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- PDB-2byr: CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA in complex wi... -

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Basic information

Entry
Database: PDB / ID: 2byr
TitleCRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA in complex with methyllycaconitine
ComponentsACETYLCHOLINE-BINDING PROTEIN
KeywordsRECEPTOR / NICOTINIC ACETYLCHOLINE RECEPTOR / METHYLLYCACONITINE
Function / homology
Function and homology information


extracellular ligand-gated monoatomic ion channel activity / transmembrane signaling receptor activity / membrane / identical protein binding / metal ion binding
Similarity search - Function
Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Distorted Sandwich / Mainly Beta
Similarity search - Domain/homology
METHYLLYCACONITINE / Soluble acetylcholine receptor
Similarity search - Component
Biological speciesAPLYSIA CALIFORNICA (California sea hare)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 Å
AuthorsHansen, S.B. / Sulzenbacher, G. / Huxford, T. / Marchot, P. / Taylor, P. / Bourne, Y.
CitationJournal: Embo J. / Year: 2005
Title: Structures of Aplysia Achbp Complexes with Nicotinic Agonists and Antagonists Reveal Distinctive Binding Interfaces and Conformations.
Authors: Hansen, S.B. / Sulzenbacher, G. / Huxford, T. / Marchot, P. / Taylor, P. / Bourne, Y.
History
DepositionAug 3, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 5, 2005Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Refinement description / Version format compliance
Revision 1.2Apr 3, 2019Group: Data collection / Other / Source and taxonomy
Category: entity_src_gen / pdbx_database_proc / pdbx_database_status
Item: _entity_src_gen.pdbx_host_org_cell_line / _pdbx_database_status.recvd_author_approval
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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 / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ACETYLCHOLINE-BINDING PROTEIN
B: ACETYLCHOLINE-BINDING PROTEIN
C: ACETYLCHOLINE-BINDING PROTEIN
D: ACETYLCHOLINE-BINDING PROTEIN
E: ACETYLCHOLINE-BINDING PROTEIN
F: ACETYLCHOLINE-BINDING PROTEIN
G: ACETYLCHOLINE-BINDING PROTEIN
H: ACETYLCHOLINE-BINDING PROTEIN
I: ACETYLCHOLINE-BINDING PROTEIN
J: ACETYLCHOLINE-BINDING PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,35520
Polymers258,52710
Non-polymers6,82810
Water10,016556
1
A: ACETYLCHOLINE-BINDING PROTEIN
B: ACETYLCHOLINE-BINDING PROTEIN
C: ACETYLCHOLINE-BINDING PROTEIN
D: ACETYLCHOLINE-BINDING PROTEIN
E: ACETYLCHOLINE-BINDING PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,67810
