Header list of 1wco.pdb file
Complete list - l 29 2 Bytes
HEADER PEPTIDE/ANTIBIOTIC 19-NOV-04 1WCO
TITLE THE SOLUTION STRUCTURE OF THE NISIN-LIPID II COMPLEX
CAVEAT 1WCO MUB A 1 HAS WRONG CHIRALITY AT ATOM C9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALA-FGA-LYS-DAL-DAL PEPTIDE;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: LANTIBIOTIC;
COMPND 6 CHAIN: N
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MONARTHROPALPUS FLAVUS;
SOURCE 3 ORGANISM_TAXID: 71816;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS;
SOURCE 6 ORGANISM_TAXID: 1358
KEYWDS PEPTIDE-ANTIBIOTIC COMPLEX, LANTIBIOTIC, ANTIMICROBIAL, BACTERIOCIN,
KEYWDS 2 THIOESTER, PORE FORMATION, PYROPHOSPHATE CAGE, FOOD PRESERVATIVE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.-T.D.HSU,E.BREUKINK,E.TISCHENKO,M.A.G.LUTTERS,B.DE KRUIJFF,
AUTHOR 2 R.KAPTEIN,A.M.J.J.BONVIN,N.A.J.VAN NULAND
REVDAT 9 29-JUL-20 1WCO 1 CAVEAT COMPND REMARK HETNAM
REVDAT 9 2 1 LINK SITE ATOM
REVDAT 8 08-JUL-20 1WCO 1 CAVEAT COMPND SOURCE REMARK
REVDAT 8 2 1 DBREF SEQADV SEQRES HET
REVDAT 8 3 1 HETNAM HETSYN FORMUL LINK
REVDAT 8 4 1 SITE ATOM
REVDAT 7 17-JAN-18 1WCO 1 CAVEAT JRNL REMARK ATOM
REVDAT 6 13-JUL-11 1WCO 1 VERSN
REVDAT 5 24-FEB-09 1WCO 1 VERSN
REVDAT 4 15-MAY-07 1WCO 1 REMARK SEQRES MODRES HET
REVDAT 4 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 4 3 1 HETATM TER ENDMDL MODEL
REVDAT 4 4 1 CONECT
REVDAT 3 01-MAR-06 1WCO 1 HETATM
REVDAT 2 14-MAR-05 1WCO 1 SPRSDE
REVDAT 1 07-MAR-05 1WCO 0
SPRSDE 07-MAR-05 1WCO 1UZT
JRNL AUTH S.T.HSU,E.BREUKINK,E.TISCHENKO,M.A.LUTTERS,B.DE KRUIJFF,
JRNL AUTH 2 R.KAPTEIN,A.M.BONVIN,N.A.VAN NULAND
JRNL TITL THE NISIN-LIPID II COMPLEX REVEALS A PYROPHOSPHATE CAGE THAT
JRNL TITL 2 PROVIDES A BLUEPRINT FOR NOVEL ANTIBIOTICS.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 11 963 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15361862
JRNL DOI 10.1038/NSMB830
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.-T.D.HSU,E.BREUKINK,B.DE KRUIJFF,R.KAPTEIN,A.M.J.J.BONVIN,
REMARK 1 AUTH 2 N.A.J.VAN NULAND
REMARK 1 TITL MAPPING THE TARGETED MEMBRANE PORE FORMATION MECHANISM BY
REMARK 1 TITL 2 SOLUTION NMR: THE NISIN Z AND LIPID II INTERACTION IN SDS
REMARK 1 TITL 3 MICELLES
REMARK 1 REF BIOCHEMISTRY V. 41 7670 2002
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 12056898
REMARK 1 DOI 10.1021/BI025679T
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.BREUKINK,I.WIEDEMANN,C.VAN KRAAIJ,O.P.KUIPERS,H.G.SAHL,
REMARK 1 AUTH 2 B.DE KRUIJFF
REMARK 1 TITL USE OF THE CELL WALL PRECURSOR LIPID II BY A PORE- FORMING
REMARK 1 TITL 2 PEPTIDE ANTIBIOTIC
REMARK 1 REF SCIENCE V. 286 2361 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 10600751
REMARK 1 DOI 10.1126/SCIENCE.286.5448.2361
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.LINGE,M.A.WILLIAMS,C.A.E.M.SPRONK,A.M.J.J.BONVIN,M.NILGES
REMARK 1 TITL REFINEMENT OF PROTEIN STRUCTURES IN EXPLICIT SOLVENT
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 50 496 2003
REMARK 1 REF 2 GENET.
