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- PDB-5eiy: Bacterial cellulose synthase bound to a substrate analogue -

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Basic information

Entry
Database: PDB / ID: 5eiy
TitleBacterial cellulose synthase bound to a substrate analogue
Components
  • (Putative cellulose ...) x 2
  • poly(unk)
KeywordsMEMBRANE PROTEIN / cellulose biosynthesis / METAL BINDING PROTEIN
Function / homology
Function and homology information


cellulose synthase (UDP-forming) / cellulose synthase (UDP-forming) activity / cellulose biosynthetic process / UDP-alpha-D-glucose metabolic process / cyclic-di-GMP binding / endomembrane system / metal ion binding / plasma membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #4520 / Chitobiase; domain 2 - #20 / Chitobiase; domain 2 - #30 / : / Cellulose Synthase Subunit B, alpha-beta domain / Cellulose synthase, subunit A / : / Cellulose synthase BcsB, bacterial / Bacterial cellulose synthase subunit / Cellulose synthase ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #4520 / Chitobiase; domain 2 - #20 / Chitobiase; domain 2 - #30 / : / Cellulose Synthase Subunit B, alpha-beta domain / Cellulose synthase, subunit A / : / Cellulose synthase BcsB, bacterial / Bacterial cellulose synthase subunit / Cellulose synthase / predicted glycosyltransferase like domains / Glycosyltransferase like family 2 / PilZ domain / PilZ domain / Chitobiase; domain 2 / Glycosyl transferase family 2 / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Galactose-binding domain-like / Nucleotide-diphospho-sugar transferases / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Thrombin, subunit H / Jelly Rolls / Alpha-Beta Complex / Up-down Bundle / Beta Barrel / Sandwich / 2-Layer Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-43Y / Chem-660 / Chem-C2E / DIUNDECYL PHOSPHATIDYL CHOLINE / Cellulose synthase catalytic subunit [UDP-forming] / Cyclic di-GMP-binding protein
Similarity search - Component
Biological speciesRhodobacter sphaeroides (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.95 Å
AuthorsMcNamara, J.T. / Zimmer, J.
CitationJournal: Nature / Year: 2016
Title: Observing cellulose biosynthesis and membrane translocation in crystallo.
Authors: Morgan, J.L. / McNamara, J.T. / Fischer, M. / Rich, J. / Chen, H.M. / Withers, S.G. / Zimmer, J.
History
DepositionOct 30, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 9, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 23, 2016Group: Database references
Revision 1.2Mar 30, 2016Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / citation / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_oper_list / pdbx_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _citation.journal_id_CSD / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_oper_list.symmetry_operation / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 2.2Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Putative cellulose synthase
B: Putative cellulose synthase
D: poly(unk)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)174,03213
Polymers167,8123
Non-polymers6,22010
Water19811
1
A: Putative cellulose synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)96,21110
Polymers90,0151
Non-polymers6,1969
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Putative cellulose synthase
D: poly(unk)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,8223
Polymers77,7972
Non-polymers241
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)68.475, 216.654, 221.335
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Putative cellulose ... , 2 types, 2 molecules AB

#1: Protein Putative cellulose synthase


Mass: 90014.742 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (bacteria)
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 / Gene: RSP_0333 / Production host: Escherichia coli (E. coli)
References: UniProt: Q3J125, cellulose synthase (UDP-forming)
#2: Protein Putative cellulose synthase


Mass: 77013.453 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (bacteria) / Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158 / Gene: RSP_0332 / Production host: Escherichia coli (E. coli) / References: UniProt: Q3J126

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Protein/peptide / Sugars , 2 types, 2 molecules D

#3: Protein/peptide poly(unk)


Mass: 783.958 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (bacteria) / Production host: Escherichia coli (E. coli)
#4: Polysaccharide beta-D-galactopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D- ...beta-D-galactopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose


Type: oligosaccharide / Mass: 2774.409 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGalpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-4DGlcpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,17,16/[a2122h-1b_1-5][a2112h-1b_1-5]/1-1-1-1-1-1-1-1-1-1-1-1-1-1-1-1-2/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1_f4-g1_g4-h1_h4-i1_i4-j1_j4-k1_k4-l1_l4-m1_m4-n1_n4-o1_o4-p1_p4-q1WURCSPDB2Glycan 1.1.0
[][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Glcp]{[(4+1)][b-D-Galp]{}}}}}}}}}}}}}}}}}LINUCSPDB-CARE