Polymers129,2645
Non-polymers3,4145
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18740 Å2
ΔGint-88.5 kcal/mol
Surface area44480 Å2
MethodPISA
2
F: ACETYLCHOLINE-BINDING PROTEIN
G: ACETYLCHOLINE-BINDING PROTEIN
H: ACETYLCHOLINE-BINDING PROTEIN
I: ACETYLCHOLINE-BINDING PROTEIN
J: ACETYLCHOLINE-BINDING PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,67810
Polymers129,2645
Non-polymers3,4145
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18360 Å2
ΔGint-90.7 kcal/mol
Surface area43810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.267, 135.776, 147.286
Angle α, β, γ (deg.)90.00, 99.46, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLNGLNLEULEU5AA3 - 1311 - 21
21GLNGLNLEULEU5BB3 - 1311 - 21
31GLNGLNLEULEU5CC3 - 1311 - 21
41GLNGLNLEULEU5DD3 - 1311 - 21
51GLNGLNLEULEU5EE3 - 1311 - 21
61GLNGLNLEULEU5FF3 - 1311 - 21
71GLNGLNLEULEU5GG3 - 1311 - 21
81GLNGLNLEULEU5HH3 - 1311 - 21
91GLNGLNLEULEU5II3 - 1311 - 21
101GLNGLNLEULEU5JJ3 - 1311 - 21
12PROPROPROPRO5AA21 - 2829 - 36
22PROPROPROPRO5BB21 - 2829 - 36
32PROPROPROPRO5CC21 - 2829 - 36
42PROPROPROPRO5DD21 - 2829 - 36
52PROPROPROPRO5EE21 - 2829 - 36
62PROPROPROPRO5FF21 - 2829 - 36
72PROPROPROPRO5GG21 - 2829 - 36
82PROPROPROPRO5HH21 - 2829 - 36
92PROPROPROPRO5II21 - 2829 - 36
102PROPROPROPRO5JJ21 - 2829 - 36
13LEULEUASPASP5AA29 - 4437 - 52
23LEULEUASPASP5BB29 - 4437 - 52
33LEULEUASPASP5CC29 - 4437 - 52
43LEULEUASPASP5DD29 - 4437 - 52
53LEULEUASPASP5EE29 - 4437 - 52
63LEULEUASPASP5FF29 - 4437 - 52
73LEULEUASPASP5GG29 - 4437 - 52
83LEULEUASPASP5HH29 - 4437 - 52
93LEULEUASPASP5II29 - 4437 - 52
103LEULEUASPASP5JJ29 - 4437 - 52
14THRTHRLYSLYS5AA47 - 6155 - 69
24THRTHRLYSLYS5BB47 - 6155 - 69
34THRTHRLYSLYS5CC47 - 6155 - 69
44THRTHRLYSLYS5DD47 - 6155 - 69
54THRTHRLYSLYS5EE47 - 6155 - 69
64THRTHRLYSLYS5FF47 - 6155 - 69
74THRTHRLYSLYS5GG47 - 6155 - 69
84THRTHRLYSLYS5HH47 - 6155 - 69
94THRTHRLYSLYS5II47 - 6155 - 69
104THRTHRLYSLYS5JJ47 - 6155 - 69
15LEULEUASNASN5AA62 - 7470 - 82
25LEULEUASNASN5BB62 - 7470 - 82
35LEULEUASNASN5CC62 - 7470 - 82
45LEULEUASNASN5DD62 - 7470 - 82
55LEULEUASNASN5EE62 - 7470 - 82
65LEULEUASNASN5FF62 - 7470 - 82
75LEULEUASNASN5GG62 - 7470 - 82
85LEULEUASNASN5HH62 - 7470 - 82
95LEULEUASNASN5II62 - 7470 - 82
105LEULEUASNASN5JJ62 - 7470 - 82
16ILEILESERSER3AA75 - 8183 - 89
26ILEILESERSER3BB75 - 8183 - 89
36ILEILESERSER3CC75 - 8183 - 89
46ILEILESERSER3DD75 - 8183 - 89
56ILEILESERSER3EE75 - 8183 - 89
66ILEILESERSER3FF75 - 8183 - 89
76ILEILESERSER3GG75 - 8183 - 89
86ILEILESERSER3HH75 - 8183 - 89
96ILEILESERSER3II75 - 8183 - 89
