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- PDB-1kjv: TAP-B-associated rat MHC class I molecule -

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Basic information

Entry
Database: PDB / ID: 1kjv
TitleTAP-B-associated rat MHC class I molecule
Components
  • Mature alpha chain of major histocompatibility complex class I antigen (HEAVY CHAIN)
  • beta-2-microglobulin
  • peptide NPR
KeywordsIMMUNE SYSTEM / Peptide-MHC / Major Histocompatibility Complex
Function / homology
Function and homology information


negative regulation of store-operated calcium channel activity / : / Endosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / DAP12 signaling / negative regulation of toll-like receptor 3 signaling pathway ...negative regulation of store-operated calcium channel activity / : / Endosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / DAP12 signaling / negative regulation of toll-like receptor 3 signaling pathway / : / aggrephagy / Cargo recognition for clathrin-mediated endocytosis / aggresome / Neutrophil degranulation / antigen processing and presentation / regulation of protein ubiquitination / autophagosome maturation / autophagosome assembly / autophagosome / polyubiquitin modification-dependent protein binding / regulation of macroautophagy / response to cadmium ion / response to endoplasmic reticulum stress / proteasome complex / positive regulation of protein ubiquitination / cellular response to iron ion / macroautophagy / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / negative regulation of forebrain neuron differentiation / regulation of erythrocyte differentiation / peptide antigen assembly with MHC class I protein complex / regulation of iron ion transport / response to molecule of bacterial origin / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / kinase binding / negative regulation of neurogenesis / peptide antigen assembly with MHC class II protein complex / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / positive regulation of cellular senescence / peptide antigen binding / negative regulation of epithelial cell proliferation / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / sensory perception of smell / positive regulation of T cell activation / negative regulation of neuron projection development / MHC class II protein complex binding / late endosome membrane / iron ion transport / cellular response to hypoxia / T cell differentiation in thymus / protein refolding / cytoplasmic vesicle / ubiquitin-dependent protein catabolic process / protein homotetramerization / intracellular iron ion homeostasis / amyloid fibril formation / membrane => GO:0016020 / learning or memory / response to xenobiotic stimulus / immune response / protein domain specific binding / lysosomal membrane / external side of plasma membrane / structural molecule activity / perinuclear region of cytoplasm / endoplasmic reticulum / protein homodimerization activity / extracellular space / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
: / : / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / MHC class I, alpha chain, C-terminal ...: / : / Heat shock chaperonin-binding / Heat shock chaperonin-binding motif. / UBA/TS-N domain / Ubiquitin associated domain / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / MHC class I, alpha chain, C-terminal / MHC_I C-terminus / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / MHC class I alpha chain, alpha1 alpha2 domains / Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ubiquitin-like domain superfamily / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Beta-2-microglobulin / Mature alpha chain of major histocompatibility complex class I antigen / Ubiquilin-1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.48 Å
AuthorsRudolph, M.G. / Stevens, J. / Speir, J.A. / Trowsdale, J. / Butcher, G.W. / Joly, E. / Wilson, I.A.
Citation
Journal: J.Mol.Biol. / Year: 2002
Title: Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B.
Authors: Rudolph, M.G. / Stevens, J. / Speir, J.A. / Trowsdale, J. / Butcher, G.W. / Joly, E. / Wilson, I.A.
#1: Journal: Immunity / Year: 2001
Title: Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa
Authors: Speir, J.A. / Stevens, J.S. / Joly, E. / Butcher, G.W. / Wilson, I.A.
History
DepositionDec 5, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 18, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 21, 2022Group: Database references / Derived calculations / Category: database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Sep 20, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Mature alpha chain of major histocompatibility complex class I antigen (HEAVY CHAIN)
B: beta-2-microglobulin
P: peptide NPR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,2007
Polymers45,8153
Non-polymers3844
Water7,638424
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5080 Å2
ΔGint-66 kcal/mol
Surface area19070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)48.397, 50.522, 200.073
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Mature alpha chain of major histocompatibility complex class I antigen (HEAVY CHAIN) / MHC class I RT1-A1c heavy chain


