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- PDB-7v6q: Crystal structure of sNASP-ASF1A-H3.1-H4 complex -

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Basic information

Entry
Database: PDB / ID: 7v6q
TitleCrystal structure of sNASP-ASF1A-H3.1-H4 complex
Components
  • Histone H3.1
  • Histone H4
  • Histone chaperone ASF1A
  • Isoform 2 of Nuclear autoantigenic sperm protein
KeywordsCHAPERONE / Histone chaperone
Function / homology
Function and homology information


histone chaperone activity / CENP-A containing chromatin assembly / DNA replication-dependent chromatin assembly / muscle cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / response to testosterone / replication fork processing / blastocyst development / negative regulation of megakaryocyte differentiation ...histone chaperone activity / CENP-A containing chromatin assembly / DNA replication-dependent chromatin assembly / muscle cell differentiation / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / DNA repair-dependent chromatin remodeling / response to testosterone / replication fork processing / blastocyst development / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / telomere organization / Interleukin-7 signaling / Inhibition of DNA recombination at telomere / RNA Polymerase I Promoter Opening / Meiotic synapsis / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / epigenetic regulation of gene expression / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / HCMV Late Events / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / HDACs deacetylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / Nonhomologous End-Joining (NHEJ) / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / HDMs demethylate histones / G2/M DNA damage checkpoint / NoRC negatively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / male gonad development / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / HCMV Early Events / osteoblast differentiation / structural constituent of chromatin / nucleosome / protein transport / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / HATs acetylate histones / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / chromatin organization / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / Processing of DNA double-strand break ends / Senescence-Associated Secretory Phenotype (SASP) / histone binding / Oxidative Stress Induced Senescence / gene expression / Estrogen-dependent gene expression / chromosome, telomeric region / DNA replication / cadherin binding / Amyloid fiber formation / protein heterodimerization activity / DNA repair / chromatin binding / chromatin / protein-containing complex binding / protein-containing complex / DNA binding / RNA binding / extracellular exosome / extracellular region / nucleoplasm / nucleus / membrane / cytoplasm
Similarity search - Function
Tetratricopeptide, SHNi-TPR domain / : / SHNi-TPR / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats ...Tetratricopeptide, SHNi-TPR domain / : / SHNi-TPR / Histone chaperone ASF1-like / Histone chaperone ASF1-like superfamily / ASF1 like histone chaperone / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Histone-fold / Tetratricopeptide-like helical domain superfamily
Similarity search - Domain/homology
Nuclear autoantigenic sperm protein / Histone H4 / Histone H3.1 / Histone chaperone ASF1A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsLiu, C.P. / Xu, R.M.
Funding support China, 6items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2019YFA0508900 China
Ministry of Science and Technology (MoST, China)2018YFE0203300 China
Ministry of Science and Technology (MoST, China)2017YFA0506600 China
National Science Foundation (NSF, China)91853204 China
Chinese Academy of SciencesXDB37010100 China
Chinese Academy of Sciences2018125 China
CitationJournal: Genes Dev. / Year: 2021
Title: Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.
Authors: Liu, C.P. / Jin, W. / Hu, J. / Wang, M. / Chen, J. / Li, G. / Xu, R.M.
History
DepositionAug 20, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 29, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 29, 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

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Assembly

Deposited unit
A: Histone chaperone ASF1A
B: Histone H3.1
C: Histone H4
D: Isoform 2 of Nuclear autoantigenic sperm protein
E: Histone chaperone ASF1A
F: Histone H3.1
G: Histone H4
H: Isoform 2 of Nuclear autoantigenic sperm protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,96816
Polymers152,9398
Non-polymers1,0298
Water79344
1
A: Histone chaperone ASF1A
B: Histone H3.1
C: Histone H4
D: Isoform 2 of Nuclear autoantigenic sperm protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,0769
Polymers76,4694
Non-polymers6075
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12050 Å2
ΔGint-55 kcal/mol
Surface area25030 Å2
MethodPISA
2
E: Histone chaperone ASF1A
F: Histone H3.1
G: Histone H4
H: Isoform 2 of Nuclear autoantigenic sperm protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,8927
Polymers76,4694
Non-polymers4223
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11340 Å2
ΔGint-55 kcal/mol
Surface area24470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.133, 71.004, 104.394
Angle α, β, γ (deg.)105.32, 101.99, 95.75
Int Tables number1
Space group name H-MP1

