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- PDB-5v5v: Complex of NLGN2 with MDGA1 Ig1-Ig2 -

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Basic information

Entry
Database: PDB / ID: 5v5v
TitleComplex of NLGN2 with MDGA1 Ig1-Ig2
Components
  • MAM domain-containing glycosylphosphatidylinositol anchor protein 1
  • Neuroligin-2
KeywordsCELL ADHESION / synaptic organizers / regulatory complex / neuroligins / MDGAs
Function / homology
Function and homology information


spinal cord association neuron differentiation / jump response / neurotransmitter-gated ion channel clustering / positive regulation of t-SNARE clustering / postsynaptic specialization assembly / gephyrin clustering involved in postsynaptic density assembly / terminal button organization / postsynaptic density protein 95 clustering / positive regulation of synaptic vesicle clustering / postsynaptic membrane assembly ...spinal cord association neuron differentiation / jump response / neurotransmitter-gated ion channel clustering / positive regulation of t-SNARE clustering / postsynaptic specialization assembly / gephyrin clustering involved in postsynaptic density assembly / terminal button organization / postsynaptic density protein 95 clustering / positive regulation of synaptic vesicle clustering / postsynaptic membrane assembly / Neurexins and neuroligins / presynaptic membrane assembly / neurexin family protein binding / cerebral cortex radially oriented cell migration / Post-translational modification: synthesis of GPI-anchored proteins / presynapse assembly / thigmotaxis / neuron cell-cell adhesion / regulation of respiratory gaseous exchange by nervous system process / insulin metabolic process / ribbon synapse / inhibitory synapse / protein localization to synapse / dopaminergic synapse / serotonin metabolic process / positive regulation of inhibitory postsynaptic potential / glycinergic synapse / inhibitory synapse assembly / protein localization to cell surface / positive regulation of synapse assembly / regulation of synaptic membrane adhesion / neuromuscular process controlling balance / postsynaptic specialization membrane / positive regulation of protein localization to synapse / synaptic transmission, GABAergic / positive regulation of dendritic spine development / dopamine metabolic process / locomotory exploration behavior / social behavior / prepulse inhibition / regulation of presynapse assembly / positive regulation of synaptic transmission, glutamatergic / side of membrane / synapse assembly / cell adhesion molecule binding / excitatory synapse / sensory perception of pain / positive regulation of excitatory postsynaptic potential / dendritic shaft / positive regulation of synaptic transmission, GABAergic / positive regulation of insulin secretion / synapse organization / brain development / modulation of chemical synaptic transmission / GABA-ergic synapse / neuron migration / nervous system development / presynaptic membrane / postsynaptic membrane / axon / positive regulation of cell population proliferation / synapse / dendrite / cell surface / Golgi apparatus / extracellular space / extracellular region / identical protein binding / plasma membrane
Similarity search - Function
: / Neuroligin / : / Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others) / MAM domain, meprin/A5/mu / MAM domain / MAM domain profile. / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase, type B ...: / Neuroligin / : / Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others) / MAM domain, meprin/A5/mu / MAM domain / MAM domain profile. / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase, type B / Carboxylesterase family / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Alpha/Beta hydrolase fold / Concanavalin A-like lectin/glucanase domain superfamily / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Neuroligin-2 / MAM domain-containing glycosylphosphatidylinositol anchor protein 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.11 Å
AuthorsGangwar, S.P. / Machius, M. / Rudenko, G.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)R01MH077303 United States
UT Brain Pilot United States
Brain and Behavior Research Foundation United States
CitationJournal: Neuron / Year: 2017
Title: Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges.
Authors: Gangwar, S.P. / Zhong, X. / Seshadrinathan, S. / Chen, H. / Machius, M. / Rudenko, G.
History
DepositionMar 15, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 5, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 4, 2023Group: 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 / 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
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Neuroligin-2
G: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
B: Neuroligin-2
C: Neuroligin-2
D: Neuroligin-2
E: Neuroligin-2
F: Neuroligin-2
H: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
I: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
J: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
K: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
L: MAM domain-containing glycosylphosphatidylinositol anchor protein 1


Theoretical massNumber of molelcules
Total (without water)544,65512
Polymers544,65512
Non-polymers00
Water00
1
A: Neuroligin-2
G: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
B: Neuroligin-2
H: MAM domain-containing glycosylphosphatidylinositol anchor protein 1


Theoretical massNumber of molelcules
Total (without water)181,5524
Polymers181,5524
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Neuroligin-2
D: Neuroligin-2
K: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
L: MAM domain-containing glycosylphosphatidylinositol anchor protein 1


