Header list of 1oln.pdb file
Complete list - 21 20 Bytes
HEADER RIBOSOME/ANTIBIOTIC 08-AUG-03 1OLN
TITLE MODEL FOR THIOSTREPTON ANTIBIOTIC BINDING TO L11 SUBSTRATE FROM 50S
TITLE 2 RIBOSOMAL RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L11;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: THIOSTREPTON;
COMPND 6 CHAIN: B;
COMPND 7 SYNONYM: ALANINAMIDE, BRYAMYCIN, THIACTIN;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: RNA;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: RESIDUES 1051-1108
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: STREPTOMYCES AZUREUS;
SOURCE 6 ORGANISM_TAXID: 146537;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 9 ORGANISM_TAXID: 2336
KEYWDS RIBOSOME-ANTIBIOTIC COMPLEX, THIOPEPTIDE, ANTIBACTERIAL, THIAZOLE,
KEYWDS 2 OXAZOLE, RIBOSOME, L11, TRANSLATION INHIBITION
EXPDTA SOLUTION NMR; THEORETICAL MODEL
MDLTYP MINIMIZED AVERAGE
AUTHOR G.LENTZEN,R.KLINCK,N.MATASSOVA,F.ABOUL-ELA,A.I.H.MURCHIE
REVDAT 6 21-AUG-19 1OLN 1 REMARK
REVDAT 5 24-APR-19 1OLN 1 SEQRES LINK
REVDAT 4 15-NOV-17 1OLN 1 REMARK
REVDAT 3 13-JUL-11 1OLN 1 VERSN
REVDAT 2 24-FEB-09 1OLN 1 VERSN
REVDAT 1 11-SEP-03 1OLN 0
JRNL AUTH G.LENTZEN,R.KLINCK,N.MATASSOVA,F.ABOUL-ELA,A.I.H.MURCHIE
JRNL TITL STRUCTURAL BASIS FOR CONTRASTING ACTIVITIES OF RIBOSOME
JRNL TITL 2 BINDING THIAZOLE ANTIBIOTICS
JRNL REF CHEM.BIOL. V. 10 769 2003
JRNL REFN ISSN 1074-5521
JRNL PMID 12954336
JRNL DOI 10.1016/S1074-5521(03)00173-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.T.WIMBERLY,R.GUYMON,J.P.MCCUTCHEON,S.W.WHITE,
REMARK 1 AUTH 2 V.RAMAKRISHNAN
REMARK 1 TITL A DETAILED VIEW OF A RIBOSOMAL ACTIVE SITE: THE STRUCTURE OF
REMARK 1 TITL 2 THE L11-RNA COMPLEX
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 97 491 1999
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 10338213
REMARK 1 DOI 10.1016/S0092-8674(00)80759-X
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.L.CONN,D.E.DRAPER,E.E.LATTMAN,A.G.GITTIS
REMARK 1 TITL CRYSTAL STRUCTURE OF A CONSERVED RIBOSOMAL PROTEIN-RNA
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF SCIENCE V. 284 1171 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 10325228
REMARK 1 DOI 10.1126/SCIENCE.284.5417.1171
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : RDOCK
REMARK 3 AUTHORS : DAVID MORLEY
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE COORDINATES OF THE PROTEIN, RNA AND
REMARK 3 THE ANTIBIOTIC WERE HELD RIGID DURING REFINEMENT. THE
REMARK 3 COORDINATES OF THE RIBOSOMAL L11 (CHAIN A) AND THE RNA (CHAIN C)
REMARK 3 WERE FROM PDB ENTRY 1MMS. THE COORDINATES OF THE ANTIBIOTIC
REMARK 3 THIOSTREPTON (CHAIN B) WERE FROM PDB ENTRY 1E9W. REFINEMENT
REMARK 3 DETAILS CAN BE FOUND IN THE JRNL CITATION.
REMARK 4
REMARK 4 1OLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1290013289.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 100 MM NACL, 5 MM MGCL2
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DOCKING/MODELING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 BEST OVERALL DOCKING SCORE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: BEST OVERALL DOCKING SCORE AND LEAST RESTRAINT VIOLATION.
