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- PDB-3rl0: Truncated SNARE complex with complexin (P1) -

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Basic information

Entry
Database: PDB / ID: 3rl0
TitleTruncated SNARE complex with complexin (P1)
Components
  • (Synaptosomal-associated protein 25) x 2
  • Complexin-1
  • Syntaxin-1A
  • Vesicle-associated membrane protein 2
KeywordsMEMBRANE PROTEIN/EXOCYTOSIS / SNARE proteins / membrane fusion / MEMBRANE PROTEIN-EXOCYTOSIS complex
Function / homology
Function and homology information


synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex / regulation of exocytic insertion of neurotransmitter receptor to postsynaptic membrane / regulation of synaptic vesicle fusion to presynaptic active zone membrane / Toxicity of botulinum toxin type C (botC) / Toxicity of tetanus toxin (tetX) / neurotransmitter uptake / Toxicity of botulinum toxin type G (botG) / clathrin-sculpted glutamate transport vesicle membrane / regulation of delayed rectifier potassium channel activity / Toxicity of botulinum toxin type F (botF) ...synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex / regulation of exocytic insertion of neurotransmitter receptor to postsynaptic membrane / regulation of synaptic vesicle fusion to presynaptic active zone membrane / Toxicity of botulinum toxin type C (botC) / Toxicity of tetanus toxin (tetX) / neurotransmitter uptake / Toxicity of botulinum toxin type G (botG) / clathrin-sculpted glutamate transport vesicle membrane / regulation of delayed rectifier potassium channel activity / Toxicity of botulinum toxin type F (botF) / myosin head/neck binding / Toxicity of botulinum toxin type D (botD) / trans-Golgi Network Vesicle Budding / Toxicity of botulinum toxin type E (botE) / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / Other interleukin signaling / extrinsic component of presynaptic membrane / Acetylcholine Neurotransmitter Release Cycle / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / Toxicity of botulinum toxin type A (botA) / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex / Toxicity of botulinum toxin type B (botB) / synaptic vesicle fusion to presynaptic active zone membrane / regulation of synaptic vesicle priming / clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane / Glutamate Neurotransmitter Release Cycle / positive regulation of norepinephrine secretion / Norepinephrine Neurotransmitter Release Cycle / Acetylcholine Neurotransmitter Release Cycle / positive regulation of catecholamine secretion / zymogen granule membrane / clathrin-sculpted monoamine transport vesicle membrane / Serotonin Neurotransmitter Release Cycle / GABA synthesis, release, reuptake and degradation / Dopamine Neurotransmitter Release Cycle / regulated exocytosis / Serotonin Neurotransmitter Release Cycle / GABA synthesis, release, reuptake and degradation / presynaptic dense core vesicle exocytosis / ribbon synapse / synaptic vesicle docking / response to gravity / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / Dopamine Neurotransmitter Release Cycle / Norepinephrine Neurotransmitter Release Cycle / eosinophil degranulation / vesicle fusion / vesicle docking / neurotransmitter transmembrane transporter activity / positive regulation of calcium ion-dependent exocytosis / regulation of neurotransmitter secretion / chloride channel inhibitor activity / secretion by cell / SNARE complex / SNAP receptor activity / Glutamate Neurotransmitter Release Cycle / regulation of vesicle-mediated transport / LGI-ADAM interactions / hormone secretion / calcium-ion regulated exocytosis / actomyosin / positive regulation of intracellular protein transport / Golgi to plasma membrane protein transport / regulation of exocytosis / neurotransmitter receptor internalization / protein localization to membrane / ATP-dependent protein binding / neuron projection