Theoretical massNumber of molelcules
Total (without water)181,5524
Polymers181,5524
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Neuroligin-2
F: Neuroligin-2
I: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
J: MAM domain-containing glycosylphosphatidylinositol anchor protein 1


Theoretical massNumber of molelcules
Total (without water)181,5524
Polymers181,5524
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)103.118, 97.182, 190.510
Angle α, β, γ (deg.)95.52, 80.97, 88.71
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16G
26H
17G
27I
18G
28J
19G
29K
110G
210L
111B
211C
112B
212D
113B
213E
114B
214F
115C
215D
116C
216E
117C
217F
118D
218E
119D
219F
120E
220F
121H
221I
122H
222J
123H
223K
124H
224L
125I
225J
126I
226K
127I
227L
128J
228K
129J
229L
130K
230L

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11VALVALHISHISAA51 - 60911 - 569
21VALVALHISHISBC51 - 60911 - 569
12VALVALHISHISAA51 - 60911 - 569
22VALVALHISHISCD51 - 60911 - 569
13VALVALHISHISAA51 - 60911 - 569
23VALVALHISHISDE51 - 60911 - 569
14VALVALHISHISAA51 - 60911 - 569
24VALVALHISHISEF51 - 60911 - 569
15VALVALHISHISAA51 - 60911 - 569
25VALVALHISHISFG51 - 60911 - 569
16PROPROTHRTHRGB24 - 2345 - 215
26PROPROTHRTHRHH24 - 2345 - 215
17PROPROTHRTHRGB24 - 2345 - 215
27PROPROTHRTHRII24 - 2345 - 215
18PROPROTHRTHRGB24 - 2345 - 215
28PROPROTHRTHRJJ24 - 2345 - 215
19PROPROTHRTHRGB24 - 2345 - 215
29PROPROTHRTHRKK24 - 2345 - 215
110PROPROTHRTHRGB24 - 2345 - 215
210PROPROTHRTHRLL24 - 2345 - 215
111VALVALHISHISBC51 - 60911 - 569
211VALVALHISHISCD51 - 60911 - 569
112VALVALHISHISBC51 - 60911 - 569
212VALVALHISHISDE51 - 60911 - 569
113VALVALHISHISBC51 - 60911 - 569
213VALVALHISHISEF51 - 60911 - 569
114VALVALHISHISBC51 - 60911 - 569
214VALVALHISHISFG51 - 60911 - 569
115VALVALHISHISCD51 - 60911 - 569
215VALVALHISHISDE51 - 60911 - 569
116VALVALHISHISCD51 - 60911 - 569
216VALVALHISHISEF51 - 60911 - 569
117VALVALHISHISCD51 - 60911 - 569
217VALVALHISHISFG51 - 60911 - 569
118VALVALHISHISDE51 - 60911 - 569
218VALVALHISHISEF51 - 60911 - 569
119VALVALHISHISDE51 - 60911 - 569
219VALVALHISHISFG51 - 60911 - 569
120VALVALHISHISEF51 - 60911 - 569
220VALVALHISHISFG51 - 60911 - 569
121PROPROTHRTHRHH24 - 2345 - 215
221PROPROTHRTHRII24 - 2345 - 215
122PROPROTHRTHRHH24 - 2345 - 215
222PROPROTHRTHRJJ24 - 2345 - 215
123PROPROTHRTHRHH24 - 2345 - 215
223PROPROTHRTHRKK24 - 2345 - 215
124PROPROTHRTHRHH24 - 2345 - 215
224PROPROTHRTHRLL24 - 2345 - 215
125PROPROTHRTHRII24 - 2345 - 215
225PROPROTHRTHRJJ24 - 2345 - 215
126PROPROTHRTHRII24 - 2345 - 215
226PROPROTHRTHRKK24 - 2345 - 215
127PROPROTHRTHRII24 - 2345 - 215
227PROPROTHRTHRLL24 - 2345 - 215
128PROPROTHRTHRJJ24 - 2345 - 215
228PROPROTHRTHRKK24 - 2345 - 215
129PROPROTHRTHRJJ24 - 2345 - 215
229PROPROTHRTHRLL24 - 2345 - 215
130PROPROTHRTHRKK24 - 2345 - 215
230PROPROTHRTHRLL24 - 2345 - 215

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30

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Components

#1: Protein
Neuroligin-2


Mass: 64844.707 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Nlgn2 / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q62888
#2: Protein
MAM domain-containing glycosylphosphatidylinositol anchor protein 1 / GPI and MAM protein / GPIM / Glycosylphosphatidylinositol-MAM / MAM domain-containing protein 3