106ILEILESERSER3JJ75 - 8183 - 89
17ILEILELEULEU3AA85 - 10293 - 110
27ILEILELEULEU3BB85 - 10293 - 110
37ILEILELEULEU3CC85 - 10293 - 110
47ILEILELEULEU3DD85 - 10293 - 110
57ILEILELEULEU3EE85 - 10293 - 110
67ILEILELEULEU3FF85 - 10293 - 110
77ILEILELEULEU3GG85 - 10293 - 110
87ILEILELEULEU3HH85 - 10293 - 110
97ILEILELEULEU3II85 - 10293 - 110
107ILEILELEULEU3JJ85 - 10293 - 110
18ILEILEVALVAL3AA106 - 115114 - 123
28ILEILEVALVAL3BB106 - 115114 - 123
38ILEILEVALVAL3CC106 - 115114 - 123
48ILEILEVALVAL3DD106 - 115114 - 123
58ILEILEVALVAL3EE106 - 115114 - 123
68ILEILEVALVAL3FF106 - 115114 - 123
78ILEILEVALVAL3GG106 - 115114 - 123
88ILEILEVALVAL3HH106 - 115114 - 123
98ILEILEVALVAL3II106 - 115114 - 123
108ILEILEVALVAL3JJ106 - 115114 - 123
19PHEPHETHRTHR3AA117 - 130125 - 138
29PHEPHETHRTHR3BB117 - 130125 - 138
39PHEPHETHRTHR3CC117 - 130125 - 138
49PHEPHETHRTHR3DD117 - 130125 - 138
59PHEPHETHRTHR3EE117 - 130125 - 138
69PHEPHETHRTHR3FF117 - 130125 - 138
79PHEPHETHRTHR3GG117 - 130125 - 138
89PHEPHETHRTHR3HH117 - 130125 - 138
99PHEPHETHRTHR3II117 - 130125 - 138
109PHEPHETHRTHR3JJ117 - 130125 - 138
110THRTHRTHRTHR3AA139 - 158147 - 166
210THRTHRTHRTHR3BB139 - 158147 - 166
310THRTHRTHRTHR3CC139 - 158147 - 166
410THRTHRTHRTHR3DD139 - 158147 - 166
510THRTHRTHRTHR3EE139 - 158147 - 166
610THRTHRTHRTHR3FF139 - 158147 - 166
710THRTHRTHRTHR3GG139 - 158147 - 166
810THRTHRTHRTHR3HH139 - 158147 - 166
910THRTHRTHRTHR3II139 - 158147 - 166
1010THRTHRTHRTHR3JJ139 - 158147 - 166
111ASPASPSERSER5AA159 - 178167 - 186
211ASPASPSERSER5BB159 - 178167 - 186
311ASPASPSERSER5CC159 - 178167 - 186
411ASPASPSERSER5DD159 - 178167 - 186
511ASPASPSERSER5EE159 - 178167 - 186
611ASPASPSERSER5FF159 - 178167 - 186
711ASPASPSERSER5GG159 - 178167 - 186
811ASPASPSERSER5HH159 - 178167 - 186
911ASPASPSERSER5II159 - 178167 - 186
1011ASPASPSERSER5JJ159 - 178167 - 186
112ALAALAGLNGLN3AA179 - 184187 - 192
212ALAALAGLNGLN3BB179 - 184187 - 192
312ALAALAGLNGLN3CC179 - 184187 - 192
412ALAALAGLNGLN3DD179 - 184187 - 192
512ALAALAGLNGLN3EE179 - 184187 - 192
612ALAALAGLNGLN3FF179 - 184187 - 192
712ALAALAGLNGLN3GG179 - 184187 - 192
812ALAALAGLNGLN3HH179 - 184187 - 192
912ALAALAGLNGLN3II179 - 184187 - 192
1012ALAALAGLNGLN3JJ179 - 184187 - 192
113TYRTYRGLUGLU3AA195 - 206203 - 214
213TYRTYRGLUGLU3BB195 - 206203 - 214
313TYRTYRGLUGLU3CC195 - 206203 - 214
413TYRTYRGLUGLU3DD195 - 206203 - 214
513TYRTYRGLUGLU3EE195 - 206203 - 214
613TYRTYRGLUGLU3FF195 - 206203 - 214
713TYRTYRGLUGLU3GG195 - 206203 - 214
813TYRTYRGLUGLU3HH195 - 206203 - 214
913TYRTYRGLUGLU3II195 - 206203 - 214
1013TYRTYRGLUGLU3JJ195 - 206203 - 214

