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- PDB-5vnj: Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-termi... -

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Basic information

Entry
Database: PDB / ID: 5vnj
TitleCrystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal FF sorting motif (ERGIC-53)
Components
  • (Protein transport protein ...Protein targeting) x 2
  • C-terminal FF Ergic-53
  • Vesicle-trafficking protein SEC22b
KeywordsPROTEIN TRANSPORT / COPII / ERGIC-53 / p24 / ER retention
Function / homology
Function and homology information


Cargo concentration in the ER / COPII-mediated vesicle transport / vesicle fusion with Golgi apparatus / COPI-coated vesicle / regulation of cholesterol transport / COPII-coated vesicle cargo loading / COPI-dependent Golgi-to-ER retrograde traffic / COPII vesicle coat / negative regulation of autophagosome assembly / SNARE complex ...Cargo concentration in the ER / COPII-mediated vesicle transport / vesicle fusion with Golgi apparatus / COPI-coated vesicle / regulation of cholesterol transport / COPII-coated vesicle cargo loading / COPI-dependent Golgi-to-ER retrograde traffic / COPII vesicle coat / negative regulation of autophagosome assembly / SNARE complex / SNAP receptor activity / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / COPII-mediated vesicle transport / ER-Phagosome pathway / syntaxin binding / endoplasmic reticulum-Golgi intermediate compartment / endoplasmic reticulum to Golgi vesicle-mediated transport / endoplasmic reticulum exit site / vesicle-mediated transport / MHC class II antigen presentation / endoplasmic reticulum-Golgi intermediate compartment membrane / GTPase activator activity / SNARE binding / cholesterol homeostasis / protein localization to plasma membrane / positive regulation of protein secretion / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / intracellular protein transport / ER to Golgi transport vesicle membrane / positive regulation of protein catabolic process / melanosome / synaptic vesicle / protein transport / Golgi membrane / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / perinuclear region of cytoplasm / zinc ion binding / cytosol
Similarity search - Function
Vesicle-trafficking protein Sec22 / Longin domain / Longin domain profile. / Sec23/Sec24 helical domain / beta-sandwich domain of Sec23/24 / Longin domain / Regulated-SNARE-like domain / Regulated-SNARE-like domain / Protein transport protein Sec23 / Sec23, C-terminal ...Vesicle-trafficking protein Sec22 / Longin domain / Longin domain profile. / Sec23/Sec24 helical domain / beta-sandwich domain of Sec23/24 / Longin domain / Regulated-SNARE-like domain / Regulated-SNARE-like domain / Protein transport protein Sec23 / Sec23, C-terminal / Zn-finger domain of Sec23/24 / Sec24-like, trunk domain / Zinc finger, Sec23/Sec24-type / Sec23/Sec24, trunk domain / Sec23/Sec24, helical domain / Sec23/Sec24 beta-sandwich / Zinc finger, Sec23/Sec24-type superfamily / Sec23/Sec24 helical domain superfamily / Sec23/Sec24 zinc finger / Sec23/Sec24 trunk domain / Sec23/Sec24 helical domain / Sec23/Sec24 beta-sandwich domain / Synaptobrevin-like / Synaptobrevin / v-SNARE, coiled-coil homology domain / v-SNARE coiled-coil homology domain profile. / Gelsolin-like domain superfamily / Severin / Severin / Gelsolin-like domain / Gelsolin repeat / Longin-like domain superfamily / von Willebrand factor, type A domain / ADF-H/Gelsolin-like domain superfamily / Beta-Lactamase / von Willebrand factor A-like domain superfamily / Four Helix Bundle (Hemerythrin (Met), subunit A) / SH3 type barrels. / Roll / Up-down Bundle / Immunoglobulin-like / Sandwich / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Vesicle-trafficking protein SEC22b / Protein transport protein Sec24A / Protein transport protein Sec23A
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.806 Å
AuthorsMa, W. / Goldberg, J.
CitationJournal: Elife / Year: 2017
Title: ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Authors: Ma, W. / Goldberg, E. / Goldberg, J.
History
DepositionApr 30, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 5, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein transport protein Sec23A
B: Protein transport protein Sec24A
C: Vesicle-trafficking protein SEC22b
D: C-terminal FF Ergic-53
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,2776
Polymers189,1474
Non-polymers1312
Water1,35175
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: monomer
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4790 Å2
ΔGint-17 kcal/mol
Surface area65710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)147.955, 96.978, 129.549
Angle α, β, γ (deg.)90.00, 90.22, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein transport protein ... , 2 types, 2 molecules AB

