Header list of 1zrx.pdb file
Complete list - 2 20 Bytes
HEADER ANTIMICROBIAL PROTEIN, ANTIBIOTIC 23-MAY-05 1ZRX
TITLE SOLUTION STRUCTURE OF STOMOXYN IN H20/TFE 50%
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STOMOXYN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SOLID-PHASE SYNTHESIS (BOC). SEQUENCE OCCURS
SOURCE 4 NATURALLY IN STOMOXYS CALCITRANS, STABLE FLY
KEYWDS HELICAL PEPTIDE IN TFE, ANTIMICROBIAL PROTEIN, ANTIBIOTIC
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.LANDON,H.MEUDAL,N.BOULANGER,P.BULET,F.VOVELLE
REVDAT 4 02-MAR-22 1ZRX 1 REMARK
REVDAT 3 24-FEB-09 1ZRX 1 VERSN
REVDAT 2 28-MAR-06 1ZRX 1 JRNL
REVDAT 1 04-OCT-05 1ZRX 0
JRNL AUTH C.LANDON,H.MEUDAL,N.BOULANGER,P.BULET,F.VOVELLE
JRNL TITL SOLUTION STRUCTURES OF STOMOXYN AND SPINIGERIN, TWO INSECT
JRNL TITL 2 ANTIMICROBIAL PEPTIDES WITH AN ALPHA-HELICAL CONFORMATION.
JRNL REF BIOPOLYMERS V. 81 92 2006
JRNL REFN ISSN 0006-3525
JRNL PMID 16170803
JRNL DOI 10.1002/BIP.20370
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.LAMBERTY,D.ZACHARY,R.LANOT,C.BORDEREAU,A.ROBERT,
REMARK 1 AUTH 2 J.A.HOFFMANN,P.BULET
REMARK 1 TITL INSECT IMMUNITY. CONSTITUTIVE EXPRESSION OF A CYSTEINE-RICH
REMARK 1 TITL 2 ANTIFUNGAL AND A LINEAR ANTIBACTERIAL PEPTIDE IN A TERMITE
REMARK 1 TITL 3 INSECT
REMARK 1 REF J.BIOL.CHEM. V. 276 4085 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 739 DISTANCE NOE-DERIVED RESTRAINTS
REMARK 4
REMARK 4 1ZRX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033047.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM STOMOXYN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2002.044.17.08, NMRVIEW
REMARK 210 5.0.16, ARIA 1.1, CNS 1.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY AND THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 PHE A 3 48.69 -77.15
REMARK 500 1 ILE A 31 -45.21 -130.43
REMARK 500 1 SER A 34 32.55 -163.30
REMARK 500 2 ALA A 29 38.79 -163.72
REMARK 500 2 SER A 34 57.73 -103.75
REMARK 500 3 ALA A 29 -15.26 -151.15
REMARK 500 3 SER A 34 39.75 -88.08
REMARK 500 4 ASP A 27 42.00 -98.74
REMARK 500 4 ALA A 32 48.15 -78.85
REMARK 500 5 ALA A 29 42.50 -171.61
REMARK 500 6 ASP A 27 41.43 -93.33
REMARK 500 6 ALA A 29 25.18 -163.59
REMARK 500 6 ALA A 32 38.70 -75.34
REMARK 500 7 ARG A 4 -18.03 71.33
REMARK 500 7 SER A 34 51.24 -94.92
REMARK 500 8 PHE A 3 48.26 -77.58
REMARK 500 8 ALA A 22 43.23 -162.41
REMARK 500 8 HIS A 23 22.81 -79.28
REMARK 500 8 ASP A 27 44.55 -94.13
REMARK 500 8 SER A 34 46.37 -83.33
REMARK 500 8 ALA A 37 37.26 -80.69
REMARK 500 8 VAL A 38 -63.61 -141.84
REMARK 500 8 ALA A 41 52.26 -93.99
REMARK 500 9 ASP A 27 38.77 -84.98
REMARK 500 9 SER A 34 46.70 -90.46
REMARK 500 9 ALA A 41 43.37 -89.94
REMARK 500 10 PHE A 3 34.14 -84.05
REMARK 500 10 ASP A 27 39.86 -88.09
REMARK 500 10 SER A 34 44.75 -97.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZRV RELATED DB: PDB
REMARK 900 RELATED ID: 1ZRW RELATED DB: PDB
DBREF 1ZRX A 1 42 UNP Q8T9R8 STMX_STOCA 25 66
SEQRES 1 A 42 ARG GLY PHE ARG LYS HIS PHE ASN LYS LEU VAL LYS LYS
SEQRES 2 A 42 VAL LYS HIS THR ILE SER GLU THR ALA HIS VAL ALA LYS
SEQRES 3 A 42 ASP THR ALA VAL ILE ALA GLY SER GLY ALA ALA VAL VAL
SEQRES 4 A 42 ALA ALA THR
HELIX 1 1 PHE A 3 HIS A 23 1 21
HELIX 2 2 HIS A 23 THR A 28 1 6
HELIX 3 3 ALA A 29 VAL A 30 5 2
HELIX 4 4 ILE A 31 SER A 34 5 4
HELIX 5 5 GLY A 35 THR A 42 1 8
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 - 2 20 Bytes