[English] 日本語
Yorodumi
- PDB-4v7t: Crystal structure of the E. coli ribosome bound to chloramphenicol. -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4v7t
TitleCrystal structure of the E. coli ribosome bound to chloramphenicol.
Components
  • (16S rRNA) x 2
  • (23S rRNA23S ribosomal RNA) x 2
  • (30S ribosomal protein ...) x 23
  • (50S ribosomal protein ...) x 30
  • (5S rRNA5S ribosomal RNA) x 2
KeywordsRIBOSOME/ANTIBIOTIC / Protein biosynthesis / ribosomes / RNA / tRNA / transfer / erythromycin / ketolide / macrolide / antibiotic / exit / peptidyl / 30S / 70S / 16S / ribosomal subunit / small / RIBOSOME-ANTIBIOTIC complex
Function / homology
Function and homology information


stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / misfolded RNA binding / transcription antitermination factor activity, RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity ...stringent response / mRNA base-pairing translational repressor activity / ornithine decarboxylase inhibitor activity / misfolded RNA binding / transcription antitermination factor activity, RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / translational termination / DnaA-L2 complex / negative regulation of translational initiation / four-way junction DNA binding / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / regulation of mRNA stability / ribosome assembly / mRNA regulatory element binding translation repressor activity / response to reactive oxygen species / assembly of large subunit precursor of preribosome / transcription elongation factor complex / positive regulation of RNA splicing / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / transcription antitermination / DNA endonuclease activity / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / : / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / regulation of translation / ribosome biogenesis / ribosome binding / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / cytosolic large ribosomal subunit / small ribosomal subunit / cytoplasmic translation / transferase activity / tRNA binding / negative regulation of translation / molecular adaptor activity / ribosome / rRNA binding / structural constituent of ribosome / translation / response to antibiotic / mRNA binding / negative regulation of DNA-templated transcription / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm
Similarity search - Function
Ribosomal protein S21, conserved site / Ribosomal protein S21 signature. / Ribosomal protein L25, short-form / Ribosomal protein S14, bacterial/plastid / Ribosomal protein L11, bacterial-type / Ribosomal protein S21 superfamily / Ribosomal protein S21 / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein S21 ...Ribosomal protein S21, conserved site / Ribosomal protein S21 signature. / Ribosomal protein L25, short-form / Ribosomal protein S14, bacterial/plastid / Ribosomal protein L11, bacterial-type / Ribosomal protein S21 superfamily / Ribosomal protein S21 / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein S21 / Ribosomal protein L21, conserved site / Ribosomal protein L21 signature. / Ribosomal protein L11, conserved site / Ribosomal protein L11 signature. / Ribosomal protein L16 signature 1. / : / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / Ribosomal protein L16, conserved site / Ribosomal protein L16 signature 2. / Ribosomal protein L17 signature. / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal L25p family / Ribosomal protein L25 / Ribosomal protein L11, N-terminal / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11, RNA binding domain / Ribosomal protein L11/L12 / Ribosomal protein L28/L24 superfamily / Ribosomal protein L36 signature. / Ribosomal protein L25/Gln-tRNA synthetase, N-terminal / Ribosomal protein L32p, bacterial type / Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal / Ribosomal protein L9, N-terminal domain / Ribosomal protein L28 / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L5, bacterial-type / Ribosomal protein L6, bacterial-type / Ribosomal protein L18, bacterial-type / Ribosomal protein L19, conserved site / Ribosomal protein L19 signature. / Ribosomal protein L36 / Ribosomal protein L36 superfamily / Ribosomal protein L36 / Ribosomal protein L9/RNase H1, N-terminal / Ribosomal protein L20 signature. / Ribosomal protein S3, bacterial-type / Ribosomal protein L27, conserved site / Ribosomal protein S6, conserved site / Ribosomal protein L27 signature. / Ribosomal protein S6 signature. / Ribosomal protein S19, bacterial-type / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S11, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein S9, bacterial/plastid / Ribosomal protein L14P, bacterial-type / Ribosomal protein S4, bacterial-type / Ribosomal protein L34, conserved site / Ribosomal protein L34 signature. / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein L22, bacterial/chloroplast-type / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein L35 / Ribosomal protein L35 superfamily / Ribosomal protein L2, bacterial/organellar-type / Ribosomal protein L35 / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal L28 family / Ribosomal protein L33 / Ribosomal protein L33 / Ribosomal protein L28/L24 / Ribosomal protein L33 superfamily / : / Ribosomal protein L30, bacterial-type / Ribosomal protein L16 / Ribosomal protein L18 / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / Ribosomal protein S18, conserved site / Ribosomal protein S18 signature. / L28p-like