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Components

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Protein , 4 types, 8 molecules AEBFCGDH

#1: Protein Histone chaperone ASF1A / Anti-silencing function protein 1 homolog A / hAsf1 / hAsf1a / CCG1-interacting factor A / CIA / hCIA


Mass: 17799.869 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ASF1A, CGI-98, HSPC146 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y294
#2: Protein Histone H3.1


Mass: 15437.167 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P68431
#3: Protein Histone H4


Mass: 11307.349 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, ...Gene: H4C1, H4/A, H4FA, HIST1H4A, H4C2, H4/I, H4FI, HIST1H4B, H4C3, H4/G, H4FG, HIST1H4C, H4C4, H4/B, H4FB, HIST1H4D, H4C5, H4/J, H4FJ, HIST1H4E, H4C6, H4/C, H4FC, HIST1H4F, H4C8, H4/H, H4FH, HIST1H4H, H4C9, H4/M, H4FM, HIST1H4I, H4C11, H4/E, H4FE, HIST1H4J, H4C12, H4/D, H4FD, HIST1H4K, H4C13, H4/K, H4FK, HIST1H4L, H4C14, H4/N, H4F2, H4FN, HIST2H4, HIST2H4A, H4C15, H4/O, H4FO, HIST2H4B, H4-16, HIST4H4
Production host: Escherichia coli (E. coli) / References: UniProt: P62805
#4: Protein Isoform 2 of Nuclear autoantigenic sperm protein / NASP


Mass: 31924.900 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NASP / Production host: Escherichia coli (E. coli) / References: UniProt: P49321

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Non-polymers , 3 types, 52 molecules

#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400


Mass: 238.278 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 44 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 3.21 Å3/Da / Density % sol: 61.66 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / Details: 18% (v/v) Tacsimate, pH 5.0 11% (v/v) PEG2000MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97913 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 15, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97913 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 33846 / % possible obs: 90.7 % / Redundancy: 13.9 % / Rmerge(I) obs: 0.096 / Net I/σ(I): 13.9
Reflection shellResolution: 3→3.11 Å / Rmerge(I) obs: 0.569 / Mean I/σ(I) obs: 2.3 / Num. unique obs: 1865

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Processing

Software
NameVersionClassification
PHENIX(1.19.2_4158)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIX(1.19.2_4158)phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2IO5, 7V6P

