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- PDB-2c7n: Human Rabex-5 residues 1-74 in complex with Ubiquitin -

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Basic information

Entry
Database: PDB / ID: 2c7n
TitleHuman Rabex-5 residues 1-74 in complex with Ubiquitin
Components
  • RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
  • UBIQUITIN
KeywordsPROTEIN BINDING / PROTEIN-BINDING / UBIQUITIN BINDING DOMAIN / ENDOCYTOSIS / NUCLEAR PROTEIN / POLYPROTEIN / UBIQUITIN COMPLEX
Function / homology
Function and homology information


dendritic transport / negative regulation of Kit signaling pathway / regulation of Fc receptor mediated stimulatory signaling pathway / mast cell migration / : / Kit signaling pathway / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling ...dendritic transport / negative regulation of Kit signaling pathway / regulation of Fc receptor mediated stimulatory signaling pathway / mast cell migration / : / Kit signaling pathway / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling / Spry regulation of FGF signaling / Downregulation of ERBB2:ERBB3 signaling / NOD1/2 Signaling Pathway / APC/C:Cdc20 mediated degradation of Cyclin B / SCF-beta-TrCP mediated degradation of Emi1 / APC-Cdc20 mediated degradation of Nek2A / EGFR downregulation / TCF dependent signaling in response to WNT / NRIF signals cell death from the nucleus / p75NTR recruits signalling complexes / NF-kB is activated and signals survival / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Downregulation of SMAD2/3:SMAD4 transcriptional activity / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Senescence-Associated Secretory Phenotype (SASP) / Regulation of innate immune responses to cytosolic DNA / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of FZD by ubiquitination / PINK1-PRKN Mediated Mitophagy / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of TNFR1 signaling / TNFR1-induced NFkappaB signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death / MAP3K8 (TPL2)-dependent MAPK1/3 activation / HDR through Homologous Recombination (HRR) / Josephin domain DUBs / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / DNA Damage Recognition in GG-NER / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in GG-NER / Dual Incision in GG-NER / Fanconi Anemia Pathway / Regulation of TP53 Activity through Phosphorylation / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Negative regulation of MET activity / Cyclin D associated events in G1 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Downregulation of ERBB2 signaling / E3 ubiquitin ligases ubiquitinate target proteins / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / Regulation of expression of SLITs and ROBOs / Endosomal Sorting Complex Required For Transport (ESCRT) / Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / RAS processing / Pexophagy / Inactivation of CSF3 (G-CSF) signaling / Negative regulation of FLT3 / Regulation of BACH1 activity / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Termination of translesion DNA synthesis / Ovarian tumor domain proteases / Negative regulators of DDX58/IFIH1 signaling / Negative regulation of FGFR1 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / Negative regulation of MAPK pathway / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Iron uptake and transport / Deactivation of the beta-catenin transactivating complex / Metalloprotease DUBs / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Activation of NF-kappaB in B cells / L13a-mediated translational silencing of Ceruloplasmin expression / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SRP-dependent cotranslational protein targeting to membrane / SCF(Skp2)-mediated degradation of p27/p21 / FCERI mediated NF-kB activation / Autodegradation of the E3 ubiquitin ligase COP1 / Asymmetric localization of PCP proteins / Degradation of AXIN / Degradation of DVL / Hedgehog ligand biogenesis
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #4770 / RABX5, catalytic core helical domain / Domain of unknown function (DUF5601) / Vacuolar protein sorting-associated protein 9-like / VPS9 domain / VPS9 domain superfamily / Vacuolar sorting protein 9 (VPS9) domain / VPS9 domain profile. / Domain present in VPS9 / Zinc finger, A20-type ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #4770 / RABX5, catalytic core helical domain / Domain of unknown function (DUF5601) / Vacuolar protein sorting-associated protein 9-like / VPS9 domain / VPS9 domain superfamily / Vacuolar sorting protein 9 (VPS9) domain / VPS9 domain profile. / Domain present in VPS9 / Zinc finger, A20-type / A20-like zinc finger / Zinc finger A20-type profile. / A20-like zinc fingers / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin-like (UB roll) / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Up-down Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin-60S ribosomal protein L40 / Rab5 GDP/GTP exchange factor / Rab5 GDP/GTP exchange factor
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
BOS TAURUS (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.1 Å
AuthorsPenengo, L. / Mapelli, M. / Murachelli, A.G. / Confalioneri, S. / Magri, L. / Musacchio, A. / Di Fiore, P.P. / Polo, S. / Schneider, T.R.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2006
Title: Crystal Structure of the Ubiquitin Binding Domains of Rabex-5 Reveals Two Modes of Interaction with Ubiquitin.
Authors: Penengo, L. / Mapelli, M. / Murachelli, A.G. / Confalonieri, S. / Magri, L. / Musacchio, A. / Di Fiore, P.P. / Polo, S. / Schneider, T.R.
History
DepositionNov 25, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 15, 2006Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
B: UBIQUITIN
C: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
D: UBIQUITIN
E: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
F: UBIQUITIN
G: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
H: UBIQUITIN
I: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
J: UBIQUITIN
K: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
L: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)104,56218
Polymers104,17012
Non-polymers3926
Water4,558253
1
A: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
B: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1760 Å2
ΔGint-10.9 kcal/mol
Surface area9570 Å2
MethodPQS
2
C: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
D: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1730 Å2
ΔGint-12.4 kcal/mol
Surface area9600 Å2
MethodPQS
3
E: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
F: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1290 Å2
ΔGint-6.9 kcal/mol
Surface area8890 Å2
MethodPQS
4
G: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
H: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1470 Å2
ΔGint-6.2 kcal/mol
Surface area9580 Å2
MethodPQS
5
I: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
J: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1440 Å2
ΔGint-6.9 kcal/mol
Surface area9820 Å2
MethodPQS
6
K: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1
L: UBIQUITIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,4273
Polymers17,3622
Non-polymers651
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1330 Å2
ΔGint-6.7 kcal/mol
Surface area9270 Å2
MethodPQS
Unit cell
Length a, b, c (Å)44.300, 68.900, 98.500
Angle α, β, γ (deg.)108.20, 102.70, 90.40
Int Tables number1
Space group name H-MP1
DetailsTHE QUATERNARY STRUCTURE FOR THIS ENTRY IS NOT RELEVANTSINCE THE COMPLEX IS ONLY MADE UP OF FRAGMENTS OF RABEX-5IN COMPLEX WITH UBIQUITIN. HOWEVER, THESE REMARKSONLY INDICATE THE COMPLEX AS SEEN IN THE PDB FILE, ANDDO NOT HAVE RELEVANCE TO THE BIOLOGICAL STATE OF THEMOLECULE.