Similarity search - Domain/homology
CHLORAMPHENICOL / : / : / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 ...CHLORAMPHENICOL / : / : / : / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 / Large ribosomal subunit protein uL15 / Large ribosomal subunit protein uL11 / Large ribosomal subunit protein bL19 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein bL27 / Large ribosomal subunit protein bL28 / Large ribosomal subunit protein uL29 / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein bL33 / Large ribosomal subunit protein bL34 / Large ribosomal subunit protein bL35 / Large ribosomal subunit protein bL36A / Large ribosomal subunit protein bL9 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS9 / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL23 / Small ribosomal subunit protein uS15 / Large ribosomal subunit protein bL17 / Large ribosomal subunit protein bL21 / Large ribosomal subunit protein uL30 / Large ribosomal subunit protein uL6 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS17 / Large ribosomal subunit protein uL18 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL24 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein uL5 / Small ribosomal subunit protein bS21 / Large ribosomal subunit protein bL25
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3.1942 Å
AuthorsDunkle, J.A. / Xiong, L. / Mankin, A.S. / Cate, J.H.D.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2010
Title: Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action.
Authors: Dunkle, J.A. / Xiong, L. / Mankin, A.S. / Cate, J.H.
History
DepositionAug 14, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 9, 2014Provider: repository / Type: Initial release
SupersessionDec 10, 2014ID: 3OFA, 3OFB, 3OFC, 3OFD
Revision 1.1Dec 10, 2014Group: Other
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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 / _struct_conn.pdbx_dist_value / _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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
AA: 16S rRNA
AB: 30S ribosomal protein S2
AC: 30S ribosomal protein S3
AD: 30S ribosomal protein S4
AE: 30S ribosomal protein S5
AF: 30S ribosomal protein S6
AG: 30S ribosomal protein S7
AH: 30S ribosomal protein S8
AI: 30S ribosomal protein S9
AJ: 30S ribosomal protein S10
AK: 30S ribosomal protein S11
AL: 30S ribosomal protein S12
AM: 30S ribosomal protein S13
AN: 30S ribosomal protein S14
AO: 30S ribosomal protein S15
AP: 30S ribosomal protein S16
AQ: 30S ribosomal protein S17
AR: 30S ribosomal protein S18
AS: 30S ribosomal protein S19
AT: 30S ribosomal protein S20
AU: 30S ribosomal protein S21
BA: 23S rRNA
BB: 5S rRNA
BC: 50S ribosomal protein L2
BD: 50S ribosomal protein L3
BE: 50S ribosomal protein L4
BF: 50S ribosomal protein L5
BG: 50S ribosomal protein L6
BH: 50S ribosomal protein L9
BI: 50S ribosomal protein L11
BJ: 50S ribosomal protein L13
BK: 50S ribosomal protein L14
BL: 50S ribosomal protein L15
BM: 50S ribosomal protein L16
BN: 50S ribosomal protein L17
BO: 50S ribosomal protein L18
BP: 50S ribosomal protein L19
BQ: 50S ribosomal protein L20
BR: 50S ribosomal protein L21
BS: 50S ribosomal protein L22
BT: 50S ribosomal protein L23
BU: 50S ribosomal protein L24
BV: 50S ribosomal protein L25
BW: 50S ribosomal protein L27
BX: 50S ribosomal protein L28
BY: 50S ribosomal protein L29
BZ: 50S ribosomal protein L30
B0: 50S ribosomal protein L32
B1: 50S ribosomal protein L33
B2: 50S ribosomal protein L34
B3: 50S ribosomal protein L35
B4: 50S ribosomal protein L36
CA: 16S rRNA
CB: 30S ribosomal protein S2
CC: 30S ribosomal protein S3
CD: 30S ribosomal protein S4
CE: 30S ribosomal protein S5
CF: 30S ribosomal protein S6
CG: 30S ribosomal protein S7
CH: 30S ribosomal protein S8
CI: 30S ribosomal protein S9
CJ: 30S ribosomal protein S10
CK: 30S ribosomal protein S11
CL: 30S ribosomal protein S12
CM: 30S ribosomal protein S13
CN: 30S ribosomal protein S14
CO: 30S ribosomal protein S15
CP: 30S ribosomal protein S16
CQ: 30S ribosomal protein S17
CR: 30S ribosomal protein S18
CS: 30S ribosomal protein S19
CT: 30S ribosomal protein S20
CU: 30S ribosomal protein S21
DA: 23S rRNA
DB: 5S rRNA
DC: 50S ribosomal protein L2
DD: 50S ribosomal protein L3
DE: 50S ribosomal protein L4
DF: 50S ribosomal protein L5
DG: 50S ribosomal protein L6
DH: 50S ribosomal protein L9
DI: 50S ribosomal protein L11
DJ: 50S ribosomal protein L13
DK: 50S ribosomal protein L14
DL: 50S ribosomal protein L15
DM: 50S ribosomal protein L16
DN: 50S ribosomal protein L17
DO: 50S ribosomal protein L18
DP: 50S ribosomal protein L19
DQ: 50S ribosomal protein L20
DR: 50S ribosomal protein L21
DS: 50S ribosomal protein L22
DT: 50S ribosomal protein L23
DU: 50S ribosomal protein L24
DV: 50S ribosomal protein L25
DW: 50S ribosomal protein L27
DX: 50S ribosomal protein L28
DY: 50S ribosomal protein L29
DZ: 50S ribosomal protein L30
D0: 50S ribosomal protein L32
D1: 50S ribosomal protein L33
D2: 50S ribosomal protein L34
D3: 50S ribosomal protein L35
D4: 50S ribosomal protein L36
hetero molecules