2io5

7v6p


Resolution: 3→14.97 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 21.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2033 922 5.93 %
Rwork0.1651 --
obs0.1674 33326 88.27 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3→14.97 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8482 0 68 44 8594
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0038686
X-RAY DIFFRACTIONf_angle_d0.5411725
X-RAY DIFFRACTIONf_dihedral_angle_d16.3533245
X-RAY DIFFRACTIONf_chiral_restr0.041305
X-RAY DIFFRACTIONf_plane_restr0.0041533
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3-3.070.28631160.23451865X-RAY DIFFRACTION73
3.07-3.160.30731280.23732036X-RAY DIFFRACTION81
3.16-3.250.27231340.21162231X-RAY DIFFRACTION87
3.25-3.350.26281500.20792185X-RAY DIFFRACTION87
3.35-3.470.22211250.18872080X-RAY DIFFRACTION83
3.47-3.610.23931530.16992399X-RAY DIFFRACTION95
3.61-3.770.17551490.16542428X-RAY DIFFRACTION94
3.77-3.960.22371580.15892364X-RAY DIFFRACTION93
3.97-4.210.17531420.1492387X-RAY DIFFRACTION93
4.21-4.520.18571480.13792286X-RAY DIFFRACTION91
4.53-4.960.14791320.13632137X-RAY DIFFRACTION84
4.97-5.650.18391490.15522285X-RAY DIFFRACTION91
5.65-6.990.19761570.17932423X-RAY DIFFRACTION96
6.99-14.970.18851350.14512244X-RAY DIFFRACTION88
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)
13.3398-2.9675-4.37534.35812.67998.70050.0939-1.3852-0.39240.35140.14190.04440.44740.8281-0.23690.4317-0.0347-0.16880.5440.01840.489333.7236-10.39118.5202
24.7813-3.33931.77162.9054-1.97952.1563-0.7457-0.41770.19070.07470.2386-0.0802-0.9954-0.06170.39520.51030.0076-0.00130.4687-0.22470.569417.35665.695817.4977
36.1861-0.50770.59734.041-0.72334.53510.38390.28460.10470.1556-0.3724-0.3345-0.09420.6625-0.06640.2757-0.06660.07190.3203-0.00640.39732.0973-5.653211.32
42.4084-2.76161.69823.2597-1.87221.2263-0.08420.79530.37780.26420.00480.3307-0.30770.13620.05850.3491-0.01020.130.36430.00580.271125.753-1.08473.4347
58.8397-0.2355-0.78785.9566-0.23355.24390.2877-1.39140.63050.7948-0.5766-0.83620.03310.73170.08480.3605-0.1311-0.13510.61930.01090.754238.4588-2.310817.1429
61.4090.26190.67182.3011-0.52240.8520.3022-0.1043-0.099-0.1307-0.24460.0273-0.16530.4438-0.13220.22940.02990.08510.36710.0270.325420.6631-2.33656.6416
73.1753-1.92960.95044.29560.08940.69210.00160.3952-0.21390.4036-0.20460.07990.1065-0.37060.16290.36690.06010.11780.37430.03270.230520.7705-7.250811.955
82.7886-0.24520.29784.06124.35415.72460.3745-1.55150.65030.26440.30950.04630.1695-0.5370.27230.80760.10430.51481.12250.17010.7155-0.33395.460218.6937
96.0049-2.1123.5922.7756-1.56983.1246-0.4395-0.7757-0.02790.2370.5830.1142-0.521-0.342-0.06890.3820.04660.13890.4158-0.01610.44697.37255.259712.6814
102.54953.8495-0.88856.0268-0.81632.6428-0.421-0.7796-1.25280.0707-0.086-0.8650.65370.70020.51230.36870.0421-0.04420.54790.18920.415430.2287-15.491411.9921
110.75090.64390.76370.6731-0.7788.49050.5867-0.4015-0.15370.2675-0.1581-0.10381.5997-1.3423-0.17910.8956-0.2965-0.19920.76960.12420.59066.2768-32.932320.0277