REMARK 210 THE NOES INCLUDED IN THE RESTRAINTED MODELING WERE OBTAINED FROM
REMARK 210 A FILTERED NOESY EXPERIMENT ON A COMPLEX OF UNLABELED
REMARK 210 THIOSTREPTON WITH THE RNA. AS ALL INTERNAL COORDINATES WERE HELD
REMARK 210 RIGID ACCORDING TO THE X-RAY STRUCTURES, ONLY INTERMOLECULAR
REMARK 210 NOES WERE INCLUDED. ASSIGNMENTS FOR RNA WERE CHOSEN FROM AN
REMARK 210 ITERATIVE DOCKING PROCESS (SEE LENTZEN ET AL AND MANUSCRIPT TO
REMARK 210 BE PUBLISHED)
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING
REMARK 220
REMARK 220 REMARK: THIS THEORETICAL MODEL ENTRY WAS NOT ANNOTATED AND NOT
REMARK 220 VALIDATED BY THE WWPDB STAFF AND THEREFORE MAY NOT CONFORM
REMARK 220 TO THE PDB FORMAT.
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THIOSTREPTON IS A MEMBER OF A SULPHUR-RICH HETEROCYCLIC PEPTIDES
REMARK 400 CLASS. ALL SHARE A MACROCYLIC CORE, CONSISTING OF A
REMARK 400 NITROGEN CONTAINING, SIX-MEMBERED RING CENTRAL TO DEHYDROAMINO
REMARK 400 ACIDS AND A SUBSET OF FIVE MEMBER RING STRUCTURES INCLUDING
REMARK 400 THIAZOLES, THIAZOLINES AND OXAZOLES.
REMARK 400 HERE, THIOSTREPTON IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: THIOSTREPTON
REMARK 400 CHAIN: B
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 0 TO 18
REMARK 400 DESCRIPTION: THIOSTREPTON IS A HETEROCYCLIC THIOPEPTIDE,
REMARK 400 CONSISTING OF FOUR THIAZOLES ONE THIAZOLINE
REMARK 400 ONE PIPERIDEINE RINGS.
REMARK 400 A MODIFIED QUINOLINE LINKED TO MAIN-CHAIN
REMARK 400 RESIDUE 1 AND SIDE-CHAIN OF RESIDUE 12.
REMARK 400 THE OBSERVED C-TERMINAL AMINO GROUP NH2(18) IS
REMARK 400 LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED
REMARK 400 REMNANT OF A SER C-TERMINAL RESIDUE.
REMARK 400
REMARK 400 THE THIOSTREPTON IS THIOPEPTIDE, A MEMBER OF ANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: THIOSTREPTON
REMARK 400 CHAIN: B
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: Thiostrepton is a hetrocyclic thiopeptide belonging
REMARK 400 to the thiocillin family, consisting of four
REMARK 400 thiazole, one thiozoline and one piperideine rings.
REMARK 400 A modified quinoline linked to main-chain residue 1
REMARK 400 and side-chain of residue 12. Post translational
REMARK 400 maturation of thiazole and oxazole containing
REMARK 400 antibiotics involves the enzymic condensation of a
REMARK 400 Cys or Ser with the alpha-carbonyl of the preceding
REMARK 400 amino acid to form a thioether or ether bond, then
REMARK 400 dehydration to form a double bond with the alpha-
REMARK 400 amino nitrogen. Thiazoline or oxazoline ring are
REMARK 400 dehydrogenated to form thiazole or oxazole rings.
