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- PDB-2r1d: Crystal structure of rat neurexin 1beta in the Ca2+ containing form -

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Basic information

Entry
Database: PDB / ID: 2r1d
TitleCrystal structure of rat neurexin 1beta in the Ca2+ containing form
ComponentsNeurexin-1-beta
KeywordsCELL ADHESION / SPLICING / beta-sandwich
Function / homology
Function and homology information


protein-containing complex assembly involved in synapse maturation / : / positive regulation of presynaptic active zone assembly / cell-cell adhesion involved in synapse maturation / guanylate kinase-associated protein clustering / protein complex involved in cell-cell adhesion / positive regulation of neuromuscular synaptic transmission / neuron to neuron synapse / neuroligin clustering involved in postsynaptic membrane assembly / regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission ...protein-containing complex assembly involved in synapse maturation / : / positive regulation of presynaptic active zone assembly / cell-cell adhesion involved in synapse maturation / guanylate kinase-associated protein clustering / protein complex involved in cell-cell adhesion / positive regulation of neuromuscular synaptic transmission / neuron to neuron synapse / neuroligin clustering involved in postsynaptic membrane assembly / regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission / type 1 fibroblast growth factor receptor binding / trans-synaptic signaling, modulating synaptic transmission / trans-synaptic protein complex / negative regulation of filopodium assembly / gephyrin clustering involved in postsynaptic density assembly / cerebellar granule cell differentiation / slit diaphragm / postsynaptic density protein 95 clustering / postsynaptic membrane assembly / synapse maturation / gamma-aminobutyric acid receptor clustering / vocal learning / presynaptic membrane assembly / neuroligin family protein binding / positive regulation of synapse maturation / maintenance of synapse structure / regulation of grooming behavior / synaptic vesicle clustering / presynapse assembly / synaptic membrane adhesion / regulation of postsynaptic specialization assembly / positive regulation of fibroblast growth factor receptor signaling pathway / receptor localization to synapse / neuron cell-cell adhesion / NMDA glutamate receptor clustering / inhibitory synapse / calcium-dependent cell-cell adhesion / vocalization behavior / regulation of postsynaptic density assembly / protein localization to synapse / acetylcholine receptor binding / neurotransmitter secretion / regulation of synaptic vesicle cycle / AMPA selective glutamate receptor signaling pathway / positive regulation of synapse assembly / NMDA selective glutamate receptor signaling pathway / heterophilic cell-cell adhesion / neuromuscular process controlling balance / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / adult behavior / excitatory synapse / endocytic vesicle / social behavior / positive regulation of excitatory postsynaptic potential / regulation of presynapse assembly / prepulse inhibition / positive regulation of synaptic transmission, glutamatergic / axonal growth cone / synapse assembly / cell adhesion molecule binding / neuron projection morphogenesis / presynaptic active zone membrane / cellular response to calcium ion / positive regulation of synaptic transmission, GABAergic / learning / positive regulation of protein localization to plasma membrane / calcium channel regulator activity / neuromuscular junction / establishment of protein localization / positive regulation of neuron projection development / circadian rhythm / GABA-ergic synapse / Schaffer collateral - CA1 synapse / neuron projection development / calcium-dependent protein binding / transmembrane signaling receptor activity / presynaptic membrane / angiogenesis / nuclear membrane / vesicle / chemical synaptic transmission / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / signaling receptor binding / negative regulation of gene expression / neuronal cell body / calcium ion binding / positive regulation of gene expression / protein-containing complex binding / glutamatergic synapse / cell surface / endoplasmic reticulum / signal transduction / protein-containing complex / plasma membrane
Similarity search - Function
Syndecan/Neurexin domain / Syndecan domain / Neurexin/syndecan/glycophorin C / putative band 4.1 homologues' binding motif / : / Laminin G domain / Laminin G domain profile. / Laminin G domain / Laminin G domain / Jelly Rolls - #200 ...Syndecan/Neurexin domain / Syndecan domain / Neurexin/syndecan/glycophorin C / putative band 4.1 homologues' binding motif / : / Laminin G domain / Laminin G domain profile. / Laminin G domain / Laminin G domain / Jelly Rolls - #200 / Concanavalin A-like lectin/glucanase domain superfamily / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.6 Å
AuthorsRudenko, G.
CitationJournal: Structure / Year: 2008
Title: Regulation of Neurexin 1beta Tertiary Structure and Ligand Binding through Alternative Splicing
Authors: Shen, K.C. / Kuczynska, D.A. / Wu, I.J. / Murray, B.H. / Sheckler, L.R. / Rudenko, G.
History
DepositionAug 22, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 1, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 25, 2017Group: Refinement description / Category: software
Revision 1.3Aug 30, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / 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_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Neurexin-1-beta
B: Neurexin-1-beta
C: Neurexin-1-beta
D: Neurexin-1-beta
E: Neurexin-1-beta
F: Neurexin-1-beta
G: Neurexin-1-beta
H: Neurexin-1-beta
I: Neurexin-1-beta
W: Neurexin-1-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)243,33213
Polymers243,21210
Non-polymers1203
Water2,036113
1
A: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Neurexin-1-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,3612
Polymers24,3211
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Neurexin-1-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,3612
Polymers24,3211
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
7
G: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
8
H: Neurexin-1-beta


Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
9
I: Neurexin-1-beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,3612
Polymers24,3211
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
10
W: Neurexin-1-beta


  • defined by author&software
  • 24.3 kDa, 1 polymers
Theoretical massNumber of molelcules
Total (without water)24,3211
Polymers24,3211
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)116.683, 195.719, 103.867
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101A
111B
121C
131D
141E
151F
161G
171H
181I
191A
201B
211C
221D
231E
241F
251G
261H
271I
281A
291B
301C
311D
321E
331F
341G
351H
361I
371A
381B
391C
401D
411E
421F
431G
441H
451I
461A
471B
481C
491D
501E
511F
521G
531H
541I
551A
561B
571C
581D
591E
601F
611G
621H
631I
641A
651B
661C
671D
681E
691F
701G
711H
721I
731A
741B
751C
761D
771E
781F
791G
801H
811I
821A
831B
841C
851D
861E
871F
881G
891H
901I

NCS domain segments:

Ens-ID: 1 / Refine code: 4

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11TYRTYRPHEPHEAA41 - 4341 - 43
21TYRTYRPHEPHEBB41 - 4341 - 43
31TYRTYRPHEPHECC41 - 4341 - 43
41TYRTYRPHEPHEDD41 - 4341 - 43
51TYRTYRPHEPHEEE41 - 4341 - 43
61TYRTYRPHEPHEFF41 - 4341 - 43
71TYRTYRPHEPHEGG41 - 4341 - 43
81TYRTYRPHEPHEHH41 - 4341 - 43
91TYRTYRPHEPHEII41 - 4341 - 43
102TYRTYRTRPTRPAA52 - 5452 - 54
112TYRTYRTRPTRPBB52 - 5452 - 54
122TYRTYRTRPTRPCC52 - 5452 - 54
132TYRTYRTRPTRPDD52 - 5452 - 54
142TYRTYRTRPTRPEE52 - 5452 - 54
152TYRTYRTRPTRPFF52 - 5452 - 54
162TYRTYRTRPTRPGG52 - 5452 - 54
172TYRTYRTRPTRPHH52 - 5452 - 54
182TYRTYRTRPTRPII52 - 5452 - 54
193ARGARGSERSERAA59 - 8659 - 86
203ARGARGSERSERBB59 - 8659 - 86
213ARGARGSERSERCC59 - 8659 - 86
223ARGARGSERSERDD59 - 8659 - 86
233ARGARGSERSEREE59 - 8659 - 86
243ARGARGSERSERFF59 - 8659 - 86
253ARGARGSERSERGG59 - 8659 - 86
263ARGARGSERSERHH59 - 8659 - 86
273ARGARGSERSERII59 - 8659 - 86
284LEULEUHISHISAA89 - 9889 - 98
294LEULEUHISHISBB89 - 9889 - 98
304LEULEUHISHISCC89 - 9889 - 98
314LEULEUHISHISDD89 - 9889 - 98
324LEULEUHISHISEE89 - 9889 - 98
334LEULEUHISHISFF89 - 9889 - 98
344LEULEUHISHISGG89 - 9889 - 98
354LEULEUHISHISHH89 - 9889 - 98
364LEULEUHISHISII89 - 9889 - 98
375ILEILEPHEPHEAA102 - 106102 - 106
385ILEILEPHEPHEBB102 - 106102 - 106
395ILEILEPHEPHECC102 - 106102 - 106
405ILEILEPHEPHEDD102 - 106102 - 106
415ILEILEPHEPHEEE102 - 106102 - 106
425ILEILEPHEPHEFF102 - 106102 - 106
435ILEILEPHEPHEGG102 - 106102 - 106
445ILEILEPHEPHEHH102 - 106102 - 106
455ILEILEPHEPHEII102 - 106102 - 106
466ASPASPSERSERAA112 - 118112 - 118
476ASPASPSERSERBB112 - 118112 - 118
486ASPASPSERSERCC112 - 118112 - 118
496ASPASPSERSERDD112 - 118112 - 118
506ASPASPSERSEREE112 - 118112 - 118
516ASPASPSERSERFF112 - 118112 - 118
526ASPASPSERSERGG112 - 118112 - 118
536ASPASPSERSERHH112 - 118112 - 118
546ASPASPSERSERII112 - 118112 - 118
557ASPASPARGARGAA124 - 134124 - 134
567ASPASPARGARGBB124 - 134124 - 134
577ASPASPARGARGCC124 - 134124 - 134
587ASPASPARGARGDD124 - 134124 - 134
597ASPASPARGARGEE124 - 134124 - 134
607ASPASPARGARGFF124 - 134124 - 134
617ASPASPARGARGGG124 - 134124 - 134
627ASPASPARGARGHH124 - 134124 - 134
637ASPASPARGARGII124 - 134124 - 134
648ALAALAARGARGAA139 - 151139 - 151
658ALAALAARGARGBB139 - 151139 - 151
668ALAALAARGARGCC139 - 151139 - 151
678ALAALAARGARGDD139 - 151139 - 151
688ALAALAARGARGEE139 - 151139 - 151
698ALAALAARGARGFF139 - 151139 - 151
708ALAALAARGARGGG139 - 151139 - 151
718ALAALAARGARGHH139 - 151139 - 151
728ALAALAARGARGII139 - 151139 - 151
739GLNGLNGLYGLYAA164 - 171164 - 171
749GLNGLNGLYGLYBB164 - 171164 - 171
759GLNGLNGLYGLYCC164 - 171164 - 171
769GLNGLNGLYGLYDD164 - 171164 - 171
779GLNGLNGLYGLYEE164 - 171164 - 171
789GLNGLNGLYGLYFF164 - 171164 - 171
799GLNGLNGLYGLYGG164 - 171164 - 171
809GLNGLNGLYGLYHH164 - 171164 - 171
819GLNGLNGLYGLYII164 - 171164 - 171
8210GLNGLNLEULEUAA176 - 193176 - 193
8310GLNGLNLEULEUBB176 - 193176 - 193
8410GLNGLNLEULEUCC176 - 193176 - 193
8510GLNGLNLEULEUDD176 - 193176 - 193
8610GLNGLNLEULEUEE176 - 193176 - 193
8710GLNGLNLEULEUFF176 - 193176 - 193
8810GLNGLNLEULEUGG176 - 193176 - 193
8910GLNGLNLEULEUHH176 - 193176 - 193
9010GLNGLNLEULEUII176 - 193176 - 193