Mass: 33017.570 Da / Num. of mol.: 1
Fragment: extracellular domain, residues 1-276 plus C-terminal His tag
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Production host: Escherichia coli (E. coli) / References: UniProt: Q95565
#2: Protein beta-2-microglobulin


Mass: 11783.478 Da / Num. of mol.: 1 / Fragment: residues 21-119, numbered 2-100
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Production host: Escherichia coli (E. coli) / References: UniProt: P07151
#3: Protein/peptide peptide NPR


Mass: 1014.222 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence of the peptide was designed from biochemical studies.
References: UniProt: Q9JJP9
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 424 / 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: 2.67 Å3/Da / Density % sol: 53.9 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 26% PEG 4000, 0.2 M Li2SO4, 2% MPD, 0.1 M Tris/HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K
Crystal grow
*PLUS
Temperature: 17 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
115 mg/mlprotein1drop
226 %(w/v)PEG40001reservoir
30.2 M1reservoirLi2SO4
42 %(v/v)MPD1reservoir
50.1 MTris-HCl1reservoirpH8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.95007 Å
DetectorType: CUSTOM-MADE / Detector: CCD / Date: Jun 28, 2000
RadiationMonochromator: Si-111 double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.95007 Å / Relative weight: 1
ReflectionResolution: 1.48→35 Å / Num. obs: 82429 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Rsym value: 0.049 / Net I/σ(I): 32.4
Reflection shellResolution: 1.48→1.5 Å / Redundancy: 3 % / Mean I/σ(I) obs: 2 / Num. unique all: 2721 / Rsym value: 0.693 / % possible all: 100
Reflection
*PLUS
Rmerge(I) obs: 0.049
Reflection shell
*PLUS
% possible obs: 100 % / Num. unique obs: 2721 / Rmerge(I) obs: 0.693

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMAC5refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1ED3, molecule 1