Theoretical massNumber of molelcules
Total (without water)4,235,068469
Polymers4,225,816104
Non-polymers9,252365
Water30,8421712
1
AA: 16S rRNA
AB: 30S ribosomal protein S2
AC: 30S ribosomal protein S3
AD: 30S ribosomal protein S4
AE: 30S ribosomal protein S5
AF: 30S ribosomal protein S6
AG: 30S ribosomal protein S7
AH: 30S ribosomal protein S8
AI: 30S ribosomal protein S9
AJ: 30S ribosomal protein S10
AK: 30S ribosomal protein S11
AL: 30S ribosomal protein S12
AM: 30S ribosomal protein S13
AN: 30S ribosomal protein S14
AO: 30S ribosomal protein S15
AP: 30S ribosomal protein S16
AQ: 30S ribosomal protein S17
AR: 30S ribosomal protein S18
AS: 30S ribosomal protein S19
AT: 30S ribosomal protein S20
AU: 30S ribosomal protein S21
BA: 23S rRNA
BB: 5S rRNA
BC: 50S ribosomal protein L2
BD: 50S ribosomal protein L3
BE: 50S ribosomal protein L4
BF: 50S ribosomal protein L5
BG: 50S ribosomal protein L6
BH: 50S ribosomal protein L9
BI: 50S ribosomal protein L11
BJ: 50S ribosomal protein L13
BK: 50S ribosomal protein L14
BL: 50S ribosomal protein L15
BM: 50S ribosomal protein L16
BN: 50S ribosomal protein L17
BO: 50S ribosomal protein L18
BP: 50S ribosomal protein L19
BQ: 50S ribosomal protein L20
BR: 50S ribosomal protein L21
BS: 50S ribosomal protein L22
BT: 50S ribosomal protein L23
BU: 50S ribosomal protein L24
BV: 50S ribosomal protein L25
BW: 50S ribosomal protein L27
BX: 50S ribosomal protein L28
BY: 50S ribosomal protein L29
BZ: 50S ribosomal protein L30
B0: 50S ribosomal protein L32
B1: 50S ribosomal protein L33
B2: 50S ribosomal protein L34
B3: 50S ribosomal protein L35
B4: 50S ribosomal protein L36
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,118,342237
Polymers2,113,50552
Non-polymers4,836185
Water32418
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
CA: 16S rRNA
CB: 30S ribosomal protein S2
CC: 30S ribosomal protein S3
CD: 30S ribosomal protein S4
CE: 30S ribosomal protein S5
CF: 30S ribosomal protein S6
CG: 30S ribosomal protein S7
CH: 30S ribosomal protein S8
CI: 30S ribosomal protein S9
CJ: 30S ribosomal protein S10
CK: 30S ribosomal protein S11
CL: 30S ribosomal protein S12
CM: 30S ribosomal protein S13
CN: 30S ribosomal protein S14
CO: 30S ribosomal protein S15
CP: 30S ribosomal protein S16
CQ: 30S ribosomal protein S17
CR: 30S ribosomal protein S18
CS: 30S ribosomal protein S19
CT: 30S ribosomal protein S20
CU: 30S ribosomal protein S21
DA: 23S rRNA
DB: 5S rRNA
DC: 50S ribosomal protein L2
DD: 50S ribosomal protein L3
DE: 50S ribosomal protein L4
DF: 50S ribosomal protein L5
DG: 50S ribosomal protein L6
DH: 50S ribosomal protein L9
DI: 50S ribosomal protein L11
DJ: 50S ribosomal protein L13
DK: 50S ribosomal protein L14
DL: 50S ribosomal protein L15
DM: 50S ribosomal protein L16
DN: 50S ribosomal protein L17
DO: 50S ribosomal protein L18
DP: 50S ribosomal protein L19
DQ: 50S ribosomal protein L20
DR: 50S ribosomal protein L21
DS: 50S ribosomal protein L22
DT: 50S ribosomal protein L23
DU: 50S ribosomal protein L24
DV: 50S ribosomal protein L25
DW: 50S ribosomal protein L27
DX: 50S ribosomal protein L28
DY: 50S ribosomal protein L29
DZ: 50S ribosomal protein L30
D0: 50S ribosomal protein L32
D1: 50S ribosomal protein L33
D2: 50S ribosomal protein L34
D3: 50S ribosomal protein L35
D4: 50S ribosomal protein L36
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,116,727232
Polymers2,112,31152
Non-polymers4,416180
Water37821
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)211.456, 434.084, 621.233
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

-
RNA chain , 6 types, 6 molecules AABABBCADADB

#1: RNA chain 16S rRNA /


Mass: 496892.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: AP009048.1
#22: RNA chain 23S rRNA / 23S ribosomal RNA


Mass: 941306.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: 33357927
#23: RNA chain 5S rRNA / 5S ribosomal RNA


Mass: 38177.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: GenBank: CP000948.1
#53: RNA chain 16S rRNA /


Mass: 495927.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: AP009048.1
#57: RNA chain 23S rRNA / 23S ribosomal RNA


Mass: 941612.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: 33357927
#58: RNA chain 5S rRNA / 5S ribosomal RNA


Mass: 37848.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: GenBank: CP000948.1

+
30S ribosomal protein ... , 23 types, 40 molecules ABCBACCCADCDAECEAFCFAGAHCHAICIAJCJAKCKALCLAMANCNAOCOAPAQCQAR...