#1: Protein Protein transport protein Sec23A / Protein targeting / SEC23-related protein A


Mass: 86178.414 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEC23A / Cell line (production host): Hi-5 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15436
#2: Protein Protein transport protein Sec24A / Protein targeting / SEC24-related protein A


Mass: 84336.820 Da / Num. of mol.: 1 / Fragment: UNP residues 346-1093
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEC24A / Cell line (production host): Hi-5 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O95486

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Protein / Protein/peptide , 2 types, 2 molecules CD

#3: Protein Vesicle-trafficking protein SEC22b / ER-Golgi SNARE of 24 kDa / ERS24 / SEC22 vesicle-trafficking protein homolog B / SEC22 vesicle- ...ER-Golgi SNARE of 24 kDa / ERS24 / SEC22 vesicle-trafficking protein homolog B / SEC22 vesicle-trafficking protein-like 1 / mSec22b


Mass: 18031.645 Da / Num. of mol.: 1 / Fragment: UNP residues 1-157
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Sec22b, Sec22l1 / Production host: Escherichia coli (E. coli) / References: UniProt: O08547
#4: Protein/peptide C-terminal FF Ergic-53


Mass: 599.675 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

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Non-polymers , 2 types, 77 molecules

#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 75 / 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: 2.46 Å3/Da / Density % sol: 49.94 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / Details: 50mM HEPES PH 7.8, 0.5M NaAc and 12% PEG4K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.987 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 14, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 2.8→48.826 Å / Num. obs: 44706 / % possible obs: 98.2 % / Redundancy: 2.5 % / Net I/σ(I): 1

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Processing

Software
NameVersionClassification
PHENIX1.10_2155refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2NUT