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 12557191
REMARK 1 DOI 10.1002/PROT.10299
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.DOMINGUEZ,R.BOELENS,A.M.J.J.BONVIN
REMARK 1 TITL HADDOCK: A PROTEIN-PROTEIN DOCKING APPROACH BASED ON
REMARK 1 TITL 2 BIOCHEMICAL OR BIOPHYSICAL INFORMATION
REMARK 1 REF J.AM.CHEM.SOC. V. 125 1731 2003
REMARK 1 REFN ISSN 0002-7863
REMARK 1 PMID 12580598
REMARK 1 DOI 10.1021/JA026939X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. THE ENSEMBLE OF STRUCTURES IS SUPERIMPOSED
REMARK 3 ON THE CA OF NISIN RESIDUES 1-12 (CHAIN N), THE HEAVY ATOMS OF
REMARK 3 MURNAC, PYROPHOSPHATE AND THE FIRST ISOPRENE OF 3-LIPID II
REMARK 3 (CHAIN L) AS THESE ARE THE ONLY SEGMENTS THAT HAVE SUFFICIENT
REMARK 3 DISTANCE RESTRAINTS TO DEFINE THE COMPLEX STRUCTURE. OTHER
REMARK 3 RESIDUES NAMELY RESIDUES 13-34 (ESPECIALLY RESIDUES 20-34) OF
REMARK 3 NISIN, THE PENTAPEPTIDE AND TERMINAL ISOPRENE UNITS OF 3-LIPID
REMARK 3 II ARE FLEXIBLE AS SUPPORTED BY DYNAMICS DATA. THE ATOM
REMARK 3 OCCUPANCY OF THE C- TERMINAL TAIL OF NISIN (RESIDUES 20-34) HAS
REMARK 3 BEEN MODIFIED TO BE 0.3 TO REFLECT THEIR DISORDER/FLEXIBILITY.
REMARK 4
REMARK 4 1WCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1290021726.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300.0
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1.0 ATM
REMARK 210 SAMPLE CONTENTS : 100% D6-DMSO
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N CT HSQC; 31P 1D; 1H-13C
REMARK 210 HSQC; 1H-13C HMBC; 1H-15N-NOESY
REMARK 210 HSQC; 1H-1H NOESY; 1H-15N TOCSY-
REMARK 210 HSQC; 1H-1H TOCSY; 1H-1H COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 900
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW VIEW, CNS
REMARK 210 METHOD USED : HADDOCK
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : RMSD CLUSTERING AND LOWEST TOTAL
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING MULTIDIMENSIONAL NMR
REMARK 210 SPECTROSCOPY ON 15N-LABELLED NISIN IN COMPLEX WITH UNLABELLED 3-
REMARK 210 LIPID II. INTERMOLECULAR HYDROGEN BONDS WERE IDENTIFIED AND USED
REMARK 210 IN STRUCTURAL CALCULATION BY 31P- EDITED 1H-15N CT HSQC.
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 3620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, N, A
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 NISIN Z IS A LANTIBIOTIC. THE LANTIBIOTICS
REMARK 400 ARE CHARACTERIZED BY LANTHIONINE AND/OR METHYLLANTHIONINE
REMARK 400 NONPROTEINOGENIC AMINO ACIDS.