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Non-polymers , 7 types, 20 molecules

#5: Chemical ChemComp-PLC / DIUNDECYL PHOSPHATIDYL CHOLINE


Mass: 622.834 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C32H65NO8P / Comment: phospholipid*YM
#6: Chemical ChemComp-43Y / [(2R)-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] propanoate / 1,2-dipropionyl-sn-glycero-3-phosphocholine


Mass: 370.356 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H29NO8P
#7: Chemical ChemComp-C2E / 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) / c-di-GMP / Cyclic diguanosine monophosphate


Mass: 690.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H24N10O14P2
#8: Chemical ChemComp-LDA / LAURYL DIMETHYLAMINE-N-OXIDE


Mass: 229.402 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H31NO / Comment: LDAO, detergent*YM
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#10: Chemical ChemComp-660 / [[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-[[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]methyl]phosphinic acid / UDP-glucose phosphonate


Mass: 564.329 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H26N2O16P2
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 5.36 Å3/Da / Density % sol: 77.04 %
Crystal growTemperature: 300 K / Method: vapor diffusion, sitting drop / pH: 5.6 / Details: sodium acetate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 1 / Detector: CCD / Date: Oct 15, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→35 Å / Num. obs: 133706 / % possible obs: 99.3 % / Redundancy: 10.4 % / Rmerge(I) obs: 0.28 / Net I/σ(I): 5.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
Aimlessdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4P00