Mass: 25931.156 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MDGA1, MAMDC3 / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q8NFP4
Has protein modificationY

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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: 3.44 Å3/Da / Density % sol: 64.28 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.03 M NaNO3, 0.03 M Na2HPO4, 0.03 M (NH4)2SO4, 0.05 M HEPES pH 7.5, 0.05 M MOPS pH 7.5, 12 % (v/v) ethylene glycol, 9 % (w/v) PEG 8000

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 31, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 4.11→49.77 Å / Num. obs: 53553 / % possible obs: 94.4 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 18.8
Reflection shellResolution: 4.11→4.18 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.586 / Num. unique obs: 2112 / % possible all: 76.1

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3BL8

3bl8


Resolution: 4.11→49.77 Å / Cor.coef. Fo:Fc: 0.79 / Cor.coef. Fo:Fc free: 0.741 / SU B: 176.476 / SU ML: 1.012 / Cross valid method: THROUGHOUT / ESU R Free: 1.244
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS Individual B-factors were not refined due to the low resolution of the diffraction data. PLEASE NOTE THAT REFINEMENT OF THE MODEL IS ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS Individual B-factors were not refined due to the low resolution of the diffraction data. PLEASE NOTE THAT REFINEMENT OF THE MODEL IS DIFFICULT GIVEN THE LOW RESOLUTION OF THE DATA (4.1 A) AND THE LARGE NUMBER OF ATOMS IN THE ASYMMETRIC UNIT. THE ELECTRON DENSITY OF MANY SIDE CHAINS IS NOT WELL RESOLVED AND THE GEOMETRY OF THE MODEL IS NOT OPTIMAL.
RfactorNum. reflection% reflectionSelection details
Rfree0.31861 2200 4.8 %RANDOM
Rwork0.28887 ---
obs0.29032 43940 81.29 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 112.283 Å2
Baniso -1Baniso -2Baniso -3
1--1.26 Å20.59 Å20.79 Å2
2--15.66 Å2-6.26 Å2
3----11.96 Å2
Refinement stepCycle: 1 / Resolution: 4.11→49.77 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms33540 0 0 0 33540
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01934362
X-RAY DIFFRACTIONr_bond_other_d0.0030.0231248
X-RAY DIFFRACTIONr_angle_refined_deg1.551.9546680
X-RAY DIFFRACTIONr_angle_other_deg1.115372408
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.00154194
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.25723.9111626
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.174155466
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.47615228
X-RAY DIFFRACTIONr_chiral_restr0.1040.25124
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02138178
X-RAY DIFFRACTIONr_gen_planes_other0.0040.027122
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A337380.01
12B337380.01
21A336400.01
22C336400.01
31A336720.01
32D336720.01
41A336460.01
42E336460.01
51A336640.01
52F336640.01
61G100480.01
62H100480.01
71G100300.01
72I100300.01
81G100420.01
82J100420.01
91G100360.01
92K100360.01
101G99920.01
102L99920.01
111B336500.01
112C336500.01
121B336640.01
122D336640.01
131B336620.01
132E336620.01
141B336880.01
142F336880.01
151C336740.01
152D336740.01
161C337380.01
162E337380.01
171C337020.01
172F337020.01
181D336660.01
182E336660.01
191D337540.01
192F337540.01
201E337140.01
202F337140.01
211H100220.01
212I100220.01
221H100420.01
222J100420.01
231H100240.01
232K100240.01
241H99860.01
242L99860.01
251I100660.01
252J100660.01
261I100580.02
262K100580.02
271I100380.02
272L100380.02
281J100900.01
282K100900.01
291J100480.01
292L100480.01
301K100380.01
302L100380.01
