Header list of 1iyc.pdb file
Complete list - 23 20 Bytes
HEADER ANTIFUNGAL PROTEIN 05-AUG-02 1IYC
TITLE SOLUTION STRUCTURE OF ANTIFUNGAL PEPTIDE, SCARABAECIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCARABAECIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN THE COCONUT
SOURCE 4 RHINOCEROS BEETLE.
KEYWDS ANTIFUNGAL PEPTIDE, ANTIMICROBIAL PEPTIDE, BEETLE, CHITIN-BINDING,
KEYWDS 2 ANTIFUNGAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.HEMMI,J.ISHIBASHI,T.TOMIE,M.YAMAKAWA
REVDAT 3 23-FEB-22 1IYC 1 REMARK
REVDAT 2 24-FEB-09 1IYC 1 VERSN
REVDAT 1 24-JUN-03 1IYC 0
JRNL AUTH H.HEMMI,J.ISHIBASHI,T.TOMIE,M.YAMAKAWA
JRNL TITL STRUCTURAL BASIS FOR NEW PATTERN OF CONSERVED AMINO ACID
JRNL TITL 2 RESIDUES RELATED TO CHITIN-BINDING IN THE ANTIFUNGAL PEPTIDE
JRNL TITL 3 FROM THE COCONUT RHINOCEROS BEETLE ORYCTES RHINOCEROS
JRNL REF J.BIOL.CHEM. V. 278 22820 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12676931
JRNL DOI 10.1074/JBC.M301025200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IYC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000005402.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM SCARABAECIN; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; E-COSY; TOCSY;
REMARK 210 ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.105, FELIX 2000
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 O PRO A 32 H SER A 36 1.52
REMARK 500 O SER A 16 HD21 ASN A 17 1.54
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 LEU A 5 38.19 -150.27
REMARK 500 1 ASP A 7 -42.26 179.12
REMARK 500 1 LYS A 9 -63.81 -135.08
REMARK 500 1 VAL A 10 -36.45 -132.20
REMARK 500 1 LEU A 11 46.60 37.85
REMARK 500 1 SER A 14 -85.59 -23.60
REMARK 500 1 ARG A 15 34.86 -176.65
REMARK 500 1 SER A 16 52.69 -167.91
REMARK 500 1 PRO A 19 -180.00 -56.03
REMARK 500 1 PHE A 27 47.23 -162.44
REMARK 500 1 ASP A 28 129.63 -170.77
REMARK 500 1 SER A 31 158.58 -49.16
REMARK 500 1 PHE A 35 -40.95 -167.79
REMARK 500 2 PRO A 3 58.37 -67.50
REMARK 500 2 LYS A 4 58.57 -63.31
REMARK 500 2 LEU A 5 23.87 -143.72
REMARK 500 2 ASP A 7 87.02 179.40
REMARK 500 2 ASP A 8 28.98 -146.70
REMARK 500 2 LYS A 9 17.62 55.45
REMARK 500 2 LEU A 11 -172.50 -49.79
REMARK 500 2 SER A 14 -86.38 -25.85
REMARK 500 2 ARG A 15 34.22 -177.68
REMARK 500 2 SER A 16 50.16 -169.53
REMARK 500 2 PRO A 19 -155.47 -70.49
REMARK 500 2 LYS A 22 -167.83 -110.48
REMARK 500 2 VAL A 23 118.05 -161.86
REMARK 500 2 PHE A 27 45.73 -163.38
REMARK 500 2 ASP A 28 148.84 -170.47
REMARK 500 2 SER A 31 171.92 -43.20
REMARK 500 2 PHE A 35 37.00 -165.79
REMARK 500 3 LEU A 5 44.18 -155.36
REMARK 500 3 ASP A 7 127.51 179.09
REMARK 500 3 ASP A 8 52.00 -174.05
REMARK 500 3 LYS A 9 34.94 34.26
REMARK 500 3 VAL A 10 -68.93 -150.76
REMARK 500 3 LEU A 11 -170.64 37.42
REMARK 500 3 SER A 14 -85.02 -26.15
REMARK 500 3 ARG A 15 33.71 -178.51
REMARK 500 3 SER A 16 45.23 -161.23
REMARK 500 3 PRO A 19 -174.38 -55.10
REMARK 500 3 PHE A 27 43.65 -162.88
REMARK 500 3 ASP A 28 136.13 -170.71
REMARK 500 3 SER A 31 169.40 -45.54
REMARK 500 3 ALA A 34 -146.83 -69.79
REMARK 500 3 PHE A 35 95.51 -17.21
REMARK 500 4 PRO A 3 78.95 -50.06
REMARK 500 4 LEU A 5 36.63 -144.99
REMARK 500 4 ASP A 7 120.85 178.91
REMARK 500 4 ASP A 8 24.38 -166.12
REMARK 500 4 VAL A 10 -66.31 -126.82
REMARK 500
REMARK 500 THIS ENTRY HAS 297 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IYC A 1 36 UNP Q86SC0 Q86SC0_ORYRH 29 64
SEQRES 1 A 36 GLU LEU PRO LYS LEU PRO ASP ASP LYS VAL LEU ILE ARG
SEQRES 2 A 36 SER ARG SER ASN CYS PRO LYS GLY LYS VAL TRP ASN GLY
SEQRES 3 A 36 PHE ASP CYS LYS SER PRO PHE ALA PHE SER
HELIX 1 1 SER A 31 PHE A 35 5 5
SHEET 1 A 2 VAL A 23 ASN A 25 0
SHEET 2 A 2 ASP A 28 LYS A 30 -1 O ASP A 28 N ASN A 25
SSBOND 1 CYS A 18 CYS A 29 1555 1555 2.03
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