REMARK 400 HERE, NISIN Z IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: NISIN Z
REMARK 400 CHAIN: N
REMARK 400 COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 34
REMARK 400 DESCRIPTION: NISIN Z IS A PENTACYCLIC PEPTIDE. THIOETHER BONDS
REMARK 400 WITH CYSTEINE RESULT IN FIVE CYCLIC STRUCTURES ALONG
REMARK 400 THE PEPTIDE CHAIN.
REMARK 400 CROSSLINK 3-7 METHYLLANTHIONINE (DAL-CYS)
REMARK 400 CROSSLINK 8-11 BETA-METHYLLANTHIONINE (DBB-CYS)
REMARK 400 CROSSLINK 13-19 BETA-METHYLLANTHIONINE (DBB-CYS)
REMARK 400 CROSSLINK 23-26 BETA-METHYLLANTHIONINE (DBB-CYS)
REMARK 400 CROSSLINK 25-28 BETA-METHYLLANTHIONINE (DBB-CYS)
REMARK 400
REMARK 400 THE NISIN A IS POLYPEPTIDE, A MEMBER OF LANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: NISIN A
REMARK 400 CHAIN: N
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: Nisin Z is a heptacyclic peptide. Post Translational
REMARK 400 maturation of lantibiotics involves the enzymic
REMARK 400 conversion of Thr, and Ser into dehydrated AA and
REMARK 400 the formation of thioether bonds with cysteine.
REMARK 400 Thioether bonds with cysteine result in five cyclic
REMARK 400 structures along the peptide chain. This is followed
REMARK 400 by membrane translocation and cleavage of the
REMARK 400 modified precursor.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HZ3 LYS L 5 O DAL L 7 1.56
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 1 DBB N 8 -58.97 147.76
REMARK 500 1 LYS N 12 1.93 -151.30
REMARK 500 1 MET N 17 -46.71 -154.38
REMARK 500 1 CYS N 19 82.90 63.18
REMARK 500 1 ASN N 20 -81.18 -57.88
REMARK 500 1 HIS N 31 -82.45 -126.21
REMARK 500 2 DAL L 6 -73.98 -71.81
REMARK 500 2 DBB N 13 46.61 -73.72
REMARK 500 2 MET N 17 -33.77 -160.00
REMARK 500 2 CYS N 19 91.33 65.39
REMARK 500 2 MET N 21 39.53 73.82
REMARK 500 3 DAL L 6 21.26 -74.60
REMARK 500 3 DBB N 8 -53.57 150.47
REMARK 500 3 DBB N 13 46.83 -73.72
REMARK 500 3 MET N 17 -30.53 -138.14
REMARK 500 3 CYS N 19 79.16 60.11
REMARK 500 3 ASN N 20 -80.10 -68.09
REMARK 500 3 MET N 21 -31.16 75.27
REMARK 500 3 DBB N 23 38.88 174.54
REMARK 500 3 ALA N 24 74.54 -117.37
REMARK 500 3 ILE N 30 55.63 -90.11
REMARK 500 4 DAL L 6 -82.63 -178.22
REMARK 500 4 LEU N 6 68.85 -101.79
REMARK 500 4 CYS N 7 99.10 -63.52
REMARK 500 4 DBB N 8 -57.27 150.92
REMARK 500 4 DBB N 13 44.97 -73.79
REMARK 500 4 MET N 17 -36.02 -150.61
REMARK 500 4 CYS N 19 87.97 70.22
REMARK 500 4 MET N 21 -49.92 74.53
REMARK 500 5 DAL L 6 40.04 145.50
REMARK 500 5 DBB N 8 -53.07 153.14
REMARK 500 5 DBB N 13 25.69 -81.60