terminus / neurotransmitter transport / Sensory processing of sound by inner hair cells of the cochlea / insulin secretion / syntaxin-1 binding / SNARE complex assembly / positive regulation of neurotransmitter secretion / syntaxin binding / clathrin-coated vesicle / synaptic vesicle priming / Lysosome Vesicle Biogenesis / regulation of synapse assembly / regulation of neuron projection development / endosomal transport / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / Other interleukin signaling / Golgi Associated Vesicle Biogenesis / myosin binding / Insulin processing / exocytosis / voltage-gated potassium channel activity / synaptic vesicle exocytosis / positive regulation of exocytosis / modulation of excitatory postsynaptic potential / associative learning / calyx of Held / regulation of insulin secretion / positive regulation of excitatory postsynaptic potential / tertiary granule membrane / protein sumoylation / synaptic vesicle endocytosis / calcium channel inhibitor activity
Similarity search - Function
Single Helix bin / Synaphin / Synaphin protein / Synaptobrevin/Vesicle-associated membrane protein / Synaptosomal-associated protein 25 / SNAP-25 domain / SNAP-25 family / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #110 / Synaptobrevin signature. / Syntaxin ...Single Helix bin / Synaphin / Synaphin protein / Synaptobrevin/Vesicle-associated membrane protein / Synaptosomal-associated protein 25 / SNAP-25 domain / SNAP-25 family / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #110 / Synaptobrevin signature. / Syntaxin / Syntaxin N-terminal domain / Syntaxin, N-terminal domain / Syntaxin / SNARE domain / Synaptobrevin-like / Syntaxin/epimorphin, conserved site / Synaptobrevin / Syntaxin / epimorphin family signature. / v-SNARE, coiled-coil homology domain / v-SNARE coiled-coil homology domain profile. / SNARE / Helical region found in SNAREs / t-SNARE coiled-coil homology domain profile. / Target SNARE coiled-coil homology domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Complexin-1 / Syntaxin-1A / Synaptosomal-associated protein 25 / Vesicle-associated membrane protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Rattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å
AuthorsKuemmel, D. / Reinisch, K.M.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2011
Title: Complexin cross-links prefusion SNAREs into a zigzag array.
Authors: Kummel, D. / Krishnakumar, S.S. / Radoff, D.T. / Li, F. / Giraudo, C.G. / Pincet, F. / Rothman, J.E. / Reinisch, K.M.
History
DepositionApr 19, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 27, 2011Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2011Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Vesicle-associated membrane protein 2
B: Syntaxin-1A
C: Synaptosomal-associated protein 25
D: Synaptosomal-associated protein 25
E: Vesicle-associated membrane protein 2
F: Syntaxin-1A
G: Synaptosomal-associated protein 25
H: Synaptosomal-associated protein 25
I: Vesicle-associated membrane protein 2
J: Syntaxin-1A
K: Synaptosomal-associated protein 25
L: Synaptosomal-associated protein 25
M: Vesicle-associated membrane protein 2
N: Syntaxin-1A
O: Synaptosomal-associated protein 25
P: Synaptosomal-associated protein 25
Q: Vesicle-associated membrane protein 2
R: Syntaxin-1A
S: Synaptosomal-associated protein 25
T: Synaptosomal-associated protein 25
U: Vesicle-associated membrane protein 2
V: Syntaxin-1A
W: Synaptosomal-associated protein 25
X: Synaptosomal-associated protein 25
Y: Vesicle-associated membrane protein 2
Z: Syntaxin-1A
a: Synaptosomal-associated protein 25
b: Synaptosomal-associated protein 25
c: Vesicle-associated membrane protein 2
d: Syntaxin-1A
e: Synaptosomal-associated protein 25
f: Synaptosomal-associated protein 25
g: Complexin-1
h: Complexin-1
i: Complexin-1
j: Complexin-1
k: Complexin-1
l: Complexin-1
m: Complexin-1
n: Complexin-1