#2: Protein 30S ribosomal protein S2 /


Mass: 24253.943 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7V0
#3: Protein 30S ribosomal protein S3 /


Mass: 23078.785 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7V3
#4: Protein 30S ribosomal protein S4 /


Mass: 23383.002 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7V8
#5: Protein 30S ribosomal protein S5 /


Mass: 15804.282 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7W1
#6: Protein 30S ribosomal protein S6 /


Mass: 11669.371 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P02358
#7: Protein 30S ribosomal protein S7 /


Mass: 16861.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P02359
#8: Protein 30S ribosomal protein S8 /


Mass: 14015.361 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7W7
#9: Protein 30S ribosomal protein S9 /


Mass: 14554.882 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7X3
#10: Protein 30S ribosomal protein S10 /


Mass: 11196.988 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7R5
#11: Protein 30S ribosomal protein S11 /


Mass: 12487.200 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7R9
#12: Protein 30S ribosomal protein S12 /


Mass: 13636.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7S3
#13: Protein 30S ribosomal protein S13 /


Mass: 12625.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7S9
#14: Protein 30S ribosomal protein S14 /


Mass: 11475.364 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG59
#15: Protein 30S ribosomal protein S15 /


Mass: 10159.621 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0ADZ4
#16: Protein 30S ribosomal protein S16 /


Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7T3
#17: Protein 30S ribosomal protein S17 /


Mass: 9263.946 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG63
#18: Protein 30S ribosomal protein S18 /


Mass: 6466.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7T7
#19: Protein 30S ribosomal protein S19 /


Mass: 9057.626 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7U3
#20: Protein 30S ribosomal protein S20 /


Mass: 9506.190 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7U7
#21: Protein 30S ribosomal protein S21 /


Mass: 6067.081 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P68679
#54: Protein 30S ribosomal protein S7 /


Mass: 16764.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P02359
#55: Protein 30S ribosomal protein S13 /


Mass: 12528.639 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7S9
#56: Protein 30S ribosomal protein S16 /


Mass: 9065.417 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7T3

+
50S ribosomal protein ... , 30 types, 58 molecules BCDCBDDDBEDEBFBGDGBHDHBIDIBJDJBKDKBLDLBMDMBNDNBODOBPDPBQDQBR...

#24: Protein 50S ribosomal protein L2 /


Mass: 29663.244 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P60422
#25: Protein 50S ribosomal protein L3 /


Mass: 22277.535 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P60438
#26: Protein 50S ribosomal protein L4 /


Mass: 22121.566 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P60723
#27: Protein 50S ribosomal protein L5 /


Mass: 20073.234 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P62399
#28: Protein 50S ribosomal protein L6 /


Mass: 18801.598 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG55
#29: Protein 50S ribosomal protein L9 /


Mass: 15789.020 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7R1
#30: Protein 50S ribosomal protein L11 /


Mass: 14763.165 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7J7
#31: Protein 50S ribosomal protein L13 /


Mass: 16050.606 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AA10
#32: Protein 50S ribosomal protein L14 /


Mass: 13451.910 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0ADY3
#33: Protein 50S ribosomal protein L15 /


Mass: 14877.273 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P02413
#34: Protein 50S ribosomal protein L16 /


Mass: 15312.269 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0ADY7
#35: Protein 50S ribosomal protein L17 /


Mass: 13721.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG44
#36: Protein 50S ribosomal protein L18 /


Mass: 12663.471 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0C018
#37: Protein 50S ribosomal protein L19 /


Mass: 13028.082 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7K6
#38: Protein 50S ribosomal protein L20 /


Mass: 13396.828 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7L3
#39: Protein 50S ribosomal protein L21 /


Mass: 11586.374 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG48
#40: Protein 50S ribosomal protein L22 /


Mass: 12253.359 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P61175
#41: Protein 50S ribosomal protein L23 /


Mass: 10546.472 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0ADZ0
#42: Protein 50S ribosomal protein L24 /


Mass: 11078.874 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P60624
#43: Protein 50S ribosomal protein L25 /


Mass: 10713.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P68919
#44: Protein 50S ribosomal protein L27 /


Mass: 8476.680 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7L8
#45: Protein 50S ribosomal protein L28 /


Mass: 8896.354 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7M2
#46: Protein 50S ribosomal protein L29 /


Mass: 7286.464 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7M6
#47: Protein 50S ribosomal protein L30 /


Mass: 6423.625 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0AG51
#48: Protein 50S ribosomal protein L32 /


Mass: 6332.249 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7N4
#49: Protein/peptide 50S ribosomal protein L33 /


