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- PDB-5i8r: aSMase with zinc -

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Basic information

Entry
Database: PDB / ID: 5i8r
TitleaSMase with zinc
ComponentsSphingomyelin phosphodiesterase
KeywordsHYDROLASE / acid sphingomyelinase / olipudase alfa / zinc
Function / homology
Function and homology information


acid sphingomyelin phosphodiesterase activity / sphingomyelin metabolic process / sphingomyelin catabolic process / sphingomyelin phosphodiesterase / lamellar body / sphingomyelin phosphodiesterase activity / phospholipase C / phosphatidylcholine phospholipase C activity / endolysosome / termination of signal transduction ...acid sphingomyelin phosphodiesterase activity / sphingomyelin metabolic process / sphingomyelin catabolic process / sphingomyelin phosphodiesterase / lamellar body / sphingomyelin phosphodiesterase activity / phospholipase C / phosphatidylcholine phospholipase C activity / endolysosome / termination of signal transduction / glycosphingolipid catabolic process / plasma membrane repair / Glycosphingolipid catabolism / ceramide biosynthetic process / hydrolase activity, acting on glycosyl bonds / response to type I interferon / response to ionizing radiation / positive regulation of endocytosis / response to tumor necrosis factor / negative regulation of MAPK cascade / lipid droplet / response to interleukin-1 / cholesterol metabolic process / lysosomal lumen / cellular response to calcium ion / response to cocaine / wound healing / response to virus / cellular response to UV / nervous system development / positive regulation of viral entry into host cell / lysosome / endosome / positive regulation of apoptotic process / symbiont entry into host cell / response to xenobiotic stimulus / signal transduction / extracellular space / extracellular exosome / zinc ion binding / plasma membrane
Similarity search - Function
Sphingomyelin phosphodiesterase / Acid sphingomyelinase/endopolyphosphatase, metallophosphatase domain / Sphingomyelin phosphodiesterase, C-terminal domain / Acid sphingomyelin phosphodiesterase C-terminal region / Saposin (B) Domains / Saposin B type domain / Saposin-like / Saposin B type domain profile. / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like
Similarity search - Domain/homology
beta-D-mannopyranose / alpha-D-mannopyranose / Sphingomyelin phosphodiesterase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.646 Å
AuthorsZhou, Y.F. / Wei, R.R.
CitationJournal: Nat Commun / Year: 2016
Title: Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease.
Authors: Zhou, Y.F. / Metcalf, M.C. / Garman, S.C. / Edmunds, T. / Qiu, H. / Wei, R.R.
History
DepositionFeb 19, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 7, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 16, 2016Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / 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 / pdbx_validate_close_contact / struct_asym / struct_conn / 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.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_oper_list.symmetry_operation / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_seq_id_1 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 23, 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: Sphingomyelin phosphodiesterase
B: Sphingomyelin phosphodiesterase
C: Sphingomyelin phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)201,86031
Polymers195,3433
Non-polymers6,51728
Water00
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A: Sphingomyelin phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,56012
Polymers65,1141
Non-polymers2,44611
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Sphingomyelin phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,74511
Polymers65,1141
Non-polymers2,63110
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Sphingomyelin phosphodiesterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,5548
Polymers65,1141
Non-polymers1,4407
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)191.020, 230.870, 252.320
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

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Protein / Non-polymers , 2 types, 9 molecules ABC

#1: Protein Sphingomyelin phosphodiesterase / Acid sphingomyelinase / aSMase


Mass: 65114.270 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SMPD1, ASM / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): CHO
References: UniProt: P17405, sphingomyelin phosphodiesterase
#7: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn

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Sugars , 5 types, 22 molecules

#2: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 13
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Sugar ChemComp-BMA / beta-D-mannopyranose / beta-D-mannose / D-mannose / mannose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-mannopyranoseCOMMON NAMEGMML 1.0
b-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#6: Sugar ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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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: 6.4 Å3/Da / Density % sol: 81 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop
Details: 1.5 M ammonium sulfate, 0.1 M sodium acetate pH 5.0-5.5, 12% glycerol
PH range: 5.0-5.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 1.282 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Sep 14, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.282 Å / Relative weight: 1
ReflectionResolution: 3.646→45 Å / Num. obs: 118927 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 6.9 % / Biso Wilson estimate: 187.51 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.229 / Net I/σ(I): 7.44
Reflection shell
Resolution (Å)Rmerge(I) obsMean I/σ(I) obsDiffraction-ID% possible all
3.65-3.745.3490.34186.3
3.74-3.844.8050.5199.9
3.84-3.954.0250.63199.9
3.95-4.082.7880.961100
4.08-4.212.091.31100
4.21-4.361.4341.9199.9
4.36-4.520.9992.721100
4.52-4.710.7293.63199.9
4.71-4.920.6014.261100
4.92-5.160.5054.961100
5.16-5.440.4525.38199.9
5.44-5.770.45.891100
5.77-6.160.3187.291100
6.16-6.660.239.411100
6.66-7.290.1314.971100
7.29-8.150.07921.621100
8.15-9.410.04832.91100
9.41-11.530.03839.51100
11.53-16.310.03642.561100
16.31-450.03245.78194.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(dev_2229: ???)refinement
HKL-2000data collection
XDSdata reduction
XSCALEdata scaling
PHASER2.5.7phasing
PDB_EXTRACT3.2data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5I81