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Components

#1: Protein
Neurexin-1-beta / neurexin I-beta


Mass: 24321.201 Da / Num. of mol.: 10 / Fragment: LNS/LG domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Nrxn1 / Plasmid: pGEX-KG / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q63373
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 113 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHE RESIDUE NUMBERING IN THIS ENTRY IS DIFFERENT THAN THE CONVENTION USED FOR THE NEUREXIN 1BETA ...THE RESIDUE NUMBERING IN THIS ENTRY IS DIFFERENT THAN THE CONVENTION USED FOR THE NEUREXIN 1BETA CA2+-FREE FORM, PDB ENTRY 1C4R. CHAIN W IS A FRAGMENT FROM ONE OF CHAINS A-I BUT IT CANNOT BE UNEQUIVOCALLY ASSIGNED TO ANY OF THEM.

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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: 2.44 Å3/Da / Density % sol: 49.55 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 21% Peg 5000 MME, 0.1 M sodium cacodylate pH 6.5, 0.2 M AmSO4, 1.86% 1,2,3-heptanetriol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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Data collection

DiffractionMean temperature: 103 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.97949 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Jan 15, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 2.6→40.6 Å / Num. all: 73949 / Num. obs: 73949 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Biso Wilson estimate: 51 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 24.8
Reflection shellResolution: 2.6→2.64 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.423 / Mean I/σ(I) obs: 4.3 / Num. unique all: 3636 / Rsym value: 0.423 / % possible all: 99.8

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Processing

Software
NameVersionClassification
REFMAC5.2refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 1C4R