Theoretical massNumber of molelcules
Total (without water)288,37740
Polymers288,37740
Non-polymers00
Water00
1
A: Vesicle-associated membrane protein 2
B: Syntaxin-1A
C: Synaptosomal-associated protein 25
D: Synaptosomal-associated protein 25
g: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10590 Å2
ΔGint-84 kcal/mol
Surface area17640 Å2
2
E: Vesicle-associated membrane protein 2
F: Syntaxin-1A
G: Synaptosomal-associated protein 25
H: Synaptosomal-associated protein 25
h: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10350 Å2
ΔGint-86 kcal/mol
Surface area17960 Å2
3
I: Vesicle-associated membrane protein 2
J: Syntaxin-1A
K: Synaptosomal-associated protein 25
L: Synaptosomal-associated protein 25
i: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10900 Å2
ΔGint-94 kcal/mol
Surface area17250 Å2
4
M: Vesicle-associated membrane protein 2
N: Syntaxin-1A
O: Synaptosomal-associated protein 25
P: Synaptosomal-associated protein 25
j: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10940 Å2
ΔGint-90 kcal/mol
Surface area17150 Å2
5
Q: Vesicle-associated membrane protein 2
R: Syntaxin-1A
S: Synaptosomal-associated protein 25
T: Synaptosomal-associated protein 25
k: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10450 Å2
ΔGint-83 kcal/mol
Surface area17770 Å2
6
U: Vesicle-associated membrane protein 2
V: Syntaxin-1A
W: Synaptosomal-associated protein 25
X: Synaptosomal-associated protein 25
l: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10240 Å2
ΔGint-82 kcal/mol
Surface area17680 Å2
7
Y: Vesicle-associated membrane protein 2
Z: Syntaxin-1A
a: Synaptosomal-associated protein 25
b: Synaptosomal-associated protein 25
m: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10730 Å2
ΔGint-88 kcal/mol
Surface area16940 Å2
8
c: Vesicle-associated membrane protein 2
d: Syntaxin-1A
e: Synaptosomal-associated protein 25
f: Synaptosomal-associated protein 25
n: Complexin-1


Theoretical massNumber of molelcules
Total (without water)36,0475
Polymers36,0475
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10690 Å2
ΔGint-92 kcal/mol
Surface area16780 Å2
Unit cell
Length a, b, c (Å)53.745, 127.357, 142.725
Angle α, β, γ (deg.)107.49, 90.01, 90.05
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21E
31I
41M
51Q
61U
71Y
81c
12B
22F
32J
42N
52R
62V
72Z
82d
13C
23G
33K
43O
53S
63W
73a
83e
14D
24H
34L
44P
54T
64X
74b
84f
15g
25h
35k
45I
16i
26j
36m
46n

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A28 - 60
2111E28 - 60
3111I28 - 60
4111M28 - 60
5111Q28 - 60
6111U28 - 60
7111Y28 - 60
8111c28 - 60
1121B190 - 248
2121F190 - 248
3121J190 - 248
4121N190 - 248
5121R190 - 248
6121V190 - 248
7121Z190 - 248
8121d190 - 248
1131C15 - 78
2131G15 - 78
3131K15 - 78
4131O15 - 78
5131S15 - 78
6131W15 - 78
7131a15 - 78
8131e15 - 78
1141D141 - 199
2141H141 - 199
3141L141 - 199
4141P141 - 199
5141T141 - 199
6141X141 - 199
7141b141 - 199
8141f141 - 199
1154g27 - 70
2154h27 - 70
3154k27 - 70
4154I27 - 70
1164i28 - 70
2164j28 - 70
3164m28 - 70
4164n28 - 70

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein/peptide
Vesicle-associated membrane protein 2 / VAMP-2 / Synaptobrevin-2


Mass: 4254.826 Da / Num. of mol.: 8 / Fragment: UNP residues 28-60
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VAMP2, SYB2 / Production host: Escherichia coli (E. coli) / References: UniProt: P63027
#2: Protein
Syntaxin-1A / Neuron-specific antigen HPC-1 / Synaptotagmin-associated 35 kDa protein / P35A


