Header list of 1myn.pdb file
Complete list - 23 20 Bytes
HEADER SIGNAL PROTEIN 26-DEC-96 1MYN
TITLE SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE ANTIFUNGAL
TITLE 2 PROTEIN FROM INSECTS, NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DROSOMYCIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 STRAIN: OREGON R;
SOURCE 6 ORGAN: FRUIT;
SOURCE 7 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS DROSOMYCIN, INSECT IMMUNITY, ANTIFUNGAL, CSALPHA-BETA MOTIF, SIGNAL
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.LANDON,P.SODANO,C.HETRU,J.A.HOFFMANN,M.PTAK
REVDAT 3 23-FEB-22 1MYN 1 REMARK
REVDAT 2 24-FEB-09 1MYN 1 VERSN
REVDAT 1 31-DEC-97 1MYN 0
JRNL AUTH C.LANDON,P.SODANO,C.HETRU,J.HOFFMANN,M.PTAK
JRNL TITL SOLUTION STRUCTURE OF DROSOMYCIN, THE FIRST INDUCIBLE
JRNL TITL 2 ANTIFUNGAL PROTEIN FROM INSECTS.
JRNL REF PROTEIN SCI. V. 6 1878 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9300487
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.MICHAUT,P.FEHLBAUM,M.MONIATTE,A.VAN DORSSELAER,
REMARK 1 AUTH 2 J.M.REICHHART,P.BULET
REMARK 1 TITL DETERMINATION OF THE DISULFIDE ARRAY OF THE FIRST INDUCIBLE
REMARK 1 TITL 2 ANTIFUNGAL PEPTIDE FROM INSECTS: DROSOMYCIN FROM DROSOPHILA
REMARK 1 TITL 3 MELANOGASTER
REMARK 1 REF FEBS LETT. V. 395 6 1996
REMARK 1 REFN ISSN 0014-5793
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.FEHLBAUM,P.BULET,L.MICHAUT,M.LAGUEUX,W.F.BROEKAERT,
REMARK 1 AUTH 2 C.HETRU,J.A.HOFFMANN
REMARK 1 TITL INSECT IMMUNITY. SEPTIC INJURY OF DROSOPHILA INDUCES THE
REMARK 1 TITL 2 SYNTHESIS OF A POTENT ANTIFUNGAL PEPTIDE WITH SEQUENCE
REMARK 1 TITL 3 HOMOLOGY TO PLANT ANTIFUNGAL PEPTIDES
REMARK 1 REF J.BIOL.CHEM. V. 269 33159 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE 30 BEST STRUCTURES FROM THE 200
REMARK 3 GENERATED WITH THE DIANA PROGRAM WERE REFINED WITH A SIMULATED
REMARK 3 ANNEALING/ENERGY MINIMIZATION PROTOCOL USING THE X-PLOR COMPUTER
REMARK 3 PROGRAM.
REMARK 4
REMARK 4 1MYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175193.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 SIMULATED ANNEALING AND ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NUMBER OF RESIDUAL VIOLATIONS
REMARK 210 AND INTERNAL GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 2 HIS A 32 NE2 HIS A 32 CD2 -0.073
REMARK 500 3 HIS A 32 CG HIS A 32 CD2 0.061
REMARK 500 5 HIS A 32 NE2 HIS A 32 CD2 -0.068
REMARK 500 7 HIS A 32 NE2 HIS A 32 CD2 -0.067
REMARK 500 10 HIS A 32 NE2 HIS A 32 CD2 -0.069
REMARK 500 11 HIS A 32 NE2 HIS A 32 CD2 -0.068
REMARK 500 13 HIS A 32 NE2 HIS A 32 CD2 -0.067
REMARK 500 15 HIS A 32 NE2 HIS A 32 CD2 -0.066
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 TRP A 14 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 1 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 1 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 1 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 1 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 CYS A 44 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 2 TRP A 14 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 2 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 40 CG - CD2 - CE3 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 ASP A 1 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 3 TRP A 14 NE1 - CE2 - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 TRP A 14 CG - CD2 - CE3 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 3 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 CYS A 44 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 TRP A 14 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 4 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 ASP A 15 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 4 ARG A 21 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 4 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 4 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 4 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 4 TRP A 40 CG - CD2 - CE3 ANGL. DEV. = -5.4 DEGREES
REMARK 500 5 ARG A 6 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 TRP A 14 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TRP A 14 CD1 - NE1 - CE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 5 TRP A 14 NE1 - CE2 - CZ2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 5 ASP A 15 CB - CG - OD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 5 CYS A 19 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 5 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 155 ANGLE DEVIATIONS.