1c4r


Resolution: 2.6→20 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.916 / SU B: 19.07 / SU ML: 0.194 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.41 / ESU R Free: 0.27 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.24401 3741 5.1 %RANDOM
Rwork0.20273 ---
all0.20482 73564 --
obs0.20482 69823 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: 40.116 Å2
Baniso -1Baniso -2Baniso -3
1-2.91 Å20 Å20 Å2
2---2.49 Å20 Å2
3----0.42 Å2
Refinement stepCycle: LAST / Resolution: 2.6→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12101 0 3 113 12217
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.02212342
X-RAY DIFFRACTIONr_angle_refined_deg1.6141.92716753
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.4351585
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.6824.531565
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.132151929
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.1551568
X-RAY DIFFRACTIONr_chiral_restr0.1010.21866
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.029526
X-RAY DIFFRACTIONr_nbd_refined0.220.24820
X-RAY DIFFRACTIONr_nbtor_refined0.3130.28255
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1340.2492
X-RAY DIFFRACTIONr_metal_ion_refined0.1130.28
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2030.292
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1060.215
X-RAY DIFFRACTIONr_mcbond_it0.6661.58026
X-RAY DIFFRACTIONr_mcangle_it1.143212548
X-RAY DIFFRACTIONr_scbond_it1.72934876
X-RAY DIFFRACTIONr_scangle_it2.7784.54205
Refine LS restraints NCS

Ens-ID: 1 / Number: 807 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDTypeRms dev position (Å)Weight position
1Amedium positional0.290.5
2Bmedium positional0.410.5
3Cmedium positional0.30.5
4Dmedium positional0.340.5
5Emedium positional0.310.5
6Fmedium positional0.370.5
7Gmedium positional0.330.5
8Hmedium positional0.330.5
9Imedium positional0.470.5
1Amedium thermal0.732
2Bmedium thermal0.92
3Cmedium thermal0.832
4Dmedium thermal0.882
5Emedium thermal0.762
6Fmedium thermal0.842
7Gmedium thermal0.842
8Hmedium thermal0.812
9Imedium thermal0.652
LS refinement shellResolution: 2.6→2.666 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.349 291 -
Rwork0.283 5014 -
obs-5305 100 %
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)
12.30520.06260.79339.6745-0.54571.72650.2810.1358-0.4185-0.6307-0.04650.15160.353-0.0377-0.23450.00220.0523-0.0403-0.1414-0.0248-0.065534.64219.665650.8275
21.4089-0.36710.58972.5802-0.79984.6616-0.0189-0.09810.17520.0886-0.062-0.076-0.20560.21060.0809-0.2943-0.02290.0222-0.1510.0088-0.18735.813855.103167.8686
32.28870.2148-0.86867.4692-0.01352.16540.0778-0.02490.1955-0.3854-0.02220.2178-0.1504-0.0086-0.0555-0.09510.02980.0211-0.18090.014-0.083922.435794.3727-1.4657
41.0676-0.4318-1.11173.67050.39085.89190.02620.0024-0.15430.1673-0.01580.02260.2675-0.2305-0.0104-0.2308-0.0075-0.0019-0.14050.0071-0.192220.967458.959715.7013
52.047-0.6080.29747.0878-0.03641.3278-0.1860.01510.5825-0.1867-0.0762-0.3942-0.32680.12990.2623-0.0433-0.0304-0.0894-0.15740.0314-0.075925.687881.181344.5851
65.6166-0.6282-0.36142.7296-0.84882.6481-0.014-0.1606-0.2644-0.04660.15040.23170.3751-0.4699-0.1364-0.1545-0.1001-0.0945-0.04820.0448-0.21628.165447.297553.4978
72.4777-0.1744-0.21466.3064-0.32711.7308-0.03160.0225-0.31890.2439-0.1084-0.03040.14150.02020.14-0.1574-0.02160.0495-0.177-0.0533-0.232532.206232.617896.7281
86.0025-0.34791.26053.93331.12223.28510.0254-0.09160.21840.00620.2237-0.4658-0.24160.5417-0.2491-0.2013-0.08830.0550.006-0.0825-0.098447.99667.0218105.0453
92.95250.3046-1.313115.8684.75276.5899-0.217-0.17940.00741.1839-0.72391.52260.2799-0.7310.94090.3997-0.05240.14550.2958-0.10890.307214.369819.806123.6937
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA35 - 21635 - 216
2X-RAY DIFFRACTION2BB35 - 21435 - 214
3X-RAY DIFFRACTION2BK10001
4X-RAY DIFFRACTION3CC34 - 21634 - 216
5X-RAY DIFFRACTION4DD35 - 21335 - 213
6X-RAY DIFFRACTION4DL20001
7X-RAY DIFFRACTION5EE35 - 21635 - 216
8X-RAY DIFFRACTION6FF35 - 21235 - 212
9X-RAY DIFFRACTION7GG35 - 21635 - 216
10X-RAY DIFFRACTION8HH36 - 21136 - 211
11X-RAY DIFFRACTION9II39 - 21139 - 211
12X-RAY DIFFRACTION9IM30001

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