Header list of 1ueo.pdb file
Complete list - v 10 2 Bytes
HEADER ANTIBIOTIC 20-MAY-03 1UEO
TITLE SOLUTION STRUCTURE OF THE [T8A]-PENAEIDIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENAEIDIN-3A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PENAEIDIN-3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LITOPENAEUS VANNAMEI;
SOURCE 3 ORGANISM_COMMON: PACIFIC WHITE SHRIMP;
SOURCE 4 ORGANISM_TAXID: 6689;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TGY 48-1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTG4812
KEYWDS HELIX, COIL-HELIX-COIL, PROLINE-RICH, CYSTEINE-RICH, DISULFIDE BOND,
KEYWDS 2 ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.YANG,J.PONCET,J.GARNIER,C.ZATYLNY,E.BACHERE,A.AUMELAS
REVDAT 3 10-NOV-21 1UEO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UEO 1 VERSN
REVDAT 1 21-OCT-03 1UEO 0
JRNL AUTH Y.YANG,J.PONCET,J.GARNIER,C.ZATYLNY,E.BACHERE,A.AUMELAS
JRNL TITL SOLUTION STRUCTURE OF THE RECOMBINANT PENAEIDIN-3, A SHRIMP
JRNL TITL 2 ANTIMICROBIAL PEPTIDE
JRNL REF J.BIOL.CHEM. V. 278 36859 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12842879
JRNL DOI 10.1074/JBC.M305450200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 552 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 28 DIHEDRAL ANGLE RESTRAINTS. THE
REMARK 3 ARRANGEMENT OF THE THREE DISULFIDE BONDS WAS DETERMINED IN THIS
REMARK 3 STUDY.
REMARK 4
REMARK 4 1UEO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005739.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293
REMARK 210 PH : 3.9; 3.9
REMARK 210 IONIC STRENGTH : ND; ND
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM; 0.7MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, TOCSY, NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 4.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
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 : 1
REMARK 210
REMARK 210 REMARK: A 0.3ML SOLUTION OF PENAEIDIN-3 WAS USED IN A SHIGEMI
REMARK 210 TUBE. THE 500 MHZ SPECTROMETER WAS EQUIPPED WITH A CRYOPROBE.
REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 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: 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 8 -58.65 70.16
REMARK 500 1 CYS A 32 78.60 -176.21
REMARK 500 1 LEU A 51 18.29 -144.49
REMARK 500 2 ILE A 11 75.92 54.74
REMARK 500 2 ASN A 30 41.36 -151.09
REMARK 500 2 CYS A 32 89.08 -175.03
REMARK 500 3 ILE A 11 131.22 65.84
REMARK 500 3 TYR A 29 49.30 -93.36
REMARK 500 3 CYS A 32 112.49 -173.25
REMARK 500 4 VAL A 2 161.49 63.79
REMARK 500 4 PRO A 28 -159.70 -76.28
REMARK 500 4 TYR A 29 79.36 -69.36
REMARK 500 4 ASN A 30 42.94 -159.49
REMARK 500 4 CYS A 32 95.43 -174.31
REMARK 500 5 ALA A 8 -90.23 56.34
REMARK 500 5 ASN A 30 46.75 -147.43
REMARK 500 5 CYS A 32 81.01 178.91
REMARK 500 6 TYR A 3 174.79 60.02
REMARK 500 6 PRO A 12 -164.96 -78.32
REMARK 500 6 VAL A 18 165.51 60.37
REMARK 500 6 CYS A 32 78.67 -172.40
REMARK 500 6 LEU A 51 12.67 -142.82
REMARK 500 6 LYS A 59 103.21 62.58
REMARK 500 7 VAL A 2 73.11 52.68
REMARK 500 7 TYR A 3 144.00 68.23
REMARK 500 7 LYS A 4 81.18 56.77
REMARK 500 7 ILE A 11 75.94 57.04
REMARK 500 7 PRO A 28 -169.74 -74.04
REMARK 500 7 CYS A 32 81.74 -175.01
REMARK 500 8 ALA A 8 79.65 -159.10
REMARK 500 8 ILE A 11 99.61 60.04
REMARK 500 8 PRO A 12 -160.88 -72.79
