Header list of 1n4n.pdb file
Complete list - b 23 2 Bytes
HEADER PLANT PROTEIN 01-NOV-02 1N4N
TITLE STRUCTURE OF THE PLANT DEFENSIN PHD1 FROM PETUNIA HYBRIDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLORAL DEFENSIN-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-47;
COMPND 5 SYNONYM: PHD1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PETUNIA X HYBRIDA;
SOURCE 3 ORGANISM_TAXID: 4102
KEYWDS CYSTEINE-STABILISED ALPHA-BETA MOTIF, FIFTH DISULFIDE BOND, PLANT
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.J.C.JANSSEN,H.J.SCHIRRA,F.T.LAY,M.A.ANDERSON,D.J.CRAIK
REVDAT 3 23-FEB-22 1N4N 1 REMARK
REVDAT 2 24-FEB-09 1N4N 1 VERSN
REVDAT 1 01-NOV-03 1N4N 0
JRNL AUTH B.J.C.JANSSEN,H.J.SCHIRRA,F.T.LAY,M.A.ANDERSON,D.J.CRAIK
JRNL TITL STRUCTURE OF PETUNIA HYBRIDA DEFENSIN 1, A NOVEL PLANT
JRNL TITL 2 DEFENSIN WITH FIVE DISULFIDE BONDS
JRNL REF BIOCHEMISTRY V. 42 8214 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12846570
JRNL DOI 10.1021/BI034379O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON 407 NOE-DERIVED INTER-RESIDUAL
REMARK 3 DISTANCE CONSTRAINTS,
REMARK 3 26 PHI- AND 28 CHI1- ANGLE CONSTRAINTS, AND 30 DISTANCE
REMARK 3 CONSTRAINTS FOR 15 HYDROGEN BONDS.
REMARK 4
REMARK 4 1N4N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017513.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 280
REMARK 210 PH : 3.1; 3.1
REMARK 210 IONIC STRENGTH : 0.94MM; 0.94MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.94MM 1H-PHD1; 0.94MM 1H-PHD1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, CCNMR
REMARK 210 GLXCCEXPLORER, X-PLOR 3.851, CNS
REMARK 210 1.1
REMARK 210 METHOD USED : TORSION ANGLE SIMULATED
REMARK 210 ANNEALING PROTOCOL, INCORPORATED
REMARK 210 IN CNS. REFINEMENT IN A BOX WITH
REMARK 210 EXPLICIT WATER MOLECULES USING
REMARK 210 THE METHOD OF LINGE & NILGES
REMARK 210 (1999)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
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 HZ1 LYS A 4 OE1 GLU A 6 1.59
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 THR A 9 44.50 -89.52
REMARK 500 1 ASP A 11 51.44 -150.36
REMARK 500 1 LYS A 28 49.46 72.52
REMARK 500 1 ILE A 37 -100.64 -69.45
REMARK 500 2 ASP A 11 62.97 -150.75
REMARK 500 2 ILE A 15 -61.09 -130.76
REMARK 500 2 ILE A 37 -82.59 -64.69
REMARK 500 3 THR A 9 47.26 -98.31
REMARK 500 3 ASP A 11 -20.78 -147.63
REMARK 500 3 LYS A 45 -156.23 -161.52
REMARK 500 4 THR A 9 44.10 -97.36
REMARK 500 4 ASP A 11 67.76 -151.11
REMARK 500 4 LYS A 28 61.96 64.29
REMARK 500 4 ILE A 37 -72.19 -67.62
REMARK 500 4 ARG A 40 -145.54 -83.79
REMARK 500 5 THR A 9 48.56 -91.97
REMARK 500 5 SER A 12 -169.21 -100.60
REMARK 500 5 ILE A 37 -105.88 -67.72
REMARK 500 6 THR A 9 49.74 -92.09
REMARK 500 6 ASP A 11 -29.84 -150.11
REMARK 500 6 LYS A 28 70.84 66.55
REMARK 500 6 SER A 35 -159.54 -74.18
REMARK 500 7 THR A 9 46.02 -90.63
REMARK 500 7 ASP A 11 53.07 -150.34
REMARK 500 7 LYS A 28 45.71 72.39
REMARK 500 7 SER A 35 -165.12 -77.97
REMARK 500 7 ILE A 37 -100.74 -77.99
REMARK 500 8 THR A 9 43.71 -90.99
REMARK 500 8 ASP A 11 59.85 -151.20
REMARK 500 8 LYS A 28 43.67 71.07
REMARK 500 8 SER A 35 -157.27 -99.19
REMARK 500 8 LYS A 36 -39.47 -150.32
REMARK 500 8 ILE A 37 -76.93 -55.34
REMARK 500 8 ARG A 40 -91.22 -87.46
REMARK 500 8 CYS A 41 106.76 -176.23
REMARK 500 9 THR A 9 43.56 -90.86
REMARK 500 9 TRP A 10 85.91 -150.32
REMARK 500 9 LYS A 28 35.98 71.55
REMARK 500 9 SER A 35 -156.08 -87.80
REMARK 500 9 LYS A 36 -34.28 -133.58
REMARK 500 9 ILE A 37 -98.96 -61.28
REMARK 500 10 THR A 9 44.48 -86.80
REMARK 500 10 ASP A 11 66.66 -151.22
REMARK 500 10 SER A 35 -159.00 -92.84
REMARK 500 10 ILE A 37 -102.30 -67.43
REMARK 500 11 THR A 9 50.64 -92.83
REMARK 500 11 ASP A 11 -29.51 -150.54
REMARK 500 11 LYS A 28 68.17 65.22
REMARK 500 11 ILE A 37 -101.76 -69.96
REMARK 500 12 THR A 9 45.36 -97.78
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N4N A 1 47 UNP Q8H6Q1 DEF1_PETHY 26 72
SEQRES 1 A 47 ALA THR CYS LYS ALA GLU CYS PRO THR TRP ASP SER VAL
SEQRES 2 A 47 CYS ILE ASN LYS LYS PRO CYS VAL ALA CYS CYS LYS LYS
SEQRES 3 A 47 ALA LYS PHE SER ASP GLY HIS CYS SER LYS ILE LEU ARG
SEQRES 4 A 47 ARG CYS LEU CYS THR LYS GLU CYS
HELIX 1 1 ASN A 16 ALA A 27 1 12
SHEET 1 A 3 CYS A 3 GLU A 6 0
SHEET 2 A 3 CYS A 41 LYS A 45 -1 O LYS A 45 N CYS A 3
SHEET 3 A 3 ASP A 31 CYS A 34 -1 N HIS A 33 O LEU A 42
SSBOND 1 CYS A 3 CYS A 47 1555 1555 2.03
SSBOND 2 CYS A 7 CYS A 23 1555 1555 2.02
SSBOND 3 CYS A 14 CYS A 34 1555 1555 2.03
SSBOND 4 CYS A 20 CYS A 41 1555 1555 2.02
SSBOND 5 CYS A 24 CYS A 43 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 23 2 Bytes