4p00


Resolution: 2.95→34.92 Å / FOM work R set: 0.7935 / SU ML: 0.4 / Cross valid method: FREE R-VALUE / σ(F): 0.03 / Phase error: 28.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2481 6659 4.98 %
Rwork0.2215 127047 -
obs0.2229 133706 99.87 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 239.95 Å2 / Biso mean: 83.94 Å2 / Biso min: 38.99 Å2
Refinement stepCycle: final / Resolution: 2.95→34.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10689 0 408 11 11108
Biso mean--88.18 62.72 -
Num. residues----1395
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00311423
X-RAY DIFFRACTIONf_angle_d0.90515635
X-RAY DIFFRACTIONf_chiral_restr0.0321827
X-RAY DIFFRACTIONf_plane_restr0.0041980
X-RAY DIFFRACTIONf_dihedral_angle_d13.8034151
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.95-2.98350.39172070.357242984505100
2.9835-3.01860.32991840.340242664450100
3.0186-3.05540.3462200.334841834403100
3.0554-3.09410.36522520.326942684520100
3.0941-3.13480.35562440.329242394483100
3.1348-3.17770.38192070.336942194426100
3.1777-3.2230.38962040.316442404444100
3.223-3.27110.36252540.298242434497100
3.2711-3.32220.31442320.297841934425100
3.3222-3.37660.34442030.277342504453100
3.3766-3.43480.23552340.261642774511100
3.4348-3.49720.28182130.273441874400100
3.4972-3.56440.30942460.259542654511100
3.5644-3.63710.3092170.257742284445100
3.6371-3.71610.33272390.253842044443100
3.7161-3.80240.29912070.253442914498100
3.8024-3.89740.26442240.236141704394100
3.8974-4.00260.23542570.217742524509100
4.0026-4.12020.26511720.219142534425100
4.1202-4.2530.27082140.20142704484100
4.253-4.40470.20012330.199142034436100
4.4047-4.58070.22172030.190542944497100
4.5807-4.78870.19882520.181441574409100
4.7887-5.04050.17842400.177242314471100
5.0405-5.35520.24022450.178741964441100
5.3552-5.7670.20472020.192242624464100
5.767-6.34420.21451700.185743004470100
6.3442-7.25510.21191790.184142444423100
7.2551-9.11370.15462160.16164201441799
9.1137-34.92240.22762890.20164163445299
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)
10.8755-0.64080.99260.5421-0.621.53470.33480.2303-0.07130.7717-0.15850.77670.33960.7908-0.22571.0966-0.47450.23450.7391-0.34410.8894-23.5477-21.575576.1689
21.4789-0.17680.68981.94520.84473.40140.0328-0.13750.06650.4525-0.18450.08670.4724-0.2360.16290.6578-0.16410.050.5972-0.21410.5617-10.4367-12.852667.19
33.9479-4.3232-5.50879.05253.26849.5723-0.34510.2239-0.44510.0673-0.13170.22150.2337-0.65560.25460.8516-0.34020.03131.0745-0.32820.8103-23.02982.044592.7283
44.42030.5588-0.66544.57291.08043.87160.0787-0.6164-0.04031.11160.1233-0.45670.82280.4938-0.16321.18460.0008-0.05730.7256-0.18820.5655-3.280811.1685109.0788
54.40711.3626-1.26355.34893.25023.12860.1441-0.32690.3948-0.08930.0946-0.261-0.5301-0.36090.03850.6004-0.0713-00.7278-0.13090.6203-1.483614.950880.6888
60.6338-0.2687-0.76371.8841.86473.73080.0093-0.1107-0.1910.79490.1061-0.06570.69980.223-0.0990.86-0.0524-0.00350.6218-0.19650.6969-4.3082-3.640985.2362
78.7731.6527-5.3495.4798-5.01449.01020.4890.2043-0.6213-0.2566-0.8883-0.60480.59672.23980.40021.42330.5068-0.3951.1335-0.27831.014912.0814-9.343991.8221
83.51-1.51640.1014.1155-4.21075.1429-0.008-0.56910.64491.43010.7049-0.2737-0.65221.2041-0.76190.91490.0575-0.02791.2315-0.50171.04913.472513.891386.9406
91.6950.41410.22512.43280.26213.044-0.2350.488-0.1796-0.20580.7329-0.53120.01341.1626-0.46580.5443-0.12710.09180.9157-0.45360.818310.28570.262162.1181
103.327-0.6297-0.00685.30061.12222.6548-0.12250.48890.0759-0.2330.1005-0.1097-0.2147-0.010.04060.4941-0.10830.01370.5522-0.0950.4558-4.716139.238393.3835
117.33733.21986.88855.11345.14289.1975-0.13370.62710.2339-0.149-0.14170.59510.14670.23280.36240.58560.01240.10350.6839-0.06320.5536-10.655923.005394.2742
127.56632.30021.03122.9876-0.89683.4178-0.52290.50570.6385-0.50360.5403-0.6325-0.80120.7013-0.00420.8265-0.20340.24491.0254-0.49490.88428.68115.088469.524