Mass: 5814.842 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7N9
#50: Protein/peptide 50S ribosomal protein L34 /


Mass: 5397.463 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7P5
#51: Protein 50S ribosomal protein L35 /


Mass: 7181.835 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7Q1
#52: Protein/peptide 50S ribosomal protein L36 /


Mass: 4377.390 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P0A7Q6
#59: Protein 50S ribosomal protein L5 /


Mass: 20202.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K-12 / References: UniProt: P62399

-
Non-polymers , 4 types, 2077 molecules

#60: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 362 / Source method: obtained synthetically / Formula: Mg
#61: Chemical ChemComp-CLM / CHLORAMPHENICOL / Chloramphenicol


Mass: 323.129 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H12Cl2N2O5 / Comment: antibiotic*YM
#62: Chemical ChemComp-ZN / ZINC ION


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


Mass: 18.015 Da / Num. of mol.: 1712 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.37 Å3/Da / Density % sol: 63.54 %
Crystal growTemperature: 291 K / Method: microbatch / pH: 6.5 / Details: PEG8k, MPD, pH 6.5, microbatch, temperature 291K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.1158 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 17, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1158 Å / Relative weight: 1
ReflectionResolution: 3.194→100 Å / Num. all: 703312 / Num. obs: 708760 / % possible obs: 82.6 % / Observed criterion σ(F): 1.8 / Observed criterion σ(I): 1.8 / Redundancy: 2 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 12.7
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
3.194-3.421.50.435169.7
3.42-3.551.60.356172.9
3.55-3.721.60.274175.7
3.72-3.911.70.216179.1
3.91-4.161.70.165182.4
4.16-4.481.80.133184.3
4.48-4.932.10.119186.5
4.93-5.642.20.084188.6
5.64-7.112.30.063193
7.11-1002.90.036193

-
Processing

Software
NameVersionClassificationNB
SCALEPACKdata scaling
PHENIXrefinement
PDB_EXTRACT3.1data extraction
PHENIX(phenix.refine)refinement
DENZOdata reduction
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB ENTRY 3I1M, 3I1N, 3I1O, 3I1P