2nut


Resolution: 2.806→48.826 Å / SU ML: 0.39 / Cross valid method: NONE / σ(F): 1.34 / Phase error: 29.3
RfactorNum. reflection% reflection
Rfree0.2606 1999 4.48 %
Rwork0.2208 --
obs0.2226 44670 99.27 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.806→48.826 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12420 0 2 75 12497
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00212713
X-RAY DIFFRACTIONf_angle_d0.49917232
X-RAY DIFFRACTIONf_dihedral_angle_d11.1927744
X-RAY DIFFRACTIONf_chiral_restr0.0411948
X-RAY DIFFRACTIONf_plane_restr0.0042227
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.806-2.87620.34891330.3412829X-RAY DIFFRACTION93
2.8762-2.9540.35791370.3143038X-RAY DIFFRACTION99
2.954-3.04090.32951440.3033033X-RAY DIFFRACTION99
3.0409-3.1390.3491430.29543044X-RAY DIFFRACTION99
3.139-3.25120.34321460.2653024X-RAY DIFFRACTION100
3.2512-3.38130.28321400.25563035X-RAY DIFFRACTION100
3.3813-3.53520.2831490.25053070X-RAY DIFFRACTION100
3.5352-3.72150.2641400.23923065X-RAY DIFFRACTION100
3.7215-3.95450.29741420.22123047X-RAY DIFFRACTION100
3.9545-4.25970.26231470.19463080X-RAY DIFFRACTION100
4.2597-4.68810.21551430.17333070X-RAY DIFFRACTION100
4.6881-5.36570.22921460.18973078X-RAY DIFFRACTION100
5.3657-6.75740.2521430.21133112X-RAY DIFFRACTION100
6.7574-48.83340.20191460.18713146X-RAY DIFFRACTION100
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)
14.30371.3249-0.35393.6675-0.93223.2666-0.1445-0.0845-0.4025-0.33190.011-0.2480.4578-0.01890.18960.66460.03450.05510.48-0.22520.4281181.548-113.8773-2.013
20.45450.5636-0.450.6817-0.55730.44590.33561.8156-0.30240.47720.42370.74370.8049-1.02380.29651.0239-0.2097-0.08711.126-0.4480.407167.7506-117.4804-12.4817
35.75423.7148-0.7976.2551-0.59762.2879-0.1694-0.4863-0.23350.3392-0.1254-0.6229-0.46630.4915-0.18430.61430.05970.22120.5012-0.07510.576185.1636-97.32864.6462
46.45440.8276-1.82934.2443-1.23411.7411-0.12260.41980.1611-0.4551-0.0117-0.6336-0.0817-0.0938-0.02890.96720.12680.250.5374-0.01740.5957190.1156-93.3696-13.1829
53.5692-0.5015-0.9923.12551.12973.06910.1151-0.0220.5449-0.0957-0.03490.3063-0.1613-0.2655-0.13410.25140.04880.01440.2925-0.00840.4362163.8997-82.542722.7674
66.1263-2.501-0.50443.91492.43212.24160.64180.18271.520.12030.0199-0.0658-0.69370.921-0.27880.40460.08860.14110.50180.01610.5972170.0041-75.716126.5467
71.68850.024-0.88253.16811.3732.5095-0.02340.2209-0.1933-0.0273-0.05830.88520.2254-0.47810.20140.31060.06570.07470.5443-0.05870.7171150.8366-93.108420.9104
81.7231-0.617-1.40081.44440.91583.25-0.05860.1813-0.1283-0.2343-0.1280.10450.1095-0.05010.05730.45740.02420.11210.3669-0.11480.4522167.9752-97.255817.3017
92.5746-0.6096-0.72527.03880.64060.23070.38510.7375-0.0433-0.7696-0.43720.6848-0.3597-0.779-0.05670.73120.13960.04360.7702-0.09730.5803166.9522-100.5998-3.3283
102.61510.59850.55344.46840.35543.82430.43520.56090.0337-1.29280.3347-1.283-0.29640.1329-0.14060.5120.08260.17630.6182-0.01590.3517180.5061-98.8469-2.4486
110.4870.6729-1.18560.9435-1.64362.84270.42431.4225-0.6818-1.8647-0.9039-0.38940.50450.8154-0.10431.27380.3710.08351.1961-0.35730.6474177.8714-122.694-10.9644