REMARK 500 5 MET N 17 -57.69 -149.99
REMARK 500 5 CYS N 19 70.83 65.63
REMARK 500 5 ASN N 20 -81.51 70.51
REMARK 500 6 DAL L 6 46.55 -75.27
REMARK 500 6 CYS N 7 90.44 -59.40
REMARK 500 6 DBB N 8 -54.95 150.13
REMARK 500 6 DBB N 13 32.70 -73.93
REMARK 500 6 MET N 17 -42.41 -152.97
REMARK 500 6 ASN N 20 -23.20 174.42
REMARK 500 6 ILE N 30 32.34 -91.79
REMARK 500 7 DAL L 6 -37.64 170.25
REMARK 500 7 CYS N 7 99.45 -59.99
REMARK 500 7 DBB N 8 -53.50 146.75
REMARK 500 7 DBB N 13 52.35 -70.51
REMARK 500 7 MET N 17 -58.47 -136.07
REMARK 500 7 CYS N 19 177.59 64.80
REMARK 500 7 ASN N 20 -71.63 -119.19
REMARK 500 7 MET N 21 -47.13 73.57
REMARK 500
REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1 FDF L 101
REMARK 610 2 FDF L 101
REMARK 610 3 FDF L 101
REMARK 610 4 FDF L 101
REMARK 610 5 FDF L 101
REMARK 610 6 FDF L 101
REMARK 610 7 FDF L 101
REMARK 610 8 FDF L 101
REMARK 610 9 FDF L 101
REMARK 610 10 FDF L 101
REMARK 610 11 FDF L 101
REMARK 610 12 FDF L 101
REMARK 610 13 FDF L 101
REMARK 610 14 FDF L 101
REMARK 610 15 FDF L 101
REMARK 610 16 FDF L 101
REMARK 610 17 FDF L 101
REMARK 610 18 FDF L 101
REMARK 610 19 FDF L 101
REMARK 610 20 FDF L 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJ1 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE
REMARK 900 RELATED ID: 1MQX RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN IN MEOH/H2O
REMARK 900 MIXTURE
REMARK 900 RELATED ID: 1MQY RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN IN DPC MICELLES
REMARK 900 RELATED ID: 1MQZ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN BOUND TO LIPID
REMARK 900 II IN DPC MICELLES
REMARK 900 RELATED ID: 1QOW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TUPE B LANTIBIOTIC MERSACIDIN
REMARK 900 RELATED ID: 1W9N RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LANTIBIOTIC EPILANCIN 15X
REMARK 900 RELATED ID: 2DDE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LANTIBIOTIC CINNAMYCIN COMPLEXED WITH
REMARK 900 LYSOPHOSPHATIDYLETHANOLAMINE
REMARK 900 RELATED ID: 2KTN RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LCH-ALPHA PEPTIDE FROM TWO-COMPONENT
REMARK 900 LANTIBIOTIC SYSTEM LICHENICIDIN VK21 A1
REMARK 900 RELATED ID: 2KTO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LCH-BETA PEPTIDE FROM TWO-COMPONENT
REMARK 900 LANTIBIOTIC LICHENICIDIN VK21 A2
DBREF 1WCO L 3 7 PDB 1WCO 1WCO 3 7
DBREF 1WCO N 1 34 UNP Q7BB86 Q7BB86_9LACT 24 57
SEQADV 1WCO DAL N 3 UNP Q7BB86 SER 26 CONFLICT
SEQADV 1WCO DBB N 8 UNP Q7BB86 THR 31 CONFLICT
SEQADV 1WCO DBB N 13 UNP Q7BB86 THR 36 CONFLICT