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 ALA A 12 -169.13 -114.30
REMARK 500 1 VAL A 13 -16.43 -48.64
REMARK 500 1 LEU A 37 54.52 39.16
REMARK 500 2 SER A 30 177.05 174.94
REMARK 500 2 SER A 36 42.34 -87.69
REMARK 500 3 ARG A 28 -165.36 -103.80
REMARK 500 3 SER A 30 169.06 179.71
REMARK 500 3 SER A 36 39.77 -90.33
REMARK 500 3 LEU A 37 61.14 39.44
REMARK 500 4 ASN A 16 -58.65 -25.62
REMARK 500 4 ARG A 28 -163.46 -106.83
REMARK 500 4 SER A 30 164.24 175.62
REMARK 500 4 SER A 36 53.69 -97.87
REMARK 500 4 LEU A 37 57.06 25.09
REMARK 500 5 ALA A 12 -167.80 -121.13
REMARK 500 5 SER A 36 41.51 -88.11
REMARK 500 5 LEU A 37 55.69 39.43
REMARK 500 6 ARG A 28 -157.83 -100.03
REMARK 500 6 SER A 30 170.61 174.50
REMARK 500 6 SER A 36 37.04 -81.97
REMARK 500 7 VAL A 13 -17.52 -44.80
REMARK 500 7 ARG A 28 -168.13 -106.09
REMARK 500 7 SER A 30 153.12 166.81
REMARK 500 7 CYS A 33 -177.08 47.66
REMARK 500 7 LEU A 37 61.56 26.43
REMARK 500 8 ALA A 12 -166.90 -120.71
REMARK 500 8 ASN A 16 -53.35 -17.85
REMARK 500 8 ARG A 28 -155.27 -100.91
REMARK 500 8 SER A 36 40.79 -94.87
REMARK 500 8 LEU A 37 48.93 39.44
REMARK 500 9 CYS A 33 152.30 -40.73
REMARK 500 9 SER A 36 -80.24 -87.93
REMARK 500 9 LEU A 37 65.89 178.11
REMARK 500 10 ASN A 16 -56.93 -21.58
REMARK 500 10 ARG A 28 -169.70 -101.71
REMARK 500 10 SER A 30 172.13 172.97
REMARK 500 10 SER A 36 57.36 -98.41
REMARK 500 10 LEU A 37 64.20 14.07
REMARK 500 11 SER A 36 41.67 -88.71
REMARK 500 12 TYR A 7 95.79 -68.90
REMARK 500 12 LYS A 8 67.17 -114.81
REMARK 500 12 ARG A 28 -106.06 -97.17
REMARK 500 12 SER A 29 -62.08 -143.52
REMARK 500 12 SER A 36 41.71 -95.89
REMARK 500 12 LEU A 37 53.19 38.76
REMARK 500 13 SER A 4 79.79 -58.98
REMARK 500 13 ARG A 28 -161.66 -103.92
REMARK 500 13 SER A 36 42.01 -89.36
REMARK 500 13 LEU A 37 62.60 38.08
REMARK 500 14 ARG A 28 -165.78 -110.42
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
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 1 ARG A 6 0.10 SIDE CHAIN
REMARK 500 1 ARG A 20 0.09 SIDE CHAIN
REMARK 500 1 ARG A 28 0.24 SIDE CHAIN
REMARK 500 2 ARG A 28 0.22 SIDE CHAIN