1ed3


Resolution: 1.48→34.92 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.956 / SU B: 3.101 / SU ML: 0.06 / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.077 / ESU R Free: 0.067 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19113 5912 7.6 %RANDOM
Rwork0.16177 ---
obs0.16404 77790 94.47 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 7.66 Å2
Baniso -1Baniso -2Baniso -3
1--0.7 Å20 Å20 Å2
2--0.42 Å20 Å2
3---0.28 Å2
Refinement stepCycle: LAST / Resolution: 1.48→34.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3226 0 20 424 3670
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0213330
X-RAY DIFFRACTIONr_bond_other_d0.0010.022927
X-RAY DIFFRACTIONr_angle_refined_deg1.5561.9554516
X-RAY DIFFRACTIONr_angle_other_deg1.17236825
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.6983382
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.24115637
X-RAY DIFFRACTIONr_chiral_restr0.0960.2463
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.023672
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02715
X-RAY DIFFRACTIONr_nbd_refined0.2250.3631
X-RAY DIFFRACTIONr_nbd_other0.2070.32887
X-RAY DIFFRACTIONr_nbtor_other0.3570.52
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1740.5392
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.0980.312
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.250.53
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2070.337
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.180.521
X-RAY DIFFRACTIONr_symmetry_hbond_other0.0910.52
X-RAY DIFFRACTIONr_mcbond_it0.9631.51933
X-RAY DIFFRACTIONr_mcangle_it1.41323145
X-RAY DIFFRACTIONr_scbond_it2.07231397
X-RAY DIFFRACTIONr_scangle_it3.0494.51371
X-RAY DIFFRACTIONr_rigid_bond_restr1.15723330
X-RAY DIFFRACTIONr_sphericity_free5.1022424
X-RAY DIFFRACTIONr_sphericity_bonded1.80723247
LS refinement shellResolution: 1.48→1.5 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.248 391 -
Rwork0.223 --
obs-5114 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)
112.1546-7.82520.20097.16970.37311.44190.09630.59960.5396-0.0701-0.0928-0.6216-0.01980.2381-0.00350.1063-0.00810.0010.06750.00360.104114.496218.250136.695
217.4828-0.1066-7.179715.75263.10438.6630.06781.0199-0.0083-0.5209-0.37871.54660.0841-0.87760.31090.14230.0164-0.04350.149-0.02490.2442-7.362423.324436.6738
315.6034-2.8081-2.72452.9581.11952.3653-0.00230.3852-0.1073-0.01060.0307-0.07680.03160.1471-0.02840.10540.00760.0060.0375-0.01370.079.254115.942734.9759
49.1782-2.5034-1.20464.40011.8115.6834-0.00340.4210.0956-0.05330.1473-0.35340.05490.2967-0.14390.1281-0.00680.00220.0596-0.03270.108610.802912.833632.3224
516.3731-10.5503-6.89047.534.53350.94130.11851.6378-1.1651-0.4364-0.58480.7084-0.0764-0.57030.46630.32470.01050.04530.377-0.14110.29868.6177.028828.577
61.5054-1.3007-0.76568.79712.92752.0886-0.06970.1216-0.2056-0.01560.02550.00660.09220.03720.04410.1132-0.0106-0.00130.0016-0.00560.05083.759214.087442.8373
7-0.7316-1.2331-0.71656.59293.66874.9230.09530.2047-0.0754-0.188-0.38420.5425-0.0951-0.48840.28890.17040.0226-0.00510.0539-0.00620.1221-3.936134.395441.9069
88.1223-6.0383.75685.5815-2.50130.41870.19330.58890.1545-0.0235-0.2992-0.39370.05090.21270.10590.13610.012-0.00950.05170.00790.110514.918521.004240.7786
928.5203-18.6895-22.778225.957926.537128.73520.17190.04011.26210.20050.1174-1.68750.53511.2269-0.28930.16840.0082-0.0490.26370.09710.288129.361916.591141.4445
1018.1411-14.08574.520613.3087-3.2551.69720.01380.38110.47820.1739-0.1978-0.639-0.03560.21710.1840.1452-0.0033-0.00780.01470.00420.090313.021726.530542.8949