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Components

#1: Protein
RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1 / RABEX-5 / GEF 1


Mass: 8784.761 Da / Num. of mol.: 6 / Fragment: TWO UBIQUTIN BINDING DOMAINS, RESIDUES 1-74
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q53FG0, UniProt: Q9UJ41*PLUS
#2: Protein
UBIQUITIN /


Mass: 8576.831 Da / Num. of mol.: 6 / Source method: obtained synthetically / Details: BOSTON BIOCHEM / Source: (synth.) BOS TAURUS (cattle) / References: UniProt: P62990, UniProt: P0CH28*PLUS
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 253 / Source method: isolated from a natural source / Formula: H2O
Compound detailsINVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATION OF CELLULAR PROTEINS, THE MAINTENANCE OF ...INVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATION OF CELLULAR PROTEINS, THE MAINTENANCE OF CHROMATIN STRUCTURE, THE REGULATION OF GENE EXPRESSION, THE STRESS RESPONSE, AND RIBOSOME BIOGENESIS
Sequence detailsTHE CONSTRUCT USED IN THE STRUCTURE DETERMINATION CONTAINED ONLY RESIDUES 1-74

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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: 3.08 Å3/Da / Density % sol: 59.77 %
Crystal growMethod: vapor diffusion, sitting drop / pH: 6.5
Details: SITTING DROP 300NL PLUS 300NL 0.2M AMMONIUM ACETATE 0.1M NACITRATE PH 6.5 25% PEG400
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 mg/mlprotein1drop
20.2 Mammonium acetate1reservoir
30.1 Msodium citrate1reservoir
425 %PEG40001reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9762
DetectorType: MARRESEARCH / Detector: CCD / Date: Sep 16, 2005
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 2.1→20 Å / Num. obs: 57954 / % possible obs: 92.3 % / Observed criterion σ(I): -4 / Redundancy: 2.7 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 12.7
Reflection shellResolution: 2.1→2.2 Å / Redundancy: 2 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 3.5 / % possible all: 66.4
Reflection
*PLUS
Rmerge(I) obs: 0.033
Reflection shell
*PLUS
% possible obs: 66.4 % / Rmerge(I) obs: 0.169