REMARK 500 3 ARG A 6 0.16 SIDE CHAIN
REMARK 500 3 ARG A 20 0.09 SIDE CHAIN
REMARK 500 3 ARG A 28 0.19 SIDE CHAIN
REMARK 500 4 ARG A 6 0.13 SIDE CHAIN
REMARK 500 4 ARG A 21 0.21 SIDE CHAIN
REMARK 500 4 ARG A 28 0.19 SIDE CHAIN
REMARK 500 5 ARG A 6 0.14 SIDE CHAIN
REMARK 500 5 ARG A 20 0.24 SIDE CHAIN
REMARK 500 5 ARG A 21 0.15 SIDE CHAIN
REMARK 500 5 ARG A 28 0.20 SIDE CHAIN
REMARK 500 6 ARG A 20 0.20 SIDE CHAIN
REMARK 500 6 ARG A 28 0.27 SIDE CHAIN
REMARK 500 7 ARG A 6 0.23 SIDE CHAIN
REMARK 500 7 ARG A 20 0.21 SIDE CHAIN
REMARK 500 7 ARG A 21 0.18 SIDE CHAIN
REMARK 500 7 ARG A 28 0.13 SIDE CHAIN
REMARK 500 8 ARG A 6 0.18 SIDE CHAIN
REMARK 500 8 ARG A 20 0.23 SIDE CHAIN
REMARK 500 8 ARG A 21 0.21 SIDE CHAIN
REMARK 500 8 ARG A 28 0.10 SIDE CHAIN
REMARK 500 9 ARG A 20 0.21 SIDE CHAIN
REMARK 500 9 ARG A 21 0.12 SIDE CHAIN
REMARK 500 9 ARG A 28 0.10 SIDE CHAIN
REMARK 500 10 ARG A 6 0.08 SIDE CHAIN
REMARK 500 10 ARG A 28 0.18 SIDE CHAIN
REMARK 500 11 ARG A 6 0.15 SIDE CHAIN
REMARK 500 11 ARG A 20 0.12 SIDE CHAIN
REMARK 500 11 ARG A 28 0.22 SIDE CHAIN
REMARK 500 12 ARG A 20 0.21 SIDE CHAIN
REMARK 500 12 ARG A 21 0.18 SIDE CHAIN
REMARK 500 12 ARG A 28 0.11 SIDE CHAIN
REMARK 500 13 ARG A 6 0.19 SIDE CHAIN
REMARK 500 13 ARG A 20 0.14 SIDE CHAIN
REMARK 500 14 ARG A 6 0.11 SIDE CHAIN
REMARK 500 15 ARG A 6 0.09 SIDE CHAIN
REMARK 500 15 ARG A 21 0.13 SIDE CHAIN
REMARK 500 15 ARG A 28 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MYN A 1 44 UNP P41964 DMYC_DROME 27 70
SEQRES 1 A 44 ASP CYS LEU SER GLY ARG TYR LYS GLY PRO CYS ALA VAL
SEQRES 2 A 44 TRP ASP ASN GLU THR CYS ARG ARG VAL CYS LYS GLU GLU
SEQRES 3 A 44 GLY ARG SER SER GLY HIS CYS SER PRO SER LEU LYS CYS
SEQRES 4 A 44 TRP CYS GLU GLY CYS
HELIX 1 H1 ASN A 16 GLU A 26 1 11
SHEET 1 S1 3 CYS A 2 SER A 4 0
SHEET 2 S1 3 SER A 30 SER A 34 1
SHEET 3 S1 3 LYS A 38 GLU A 42 -1
SSBOND 1 CYS A 2 CYS A 44 1555 1555 2.03
SSBOND 2 CYS A 11 CYS A 33 1555 1555 2.02
SSBOND 3 CYS A 19 CYS A 39 1555 1555 2.02
SSBOND 4 CYS A 23 CYS A 41 1555 1555 2.02
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 - 23 20 Bytes