114.27611.96350.52840.77430.81871.38010.01860.21490.2175-0.0114-0.0383-0.064-0.20470.13540.01970.1406-0.00070.00250.00680.00090.084311.171632.216543.5293
1212.1504-7.71770.124610.7844-1.40710.63280.15310.06150.18280.0335-0.2561-0.8114-0.08820.19980.1030.1659-0.0365-0.03660.04210.00010.142617.563630.610150.3932
134.6261-4.58411.718113.546-5.18336.0350.0154-0.50080.06490.48230.0235-0.2041-0.06310.0004-0.03890.129-0.0316-0.00850.0442-0.0190.08399.673431.3855.4199
142.9904-3.0883-2.38258.32864.0817.20910.0225-0.2175-0.11760.46530.0548-0.22080.23720.1619-0.07730.145-0.0134-0.05510.03440.0310.152317.567217.36951.6524
154.8604-0.1403-0.22826.6085.1811.6665-0.10580.524-0.4413-0.28590.1886-0.61050.34290.541-0.08270.17770.0320.04940.1275-0.05720.307222.49145.554135.6342
163.40963.4049-7.386945.614-40.549341.1745-0.32030.1782-0.5088-1.6233-0.1019-0.07912.13820.03590.42210.2530.05080.13850.2710.02940.377626.650912.276416.9326
174.3179-4.17251.959818.9661-10.38689.463-0.00240.6008-0.0438-0.6331-0.2956-0.1160.46220.22580.2980.11770.00080.03640.42710.04540.122925.949328.39292.9466
1821.0844-4.49088.570916.1639-10.57798.80950.06820.13660.51230.4459-0.1592-0.2681-0.2368-0.34580.0910.08450.0060.00880.48590.19450.138823.732841.17370.87
195.02135.1079-2.209317.5351-11.50289.2461-0.26420.5389-0.2434-0.25330.13680.05110.28160.03220.12740.08350.01360.03790.31190.04620.112624.671727.61038.0958
203.90734.1641-0.917711.5159-2.73997.24060.0772-0.3121-0.25460.4911-0.31810.18890.00540.31590.2410.08820.02830.05380.26320.10660.243425.023419.346620.8531
215.23453.8782-1.49018.0303-5.45917.92450.0105-0.2433-0.3280.2492-0.4399-0.3137-0.09630.38970.42940.07110.01520.01480.31670.13920.179533.69831.340512.4142
2241.769-11.6996-5.46777.88586.069417.2179-0.4087-1.10690.96460.32220.02030.1045-0.5432-0.15980.38840.1391-0.0346-0.04490.34910.14890.256537.539935.564114.141
239.50544.6512-1.19027.6061-2.50624.87230.051-0.118-0.03290.217-0.195-0.314-0.30480.18990.1440.07530.03440.02030.26320.06550.148520.773426.446616.967
244.39512.1347-2.8773.2473-3.91354.3088-0.01020.2195-0.03790.1108-0.2225-0.1207-0.16440.15640.23270.0776-0.0014-0.00040.28850.09840.143625.136531.50410.8831
253.6815-12.7271-6.91938.3274-6.172317.23170.10160.65980.1758-0.8424-0.1288-0.29740.37940.80570.02710.1298-0.0336-0.01030.63610.29090.280833.086937.8926-0.9521
266.18783.2852-1.63114.2521-13.731812.7175-0.21920.2521-0.2673-0.1405-0.1591-0.4270.26310.17880.37820.07430.01850.02410.38350.12630.213135.441128.36269.7694
278.20153.4269-2.075213.6034-7.64213.2515-0.3291-0.4779-0.9372-0.2786-0.6619-1.40070.68741.32430.9910.1270.07750.06940.41260.22420.417934.562417.285917.9153
2815.1245-0.88330.35576.4858-5.376813.714-0.1220.9237-0.7007-0.4762-0.05420.00930.9448-0.13610.17620.20380.03080.08480.45730.0410.225833.839125.7892.5321
290.7418-4.94-7.38438.175814.523455.6547-0.1665-0.03840.38610.38240.15450.1351-0.99890.36030.0120.2598-0.02730.03070.15080.05350.19727.120736.032728.8401
305.4894-0.2379-1.7324.32682.54024.0345-0.03940.5255-0.0733-0.24670.0805-0.0824-0.16770.1098-0.04120.0916-0.00280.01230.23870.07170.080611.235326.925313.1336
319.75030.9346-0.34151.7703-1.2044-0.9248-0.27251.6447-1.1975-0.5780.0934-0.28550.57360.2980.17910.2955-0.0160.06560.5999-0.19030.310914.030716.5343.3515
324.01441.5879-0.0199.249310.529718.783-0.08490.3394-0.3306-0.02260.1731-0.19460.24760.1861-0.08820.0821-0.00190.02090.21020.05050.09039.236122.772514.9053
