Header list of 1d6b.pdb file
Complete list - b 16 2 Bytes
HEADER TOXIN 12-OCT-99 1D6B
TITLE SOLUTION STRUCTURE OF DEFENSIN-LIKE PEPTIDE-2 (DLP-2) FROM PLATYPUS
TITLE 2 VENOM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFENSIN-LIKE PEPTIDE-2;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORNITHORHYNCHUS ANATINUS;
SOURCE 3 ORGANISM_COMMON: PLATYPUS;
SOURCE 4 ORGANISM_TAXID: 9258;
SOURCE 5 ORGAN: SPUR;
SOURCE 6 TISSUE: VENOM GLAND;
SOURCE 7 SECRETION: VENOM
KEYWDS HELIX, ANTIPARALLEL BETA-SHEET, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.TORRES,G.M.DE PLATER,M.DOVERSKOG,L.C BIRINYI-STRACHAN,
AUTHOR 2 G.M.NICHOLSON,C.H.GALLAGHER,P.W.KUCHEL
REVDAT 4 16-FEB-22 1D6B 1 REMARK
REVDAT 3 24-FEB-09 1D6B 1 VERSN
REVDAT 2 01-APR-03 1D6B 1 JRNL
REVDAT 1 21-JUN-00 1D6B 0
JRNL AUTH A.M.TORRES,G.M.DE PLATER,M.DOVERSKOG,L.C.BIRINYI-STRACHAN,
JRNL AUTH 2 G.M.NICHOLSON,C.H.GALLAGHER,P.W.KUCHEL
JRNL TITL DEFENSIN-LIKE PEPTIDE-2 FROM PLATYPUS VENOM: MEMBER OF A
JRNL TITL 2 CLASS OF PEPTIDES WITH A DISTINCT STRUCTURAL FOLD.
JRNL REF BIOCHEM.J. V. 348 649 2000
JRNL REFN ISSN 0264-6021
JRNL PMID 10839998
JRNL DOI 10.1042/0264-6021:3480649
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.TORRES,X.WANG,J.I.FLETCHER,D.ALEWOOD,P.F.ALEWOOD,
REMARK 1 AUTH 2 R.SMITH,R.J.SIMPSON,G.M.NICHOLSON,S.K.SUTHERLAND,
REMARK 1 AUTH 3 C.H.GALLAGHER,G.F.KING,P.W.KUCHEL
REMARK 1 TITL SOLUTION STRUCTURE OF A DEFENSIN-LIKE PEPTIDE FROM PLATYPUS
REMARK 1 TITL 2 VENOM
REMARK 1 REF BIOCHEM.J. V. 341 785 1999
REMARK 1 REFN ISSN 0264-6021
REMARK 1 DOI 10.1042/0264-6021:3410785
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.R.ZIMMERMANN,P.LEGAULT,M.E.SELSTED,A.PARDI
REMARK 1 TITL SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN-12:
REMARK 1 TITL 2 THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT
REMARK 1 TITL 3 OF THE CLASSICAL DEFENSINS
REMARK 1 REF BIOCHEMISTRY V. 34 13663 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.843
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 739 RESTRAINTS, 699 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE RESTRAINTS, 24 DIHEDRAL ANGLE RESTRAINTS, 16 DISTANCE
REMARK 3 RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS.