3i1m
PDB Unreleased entry

3i1n
PDB Unreleased entry

3i1o
PDB Unreleased entry

3i1p
PDB Unreleased entry


Resolution: 3.1942→82.146 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 3.62 / σ(F): 0.06 / Phase error: 25.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.252 14298 2.02 %
Rwork0.1906 --
obs0.1919 708760 75.81 %
all-708760 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 41.104 Å2 / ksol: 0.226 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--2.331 Å2-0 Å20 Å2
2---7.6001 Å20 Å2
3---7.0078 Å2
Refinement stepCycle: LAST / Resolution: 3.1942→82.146 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms89372 193031 384 1712 284499
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.006308513
X-RAY DIFFRACTIONf_angle_d1.427462189
X-RAY DIFFRACTIONf_dihedral_angle_d28.169160833
X-RAY DIFFRACTIONf_chiral_restr0.07758597
X-RAY DIFFRACTIONf_plane_restr0.00524721
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1942-3.30840.36159920.289748861X-RAY DIFFRACTION54
3.3084-3.44090.314211060.252455014X-RAY DIFFRACTION60
3.4409-3.59750.29912520.229659546X-RAY DIFFRACTION65
3.5975-3.78710.266113230.20164203X-RAY DIFFRACTION70
3.7871-4.02440.246314090.185369007X-RAY DIFFRACTION76
4.0244-4.33510.237315110.176972679X-RAY DIFFRACTION80
4.3351-4.77130.239915850.173675864X-RAY DIFFRACTION83
4.7713-5.46160.229215880.165478754X-RAY DIFFRACTION86
5.4616-6.88050.243117590.163184047X-RAY DIFFRACTION91
6.8805-82.17280.232917730.191486487X-RAY DIFFRACTION92
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.1002-0.0831-0.21170.3294-0.16990.16120.00080.08630.0829-0.4063-0.104-0.1384-0.1816-0.0984-0.1880.32270.1060.1580.10640.29570.1116-62.732512.5588-76.1069
2-0.0011-0.01380.00360.0184-0.02730.0053-0.02210.03660.06350.0096-0.07530.0015-0.0570.03400.37080.1120.02220.12950.11230.3304-86.062436.4537-31.0855
30.0036-0.0108-0.00030.0072-0.00280.00010.0092-0.00310.0085-0.0226-0.01570.0047-0.0199-0.009100.75680.2407-0.02370.63970.23640.8382-98.641557.1918-39.9847
40.0022-0.0041-0.00070.0038-0.00190.0009-0.02560.0183-0.0048-0.0153-0.0077-0.0042-0.01260.006600.71690.18030.03060.6810.26480.7372-80.060155.3712-47.4684
50.0080.001-0.0010.0157-0.00030.0045-0.00690.0001-0.00350.0225-0.0048-0.0221-0.01330.015201.57250.0262-0.0391.37240.14321.6656-86.423185.803-20.1709
60.0005-0.00020.00010.0011-0.00040.00060.0043-0.00220.0035-0.0036-0.0028-0.00050.0007-0.003201.43260.043-0.00441.41560.00041.4535-118.288184.5026-17.7748
70.30110.02040.0677-0.0157-0.20720.1430.0163-0.102-0.10640.07880.23150.1199-0.0493-0.1833-00.56690.26790.25090.49070.4130.9414-146.442944.3083-3.5667
80.01180.00550.00610.01250.0024-0.00110.03390.0025-0.02570.011-0.001-0.00380.0108-0.041901.4238-0.0079-0.09981.36990.15311.436-168.383320.5995-45.5516
90.1031-0.1310.03270.2832-0.0170.1261-0.0765-0.02780.21140.16640.085-0.0832-0.184-0.01360.00520.40980.0518-0.07380.06650.0170.4041-64.807638.7281-2.7265
100.01040.0562-0.04110.2153-0.16390.1076-0.1663-0.00330.069-0.1052-0.0994-0.0751-0.07760.0221-0.07560.0876-0.00370.22010.14660.19320.2638-56.3088-6.6354-41.8744
110.2913-0.0356-0.0675-0.10280.0410.3316-0.0744-0.1129-0.25460.10660.0156-0.0063-0.00190.1031-00.8783-0.0223-0.28420.21370.12440.6061-29.371434.7217104.2371
120.0020.01170.02240.01880.02630.02080.0784-0.0098-0.1144-0.03470.019-0.0498-0.0389-0.045-01.0708-0.3693-0.44680.33040.13020.422-41.181381.713975.7999
130.00190.00010.00980.00160.00120.00580.02340.0148-0.00940.01460.02870.0073-0.01370.0074-00.9415-0.1146-0.44530.7922-0.09890.7117-51.233473.754253.1019
140.00090.00210.00410.0022-0.00170.0029-0.0177-0.0082-0.0003-0.00450.0099-0.01510.01720.0305-00.9915-0.2246-0.28160.7112-0.05210.8578-34.528363.673658.7067
150.00450.0017-0.00280.0037-0.00120.00940.01860.03150.0124-0.00850.0086-0.03210.00660.0033-01.6383-0.1129-0.04911.5341-0.10291.3687-30.760590.003726.8703
160.00120.00120.00080.001-0.00010.00170.00360.00250.00260.00420.0010.00340.0001-0.0014-01.62820.0102-0.05281.63220.02241.5931-61.610596.791322.038
170.2273-0.11790.08820.03920.05540.0338-0.2602-0.04040.1670.11020.21390.25610.0535-0.150800.823-0.137-0.35830.48920.29430.7978-95.3402114.91555.5724
180.0039-0.001-0.0048-0.0006-0.01130.00460.02560.0292-0.0367-0.0135-0.02540.05970.0023-0.015802.5035-0.0732-0.01142.53110.07252.4852-125.570875.168673.9037
190.59870.21280.00560.2558-0.0146-0.03690.1932-0.0341-0.0390.0949-0.2623-0.3664-0.08130.0752-0.03030.8358-0.3504-0.29220.17560.04950.0997-15.2156106.359276.4895