NCS oper:
IDCodeMatrixVector
1given(-0.93295, -0.28304, -0.22245), (-0.29329, 0.23928, 0.92559), (-0.20875, 0.92877, -0.30625)16.9609, -14.9647, -53.1359
2given(-0.93267, -0.27348, -0.2352), (-0.30014, 0.22674, 0.92655), (-0.20006, 0.93476, -0.29356)17.4744, -14.9729, -52.8857
3given(-0.94411, -0.2585, -0.20452), (-0.27039, 0.25247, 0.92905), (-0.18852, 0.93243, -0.30825)16.4878, -14.5193, -52.5635
4given(-0.93431, -0.28124, -0.219), (-0.28837, 0.23522, 0.92817), (-0.20953, 0.93035, -0.30088)17.1313, -14.8031, -53.1602
5given(-0.93563, -0.2815, -0.21294), (-0.2868, 0.25465, 0.92352), (-0.20575, 0.92515, -0.319)17.1127, -15.0974, -53.0729

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Components

#1: Protein
ACETYLCHOLINE-BINDING PROTEIN


Mass: 25852.744 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) APLYSIA CALIFORNICA (California sea hare)
Cell: SENSORY CELL / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) / Tissue (production host): KIDNEY / References: UniProt: Q8WSF8
#2: Chemical
ChemComp-MLK / METHYLLYCACONITINE / Methyllycaconitine


Mass: 682.800 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C37H50N2O10 / Comment: alkaloid*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 556 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.4 Å3/Da / Density % sol: 48 %
Crystal growpH: 7.5 / Details: 22% PEG 4K, 0.1 M TRIS, PH 7.5, 0.4 M MG2CL

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97563
DetectorType: ADSC CCD / Detector: CCD / Date: Dec 16, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97563 Å / Relative weight: 1
ReflectionResolution: 2.45→72 Å / Num. obs: 95739 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 45.4 Å2 / Rmerge(I) obs: 0.08 / Rsym value: 0.079 / Net I/σ(I): 11.3
Reflection shellResolution: 2.45→2.51 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 2.5 / Rsym value: 0.484 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BYN

2byn


Resolution: 2.45→20 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.922 / SU B: 15.962 / SU ML: 0.188 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.439 / ESU R Free: 0.252 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.232 1916 2 %RANDOM
Rwork0.193 ---
obs0.194 93613 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 40.84 Å2
Baniso -1Baniso -2Baniso -3
1-1.2 Å20 Å2-0.31 Å2
2--0.06 Å20 Å2
3----1.36 Å2
Refinement stepCycle: LAST / Resolution: 2.45→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16760 0 490 556 17806
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02218003
X-RAY DIFFRACTIONr_bond_other_d0.0010.0215759
X-RAY DIFFRACTIONr_angle_refined_deg1.3691.98924702
X-RAY DIFFRACTIONr_angle_other_deg0.734336833
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.38352091
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.66624.234855
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.303152909
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.95815117
X-RAY DIFFRACTIONr_chiral_restr0.0710.22809
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0219443
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023578
X-RAY DIFFRACTIONr_nbd_refined0.1860.23001
X-RAY DIFFRACTIONr_nbd_other0.1890.215634
X-RAY DIFFRACTIONr_nbtor_refined0.1790.28753
X-RAY DIFFRACTIONr_nbtor_other0.0840.210338
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1650.2779
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1360.210
X-RAY DIFFRACTIONr_symmetry_vdw_other0.1710.237
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2360.26
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9542.513650
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.1263.517350
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.5732.58775
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.82737351
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A515tight positional0.10.2
2B515tight positional0.110.2
3C515tight positional0.120.2
4D515tight positional0.090.2
5E515tight positional0.10.2
6F515tight positional0.150.2
7G515tight positional0.150.2
8H515tight positional0.130.2
9I515tight positional0.090.2
10J515tight positional0.10.2
1A488medium positional0.180.4
2B488medium positional0.150.4
3C488medium positional0.210.4
4D488medium positional0.140.4
5E488medium positional0.130.4
6F488medium positional0.230.4
7G488medium positional0.310.4
8H488medium positional0.230.4
9I488medium positional0.150.4
10J488medium positional0.20.4
1A1513loose positional0.495
2B1513loose positional0.45
3C1513loose positional0.585
4D1513loose positional0.55
5E1513loose positional0.465
6F1513loose positional0.75
7G1513loose positional0.635
8H1513loose positional0.65
9I1513loose positional0.525
10J1513loose positional0.565
1A515tight thermal0.482
2B515tight thermal0.472
3C515tight thermal0.352
4D515tight thermal0.392
5E515tight thermal0.482
6F515tight thermal0.382
7G515tight thermal0.312
8H515tight thermal0.282
9I515tight thermal0.332
10J515tight thermal0.392
1A488medium thermal1.284
2B488medium thermal0.824
3C488medium thermal0.664
4D488medium thermal0.574
5E488medium thermal0.644
6F488medium thermal0.74
7G488medium thermal0.724
8H488medium thermal0.654
9I488medium thermal0.714
10J488medium thermal0.654
1A1513loose thermal1.2610
2B1513loose thermal0.9810
3C1513loose thermal0.7410
4D1513loose thermal0.7910
5E1513loose thermal0.9210
6F1513loose thermal0.7810
7G1513loose thermal0.8610
8H1513loose thermal0.8110
9I1513loose thermal0.8210
10J1513loose thermal0.8410
LS refinement shellResolution: 2.45→2.51 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.338 140
Rwork0.277 6820
Refinement TLS params.