125.4864-0.39390.79156.0466-0.26914.43270.45610.4125-0.0466-0.52890.10320.98680.0779-0.2246-0.11620.53130.0007-0.03570.4996-0.22640.4367162.9269-112.69874.2978
131.18570.0916-0.27774.0346-0.14552.70010.62530.4380.0132-1.38440.25580.76840.3132-0.91290.4910.7336-0.1408-0.2070.7244-0.41150.8455160.5265-123.8513-1.7402
141.1754-2.48680.60025.7589-0.79656.66680.72851.1519-0.6308-1.06-1.0297-0.48091.41940.3353-0.11721.12190.1025-0.1110.683-0.28751.1466166.7454-139.5977-5.4377
152.3403-0.15410.28972.93910.37232.9773-0.2161-0.0852-0.5967-0.3143-0.2599-0.09920.76360.3435-0.06140.677-0.04970.11620.459-0.22860.6062169.0954-126.87155.291
160.0323-0.17870.2860.808-1.33522.22330.25730.4749-0.7372-0.17820.19210.5273-0.251-0.32840.48180.62-0.23080.19690.4095-0.30270.9249155.5209-115.784916.6633
172.4554-0.77270.90313.10691.01682.61360.1793-0.3562-0.3833-0.4677-0.03070.43280.07430.35590.14560.52880.0140.17910.3381-0.05710.6233165.8106-109.478614.769
183.1857-0.34672.17742.646-0.77956.00580.05680.81280.4828-0.3427-0.3968-0.84631.0170.717-0.09180.67330.0230.18480.4254-0.02250.6747177.591-126.950224.079
193.1908-0.04313.65351.3566-0.00534.23260.7925-0.8108-0.37030.0576-0.2867-0.34290.8986-0.51680.35390.723-0.05510.3320.32570.07350.7616171.5468-124.98629.7462
203.1178-0.3574-0.88375.02110.38090.72940.3498-0.4440.01430.5594-0.852-0.56910.06040.56960.06740.5020.0096-0.01420.6615-0.06551.0295181.4572-117.98934.0735
212.50710.14110.45363.17280.57352.28810.1008-0.6270.1157-0.09530.0634-0.084-0.3939-0.18350.01780.5836-0.12020.29750.5663-0.20290.8037166.3767-118.373728.656
223.52990.0417-0.37974.05861.23983.07470.53070.1421-0.6903-0.8535-0.29271.23280.8876-0.4476-0.00051.0111-0.0350.13850.5565-0.3091.1966160.8034-134.10164.1127
236.9751-1.06642.13163.5619-0.64811.9051-0.03630.19971.83320.81910.28341.0877-0.67590.49770.10621.07150.11730.11180.4822-0.07140.8599119.0593-17.087445.295
242.3209-0.9509-0.48080.896-0.05020.3235-0.0655-0.19210.17610.31720.08640.3212-0.17010.0740.00670.49320.07690.12170.3584-0.03310.5105115.5299-38.588750.6529
253.38590.0071-0.09631.5653-0.33261.7987-0.1821-1.1493-1.15280.46810.52330.63420.9125-0.26230.11590.51410.12770.20790.70450.31810.9212109.8206-57.522661.8074
262.37140.27061.52032.7278-0.53991.1256-0.5977-1.1397-0.56670.05240.41430.31-0.1638-0.16070.03890.54690.21550.23070.6850.20410.7227117.3322-55.149265.288
271.9965-1.2578-0.0951.8450.69262.0591-0.1292-0.1525-0.14520.02580.0111-0.16890.28660.26170.02360.3340.0960.08330.36010.0270.5292145.4863-61.755440.98
284.4286-0.21950.71543.43660.73793.55610.14090.3509-1.1671-0.0297-0.1084-0.13681.0880.2339-0.09490.62530.07390.1850.4488-0.00450.6388152.8241-72.798733.1835
291.2877-0.2250.16731.75611.60727.4526-0.6533-0.4211-0.46160.4398-0.90670.58241.6307-0.7562-0.30640.58030.09420.140.43140.07110.9554147.1438-73.492341.073
304.6316-0.926-0.27443.85751.6132.5791-0.11990.0022-0.8446-0.0323-0.3038-1.56980.37610.3850.10550.29810.01090.06580.4342-0.01580.8864157.8227-63.192843.423