REMARK 400 the pyridinyl involves the cross-linking of a Ser
REMARK 400 and a Cys-Ser pair usually separated by 7 or 8
REMARK 400 residues along the peptide chain. The Ser residues
REMARK 400 are dehydrated to didehydroalanines, then bonded
REMARK 400 between their beta carbons. The alpha carbonyl of
REMARK 400 the Cys condenses with alpha carbon of the first Ser
REMARK 400 to form a pyridinyl ring. The ring may be mutiply
REMARK 400 dehydrogenated to form a pyridine ring with loss of
REMARK 400 the amino nitrogen of the first Ser. The amidation
REMARK 400 of Ser-17 probably does not occur by the same
REMARK 400 mechanism, oxidative cleavage of glycine, as in
REMARK 400 eukaryotes.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 LYS A 4
REMARK 465 VAL A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 ASP A 141
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 BB9 B 13 C MH6 B 14 N 0.138
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 15 -99.29 -38.18
REMARK 500 LYS A 17 140.91 -176.59
REMARK 500 THR A 19 -25.33 95.17
REMARK 500 VAL A 24 -92.82 -94.06
REMARK 500 PRO A 26 -52.70 -28.71
REMARK 500 ALA A 27 -89.24 -39.55
REMARK 500 ILE A 35 -73.68 -27.29
REMARK 500 GLU A 62 -34.92 -34.81
REMARK 500 LYS A 64 -9.28 68.48
REMARK 500 LYS A 93 -42.99 75.48
REMARK 500 SER B 5 80.85 71.83
REMARK 500 DCY B 9 -14.72 -147.29
REMARK 500 TS9 B 10 -65.50 -107.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 A C1069 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF THIOSTREPTON
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-MGGDP COMPLEXED
REMARK 900 WITH THE THIOPEPTIDE GE2270A.
REMARK 900 RELATED ID: 1E9W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THIOPEPTIDE THIOSTREPTON
REMARK 900 RELATED ID: 2C77 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-GNP COMPLEXED WITH
REMARK 900 THIOPEPTIDE GE2270A.
REMARK 900 RELATED ID: 2JQ7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE COMPLEX OF THIOPEPTIDE THIOSTREPTON AND
REMARK 900 RIBOSOMAL L11-RNA
REMARK 900 RELATED ID: 2ZJP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF NOSIHEPTIDE COMPLEXED WITH THE LARGE RIBOSOMAL
REMARK 900 SUBUNIT OF DEINOCOCCUS RADIODURANS
REMARK 900 RELATED ID: 3CF5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBOSOMAL L11-RNA COMPLEXED WITH THE
REMARK 900 THIOPEPTIDE THIOSTREPTON
REMARK 900 RELATED ID: 1MMS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN L11-RNA COMPLEX
REMARK 900 RELATED ID: 1EG0 RELATED DB: PDB
REMARK 900 FITTING OF COMPONENTS WITH KNOWN STRUCTURE INTO AN 11.5 A CRYO-EM
REMARK 900 MAP OF THE E. COLI 70S RIBOSOME
REMARK 900 RELATED ID: 1GIY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5A RESOLUTIO
REMARK 900 RELATED ID: 1JQM RELATED DB: PDB
REMARK 900 FITTING OF L11 PROTEIN AND ELONGATION FACTOR G (EF-G) IN THE CRYO-
REMARK 900 EM MAP OF E. COLI 70S RIBOSOME BOUND WITH EF-G,GDP AND FUSIDIC ACID
REMARK 900 RELATED ID: 1JQS RELATED DB: PDB
REMARK 900 FITTING OF L11 PROTEIN AND ELONGATION FACTOR G (DOMAIN G'AND V) IN
REMARK 900 THE CRYO-EM MAP OF E. COLI 70S RIBOSOME BOUNDWITH EF-G AND GMPPCP
REMARK 900 RELATED ID: 1JQT RELATED DB: PDB
REMARK 900 FITTING OF L11 PROTEIN IN THE LOW RESOLUTION CRYO-EM MAP OFE.COLI
REMARK 900 70S RIBOSOME
REMARK 900 RELATED ID: 1PN7 RELATED DB: PDB
REMARK 900 COORDINATES OF S12, L11 PROTEINS AND P-TRNA, FROM THE 70S X-RAY
REMARK 900 STRUCTURE ALIGNED TO THE 70S CRYO-EM MAP OF E. COLIRIBOSOME
REMARK 900 RELATED ID: 1PN8 RELATED DB: PDB
REMARK 900 COORDINATES OF S12, L11 PROTEINS AND E-SITE TRNA FROM 70S CRYSTAL
REMARK 900 STRUCTURE SEPARATELY FITTED INTO THE CRYO-EM MAPOF E.COLI 70S.EF-
REMARK 900 G.GDPNP COMPLEX. THE COORDINATESORIGINALLY FROM THE E-SITE TRNA
REMARK 900 WERE FITTED IN THEPOSITION OF THE HYBRID P /E-SITE TRNA.