5i81


Resolution: 3.646→44.128 Å / SU ML: 0.7 / Cross valid method: FREE R-VALUE / σ(F): 1.87 / Phase error: 34.14 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2535 3840 3.24 %
Rwork0.2482 --
obs0.2484 118574 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.646→44.128 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12483 0 400 0 12883
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01313368
X-RAY DIFFRACTIONf_angle_d0.93118295
X-RAY DIFFRACTIONf_dihedral_angle_d12.6637825
X-RAY DIFFRACTIONf_chiral_restr0.0512006
X-RAY DIFFRACTIONf_plane_restr0.0072334
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.6461-3.69220.4938980.532903X-RAY DIFFRACTION67
3.6922-3.74080.47721460.47264298X-RAY DIFFRACTION100
3.7408-3.7920.46681390.48974268X-RAY DIFFRACTION100
3.792-3.84610.41421420.43754347X-RAY DIFFRACTION100
3.8461-3.90350.42191420.43674257X-RAY DIFFRACTION100
3.9035-3.96450.42191450.4224303X-RAY DIFFRACTION100
3.9645-4.02940.42131440.41164269X-RAY DIFFRACTION100
4.0294-4.09890.4371430.39334307X-RAY DIFFRACTION100
4.0989-4.17330.33471450.37694356X-RAY DIFFRACTION100
4.1733-4.25360.32991390.34164267X-RAY DIFFRACTION100
4.2536-4.34030.32991450.31974314X-RAY DIFFRACTION100
4.3403-4.43460.3111430.30114297X-RAY DIFFRACTION100
4.4346-4.53770.31311410.28194310X-RAY DIFFRACTION100
4.5377-4.6510.30281410.26624311X-RAY DIFFRACTION100
4.651-4.77660.24491410.25754308X-RAY DIFFRACTION100
4.7766-4.9170.23771440.24134277X-RAY DIFFRACTION100
4.917-5.07550.25871450.23974296X-RAY DIFFRACTION100
5.0755-5.25660.27181470.23454313X-RAY DIFFRACTION100
5.2566-5.46670.28931460.24684296X-RAY DIFFRACTION100
5.4667-5.7150.2671450.24794276X-RAY DIFFRACTION100
5.715-6.01560.2541420.25024309X-RAY DIFFRACTION100
6.0156-6.39150.2441460.23934309X-RAY DIFFRACTION100
6.3915-6.88330.21261480.22454317X-RAY DIFFRACTION100
6.8833-7.57280.22681420.20394327X-RAY DIFFRACTION100
7.5728-8.66140.18351450.18714297X-RAY DIFFRACTION100
8.6614-10.88530.16581520.16484317X-RAY DIFFRACTION100
10.8853-44.13110.23561440.23284285X-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)
10.3095-0.20060.42061.3048-1.13021.55120.8130.0580.4916-1.13871.02340.15490.67230.02970.33451.6004-0.30480.47672.1631-1.03922.9176230.583322.463852.7848
2-0.0109-0.13980.29170.0628-0.1669-0.0710.14970.12270.18260.2995-0.0415-0.9628-0.86660.9205-0.00071.8839-0.38410.25431.9926-0.45753.4297226.300343.041648.7335
31.1260.30730.34270.38380.14910.98880.1135-0.1381-0.783-0.30280.24210.1410.12190.06270.00021.46540.03720.11941.5725-0.16882.3971197.437619.590343.3404
40.4736-0.01570.1830.4207-0.20880.19610.12010.55280.9364-0.46160.2481-0.7008-0.01330.6386-01.8787-0.09930.48071.956-0.36172.4883209.463133.614534.4418
50.55970.2397-0.38530.4390.06910.54070.1007-0.20460.58240.01310.30020.4488-0.37-0.053901.6898-0.06880.38181.6534-0.31022.2042197.054239.478345.0535
60.7127-0.15130.32940.5334-0.25871.04680.0838-0.18010.13580.13840.117-0.0165-0.2056-0.2255-01.7108-0.00470.38721.8185-0.1322.6305188.62133.105556.2755