Mass: 7551.502 Da / Num. of mol.: 8 / Fragment: UNP residues 191-253
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stx1a, Sap / Production host: Escherichia coli (E. coli) / References: UniProt: P32851
#3: Protein
Synaptosomal-associated protein 25 / SNAP-25 / Super protein / SUP / Synaptosomal-associated 25 kDa protein


Mass: 9500.615 Da / Num. of mol.: 8 / Fragment: UNP residues 7-82
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SNAP25, SNAP / Production host: Escherichia coli (E. coli) / References: UniProt: P60880
#4: Protein
Synaptosomal-associated protein 25 / SNAP-25 / Super protein / SUP / Synaptosomal-associated 25 kDa protein


Mass: 7427.250 Da / Num. of mol.: 8 / Fragment: UNP residues 141-203
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SNAP25, SNAP / Production host: Escherichia coli (E. coli) / References: UniProt: P60880
#5: Protein
Complexin-1 / Complexin I / CPX I / Synaphin-2


Mass: 7312.962 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CPLX1 / Production host: Escherichia coli (E. coli) / References: UniProt: O14810

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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: 3.23 Å3/Da / Density % sol: 61.93 %
Crystal growTemperature: 294 K / Method: vapor diffusion / pH: 7.5
Details: 13-15% polyethyleneglycol (PEG) 5000MME, 0.2 M ammonium sulfate, 0.01 M EDTA, and 0.1 M Tris pH 7.5, VAPOR DIFFUSION, temperature 294K

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Data collection

DiffractionMean temperature: 200 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9797 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 16, 2010
RadiationMonochromator: Cryogenically cooled double crystal monochrometer
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9797 Å / Relative weight: 1
Reflection twinOperator: h,-h-k,-l / Fraction: 0.47
ReflectionResolution: 3.8→30 Å / Num. all: 70400 / % possible obs: 83.5 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3
Reflection shellResolution: 3.8→3.94 Å / % possible all: 80.7

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.8→30 Å / Cor.coef. Fo:Fc: 0.909 / Cor.coef. Fo:Fc free: 0.866 / SU B: 174.715 / SU ML: 1.032 / Cross valid method: THROUGHOUT / ESU R Free: 0.987 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.345 1872 5.4 %RANDOM
Rwork0.306 ---
obs0.308 32506 97.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 116.78 Å2
Baniso -1Baniso -2Baniso -3
1--5.35 Å2-0.1 Å2-0.18 Å2
2---15.82 Å2-4.36 Å2
3---18.54 Å2
Refinement stepCycle: LAST / Resolution: 3.8→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17672 0 0 0 17672
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0350.0319545
X-RAY DIFFRACTIONr_bond_other_d0.0060.0212115
X-RAY DIFFRACTIONr_angle_refined_deg1.0111.96623222
X-RAY DIFFRACTIONr_angle_other_deg1.102329415
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.11752147
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.80925.6321012
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.014153548
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.45615181
X-RAY DIFFRACTIONr_chiral_restr0.0440.22579
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0219530
X-RAY DIFFRACTIONr_gen_planes_other0.0140.023111
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_it2.6462.512987
X-RAY DIFFRACTIONr_mcbond_other0.3722.54410
X-RAY DIFFRACTIONr_mcangle_it3.718317219
X-RAY DIFFRACTIONr_scbond_it3.83546558
X-RAY DIFFRACTIONr_scangle_it6.5366003
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