139.63224.01626.24875.1281.30054.5178-0.0821-0.59110.52370.09990.13250.2838-1.179-1.08740.32090.54760.05680.04790.5346-0.06740.6262-7.7718-37.941310.9622
144.55432.1294-0.28499.51510.76565.88420.08090.26990.1293-0.1394-0.2434-0.4882-0.71630.74580.12450.5108-0.0171-0.01210.6092-0.00870.49564.1295-35.194610.4548
156.05214.1640.97613.29312.42447.62591.3354-0.96720.74811.4516-0.23750.3073-1.76260.4998-0.92841.0276-0.25540.27640.8669-0.29040.984210.0871-18.556716.6685
167.45744.019-0.48932.7531-0.46842.4870.06020.32750.14120.10920.00410.10870.1999-0.245-0.00950.54650.06310.00110.3905-0.06050.4232-15.5241-44.85959.6402
173.49511.4834-2.36627.10042.24943.3881-0.89721.87540.5061-1.04391.4618-0.30621.74670.2497-0.68371.0873-0.14130.16891.0797-0.06980.8056-31.4646-48.01340.0313
187.2111-0.4468-1.78295.1943-0.59294.3447-0.11680.2012-1.3624-0.22240.09640.560.8776-0.32850.0690.7025-0.09-0.10350.5601-0.06790.6943-22.3462-56.88157.0486
193.20790.9095-0.26472.71990.69791.73620.1509-0.0095-0.07150.01650.0935-0.36460.18910.3371-0.25950.54750.0729-0.03670.7179-0.22110.54015.1114-27.680736.6521
202.12841.4130.86744.04112.05997.15640.1043-0.6395-0.25080.4238-0.38330.42390.424-0.70570.14650.5378-0.0820.11890.6635-0.12830.5471-24.7107-40.897929.4007
218.0994.5512-2.82742.8367-1.01452.54810.4699-0.64270.6317-0.0543-0.81091.6442-0.7656-1.79520.35970.80070.2748-0.06581.2-0.31920.9207-33.9521-23.507824.7041
220.40850.78710.81464.98892.29666.21210.1222-0.14020.5329-0.2221-0.31580.9709-0.398-1.18050.13660.73730.08210.01540.9785-0.26930.7028-15.7427-11.248842.5195
236.1434-1.91793.41826.1158-0.77774.2129-0.1588-0.12820.80160.1545-0.1974-0.2038-0.2667-0.18350.27210.5445-0.00320.03770.5362-0.18360.5453-22.3103-28.465926.694
242.3594-0.1298-1.00523.23270.0954.9260.1856-0.20140.06290.3649-0.34240.36781.0688-0.23880.22050.5685-0.3470.19310.7997-0.2940.5977-22.943-22.34863.0519
253.7798-3.1468-1.06726.18455.00725.18130.4762-0.4994-0.4037-0.0239-0.3411.314-0.70170.1639-0.17560.9614-0.18480.14150.96620.10991.1739-42.1282-19.603424.0463
263.23512.9304-2.76484.7564-3.14724.7156-0.94750.9851-0.4135-0.52190.3776-0.08370.251-0.2566-0.24751.1285-0.1521-0.51980.4682-0.37421.3736-44.3331-30.637629.2868
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(CHAIN A AND RESID 13:35)A13 - 35
2X-RAY DIFFRACTION2(CHAIN A AND RESID 36:117)A36 - 117
3X-RAY DIFFRACTION3(CHAIN A AND RESID 118:135)A118 - 135
4X-RAY DIFFRACTION4(CHAIN A AND RESID 136:277)A136 - 277
5X-RAY DIFFRACTION5(CHAIN A AND RESID 278:297)A278 - 297
6X-RAY DIFFRACTION6(CHAIN A AND RESID 298:488)A298 - 488
7X-RAY DIFFRACTION7(CHAIN A AND RESID 489:502)A489 - 502
8X-RAY DIFFRACTION8(CHAIN A AND RESID 503:522)A503 - 522
9X-RAY DIFFRACTION9(CHAIN A AND RESID 523:575)A523 - 575
10X-RAY DIFFRACTION10(CHAIN A AND RESID 576:674)A576 - 674
11X-RAY DIFFRACTION11(CHAIN A AND RESID 675:706)A675 - 706
12X-RAY DIFFRACTION12(CHAIN A AND RESID 707:740)A707 - 740
13X-RAY DIFFRACTION13(CHAIN B AND RESID 54:67)B54 - 67
14X-RAY DIFFRACTION14(CHAIN B AND RESID 68:153)B68 - 153
15X-RAY DIFFRACTION15(CHAIN B AND RESID 154:169)B154 - 169
16X-RAY DIFFRACTION16(CHAIN B AND RESID 170:242)B170 - 242
17X-RAY DIFFRACTION17(CHAIN B AND RESID 243:248)B243 - 248
18X-RAY DIFFRACTION18(CHAIN B AND RESID 249:303)B249 - 303
19X-RAY DIFFRACTION19(CHAIN B AND RESID 304:451)B304 - 451
20X-RAY DIFFRACTION20(CHAIN B AND RESID 452:504)B452 - 504
21X-RAY DIFFRACTION21(CHAIN B AND RESID 505:531)B505 - 531
22X-RAY DIFFRACTION22(CHAIN B AND RESID 544:599)B544 - 599
23X-RAY DIFFRACTION23(CHAIN B AND RESID 600:665)B600 - 665
24X-RAY DIFFRACTION24(CHAIN B AND RESID 666:720)B666 - 720
25X-RAY DIFFRACTION25(CHAIN D AND RESID 169:174)D169 - 174
26X-RAY DIFFRACTION26(CHAIN D AND RESID 175:177)D175 - 177

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