REMARK 900 RELATED ID: 487D RELATED DB: PDB
REMARK 900 SEVEN RIBOSOMAL PROTEINS FITTED TO A CRYO-EM MAP OF THE LARGE 50S
REMARK 900 SUBUNIT AT 7.5 A.
DBREF 1OLN A 2 141 UNP P29395 RL11_THEMA 2 141
DBREF 1OLN B 1 17 UNP P0C8P8 THCL_STRAJ 1 17
DBREF 1OLN C 1051 1108 PDB 1OLN 1OLN 1051 1108
SEQRES 1 A 140 ALA LYS LYS VAL ALA ALA GLN ILE LYS LEU GLN LEU PRO
SEQRES 2 A 140 ALA GLY LYS ALA THR PRO ALA PRO PRO VAL GLY PRO ALA
SEQRES 3 A 140 LEU GLY GLN HIS GLY VAL ASN ILE MET GLU PHE CYS LYS
SEQRES 4 A 140 ARG PHE ASN ALA GLU THR ALA ASP LYS ALA GLY MET ILE
SEQRES 5 A 140 LEU PRO VAL VAL ILE THR VAL TYR GLU ASP LYS SER PHE
SEQRES 6 A 140 THR PHE ILE ILE LYS THR PRO PRO ALA SER PHE LEU LEU
SEQRES 7 A 140 LYS LYS ALA ALA GLY ILE GLU LYS GLY SER SER GLU PRO
SEQRES 8 A 140 LYS ARG LYS ILE VAL GLY LYS VAL THR ARG LYS GLN ILE
SEQRES 9 A 140 GLU GLU ILE ALA LYS THR LYS MET PRO ASP LEU ASN ALA
SEQRES 10 A 140 ASN SER LEU GLU ALA ALA MET LYS ILE ILE GLU GLY THR
SEQRES 11 A 140 ALA LYS SER MET GLY ILE GLU VAL VAL ASP
SEQRES 1 B 19 QUA ILE ALA DHA ALA SER BB9 THR DBU DCY TS9 BB9 THR
SEQRES 2 B 19 BB9 MH6 BB9 DHA DHA NH2
SEQRES 1 C 58 G C U G G G A U G U U G G
SEQRES 2 C 58 C U U A G A A G C A G C C
SEQRES 3 C 58 A U C A U U U A A A G A G
SEQRES 4 C 58 U G C G U A A C A G C U C
SEQRES 5 C 58 A C C A G C
MODRES 1OLN DHA B 3 SER 2-AMINO-ACRYLIC ACID
MODRES 1OLN BB9 B 6 CYS
MODRES 1OLN DBU B 8 THR (2Z)-2-AMINOBUT-2-ENOIC ACID
MODRES 1OLN TS9 B 10 ILE
MODRES 1OLN BB9 B 11 CYS
MODRES 1OLN BB9 B 13 CYS
MODRES 1OLN MH6 B 14 SER 3-HYDROXY-2-IMINOPROPANOIC ACID
MODRES 1OLN BB9 B 15 CYS
MODRES 1OLN DHA B 16 SER 2-AMINO-ACRYLIC ACID
MODRES 1OLN DHA B 17 SER 2-AMINO-ACRYLIC ACID
HET QUA B 0 16
HET DHA B 3 5
HET BB9 B 6 6
HET DBU B 8 5
HET DCY B 9 6
HET TS9 B 10 9
HET BB9 B 11 6
HET BB9 B 13 5
HET MH6 B 14 4
HET BB9 B 15 6
HET DHA B 16 5
HET DHA B 17 5
HET NH2 B 18 1
HETNAM QUA 8-HYDROXY-4-(1-HYDROXYETHYL)QUINOLINE-2-CARBOXYLIC ACID
HETNAM DHA 2-AMINO-ACRYLIC ACID
HETNAM BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID
HETNAM DBU (2Z)-2-AMINOBUT-2-ENOIC ACID
HETNAM DCY D-CYSTEINE
HETNAM TS9 (2S,3S,4R)-2-AMINO-3,4-DIHYDROXY-3-METHYLPENTANOIC ACID
HETNAM MH6 3-HYDROXY-2-IMINOPROPANOIC ACID
HETNAM NH2 AMINO GROUP
HETSYN DHA 2,3-DIDEHYDROALANINE
HETSYN DBU Z-DEHYDROBUTYRINE
FORMUL 2 QUA C12 H13 N O4
FORMUL 2 DHA 3(C3 H5 N O2)
FORMUL 2 BB9 4(C3 H5 N O2 S)
FORMUL 2 DBU C4 H7 N O2
FORMUL 2 DCY C3 H7 N O2 S
FORMUL 2 TS9 C6 H13 N O4
FORMUL 2 MH6 C3 H5 N O3
FORMUL 2 NH2 H2 N
HELIX 1 1 GLY A 25 GLN A 30 1 6
HELIX 2 2 ASN A 34 THR A 46 1 13
HELIX 3 3 PRO A 74 GLY A 84 1 11
HELIX 4 4 ARG A 102 MET A 113 1 12
HELIX 5 5 PRO A 114 LEU A 116 5 3
HELIX 6 6 SER A 120 LYS A 133 1 14
SHEET 1 AA 3 ILE A 9 PRO A 14 0
SHEET 2 AA 3 ILE A 53 VAL A 60 -1 O LEU A 54 N LEU A 13
SHEET 3 AA 3 PHE A 66 ILE A 70 -1 O THR A 67 N THR A 59
SHEET 1 AB 2 GLY A 98 THR A 101 0
SHEET 2 AB 2 ILE A 137 VAL A 140 1 O GLU A 138 N VAL A 100
LINK C11 QUA B 0 OG1 THR B 12 1555 1555 1.33
LINK C7 QUA B 0 N ILE B 1 1555 1555 1.50
LINK C ALA B 2 N DHA B 3 1555 1555 1.38
LINK C DHA B 3 N ALA B 4 1555 1555 1.35
LINK C SER B 5 SG BB9 B 6 1555 1555 1.75
LINK CA SER B 5 C BB9 B 13 1555 1555 1.58
LINK CB SER B 5 CB MH6 B 14 1555 1555 1.52
LINK C SER B 5 N BB9 B 6 1555 1555 1.31
LINK C BB9 B 6 N THR B 7 1555 1555 1.32
LINK C THR B 7 N DBU B 8 1555 1555 1.35
LINK C DBU B 8 N DCY B 9 1555 1555 1.29
LINK C DBU B 8 SG DCY B 9 1555 1555 1.75
LINK C DCY B 9 N TS9 B 10 1555 1555 1.33
LINK C TS9 B 10 SG BB9 B 11 1555 1555 1.75
LINK C TS9 B 10 N BB9 B 11 1555 1555 1.28
LINK C BB9 B 11 N THR B 12 1555 1555 1.36
LINK C THR B 12 SG BB9 B 13 1555 1555 1.71
LINK C THR B 12 N BB9 B 13 1555 1555 1.29
LINK C BB9 B 13 N MH6 B 14 1555 1555 1.47
LINK C MH6 B 14 SG BB9 B 15 1555 1555 1.65
LINK C MH6 B 14 N BB9 B 15 1555 1555 1.30
LINK C BB9 B 15 N DHA B 16 1555 1555 1.38
LINK C DHA B 16 N DHA B 17 1555 1555 1.23
LINK C DHA B 17 N NH2 B 18 1555 1555 1.35
SITE 1 AC1 4 PRO A 22 A C1067 G C1068 A C1095
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 21 20 Bytes