REMARK 500 8 ASN A 30 43.44 -144.98
REMARK 500 8 CYS A 32 91.01 -168.87
REMARK 500 9 VAL A 2 144.91 65.80
REMARK 500 9 TYR A 3 174.30 62.49
REMARK 500 9 CYS A 32 87.86 -173.08
REMARK 500 9 LEU A 51 16.97 -144.07
REMARK 500 10 ARG A 13 91.90 59.10
REMARK 500 10 PHE A 17 151.04 63.22
REMARK 500 10 CYS A 32 96.70 -172.79
REMARK 500 10 SER A 62 178.57 59.11
REMARK 500 11 ASN A 30 43.72 -161.96
REMARK 500 11 CYS A 32 112.51 -172.76
REMARK 500 12 TYR A 7 104.23 63.06
REMARK 500 12 ARG A 13 72.74 -163.90
REMARK 500 12 ASN A 30 41.51 -155.44
REMARK 500 12 CYS A 32 106.07 -172.64
REMARK 500 13 TYR A 3 79.76 -108.95
REMARK 500 13 ALA A 8 -134.12 50.54
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 9 0.31 SIDE CHAIN
REMARK 500 1 ARG A 13 0.31 SIDE CHAIN
REMARK 500 1 ARG A 19 0.32 SIDE CHAIN
REMARK 500 1 ARG A 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 45 0.27 SIDE CHAIN
REMARK 500 1 ARG A 50 0.32 SIDE CHAIN
REMARK 500 1 ARG A 53 0.32 SIDE CHAIN
REMARK 500 2 ARG A 9 0.31 SIDE CHAIN
REMARK 500 2 ARG A 13 0.31 SIDE CHAIN
REMARK 500 2 ARG A 19 0.32 SIDE CHAIN
REMARK 500 2 ARG A 37 0.32 SIDE CHAIN
REMARK 500 2 ARG A 45 0.30 SIDE CHAIN
REMARK 500 2 ARG A 50 0.31 SIDE CHAIN
REMARK 500 2 ARG A 53 0.31 SIDE CHAIN
REMARK 500 3 ARG A 9 0.31 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 3 ARG A 19 0.32 SIDE CHAIN
REMARK 500 3 ARG A 37 0.31 SIDE CHAIN
REMARK 500 3 ARG A 45 0.32 SIDE CHAIN
REMARK 500 3 ARG A 50 0.30 SIDE CHAIN
REMARK 500 3 ARG A 53 0.26 SIDE CHAIN
REMARK 500 4 ARG A 9 0.32 SIDE CHAIN
REMARK 500 4 ARG A 13 0.32 SIDE CHAIN
REMARK 500 4 ARG A 19 0.32 SIDE CHAIN
REMARK 500 4 ARG A 37 0.31 SIDE CHAIN
REMARK 500 4 ARG A 45 0.31 SIDE CHAIN
REMARK 500 4 ARG A 50 0.31 SIDE CHAIN
REMARK 500 4 ARG A 53 0.25 SIDE CHAIN
REMARK 500 5 ARG A 9 0.32 SIDE CHAIN
REMARK 500 5 ARG A 13 0.31 SIDE CHAIN
REMARK 500 5 ARG A 19 0.29 SIDE CHAIN
REMARK 500 5 ARG A 37 0.32 SIDE CHAIN
REMARK 500 5 ARG A 45 0.31 SIDE CHAIN
REMARK 500 5 ARG A 50 0.31 SIDE CHAIN
REMARK 500 5 ARG A 53 0.31 SIDE CHAIN
REMARK 500 6 ARG A 9 0.30 SIDE CHAIN
REMARK 500 6 ARG A 13 0.32 SIDE CHAIN
REMARK 500 6 ARG A 19 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.32 SIDE CHAIN
REMARK 500 6 ARG A 45 0.32 SIDE CHAIN
REMARK 500 6 ARG A 50 0.31 SIDE CHAIN
REMARK 500 6 ARG A 53 0.26 SIDE CHAIN
REMARK 500 7 ARG A 9 0.30 SIDE CHAIN
REMARK 500 7 ARG A 13 0.32 SIDE CHAIN
REMARK 500 7 ARG A 19 0.29 SIDE CHAIN
REMARK 500 7 ARG A 37 0.31 SIDE CHAIN
REMARK 500 7 ARG A 45 0.29 SIDE CHAIN
REMARK 500 7 ARG A 50 0.31 SIDE CHAIN
REMARK 500 7 ARG A 53 0.32 SIDE CHAIN
REMARK 500 8 ARG A 9 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 140 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UEO A 1 63 UNP P81058 PEN3A_PENVA 20 82
SEQADV 1UEO ALA A 8 UNP P81058 THR 27 ENGINEERED MUTATION
SEQRES 1 A 63 GLN VAL TYR LYS GLY GLY TYR ALA ARG PRO ILE PRO ARG
SEQRES 2 A 63 PRO PRO PRO PHE VAL ARG PRO LEU PRO GLY GLY PRO ILE
SEQRES 3 A 63 GLY PRO TYR ASN GLY CYS PRO VAL SER CYS ARG GLY ILE
SEQRES 4 A 63 SER PHE SER GLN ALA ARG SER CYS CYS SER ARG LEU GLY
SEQRES 5 A 63 ARG CYS CYS HIS VAL GLY LYS GLY TYR SER GLY
HELIX 1 1 SER A 40 GLY A 52 1 13
SSBOND 1 CYS A 32 CYS A 47 1555 1555 2.02
SSBOND 2 CYS A 36 CYS A 54 1555 1555 2.02
SSBOND 3 CYS A 48 CYS A 55 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 - v 10 2 Bytes