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

IDL11 (°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)
12.141-0.3130.10781.8105-0.35581.5554-0.0149-0.0358-0.0803-0.1408-0.0016-0.09440.08640.05120.0165-0.3128-0.02460.0355-0.3245-0.0297-0.25175.7068-15.5771-1.4009
21.9603-0.3370.32041.67240.06462.1483-0.0379-0.2182-0.04510.2320.0521-0.03630.04910.0041-0.0142-0.3014-0.03850.0228-0.27590.0313-0.2171-2.5895-21.363523.067
31.72690.23760.33331.9505-0.27122.0210.0193-0.12790.11090.3591-0.01140.0161-0.22510.033-0.008-0.14210.00130.0645-0.1776-0.0369-0.2492-6.24592.027836.1441
42.40050.6983-0.36862.176-0.14311.81590.0897-0.190.2590.2949-0.0807-0.0636-0.35720.0463-0.009-0.10410.0329-0.0035-0.3088-0.0338-0.1483-0.606822.23719.1675
51.5216-0.0756-0.3532.45710.03241.3291-0.0906-0.01290.0575-0.15680.0353-0.203-0.00530.0970.0553-0.2437-0.01780.0248-0.33670.0374-0.2246.935610.8578-4.3136
62.35330.27140.52261.95320.1292.7039-0.05240.342-0.2196-0.14890.06460.02020.18660.2285-0.0122-0.14810.08170.03140.029-0.106-0.143116.6714-22.0217-67.908
71.93690.10630.65912.42140.41742.5099-0.11940.15290.1233-0.31830.10310.0756-0.54460.20170.01630.0835-0.14120.03590.15480.0506-0.205520.32021.8817-79.2054
82.1981-0.5010.47752.07510.46822.2645-0.01420.19790.3156-0.2923-0.09740.2469-0.82410.02330.11160.4952-0.0742-0.0708-0.02620.1491-0.017214.976121.3241-60.9592
92.5320.47690.00362.0030.49392.45980.00580.05030.25710.0185-0.11780.3909-0.5644-0.19610.1120.09970.05090.0071-0.14430.0104-0.0897.05488.0583-38.009
102.03810.66260.36081.77870.82483.0055-0.00770.1376-0.17470.0883-0.09410.07790.2245-0.00810.1018-0.19070.06040.0328-0.1894-0.0047-0.20358.6027-18.1756-42.8488
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A-4 - 208
2X-RAY DIFFRACTION2B0 - 209
3X-RAY DIFFRACTION3C-2 - 208
4X-RAY DIFFRACTION4D-2 - 208
5X-RAY DIFFRACTION5E-5 - 208
6X-RAY DIFFRACTION6F0 - 208
7X-RAY DIFFRACTION7G3 - 207
8X-RAY DIFFRACTION8H1 - 207
9X-RAY DIFFRACTION9I-5 - 208
10X-RAY DIFFRACTION10J-3 - 208

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