200.06220.1310.00150.12730.0970.0726-0.1021-0.0004-0.1233-0.04010.1359-0.159-0.05730.167-01.1856-0.1696-0.44020.72450.27360.6198-22.938969.1716123.9538
210.121-0.0109-0.03860.1265-0.00290.0611-0.0113-0.01380.0340.0490.0037-0.0477-0.01430.01350.04930.0169-0.0016-0.04910.0866-0.01740.093-65.6485-59.715815.2851
220.02660.0290.03420.0159-0.0385-0.00160.0934-0.07030.1199-0.11640.0681-0.1027-0.1611-0.01470.0020.23410.0144-0.23820.30020.24850.6864-139.5239-50.608-62.9387
230.0083-0.0051-0.0009-0.0029-0.00280.0009-0.0304-0.03520.0223-0.03080.04610.03830.0001-0.013600.32950.0070.04550.51050.02780.2271-103.3699-3.9086-3.1772
240.01810.0325-0.00070.0260.02310.00250.0033-0.0042-0.06890.0030.0982-0.0068-0.0684-0.1728-00.47060.03490.05080.4158-0.12440.5673-95.406518.935679.187
25-0.0006-0.001-0.00190.0007-0.00110.0007-0.01360.02870.03010.0006-0.01450.0125-0.0102-0.0069-01.6086-0.00350.0651.5208-0.01351.5976-148.5882-27.4458-12.055
260.0197-0.00150.01730.0329-0.020.018-0.00440.07920.05520.0010.03640.0433-0.14030.2124-00.0823-0.0530.02340.32890.15440.667-166.0794-23.756616.2755
270.0519-0.01130.02280.01510.00840.02470.06670.0306-0.02070.0614-0.17410.21210.0431-0.04490.00070.05580.04840.14080.305-0.01450.5634-174.5116-53.92430.3466
280.01840.01380.02350.02590.00450.0227-0.03460.03910.047-0.0337-0.04210.12580.0756-0.0980.00030.0228-0.0239-0.00960.2117-0.06150.3355-143.5929-80.2747-7.7201
29-0.00040.0004-0.00170.0028-0.00660.00870.009-0.020.0550.0150.00580.0258-0.034-0.021801.9051-0.0427-0.05231.8657-0.0631.8102-65.181720.2763122.4195
300.06240.0761-0.33330.1065-0.060.5045-0.0459-0.4413-0.05670.3060.28350.2282-0.21120.32690.27120.7601-0.3242-0.33080.6002-0.3444-0.2239-30.0769131.2368171.5278
310.02740.020.00240.00570.00390.01070.0698-0.01760.045-0.05710.00930.01170.02990.0116-02.7029-0.08780.03432.8662-0.08942.7659-116.909472.6313150.9392
32-0.00230.0043-0.00050.0005-0.00290.0085-0.02360.0005-0.00170.0104-0.03930.0163-0.0310.02401.1923-0.36150.02231.0682-0.03321.0388-60.4667115.7123110.7637
330.0062-0.016-0.0066-0.0058-0.0172-0.0028-0.03710.0190.0376-0.0243-0.07340.0812-0.0202-0.114801.15830.05530.14881.22620.00891.1937-28.7671193.581291.19
340.0007-0.0003-0.00030.00080.00020.0002-0.0037-0.00060.0076-0.0014-0.0016-0.0019-0.0009-0.0022-01.74890.0054-0.01321.7629-0.02251.7686-110.363125.1396133.0175
350.00980.0029-0.00040.00770.00150.0064-0.01480.02570.0152-0.03810.00010.0095-0.00520.0002-02.33570.0466-0.00592.41370.0082.3866-121.3874152.3692117.0347
360.0334-0.0199-0.00630.0114-0.00670.0041-0.0073-0.0096-0.06440.00160.01190.0459-0.0309-0.008201.55030.26630.06861.65670.23461.6898-129.3912170.7844144.2357
370.01470.007-0.01080.0108-0.00550.02-0.06160.05820.0173-0.0156-0.0078-0.00350.0328-0.018101.17490.18980.08241.50420.25091.349-113.7384128.714177.5545
380.0053-0.00070.00320.00670.00130.0016-0.00140.03540.0372-0.0291-0.0410.0133-0.0181-0.026101.6960.04530.08411.6550.06621.640411.0099227.665688.9835
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1((chain AA and (resid 2:8 or resid 27:557)) or (chain AD and resid 1:205) or (chain AP and resid 1:82) or (chain AT and resid 2:86) or (chain AL and resid 22:123) or (chain ZQ and (resid 299 or resid 315 or resid 362 or resid 417 or resid 509 or resid 547 or resid 533 or resid 608 or resid 536 or resid 116 or resid 352 or resid 324 or resid 100 or resid 195 or resid 259 or resid 258)))A0
2X-RAY DIFFRACTION2((chain AA and (resid 9:26 or resid 558:562 or resid 564:566 or resid 914:925 or resid 1391:1396)) or (chain AL and resid 1:21) or (chain ZQ and (resid 21 or resid 560)))A0
3X-RAY DIFFRACTION3(chain AE and resid 9:73)A0
4X-RAY DIFFRACTION4(chain AE and resid 74:149)A0
5X-RAY DIFFRACTION5(chain AB and (resid 8:107 or resid 147:225))A0
6X-RAY DIFFRACTION6(chain AB and resid 108:146)A0
7X-RAY DIFFRACTION7((chain AA and (resid 926:986 or resid 1048:1390)) or (chain AC and resid 1:206) or (chain AG and resid 1:151) or (chain AI and resid 3:129) or (chain AJ and resid 5:102) or (chain AM and resid 1:114) or (chain AN and resid 1:100) or (chain AS and resid 2:80) or (chain ZQ and (resid 934 or resid 937 or resid 980 or resid 1048 or resid 1076 or resid 1054 or resid 1303 or resid 1386 or resid 964 or resid 1222 or resid 1110 or resid 1108)))A0
8X-RAY DIFFRACTION8(chain AA and resid 987:1047)A0
9X-RAY DIFFRACTION9((chain AA and (resid 563 or resid 567:913 or resid 1496:1530)) or (chain AF and resid 1:100) or (chain AH and resid 1:129) or (chain AK and resid 12:128) or (chain AO and resid 1:88) or (chain AR and resid 19:73) or (chain AU and resid 3:53) or (chain ZQ and (resid 572 or resid 578 or resid 593 or resid 770 or resid 814 or resid 891 or resid 1500 or resid 1499 or resid 781 or resid 869 or resid 1525)))A0