REMARK 4
REMARK 4 1D6B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009827.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : NO SALT ADDED
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DLP-2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 4800
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE 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 HG2 GLU A 21 HB2 CYS A 24 1.18
REMARK 500 HG3 GLU A 21 H ASN A 23 1.25
REMARK 500 HG12 VAL A 15 H CYS A 16 1.28
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 MET A 2 -165.70 70.75
REMARK 500 1 PHE A 4 -119.04 154.55
REMARK 500 1 GLU A 5 84.26 13.82
REMARK 500 1 MET A 6 -108.66 -43.99
REMARK 500 1 ALA A 8 115.83 -23.11
REMARK 500 1 SER A 13 72.82 81.05
REMARK 500 1 ASP A 18 133.30 -35.54
REMARK 500 1 ALA A 28 176.26 -47.04
REMARK 500 1 TRP A 29 73.81 40.17
REMARK 500 1 THR A 30 137.01 159.14
REMARK 500 1 ARG A 35 12.88 -67.06
REMARK 500 1 GLU A 41 -73.01 -50.69
REMARK 500 2 MET A 2 77.58 -51.73
REMARK 500 2 PHE A 3 -126.66 -137.50
REMARK 500 2 PHE A 4 76.50 86.22
REMARK 500 2 GLU A 5 69.28 -1.85
REMARK 500 2 MET A 6 -93.83 -36.74
REMARK 500 2 ALA A 8 129.69 -21.78
REMARK 500 2 PRO A 26 96.29 -44.22
REMARK 500 2 ALA A 28 -171.58 -62.71
REMARK 500 2 TRP A 29 75.44 40.10
REMARK 500 2 THR A 30 157.49 162.88
REMARK 500 2 ARG A 35 17.52 -60.12
REMARK 500 2 GLU A 41 -74.01 -42.63
REMARK 500 3 PHE A 3 65.29 -102.22
REMARK 500 3 MET A 6 -134.66 -52.91
REMARK 500 3 ALA A 8 103.35 -30.80
REMARK 500 3 CYS A 9 -25.95 -31.20
REMARK 500 3 SER A 13 77.43 61.78
REMARK 500 3 PRO A 26 99.92 -47.66
REMARK 500 3 ALA A 28 177.58 -52.44
REMARK 500 3 TRP A 29 72.89 39.76
REMARK 500 3 THR A 30 150.06 165.11
REMARK 500 3 ARG A 35 12.48 -64.99
REMARK 500 3 GLU A 41 -76.10 -56.24
REMARK 500 4 PHE A 4 109.89 67.32
REMARK 500 4 GLU A 5 83.45 170.70
REMARK 500 4 MET A 6 -138.70 -54.60
REMARK 500 4 GLN A 7 -149.59 -127.18
REMARK 500 4 CYS A 9 -24.60 -33.60
REMARK 500 4 SER A 11 10.05 -56.30
REMARK 500 4 SER A 13 65.51 89.51
REMARK 500 4 PRO A 26 108.49 -52.86
REMARK 500 4 MET A 27 76.15 -103.39
REMARK 500 4 ALA A 28 -166.74 -46.54
REMARK 500 4 TRP A 29 66.11 36.34
REMARK 500 4 THR A 30 147.87 153.09
REMARK 500 4 ARG A 35 15.65 -66.52
REMARK 500 5 PHE A 3 39.46 -98.49
REMARK 500 5 PHE A 4 56.51 -93.90
REMARK 500
REMARK 500 THIS ENTRY HAS 262 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B8W RELATED DB: PDB
DBREF 1D6B A 1 42 UNP P82140 DLP2_ORNAN 1 42
SEQRES 1 A 42 ILE MET PHE PHE GLU MET GLN ALA CYS TRP SER HIS SER
SEQRES 2 A 42 GLY VAL CYS ARG ASP LYS SER GLU ARG ASN CYS LYS PRO
SEQRES 3 A 42 MET ALA TRP THR TYR CYS GLU ASN ARG ASN GLN LYS CYS
SEQRES 4 A 42 CYS GLU TYR
HELIX 1 1 ALA A 8 SER A 13 1 6
SHEET 1 A 2 VAL A 15 ASP A 18 0
SHEET 2 A 2 GLN A 37 CYS A 40 -1 N LYS A 38 O ARG A 17
SSBOND 1 CYS A 9 CYS A 39 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 32 1555 1555 2.03
SSBOND 3 CYS A 24 CYS A 40 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 - b 16 2 Bytes