311.8368-1.1370.62091.70670.41181.96640.10130.4709-0.2492-0.3256-0.0525-0.48360.07460.17380.06670.34280.10030.14260.3892-0.00230.6241145.0588-61.234129.0966
321.57-0.62550.10860.2315-0.04340.6241-0.63431.39360.8024-0.21820.197-0.93460.42620.59690.00750.86140.02250.00310.73830.26931.0773136.3428-39.92816.2765
332.23040.911-0.44092.9366-0.13952.4444-0.13660.2003-0.1118-0.2374-0.05120.00280.20010.0186-0.02730.38140.09110.08480.31130.00850.4691134.1007-55.320329.2937
341.4026-0.8603-0.04921.5060.83611.20290.0171-0.03960.3694-0.12870.0563-0.1278-0.09350.05950.00730.30830.03740.04580.21770.10540.4619135.5972-49.039841.4501
354.82621.16053.34157.7718-0.20517.260.18450.22930.4791-0.4158-0.29130.43960.635-0.1186-0.01350.5572-0.02860.19240.4619-0.10270.5987123.2411-57.354640.3706
361.8669-1.13131.74532.5557-0.58231.4915-0.0269-0.2023-0.4571-0.0640.08960.21140.1716-0.1032-0.00210.36750.0830.1520.39550.04940.5782116.7863-51.119250.3375
372.9009-0.7156-0.64022.4977-0.85262.3308-0.3060.1788-0.1016-0.1814-0.03350.07660.2564-0.08140.21310.30530.04930.01350.3555-0.00870.439114.8249-32.702235.7823
382.03250.92240.15910.1690.17831.5055-0.0423-0.01550.3387-0.1388-0.01220.0233-0.17760.1250.06980.42630.05030.04250.33710.06040.5028134.1777-28.297842.4906
394.35971.771-0.60172.01010.37823.25190.12550.07470.2073-0.1468-0.0823-0.2878-0.37690.41090.15370.4913-0.04040.06080.42480.05870.5455152.5826-24.892149.9119
404.11780.46690.77990.6764-0.09661.5602-0.48510.84660.9943-0.15650.099-0.1294-0.29790.27910.16240.50110.00820.06560.50020.07390.4929133.9334-24.706934.4784
415.4266-0.6280.41694.77042.96091.9640.38620.72370.7062-0.35570.4395-0.0682-0.2737-0.3766-0.25830.9774-0.01270.55670.24120.34230.7567128.2412-82.897955.2241
421.8620.09224.10753.43060.05569.21780.67120.5317-0.6211-0.73550.1890.6149-0.34480.539-0.80070.76480.03110.18750.5866-0.06870.8507132.2025-77.936348.4312
435.7511-0.8483-0.24846.0917-2.22082.0188-0.52180.11220.0553-0.36260.0810.86190.253-0.32170.74120.7291-0.12670.180.5347-0.02040.7363120.5986-85.432953.7239
447.59743.979-4.62188.813-1.6132.9081-0.52740.6887-1.16490.4230.54870.46311.8191-1.7019-0.04251.2577-0.29030.30540.656-0.23831.3638124.784-95.36450.1896
457.3019-2.8242-2.38348.30732.60686.7607-1.25860.2176-1.2829-1.1843-0.1557-1.43390.38971.22870.62240.88570.05180.51490.58120.14891.1653133.5183-89.830955.7697
467.80260.45210.63014.52521.72892.22260.1827-0.67240.39120.7806-0.4945-1.06720.0555-0.08410.13560.81750.05870.25740.60320.27570.7867130.2914-74.701865.4871
475.2211-2.0805-0.88037.09164.15082.533-0.73990.7023-0.2683-0.67590.8975-0.2894-0.01770.8625-0.0060.82950.05920.4040.87040.18771.2149142.6922-84.605850.1982
482.0002-2.42664.18951.0588-1.79653.04370.2402-0.956-1.69571.5232-0.0879-0.54642.01-0.2237-0.08212.2631-0.29920.54770.7441-0.20541.4856122.4041-99.421152.7196
498.7170.5275-1.15314.59650.5540.30450.11831.2428-0.67850.04431.24122.40071.0449-1.3696-0.99721.048-0.27580.09580.98090.11161.1093115.5201-92.231550.2327
500.20410.1011-0.22921.41121.17151.784-0.9233-1.0645-0.67432.7160.0285-0.4966-0.8768-0.32910.40892.01390.4712-0.72911.00530.0051.5348116.4505-63.551350.3292