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
DENZOdata reduction
SCALEPACKdata scaling
HKL2MAPphasing
RefinementMethod to determine structure: MAD / Resolution: 2.1→20 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.931 / SU B: 8.127 / SU ML: 0.116 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.206 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-17 ARE DISORDERED IN ALL COPIES OF RABEX-5 1-74. THE C-TERMINUS OF RABEX-5 1-74 IS ORDERED TO A VARIABLE DEGREE. RESIDUES 74-76 ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-17 ARE DISORDERED IN ALL COPIES OF RABEX-5 1-74. THE C-TERMINUS OF RABEX-5 1-74 IS ORDERED TO A VARIABLE DEGREE. RESIDUES 74-76 OF UBIQUTIN ARE DISORDERED IN ALL COPIES
RfactorNum. reflection% reflectionSelection details
Rfree0.238 2876 5.1 %RANDOM
Rwork0.195 ---
obs0.198 53884 90.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.95 Å2
Baniso -1Baniso -2Baniso -3
1-0.29 Å2-0.43 Å20.02 Å2
2--0.23 Å2-0.1 Å2
3----0.58 Å2
Refinement stepCycle: LAST / Resolution: 2.1→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6178 0 6 253 6437
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0220.0226284
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7681.9668445
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0775742
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.68625.093322
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.43151228
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.6111541
X-RAY DIFFRACTIONr_chiral_restr0.1360.2895
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.024735
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.220.22621
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3080.24171
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1450.2257
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2440.2166
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1630.267
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9941.53904
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.51726024
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.85832782
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.2684.52421
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
LS refinement shellResolution: 2.1→2.15 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.273 116
Rwork0.223 2391
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)
115.557.22598.88886.99496.441914.81040.01720.4686-0.4289-0.5265-0.15840.02330.9752-0.51850.1411-0.0920.01840.0069-0.0063-0.0689-0.2044-18.0468-51.2292-15.3409
214.60391.834713.39573.71171.148518.4930.1754-0.7411-0.02860.57-0.2457-0.08950.2021-0.02590.0703-0.33440.00110.0565-0.21960.0036-0.25680.6188-44.44379.3067
35.02982.2735-0.40965.23591.27533.2402-0.04280.0929-0.4328-0.07790.0365-0.20540.21820.15270.0063-0.35170.02630.0121-0.2805-0.0282-0.2378.2759-50.426-1.1809
415.7936-5.9115-10.39397.37046.873515.038-0.0097-0.52570.5520.3794-0.15560.1367-0.7936-0.65350.1652-0.1236-0.001-0.01420.0388-0.0909-0.2027-40.0776-98.339418.7654