10X-RAY DIFFRACTION10((chain AA and resid 1397:1495) or (chain ZQ and (resid 1417 or resid 8201)))A0
11X-RAY DIFFRACTION11((chain CA and (resid 2:8 or resid 27:557)) or (chain CD and resid 1:205) or (chain CP and resid 1:82) or (chain CT and resid 2:86) or (chain CL and resid 22:123) or (chain ZU and (resid 299 or resid 315 or resid 362 or resid 417 or resid 509 or resid 547 or resid 533 or resid 608 or resid 536 or resid 116 or resid 352 or resid 324 or resid 100 or resid 195 or resid 259 or resid 258)))C0
12X-RAY DIFFRACTION12((chain CA and (resid 9:26 or resid 558:562 or resid 564:566 or resid 914:925 or resid 1391:1396)) or (chain CL and resid 1:21) or (chain ZU and (resid 21 or resid 560)))C0
13X-RAY DIFFRACTION13(chain CE and resid 9:73)C0
14X-RAY DIFFRACTION14(chain CE and resid 74:149)C0
15X-RAY DIFFRACTION15(chain CB and (resid 8:107 or resid 147:225))C0
16X-RAY DIFFRACTION16(chain CB and resid 108:146)C0
17X-RAY DIFFRACTION17((chain CA and (resid 926:986 or resid 1048:1390)) or (chain CC and resid 1:206) or (chain CG and resid 1:151) or (chain CI and resid 3:129) or (chain CJ and resid 5:102) or (chain CM and resid 1:114) or (chain CN and resid 1:100) or (chain CS and resid 2:80) or (chain ZU and (resid 934 or resid 937 or resid 980 or resid 1048 or resid 1076 or resid 1054 or resid 1303 or resid 1386 or resid 964 or resid 1222 or resid 1110 or resid 1108)))C0
18X-RAY DIFFRACTION18(chain CA and resid 987:1047)C0
19X-RAY DIFFRACTION19((chain CA and (resid 563 or resid 567:913 or resid 1496:1530)) or (chain CF and resid 1:100) or (chain CH and resid 1:129) or (chain CK and resid 12:128) or (chain CO and resid 1:88) or (chain CR and resid 19:73) or (chain CU and resid 3:53) or (chain ZU and (resid 572 or resid 578 or resid 593 or resid 770 or resid 814 or resid 891 or resid 1500 or resid 1499 or resid 781 or resid 869 or resid 1525)))C0
20X-RAY DIFFRACTION20((chain CA and resid 1397:1495) or (chain ZU and (resid 1417 or resid 8201)))C0
21X-RAY DIFFRACTION21((chain BA and (resid 1:876 or resid 902:1038 or resid 1116:1905 or resid 1930:2092 or resid 2198:2296 or resid 2322:2903)) or (chain BC and resid 1:271) or (chain BS and resid 1:110) or (chain BT and resid 1:93) or (chain BU and resid 1:102) or (chain BD and resid 1:209) or (chain BE and resid 1:201) or (chain BG and resid 1:176) or (chain BJ and resid 1:142) or (chain BK and resid 1:122) or (chain BL and resid 2:144) or (chain BM and resid 1:136) or (chain BN and resid 1:120) or (chainRB0
22X-RAY DIFFRACTION22((chain BA and resid 1039:1115) or (chain BI and resid 1:141))B0
23X-RAY DIFFRACTION23(chain BA and resid 1906:1929)B0
24X-RAY DIFFRACTION24(chain BA and resid 2093:2197)B0
25X-RAY DIFFRACTION25(chain BA and resid 877:901)B0
26X-RAY DIFFRACTION26((chain BA and resid 2297:2321) or (chain BF and resid 1:177) or (chain ZR and resid 2304))B0
27X-RAY DIFFRACTION27((chain BB and (resid 2:69 or resid 108:119)) or (chain BO and resid 2:117))B0
28X-RAY DIFFRACTION28((chain BB and resid 70:107) or (chain BV and resid 1:94) or (chain ZR and resid 6095:6100))B0
29X-RAY DIFFRACTION29(chain BH and resid 49:149)B0
30X-RAY DIFFRACTION30((chain DA and (resid 1:876 or resid 902:1038 or resid 1116:1905 or resid 1930:2092 or resid 2198:2296 or resid 2322:2903)) or (chain DC and resid 1:271) or (chain DS and resid 1:110) or (chain DT and resid 1:93) or (chain DU and resid 1:102) or (chain DD and resid 1:209) or (chain DE and resid 1:201) or (chain DG and resid 1:176) or (chain DJ and resid 1:142) or (chain DK and resid 1:122) or (chain DL and resid 2:144) or (chain DM and resid 1:136) or (chain DN and resid 1:120) or (chainYD0
31X-RAY DIFFRACTION31((chain DA and resid 1039:1115) or (chain DI and resid 1:141))D0
32X-RAY DIFFRACTION32(chain DA and resid 1906:1929)D0
33X-RAY DIFFRACTION33(chain DA and resid 2093:2197)D0
34X-RAY DIFFRACTION34(chain DA and resid 877:901)D0
35X-RAY DIFFRACTION35((chain DA and resid 2297:2321) or (chain DF and resid 1:177) or (chain ZT and resid 2304))D0
36X-RAY DIFFRACTION36((chain DB and (resid 2:69 or resid 108:119)) or (chain DO and resid 2:117))D0
37X-RAY DIFFRACTION37((chain DB and resid 70:107) or (chain DV and resid 1:94) or (chain ZT and resid 6095:6100))D0
38X-RAY DIFFRACTION38(chain DH and resid 49:149)D0

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more