LS refinement shellResolution: 4.105→4.212 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.407 68 -
Rwork0.353 1369 -
obs--34.29 %
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)
14.31021.0117-1.92482.9175-0.2214.9227-0.83230.2277-0.65820.10370.35930.10190.9804-0.19630.4730.29620.00240.2850.09930.1650.7611-58.8092-23.6378-23.0024
25.0015-0.4136-2.18493.02190.16755.2218-0.8839-0.3416-0.7709-0.11380.3808-0.28020.875-0.03660.50310.22830.01550.23060.0736-0.01450.7895-7.993-21.1977-55.5335
35.57991.9046-0.17345.1266-0.64523.9823-0.89870.8701-1.0112-0.77170.09240.02120.92910.02870.80630.622-0.08360.50380.1803-0.27221.0639-70.8312-18.6913-102.3132
44.48721.26180.79365.2630.89572.2414-0.0477-0.17721.1111-0.7344-0.0324-0.0614-1.60650.3210.08011.3492-0.35050.0220.22220.30971.4489-43.675633.6914-90.6551
54.0221-1.9750.56816.05720.01633.8843-0.6843-0.5899-0.6460.83240.08910.01720.8511-0.26240.59510.6462-0.21220.41660.52770.250.9867-25.3521-8.2283-163.1348
63.0138-0.70470.23634.81970.21293.08870.11-0.05880.79650.4144-0.16760.191-1.7191-0.45250.05761.55550.7295-0.03710.8911-0.35741.3211-53.31144.7928-167.6279
77.135-1.8337-1.18341.2575-0.40340.95060.22830.19450.7582-0.4524-0.2617-0.6570.20580.18860.03340.9802-0.0460.17420.94860.18471.0704-18.5384-0.9299-79.0615
87.7906-1.8087-8.47674.2323-0.953211.63550.07250.1160.1292-0.17530.19110.5432-0.122-0.3001-0.26360.3001-0.2109-0.34470.80230.10720.6842-48.43832.2214-55.3538
99.37962.2995-4.04051.0972-0.6433.7541-0.031-0.61950.35140.3978-0.0540.64360.1544-0.06680.0851.06140.02860.01340.87570.02171.0107-48.3253-7.09543.1039
1010.69011.6191-8.64724.9598-0.271612.15410.1459-0.1522-0.0331-0.13440.1205-0.5682-0.23460.1931-0.26650.39030.2133-0.34730.7584-0.10460.5957-18.3926-0.3606-19.8017
111.6367-2.8057-1.600510.69232.59412.3264-0.1216-0.06680.17440.5018-0.4179-0.10030.73470.46050.53952.00550.1014-0.58691.07910.18131.7-3.50650.3341-139.9808
125.1023-6.79470.567111.02890.48461.9986-0.13740.06970.61031.0862-0.7831-0.7264-0.5202-0.10010.92052.106-0.0266-0.62211.2882-0.29471.3376-25.058931.944-138.4719
131.1847-2.7680.2286.52-0.60250.63060.0290.09930.1684-0.0529-0.1147-0.1447-0.6014-0.4490.08581.42420.03440.07481.03970.16291.7907-81.823936.2965-154.1402
146.1081-4.21481.76769.3174-4.0474.0665-0.5949-0.3608-0.32920.91920.03590.58230.1614-0.32670.5591.1631-0.04940.36621.40.26011.4912-62.61854.152-146.1554
151.60783.66341.07069.46314.28484.34450.1241-0.24890.07310.0218-0.2538-0.0482-0.7269-0.08420.12961.1858-0.16710.14511.00320.08951.5657-14.907327.1822-104.8528
167.73525.82331.89238.77681.9911.8384-0.1435-0.2674-0.6001-0.7045-0.2422-0.71590.16110.29520.38571.0175-0.09110.41910.95370.01061.3514-33.7763-3.7812-117.1515
171.08862.69550.670613.53731.11370.62820.1946-0.1527-0.0865-0.1159-0.4730.31820.4148-0.0540.27831.47350.0323-0.27381.13840.16071.415-92.3448-8.2272-124.7431
181.49732.62520.67038.9582-1.35891.9282-0.4317-0.09710.3308-0.2709-0.0215-0.0884-0.8858-0.44830.45321.83220.2398-0.43961.38270.76251.2886-71.692823.8737-121.7264
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A51 - 609
2X-RAY DIFFRACTION2B51 - 609
3X-RAY DIFFRACTION3C51 - 609
4X-RAY DIFFRACTION4D51 - 609
5X-RAY DIFFRACTION5E51 - 609
6X-RAY DIFFRACTION6F51 - 609
7X-RAY DIFFRACTION7G24 - 127
8X-RAY DIFFRACTION8G128 - 234
9X-RAY DIFFRACTION9H24 - 127
10X-RAY DIFFRACTION10H128 - 234
11X-RAY DIFFRACTION11I24 - 127
12X-RAY DIFFRACTION12I128 - 234
13X-RAY DIFFRACTION13J24 - 127
14X-RAY DIFFRACTION14J128 - 234
15X-RAY DIFFRACTION15K24 - 127
16X-RAY DIFFRACTION16K128 - 234
17X-RAY DIFFRACTION17L24 - 127
18X-RAY DIFFRACTION18L128 - 234

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