517.8515-3.6837-13.9523.74953.120717.22460.33040.77210.1635-0.4927-0.263-0.044-0.2902-0.073-0.0674-0.34820.0041-0.0522-0.2380.0276-0.2606-21.0935-105.4336-5.9608
65.0371-2.14530.20625.13511.39712.9623-0.0759-0.1310.43310.11350.047-0.1847-0.18950.1160.0289-0.3519-0.0238-0.0108-0.2742-0.0356-0.2244-13.4984-99.38254.5009
73.7231-5.1512-1.822421.28163.00097.8313-0.19760.1151-0.4923-0.42710.110.07330.9991-0.20250.0876-0.0369-0.08680.0764-0.1305-0.04980.0781-42.5476-70.0227-4.0087
813.2422-13.4181-7.693537.958915.493117.2086-0.10840.5411-1.21380.0812-0.161.26430.473-0.66440.2684-0.079-0.0380.0124-0.10480.02710.1132-33.8641-92.946-11.972
97.5836-1.8209-0.720711.1096-4.07586.52740.30251.20560.2439-0.81-0.4076-0.5308-0.15130.3970.10510.0346-0.00920.07950.03110.0674-0.1218-23.4036-85.7545-18.7282
106.89395.33314.790820.44934.431610.975-0.1678-0.07730.39320.25320.020.242-0.8785-0.00990.1478-0.04980.0933-0.0647-0.1367-0.03560.0169-64.4481-79.82097.3119
1110.467611.42947.740444.909318.081820.38980.1894-0.94851.50740.9181-0.6230.7128-1.1138-0.52320.43360.05790.04310.04480.0191-0.03140.211-54.9731-53.922718.0949
127.1351.22040.66648.7981-4.5318.82140.2647-1.1828-0.2610.8372-0.3677-0.6880.11130.44640.1030.05280.0072-0.08020.02840.0631-0.0804-45.652-64.21722.0978
134.9021-8.63693.966918.1721-12.72814.35530.5301-0.11270.28830.43160.29670.90030.9541-1.2556-0.82680.5177-0.3-0.13980.39770.32190.229-55.756-79.17431.8523
145.9823-10.49715.484452.6944-18.635612.33070.16390.144-1.20761.13720.53891.24460.9571-0.1883-0.70270.7281-0.0660.12120.21050.04370.0509-48.6809-106.45646.472
155.8396-0.90241.07125.5938-0.162913.27380.021-0.1059-0.38131.09950.2367-0.33110.61180.8079-0.25760.3650.0868-0.04340.1997-0.0554-0.1395-37.0476-100.401338.922
163.22037.369-5.621119.2918-12.40839.89690.40650.054-0.4291-0.4510.50370.6949-0.5647-0.9782-0.91020.45810.15960.0840.4540.29050.1948-55.5358-101.644562.5384
177.19388.7221-3.607659.9669-20.165316.5289-0.0576-0.11090.8676-1.21570.45241.2356-0.8304-0.2898-0.39480.51270.0413-0.19130.20490.0478-0.1171-50.498-80.252349.6011
185.83041.09070.01444.7902-0.374711.834-0.08710.20330.5267-1.04290.1945-0.1256-0.62440.6913-0.10750.3765-0.06240.01390.2272-0.0553-0.1225-37.187-79.765855.2491
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A18 - 44
2X-RAY DIFFRACTION2A45 - 73
3X-RAY DIFFRACTION3B1 - 73
4X-RAY DIFFRACTION4C17 - 44
5X-RAY DIFFRACTION5C45 - 73
6X-RAY DIFFRACTION6D1 - 73
7X-RAY DIFFRACTION7E17 - 44
8X-RAY DIFFRACTION8E45 - 65
9X-RAY DIFFRACTION9F1 - 73
10X-RAY DIFFRACTION10G17 - 44
11X-RAY DIFFRACTION11G45 - 71
12X-RAY DIFFRACTION12H1 - 73
13X-RAY DIFFRACTION13I17 - 44
14X-RAY DIFFRACTION14I45 - 74
15X-RAY DIFFRACTION15J1 - 72
16X-RAY DIFFRACTION16K17 - 44
17X-RAY DIFFRACTION17K45 - 65
18X-RAY DIFFRACTION18L1 - 73
Software
*PLUS
Name: REFMAC / Version: 5.2.0005 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.02
X-RAY DIFFRACTIONp_angle_d
X-RAY DIFFRACTIONp_angle_deg1.8
X-RAY DIFFRACTIONp_chiral_restr
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scangle_it
LS refinement shell
*PLUS
Highest resolution: 2.1 Å / Lowest resolution: 2.154 Å

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