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A444tight positional0.020.05
12E444tight positional0.020.05
13I444tight positional0.030.05
14M444tight positional0.020.05
15Q444tight positional0.020.05
16U444tight positional0.120.05
17Y444tight positional0.030.05
18c444tight positional0.020.05
21B718tight positional0.020.05
22F718tight positional0.030.05
23J718tight positional0.030.05
24N718tight positional0.020.05
25R718tight positional0.020.05
26V718tight positional0.020.05
27Z718tight positional0.020.05
28d718tight positional0.030.05
31C811tight positional0.030.05
32G811tight positional0.030.05
33K811tight positional0.090.05
34O811tight positional0.070.05
35S811tight positional0.050.05
36W811tight positional0.030.05
37a811tight positional0.030.05
38e811tight positional0.030.05
41D729tight positional0.020.05
42H729tight positional0.030.05
43L729tight positional0.050.05
44P729tight positional0.030.05
45T729tight positional0.020.05
46X729tight positional0.050.05
47b729tight positional0.020.05
48f729tight positional0.020.05
51g22medium positional0.240.5
52h22medium positional0.450.5
53k22medium positional0.190.5
54I22medium positional0.290.5
61i581medium positional0.730.5
62j581medium positional0.670.5
63m581medium positional0.710.5
64n581medium positional0.740.5
11A444tight thermal0.020.5
12E444tight thermal0.020.5
13I444tight thermal0.020.5
14M444tight thermal0.020.5
15Q444tight thermal0.020.5
16U444tight thermal0.020.5
17Y444tight thermal0.020.5
18c444tight thermal0.020.5
21B718tight thermal0.020.5
22F718tight thermal0.020.5
23J718tight thermal0.020.5
24N718tight thermal0.020.5
25R718tight thermal0.020.5
26V718tight thermal0.020.5
27Z718tight thermal0.020.5
28d718tight thermal0.020.5
31C811tight thermal0.020.5
32G811tight thermal0.020.5
33K811tight thermal0.020.5
34O811tight thermal0.020.5
35S811tight thermal0.020.5
36W811tight thermal0.020.5
37a811tight thermal0.020.5
38e811tight thermal0.020.5
41D729tight thermal0.020.5
42H729tight thermal0.020.5
43L729tight thermal0.020.5
44P729tight thermal0.020.5
45T729tight thermal0.020.5
46X729tight thermal0.020.5
47b729tight thermal0.020.5
48f729tight thermal0.020.5
51g22medium thermal0.362
52h22medium thermal0.482
53k22medium thermal0.592
54I22medium thermal0.922
61i581medium thermal0.52
62j581medium thermal0.262
63m581medium thermal0.272
64n581medium thermal0.22
LS refinement shellResolution: 3.8→3.9 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rwork0.409 2271
Rfree-0
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)
12.8617-3.9102-0.55677.84480.81571.42320.0888-0.1040.1569-0.4278-0.02070.33820.06730.0488-0.0680.1584-0.09790.04340.1438-0.13240.28387.670825.6658.2294
22.3453.48540.67138.63941.55311.11820.0134-0.01140.00210.66820.01160.37110.14650.1132-0.0250.12910.03120.03680.0879-0.08630.2151-19.142-13.884718.5063
33.3338-3.42-1.93727.54393.34243.7247-0.0443-0.09730.1355-0.1796-0.03550.027-0.01530.14910.07980.1174-0.1011-0.02390.13740.01290.0194-18.461917.80462.3887