123.40945.08890.40039.11711.61741.9458-0.10781.5312-1.8902-0.56130.3326-1.74210.54820.473-0.34620.71430.1208-0.06540.7558-0.20880.748716.65-34.795-7.6888
133.14320.5563-1.88460.3849-0.37632.23220.42480.4923-0.0252-0.03640.27470.076-0.45850.1514-0.26761.29070.4991-0.07560.8544-0.62931.217925.3881-38.3171-9.8361
145.24130.3601-1.03135.69212.15865.64310.2442-0.1423-0.06090.49590.181-0.127-0.00060.4827-0.30350.3019-0.0323-0.01310.2860.0430.471213.7111-20.58088.7253
155.89361.87752.49026.79891.41367.91750.4069-0.3975-0.65740.2409-0.17850.51-0.1220.0286-0.28850.275-0.00380.01920.2288-0.01740.62095.6815-27.65945.2399
161.5233-0.794-0.95913.87391.82933.79480.22990.335-0.7346-0.61910.2718-0.74190.19841.0792-0.36720.47680.02120.09660.5784-0.15980.724.2822-27.10080.6411
174.14942.0181-0.04693.3511-0.58045.69140.3686-0.36970.00050.3227-0.16210.27871.0165-0.7867-0.14410.6282-0.2038-0.01480.57460.02010.362515.5213-27.319532.831
183.26571.7450.5754.4465-0.8996.89290.2131-0.6768-0.43661.2520.2566-0.59540.69291.9342-0.53360.7220.2643-0.04891.32680.06180.761239.093-23.627236.2181
197.9695-3.8304-3.99095.69544.48145.8297-0.24811.2220.2801-0.38990.0444-0.2713-0.0336-0.44620.09840.5798-0.0836-0.02910.4030.110.3852-10.195729.3616-18.4535
201.8057-0.33851.92953.31332.35924.3659-0.20610.145-0.4058-0.7888-0.2249-0.5837-0.72591.00330.16130.467-0.0520.27340.60840.10510.68836.756215.22-16.9785
215.1017-3.1290.72992.98791.64065.9348-0.32790.2631.1436-0.40350.277-0.4537-1.28460.1216-0.07820.5968-0.1073-0.00070.30080.0580.7369-7.56734.8613-14.8307
224.8227-3.19621.51652.2353-0.51775.8937-0.0055-0.2126-0.1850.67220.09510.9929-0.14340.4442-0.21070.2594-0.03930.06180.2476-0.050.4448-4.003920.6885-5.4912
231.6735-2.03632.03342.522-2.77153.305-0.00990.1967-0.04270.9643-0.18090.0622-0.81430.11680.17320.49240.00580.09910.3877-0.16090.345-0.913822.9435-2.9614
242.035-1.54030.90798.6652-2.02613.2843-0.12810.23580.347-0.79950.0669-0.4074-0.11390.36790.07110.3226-0.07260.03230.3058-0.01820.43650.345523.7452-10.8926
253.7406-0.29110.9721.9209-1.70611.9009-0.4294-0.19780.3210.09560.22590.4643-0.42160.48540.11720.35710.0216-0.04640.29080.00710.2266-7.79524.5897-7.676
264.444-3.0448-1.02815.66230.19631.3986-0.35410.45610.14520.4566-0.00320.00520.19790.05880.38780.3042-0.0109-0.07780.4158-0.12260.3006-6.501917.3695-11.4535
272.1058-2.5988-1.33814.9662-0.32023.05110.89270.8082-0.6304-1.371-0.10690.31020.30540.18490.09820.96940.1194-0.11150.5729-0.38770.61417.8857-2.2356-18.2603
284.8149-3.50572.56115.7598-3.38542.34720.39440.2422-0.3016-0.5954-0.43650.05290.2665-0.14110.05810.35930.03450.08140.43-0.09720.32677.30255.2779-12.163
296.786-0.8831-1.64772.22612.32497.8636-0.03980.00620.7613-0.5803-0.220.4944-0.5918-0.53850.3170.48370.0426-0.08940.30650.00830.3893-15.700325.8685-11.6357
301.4821-0.6241-1.68710.80530.80877.9246-0.2076-0.2959-0.030.0540.58240.4441.8264-0.9225-0.47850.6752-0.1788-0.11130.77410.12130.6914-30.64360.3377-19.4269
316.36761.3508-1.22622.969-0.83994.34870.07490.04170.31220.34540.26340.5755-0.3332-0.4565-0.16710.33480.05110.04170.27080.02390.5414-24.179410.3067-2.8024