70.11320.1446-0.2610.2353-0.32650.71.7361.4202-0.7158-0.44311.05851.6609-1.1334-0.92150.81983.19820.1709-0.24644.7869-2.11782.4392135.48666.25255.1762
80.9641-0.1204-0.07590.05870.04970.02780.12811.00891.663-0.4216-0.3549-0.67860.26110.2857-0.00623.84890.8747-0.03374.2024-1.54031.8547151.097610.2433-8.9789
90.1189-0.17980.20830.21050.39960.31791.08130.00790.1282-0.0132-1.03341.6868-0.7688-1.1918-1.26873.17560.15980.37782.6204-0.94961.2863145.691137.19716.5897
100.16560.32980.2660.16970.15280.017-0.20161.6907-0.946-1.40360.32261.29570.6816-0.517104.07030.290.09173.3788-0.96672.1944146.221433.0951-3.5047
110.06360.25460.49710.26520.63640.57110.33190.428-1.0682-0.2548-0.56420.1009-0.70910.143-03.03130.32660.46893.1676-0.74951.8408161.493734.49264.6046
12-0.01680.1581-0.28370.1493-0.24070.13710.21590.4432-0.1438-0.3635-0.2414-0.169-0.1831-0.065902.7670.06720.57622.9304-0.65781.9841165.881233.683419.3481
130.1049-0.22450.0362-0.0314-0.2669-0.06040.10330.05211.1914-0.2307-0.1513-0.856-0.12111.2068-0.00431.87820.3323-0.18131.9692-0.74492.5586148.969284.730771.8973
14-0.06410.05740.0308-0.04630.01340.08340.4218-0.12320.103-0.4134-0.00370.2649-0.3528-0.1385-0.00012.08530.6885-0.34462.4221-0.63512.6441138.275782.915553.5119
150.162-0.0717-0.09780.33030.04630.1082-0.1877-0.37051.06470.2913-0.1959-0.6652-0.23590.1003-0.00021.85590.30870.15521.7938-0.20471.9049172.151566.636853.6974
160.1911-0.1091-0.23810.39920.08720.21110.3092-0.15121.3937-1.0521-0.77390.4442-1.1742-0.3999-02.47040.3231-0.06952.0271-0.20922.7563160.35980.562244.2827
170.1971-0.2401-0.19990.15740.0670.0464-0.00570.42930.0267-0.1493-0.57020.21520.4139-0.410402.05120.261-0.02412.011-0.46432.1989157.097463.890340.8445
180.3849-0.5575-0.22410.3207-0.02340.3979-0.16790.0306-0.7413-0.4382-0.2348-0.46030.2223-0.2883-02.10740.20980.28912.0232-0.47451.8134160.353650.581447.9422
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 84 through 148 )
2X-RAY DIFFRACTION2chain 'A' and (resid 149 through 181 )
3X-RAY DIFFRACTION3chain 'A' and (resid 182 through 324 )
4X-RAY DIFFRACTION4chain 'A' and (resid 325 through 416 )
5X-RAY DIFFRACTION5chain 'A' and (resid 417 through 510 )
6X-RAY DIFFRACTION6chain 'A' and (resid 511 through 611 )
7X-RAY DIFFRACTION7chain 'C' and (resid 84 through 148 )
8X-RAY DIFFRACTION8chain 'C' and (resid 149 through 181 )
9X-RAY DIFFRACTION9chain 'C' and (resid 182 through 324 )
10X-RAY DIFFRACTION10chain 'C' and (resid 325 through 416 )
11X-RAY DIFFRACTION11chain 'C' and (resid 417 through 510 )
12X-RAY DIFFRACTION12chain 'C' and (resid 511 through 611 )
13X-RAY DIFFRACTION13chain 'B' and (resid 84 through 148 )
14X-RAY DIFFRACTION14chain 'B' and (resid 149 through 181 )
15X-RAY DIFFRACTION15chain 'B' and (resid 182 through 324 )
16X-RAY DIFFRACTION16chain 'B' and (resid 325 through 416 )
17X-RAY DIFFRACTION17chain 'B' and (resid 417 through 510 )
18X-RAY DIFFRACTION18chain 'B' and (resid 511 through 611 )

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