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 27 )
2X-RAY DIFFRACTION2chain 'A' and (resid 28 through 39 )
3X-RAY DIFFRACTION3chain 'A' and (resid 40 through 57 )
4X-RAY DIFFRACTION4chain 'A' and (resid 58 through 114 )
5X-RAY DIFFRACTION5chain 'A' and (resid 115 through 205 )
6X-RAY DIFFRACTION6chain 'A' and (resid 223 through 246 )
7X-RAY DIFFRACTION7chain 'A' and (resid 247 through 341 )
8X-RAY DIFFRACTION8chain 'A' and (resid 342 through 413 )
9X-RAY DIFFRACTION9chain 'A' and (resid 414 through 464 )
10X-RAY DIFFRACTION10chain 'A' and (resid 475 through 505 )
11X-RAY DIFFRACTION11chain 'A' and (resid 506 through 518 )
12X-RAY DIFFRACTION12chain 'A' and (resid 519 through 537 )
13X-RAY DIFFRACTION13chain 'A' and (resid 541 through 557 )
14X-RAY DIFFRACTION14chain 'A' and (resid 558 through 567 )
15X-RAY DIFFRACTION15chain 'A' and (resid 568 through 586 )
16X-RAY DIFFRACTION16chain 'A' and (resid 587 through 596 )
17X-RAY DIFFRACTION17chain 'A' and (resid 597 through 619 )
18X-RAY DIFFRACTION18chain 'A' and (resid 620 through 638 )
19X-RAY DIFFRACTION19chain 'A' and (resid 639 through 666 )
20X-RAY DIFFRACTION20chain 'A' and (resid 679 through 698 )
21X-RAY DIFFRACTION21chain 'A' and (resid 699 through 723 )
22X-RAY DIFFRACTION22chain 'A' and (resid 747 through 764 )
23X-RAY DIFFRACTION23chain 'B' and (resid 346 through 361 )
24X-RAY DIFFRACTION24chain 'B' and (resid 362 through 416 )
25X-RAY DIFFRACTION25chain 'B' and (resid 417 through 466 )
26X-RAY DIFFRACTION26chain 'B' and (resid 476 through 493 )
27X-RAY DIFFRACTION27chain 'B' and (resid 494 through 557 )
28X-RAY DIFFRACTION28chain 'B' and (resid 558 through 575 )
29X-RAY DIFFRACTION29chain 'B' and (resid 576 through 591 )
30X-RAY DIFFRACTION30chain 'B' and (resid 592 through 604 )
31X-RAY DIFFRACTION31chain 'B' and (resid 605 through 647 )
32X-RAY DIFFRACTION32chain 'B' and (resid 648 through 662 )
33X-RAY DIFFRACTION33chain 'B' and (resid 666 through 709 )
34X-RAY DIFFRACTION34chain 'B' and (resid 710 through 763 )
35X-RAY DIFFRACTION35chain 'B' and (resid 764 through 780 )
36X-RAY DIFFRACTION36chain 'B' and (resid 781 through 826 )
37X-RAY DIFFRACTION37chain 'B' and (resid 827 through 882 )
38X-RAY DIFFRACTION38chain 'B' and (resid 888 through 996 )
39X-RAY DIFFRACTION39chain 'B' and (resid 997 through 1045 )
40X-RAY DIFFRACTION40chain 'B' and (resid 1046 through 1093 )
41X-RAY DIFFRACTION41chain 'C' and (resid 1 through 14 )
42X-RAY DIFFRACTION42chain 'C' and (resid 15 through 23 )
43X-RAY DIFFRACTION43chain 'C' and (resid 29 through 50 )
44X-RAY DIFFRACTION44chain 'C' and (resid 51 through 58 )
45X-RAY DIFFRACTION45chain 'C' and (resid 59 through 99 )
46X-RAY DIFFRACTION46chain 'C' and (resid 100 through 112 )
47X-RAY DIFFRACTION47chain 'C' and (resid 113 through 132 )
48X-RAY DIFFRACTION48chain 'C' and (resid 148 through 152 )
49X-RAY DIFFRACTION49chain 'C' and (resid 153 through 157 )
50X-RAY DIFFRACTION50chain 'D' and (resid 1 through 2 )

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