SEQADV 1WCO DBB N 23 UNP Q7BB86 THR 46 CONFLICT
SEQADV 1WCO DBB N 25 UNP Q7BB86 THR 48 CONFLICT
SEQRES 1 L 5 ALA FGA LYS DAL DAL
SEQRES 1 N 34 ILE DBU DAL ILE DHA LEU CYS DBB PRO GLY CYS LYS DBB
SEQRES 2 N 34 GLY ALA LEU MET GLY CYS ASN MET LYS DBB ALA DBB CYS
SEQRES 3 N 34 ASN CYS SER ILE HIS VAL DHA LYS
MODRES 1WCO DBU N 2 THR MODIFIED RESIDUE
MODRES 1WCO DHA N 5 SER MODIFIED RESIDUE
MODRES 1WCO DHA N 33 SER MODIFIED RESIDUE
HET FGA L 4 15
HET DAL L 6 10
HET DAL L 7 11
HET DBU N 2 11
HET DAL N 3 9
HET DHA N 5 8
HET DBB N 8 12
HET DBB N 13 12
HET DBB N 23 12
HET DBB N 25 12
HET DHA N 33 8
HET MUB A 1 35
HET NAG A 2 28
HET FDF L 101 48
HETNAM FGA GAMMA-D-GLUTAMIC ACID
HETNAM DAL D-ALANINE
HETNAM DBU (2Z)-2-AMINOBUT-2-ENOIC ACID
HETNAM DHA 2-AMINO-ACRYLIC ACID
HETNAM DBB D-ALPHA-AMINOBUTYRIC ACID
HETNAM MUB N-ACETYL-ALPHA-MURAMIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FDF (2E,6E)-12-FLUORO-11-(FLUOROMETHYL)-3,7-DIMETHYLDODECA-
HETNAM 2 FDF 2,6,10-TRIEN-1-YL TRIHYDROGEN DIPHOSPHATE
HETSYN FGA D-GLUTAMIC ACID
HETSYN DBU Z-DEHYDROBUTYRINE
HETSYN DHA 2,3-DIDEHYDROALANINE
FORMUL 1 FGA C5 H9 N O4
FORMUL 1 DAL 3(C3 H7 N O2)
FORMUL 2 DBU C4 H7 N O2
FORMUL 2 DHA 2(C3 H5 N O2)
FORMUL 2 DBB 4(C4 H9 N O2)
FORMUL 3 MUB C11 H19 N O8
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 FDF C15 H26 F2 O7 P2
HELIX 1 1 DBB N 8 DBB N 13 1 6
LINK C ALA L 3 N FGA L 4 1555 1555 1.32
LINK N ALA L 3 C10 MUB A 1 1555 1555 1.33
LINK CD FGA L 4 N LYS L 5 1555 1555 1.32
LINK C LYS L 5 N DAL L 6 1555 1555 1.33
LINK C DAL L 6 N DAL L 7 1555 1555 1.34
LINK PB FDF L 101 O1 MUB A 1 1555 1555 1.61
LINK C ILE N 1 N DBU N 2 1555 1555 1.34
LINK C DBU N 2 N DAL N 3 1555 1555 1.32
LINK C DAL N 3 N ILE N 4 1555 1555 1.32
LINK CB DAL N 3 SG CYS N 7 1555 1555 1.79
LINK C ILE N 4 N DHA N 5 1555 1555 1.34
LINK C DHA N 5 N LEU N 6 1555 1555 1.32
LINK C CYS N 7 N DBB N 8 1555 1555 1.32
LINK C DBB N 8 N PRO N 9 1555 1555 1.35
LINK CB DBB N 8 SG CYS N 11 1555 1555 1.82
LINK C LYS N 12 N DBB N 13 1555 1555 1.33
LINK C DBB N 13 N GLY N 14 1555 1555 1.33
LINK CB DBB N 13 SG CYS N 19 1555 1555 1.83
LINK C LYS N 22 N DBB N 23 1555 1555 1.32
LINK C DBB N 23 N ALA N 24 1555 1555 1.33
LINK CB DBB N 23 SG CYS N 26 1555 1555 1.82
LINK C ALA N 24 N DBB N 25 1555 1555 1.32
LINK C DBB N 25 N CYS N 26 1555 1555 1.32
LINK CB DBB N 25 SG CYS N 28 1555 1555 1.82
LINK C VAL N 32 N DHA N 33 1555 1555 1.33
LINK C DHA N 33 N LYS N 34 1555 1555 1.32
LINK O4 MUB A 1 C1 NAG A 2 1555 1555 1.42
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
MODEL 1
Complete list - l 29 2 Bytes