0008	-0.0078	0.171	0.0293	0.029	-50.2339	-48.0406	-5.7548
7	4.753	0.2221	0.5426	0.8727	-0.4644	1.7094	0.0767	-0.1893	0.1003	0.0048	-0.0287	0.0202	0.0284	-0.0052	-0.048	0.0494	0.0341	0.0137	0.1569	0.0907	0.0683	-13.2656	-85.4122	58.7519
8	3.9562	-0.378	0.1933	1.4066	0.4032	3.2742	0.011	0.2653	0.7743	-0.0792	-0.0989	-0.3637	-0.2963	0.5226	0.0879	0.0907	0.0027	0.0482	0.3014	0.2633	0.3757	2.8652	-70.1945	44.1887
9	1.8109	0.7344	-0.4646	2.8023	0.8234	4.202	0.1825	0.2962	0.0515	-0.43	-0.3234	-0.4698	-0.1642	0.3981	0.1409	0.2149	0.2954	0.2379	0.5212	0.375	0.3008	4.5844	-74.547	16.9582
10	1.3259	0.7539	-0.0947	3.1274	-0.2116	2.787	0.1067	0.3446	-0.1873	-0.7472	-0.3517	-0.314	1.049	0.1623	0.2449	0.7072	0.3653	0.1918	0.3636	0.0911	0.107	-11.5281	-90.7985	4.7147
11	0.8836	0.2993	-0.1821	3.3134	-1.7129	4.0844	0.2921	0.11	-0.0314	-0.5025	0.0175	0.2251	1.4935	-0.4485	-0.3096	0.8644	-0.0568	-0.1094	0.2044	0.0618	0.0429	-28.8262	-105.5092	18.7843
12	1.0899	-0.608	1.1874	1.3208	-0.4798	7.934	0.1241	-0.0442	0.0367	-0.1655	-0.0068	-0.0472	0.7008	-1.2311	-0.1173	0.1943	-0.1631	-0.0677	0.2755	0.0809	0.0544	-28.823	-103.4586	46.9323

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 219
2	X-RAY DIFFRACTION	2	B	1 - 219
3	X-RAY DIFFRACTION	3	C	1 - 219
4	X-RAY DIFFRACTION	4	D	1 - 219
5	X-RAY DIFFRACTION	5	E	1 - 219
6	X-RAY DIFFRACTION	6	F	1 - 219
7	X-RAY DIFFRACTION	7	G	1 - 219
8	X-RAY DIFFRACTION	8	H	1 - 999
9	X-RAY DIFFRACTION	9	I	1 - 219
10	X-RAY DIFFRACTION	10	J	1 - 219
11	X-RAY DIFFRACTION	11	K	1 - 219
12	X-RAY DIFFRACTION	12	L	1 - 219

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