327.59341.5478-2.45124.4894-2.81862.2452-0.27680.1635-0.459-0.35460.45410.49870.2476-0.3705-0.10640.22680.0579-0.02340.29330.05010.5996-25.13090.3789-4.1096
333.0679-0.9221.2057.93241.62473.6977-0.1333-1.62930.51830.78740.68760.0519-0.9893-0.1014-0.26560.56730.03220.25650.6061-0.09490.634-24.840714.2433.4002
340.9167-0.212-0.68920.04780.16030.5165-0.2429-0.26740.47760.1981-0.07660.104-0.0213-0.0816-0.21411.49611.15250.7561.0064-0.23062.0021-38.996125.68637.3192
358.80472.345-6.73352.0835-2.50435.93541.01290.33681.21220.0068-0.17710.7916-2.0248-0.6256-0.96190.68270.00850.00410.46870.00970.6848-25.441623.7028-8.0975
361.90751.8041.09894.94570.57086.0759-0.17940.324-0.0311-0.51450.21250.10610.2637-0.41850.01080.4647-0.0548-0.08640.4940.01260.3387-25.73979.8239-32.2878
372.80232.0641.45973.742-1.89554.93880.19610.74451.1223-1.4132-0.50730.3182-1.6781-0.76910.04221.61630.4371-0.05050.72330.09791.1103-27.437733.3163-32.0991
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 12 )
2X-RAY DIFFRACTION2chain 'A' and (resid 13 through 21 )
3X-RAY DIFFRACTION3chain 'A' and (resid 22 through 50 )
4X-RAY DIFFRACTION4chain 'A' and (resid 51 through 62 )
5X-RAY DIFFRACTION5chain 'A' and (resid 63 through 76 )
6X-RAY DIFFRACTION6chain 'A' and (resid 77 through 103 )
7X-RAY DIFFRACTION7chain 'A' and (resid 104 through 117 )
8X-RAY DIFFRACTION8chain 'A' and (resid 118 through 124 )
9X-RAY DIFFRACTION9chain 'A' and (resid 125 through 139 )
10X-RAY DIFFRACTION10chain 'A' and (resid 140 through 154 )
11X-RAY DIFFRACTION11chain 'B' and (resid 40 through 63 )
12X-RAY DIFFRACTION12chain 'B' and (resid 64 through 78 )
13X-RAY DIFFRACTION13chain 'B' and (resid 79 through 85 )
14X-RAY DIFFRACTION14chain 'B' and (resid 86 through 134 )
15X-RAY DIFFRACTION15chain 'C' and (resid 23 through 47 )
16X-RAY DIFFRACTION16chain 'C' and (resid 48 through 102 )
17X-RAY DIFFRACTION17chain 'D' and (resid 40 through 260 )
18X-RAY DIFFRACTION18chain 'D' and (resid 261 through 320 )
19X-RAY DIFFRACTION19chain 'E' and (resid 2 through 12 )
20X-RAY DIFFRACTION20chain 'E' and (resid 13 through 21 )
21X-RAY DIFFRACTION21chain 'E' and (resid 22 through 37 )
22X-RAY DIFFRACTION22chain 'E' and (resid 38 through 50 )
23X-RAY DIFFRACTION23chain 'E' and (resid 51 through 62 )
24X-RAY DIFFRACTION24chain 'E' and (resid 63 through 90 )
25X-RAY DIFFRACTION25chain 'E' and (resid 91 through 103 )
26X-RAY DIFFRACTION26chain 'E' and (resid 104 through 117 )
27X-RAY DIFFRACTION27chain 'E' and (resid 118 through 124 )
28X-RAY DIFFRACTION28chain 'E' and (resid 125 through 139 )
29X-RAY DIFFRACTION29chain 'E' and (resid 140 through 154 )
30X-RAY DIFFRACTION30chain 'F' and (resid 40 through 63 )
31X-RAY DIFFRACTION31chain 'F' and (resid 64 through 134 )
32X-RAY DIFFRACTION32chain 'G' and (resid 23 through 47 )
33X-RAY DIFFRACTION33chain 'G' and (resid 48 through 75 )
34X-RAY DIFFRACTION34chain 'G' and (resid 76 through 82 )
35X-RAY DIFFRACTION35chain 'G' and (resid 83 through 102 )
36X-RAY DIFFRACTION36chain 'H' and (resid 40 through 260 )
37X-RAY DIFFRACTION37chain 'H' and (resid 261 through 320 )

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