337.58791.34023.59733.55051.44898.54070.07570.02230.19350.1566-0.02260.0578-0.2622-0.2492-0.05310.13790.01090.02990.12470.06570.0683.12529.810226.8798
343.16760.61692.90971.31430.60428.1204-0.06940.5642-0.03310.12420.14360.10040.3753-0.269-0.07420.0941-0.01680.00230.29220.06920.08880.53225.012610.9404
350.9943-0.07351.93410.63830.03276.5640.06980.3546-0.1208-0.00780.16690.06740.416-0.1074-0.23680.1254-0.03320.0010.23140.05080.13294.377123.002921.1698
365.20981.26614.44131.82273.37121.64970.07390.463-0.4023-0.0078-0.0874-0.04270.6025-0.09880.01360.1122-0.01530.02360.20890.01350.12487.096519.792415.6593
371.0534-3.6725-0.359613.78440.91293.2531-0.2081.5217-0.2288-1.27040.3074-0.22770.3730.403-0.09940.2778-0.1250.03740.7932-0.02810.1416.560323.6776-0.9769
382.4109-0.7644-2.18351.35196.659220.7447-0.14540.51710.27080.12790.08950.03710.1663-0.48640.05590.0926-0.02120.01120.24470.13020.11940.290530.460314.4379
394.7398-0.0733.6254-0.09552.767923.0893-0.05390.51231.0430.03390.0430.1093-1.6513-0.36370.01090.23870.03520.06140.19590.12750.27840.355937.474420.3582
4026.3589-6.331-9.36415.32485.832810.44690.26770.86670.4966-0.23370.08270.2308-0.12720.1262-0.35030.06930.00610.00240.27770.1340.1245.840132.54559.7711
4135.42513.8556-1.82683.5512-8.692513.5668-0.03581.51730.0606-0.22150.2342-0.3048-0.0182-0.0086-0.19840.11440.00110.03530.42150.05430.106213.988927.97444.355
424.3251-6.2873-1.896913.84264.72651.7307-0.0585-0.1112-0.14250.41790.0209-0.05160.13850.05340.03760.1368-0.0134-0.01110.01140.00710.08138.888517.674448.8085
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 121 - 12
2X-RAY DIFFRACTION2AA13 - 2113 - 21
3X-RAY DIFFRACTION3AA22 - 2822 - 28
4X-RAY DIFFRACTION4AA29 - 3729 - 37
5X-RAY DIFFRACTION5AA38 - 5138 - 51
6X-RAY DIFFRACTION6AA52 - 8452 - 84
7X-RAY DIFFRACTION7AA85 - 9485 - 94
8X-RAY DIFFRACTION8AA95 - 10395 - 103
9X-RAY DIFFRACTION9AA104 - 111104 - 111
10X-RAY DIFFRACTION10AA112 - 118112 - 118
11X-RAY DIFFRACTION11AA119 - 126119 - 126
12X-RAY DIFFRACTION12AA127 - 138127 - 138
13X-RAY DIFFRACTION13AA139 - 149139 - 149
14X-RAY DIFFRACTION14AA150 - 163150 - 163
15X-RAY DIFFRACTION15AA164 - 180164 - 180
16X-RAY DIFFRACTION16AA181 - 186181 - 186
17X-RAY DIFFRACTION17AA187 - 193187 - 193
18X-RAY DIFFRACTION18AA194 - 199194 - 199
19X-RAY DIFFRACTION19AA200 - 206200 - 206
20X-RAY DIFFRACTION20AA207 - 214207 - 214
21X-RAY DIFFRACTION21AA215 - 219215 - 219
22X-RAY DIFFRACTION22AA220 - 225220 - 225
23X-RAY DIFFRACTION23AA226 - 241226 - 241
24X-RAY DIFFRACTION24AA242 - 249242 - 249
25X-RAY DIFFRACTION25AA250 - 254250 - 254
26X-RAY DIFFRACTION26AA255 - 262255 - 262
27X-RAY DIFFRACTION27AA263 - 270263 - 270
28X-RAY DIFFRACTION28AA271 - 276271 - 276
29X-RAY DIFFRACTION29BB1 - 72 - 8
30X-RAY DIFFRACTION30BB8 - 129 - 13
31X-RAY DIFFRACTION31BB13 - 2214 - 23
32X-RAY DIFFRACTION32BB23 - 2924 - 30
33X-RAY DIFFRACTION33BB30 - 3731 - 38
34X-RAY DIFFRACTION34BB38 - 4239 - 43
35X-RAY DIFFRACTION35BB43 - 6344 - 64
36X-RAY DIFFRACTION36BB64 - 7165 - 72
37X-RAY DIFFRACTION37BB72 - 7973 - 80
38X-RAY DIFFRACTION38BB80 - 8481 - 85
39X-RAY DIFFRACTION39BB85 - 9286 - 93
40X-RAY DIFFRACTION40BB93 - 9594 - 96
41X-RAY DIFFRACTION41BB96 - 9997 - 100
42X-RAY DIFFRACTION42PC1 - 91 - 9
Refinement
*PLUS
Lowest resolution: 35 Å / % reflection Rfree: 7.5 % / Rfactor Rfree: 0.191 / Rfactor Rwork: 0.162
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.014
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg1.56

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