43.70113.49913.31474.97283.54914.92940.0217-0.212-0.01790.1328-0.0887-0.06570.0427-0.08160.0670.08710.01190.04750.03520.00450.03948.4711-6.410126.2915
52.1998-3.334-0.69918.34271.47521.1591-0.0166-0.06790.035-0.49670.04940.3934-0.0610.0648-0.03280.1027-0.0257-0.02670.0636-0.09140.23967.5154-20.9014-51.9853
63.15264.3560.17419.93390.44010.79460.06040.0389-0.1470.4519-0.03520.3857-0.00120.0178-0.02520.14190.0928-0.02890.1262-0.06590.194-18.7666-60.04-41.634
74.2488-3.9576-3.47235.22863.34175.06140.110.17470.0778-0.1571-0.0885-0.1364-0.0372-0.1212-0.02150.0726-0.0256-0.01450.03730.00690.0113-18.451-28.5202-59.4202
84.42373.60381.89027.8042.91654.1846-0.00090.09410.02370.2252-0.0650.07230.0841-0.03660.06590.10040.11690.07670.1770.10040.06228.2257-53.7506-36.6041
92.46832.08851.11552.44770.71050.842-0.83771.24280.5421-0.15391.04551.1989-0.34680.7763-0.20790.9842-0.2610.23520.79250.07541.104420.65355.30614.1753
100.3504-0.16540.32830.0806-0.15330.4236-0.1132-0.0067-0.63650.13970.2350.334-0.31680.2947-0.12180.58190.0930.35430.79810.55612.0196-6.1893-43.111220.195
116.2946-17.2041-7.127749.764320.69158.7008-1.0154-0.3863-0.2640.99310.96050.72050.28320.58610.0551.1244-0.02570.20470.8227-0.08730.3577-8.704414.441845.5089
123.96680.0736-0.38070.0037-0.01640.1117-0.33011.53551.6816-0.03020.27250.0690.33130.02270.05761.27750.2251-0.08281.10890.20071.538820.74087.6995-53.4913
131.7526-5.2732-1.563820.83056.35452.0734-0.4536-0.332-0.1475-0.61720.62240.5021-0.24180.2905-0.16870.80510.1676-0.05910.2632-0.070.7795-6.0912-90.535-37.4695
142.49437.70092.698227.97799.75933.4562-0.61230.3457-0.0868-0.02710.8312-0.20490.04680.3102-0.21890.9872-0.0909-0.11940.7123-0.0490.2536-35.4177-50.4061-78.9744
152.6422-10.3225-2.222344.25699.42472.0149-0.5932-0.2563-0.05490.71610.6195-0.08430.20870.0858-0.02630.7860.06660.09320.8131-0.06760.3403-6.9386-28.5611-20.3604
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A26 - 60
2X-RAY DIFFRACTION1B191 - 249
3X-RAY DIFFRACTION1C8 - 79
4X-RAY DIFFRACTION1D139 - 200
5X-RAY DIFFRACTION2E26 - 60
6X-RAY DIFFRACTION2F191 - 251
7X-RAY DIFFRACTION2G8 - 81
8X-RAY DIFFRACTION2H139 - 199
9X-RAY DIFFRACTION3I27 - 60
10X-RAY DIFFRACTION3J190 - 248
11X-RAY DIFFRACTION3K9 - 79
12X-RAY DIFFRACTION3L139 - 202
13X-RAY DIFFRACTION4M25 - 60
14X-RAY DIFFRACTION4N191 - 247
15X-RAY DIFFRACTION4O8 - 79
16X-RAY DIFFRACTION4P139 - 202
17X-RAY DIFFRACTION5Q26 - 60
18X-RAY DIFFRACTION5R191 - 251
19X-RAY DIFFRACTION5S10 - 79
20X-RAY DIFFRACTION5T139 - 200
21X-RAY DIFFRACTION6U26 - 60
22X-RAY DIFFRACTION6V191 - 248
23X-RAY DIFFRACTION6W8 - 77
24X-RAY DIFFRACTION6X139 - 201
25X-RAY DIFFRACTION7Y26 - 60
26X-RAY DIFFRACTION7Z190 - 247
27X-RAY DIFFRACTION7a10 - 79
28X-RAY DIFFRACTION7b139 - 199
29X-RAY DIFFRACTION8c27 - 60
30X-RAY DIFFRACTION8d190 - 248
31X-RAY DIFFRACTION8e8 - 79
32X-RAY DIFFRACTION8f139 - 200
33X-RAY DIFFRACTION9g24 - 70
34X-RAY DIFFRACTION10h25 - 70
35X-RAY DIFFRACTION11j26 - 70
36X-RAY DIFFRACTION12k25 - 70
37X-RAY DIFFRACTION13l24 - 70
38X-RAY DIFFRACTION14m26 - 70
39X-RAY DIFFRACTION15n26 - 70

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