Header list of 1pp5.pdb file
Complete list - 25 20 Bytes
HEADER ANTIBIOTIC 16-JUN-03 1PP5
TITLE STRUCTURE OF ANTIBACTERIAL PEPTIDE MICROCIN J25: A 21-RESIDUE LARIAT
TITLE 2 PROTOKNOT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROCIN J25;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MCJA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTUC202
KEYWDS LARIAT, PROTOKNOT, BACKBONE-SIDECHAIN AMIDE LINKAGE, STRUCTURAL
KEYWDS 2 GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, NESG, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.J.BAYRO,G.V.T.SWAPNA,J.Y.HUANG,L.-C.MA,J.MUKHOPADHYAY,R.H.EBRIGHT,
AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 27-JUL-11 1PP5 1 REMARK REVDAT
REVDAT 4 13-JUL-11 1PP5 1 VERSN
REVDAT 3 24-FEB-09 1PP5 1 VERSN
REVDAT 2 25-JAN-05 1PP5 1 AUTHOR KEYWDS REMARK
REVDAT 1 28-OCT-03 1PP5 0
JRNL AUTH M.J.BAYRO,J.MUKHOPADHYAY,G.V.T.SWAPNA,J.Y.HUANG,L.-C.MA,
JRNL AUTH 2 E.SINEVA,P.E.DAWSON,G.T.MONTELIONE,R.H.EBRIGHT
JRNL TITL STRUCTURE OF ANTIBACTERIAL PEPTIDE MICROCIN J25: A
JRNL TITL 2 21-RESIDUE LARIAT PROTOKNOT.
JRNL REF J.AM.CHEM.SOC. V. 125 12382 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 14531661
JRNL DOI 10.1021/JA036677E
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PDBSTAT 3.25
REMARK 3 AUTHORS : TEJERO, R.; MONTELIONE, G.T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ENSEMBLE OF STRUCTURES IS BASED ON
REMARK 3 A TOTAL OF 198 CONFORMATIONALLY RESTRAINING CONSTRAINTS, 179 ARE
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS, 13 ARE DIHEDRAL ANGLE
REMARK 3 CONSTRAINTS, 6 ARE DISTANCE CONSTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1PP5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-03.
REMARK 100 THE RCSB ID CODE IS RCSB019472.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM MICROCIN J25 U-13C,15N;
REMARK 210 99.5% CD3OH, 0.5% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HNCACB;
REMARK 210 CBCACONH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AUTOPROC 0.8, NMRPIPE 1.4,
REMARK 210 AUTOSTRUCTURE 1.1.2, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLU A 8 OE2
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 3 35.07 -152.15
REMARK 500 1 GLU A 8 33.56 -94.31
REMARK 500 1 ILE A 13 -157.84 -56.05
REMARK 500 2 HIS A 5 -47.49 -130.79
REMARK 500 2 GLU A 8 32.10 -89.58
REMARK 500 2 ILE A 13 -146.80 -64.20
REMARK 500 2 ILE A 17 57.25 -93.97
REMARK 500 3 ALA A 3 82.87 44.31
REMARK 500 3 HIS A 5 -52.08 -127.48
REMARK 500 3 TYR A 9 89.38 -18.04
REMARK 500 3 ILE A 17 52.40 -107.23
REMARK 500 4 GLU A 8 39.29 -86.87
REMARK 500 4 ILE A 13 -152.55 35.67
REMARK 500 4 THR A 15 -64.70 -101.84
REMARK 500 4 ILE A 17 57.01 -119.35
REMARK 500 5 ALA A 3 105.20 55.68
REMARK 500 5 HIS A 5 -50.83 -124.03
REMARK 500 5 GLU A 8 33.06 -90.28
REMARK 500 5 VAL A 11 -166.91 -126.17
REMARK 500 5 ILE A 13 12.72 54.88
REMARK 500 6 ALA A 3 84.19 -68.91
REMARK 500 6 TYR A 9 72.69 -60.67
REMARK 500 7 ALA A 3 62.15 -119.87
REMARK 500 7 ILE A 13 161.44 -49.64
REMARK 500 7 ILE A 17 58.08 -95.58
REMARK 500 7 SER A 18 -164.45 -162.83
REMARK 500 8 TYR A 9 84.94 3.76
REMARK 500 8 VAL A 11 167.88 -48.44
REMARK 500 8 ILE A 13 -145.37 -139.56
REMARK 500 9 HIS A 5 -51.86 -141.05
REMARK 500 9 TYR A 9 92.39 -48.64
REMARK 500 9 PHE A 10 19.17 -152.23
REMARK 500 9 ILE A 13 -141.21 -60.81
REMARK 500 10 ALA A 3 -85.83 58.34
REMARK 500 10 HIS A 5 -49.63 -137.88
REMARK 500 10 ILE A 13 -152.05 -133.92
REMARK 500 10 THR A 15 -61.80 -90.10
REMARK 500 10 TYR A 20 -169.74 -117.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ER142 RELATED DB: TARGETDB
DBREF 1PP5 A 1 21 UNP Q9X2V7 MCJA_ECOLI 38 58
SEQRES 1 A 21 GLY GLY ALA GLY HIS VAL PRO GLU TYR PHE VAL GLY ILE
SEQRES 2 A 21 GLY THR PRO ILE SER PHE TYR GLY
SHEET 1 A 2 VAL A 6 PRO A 7 0
SHEET 2 A 2 PHE A 19 TYR A 20 -1 O TYR A 20 N VAL A 6
LINK N GLY A 1 CD GLU A 8 1555 1555 1.32
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 - 25 20 Bytes