Header list of 1ayj.pdb file
Complete list - c 25 2 Bytes
HEADER FUNGICIDE 05-NOV-97 1AYJ
TITLE DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF RAPHANUS
TITLE 2 SATIVUS ANTIFUNGAL PROTEIN 1 (RS-AFP1) BY 1H NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIFUNGAL PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RS-AFP1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAPHANUS SATIVUS VAR. NIGER;
SOURCE 3 ORGANISM_COMMON: CHINESE RADISH;
SOURCE 4 ORGANISM_TAXID: 41679;
SOURCE 5 STRAIN: VAR. NIGER;
SOURCE 6 ORGAN: SEED
KEYWDS FUNGICIDE, PLANT DEFENSIN, CYSTEINE-STABILIZED ALFA/BETA MOTIF
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.FANT,F.A.M.BORREMANS
REVDAT 4 25-DEC-19 1AYJ 1 REMARK SEQRES LINK
REVDAT 3 29-NOV-17 1AYJ 1 REMARK HELIX
REVDAT 2 24-FEB-09 1AYJ 1 VERSN
REVDAT 1 28-JAN-98 1AYJ 0
JRNL AUTH F.FANT,W.VRANKEN,W.BROEKAERT,F.BORREMANS
JRNL TITL DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 RAPHANUS SATIVUS ANTIFUNGAL PROTEIN 1 BY 1H NMR.
JRNL REF J.MOL.BIOL. V. 279 257 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9636715
JRNL DOI 10.1006/JMBI.1998.1767
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.FANT,W.F.VRANKEN,J.C.MARTINS,F.A.M.BORREMANS
REMARK 1 TITL SOLUTION CONFORMATION OF RAPHANUS SATIVUS ANTIFUNGAL PROTEIN
REMARK 1 TITL 2 1 (RS-AFP1) BY 1H NUCLEAR MAGNETIC RESONANCE. RESONANCE
REMARK 1 TITL 3 ASSIGNMENTS, SECONDARY STRUCTURE AND GLOBAL FOLD
REMARK 1 REF BULL.SOC.CHIM.BELG. V. 106 51 1997
REMARK 1 REFN ISSN 0037-9646
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : MSI/BIOSYM TECHNOLOGIES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING PROTOCOL ADOPTED
REMARK 3 NILGES ET AL. 1988, FEBS LETTERS, VOL. 239, PP129-136. INSIGHT
REMARK 3 II ALSO WAS USED.
REMARK 4
REMARK 4 1AYJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171412.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; E.COSY; NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA/REDAC, INSIGHTII/DISCOVER
REMARK 210 METHOD USED : DIANA AND SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 1 GLU A 29 CD GLU A 29 OE2 0.105
REMARK 500 1 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 2 GLU A 5 CD GLU A 5 OE2 0.106
REMARK 500 2 GLU A 29 CD GLU A 29 OE2 0.108
REMARK 500 2 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 3 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 3 GLU A 29 CD GLU A 29 OE2 0.107
REMARK 500 3 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 4 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 4 GLU A 29 CD GLU A 29 OE2 0.108
REMARK 500 4 CYS A 51 C CYS A 51 OXT 0.131
REMARK 500 5 GLU A 5 CD GLU A 5 OE2 0.107
REMARK 500 5 GLU A 29 CD GLU A 29 OE2 0.106
REMARK 500 5 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 6 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 6 GLU A 29 CD GLU A 29 OE2 0.105
REMARK 500 6 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 7 GLU A 5 CD GLU A 5 OE2 0.111
REMARK 500 7 GLU A 29 CD GLU A 29 OE2 0.115
REMARK 500 7 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 8 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 8 GLU A 29 CD GLU A 29 OE2 0.106
REMARK 500 8 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 9 GLU A 5 CD GLU A 5 OE2 0.106
REMARK 500 9 GLU A 29 CD GLU A 29 OE2 0.109
REMARK 500 9 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 10 GLU A 5 CD GLU A 5 OE2 0.107
REMARK 500 10 GLU A 29 CD GLU A 29 OE2 0.108
REMARK 500 10 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 11 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 11 GLU A 29 CD GLU A 29 OE2 0.108
REMARK 500 11 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 12 GLU A 5 CD GLU A 5 OE2 0.109
REMARK 500 12 GLU A 29 CD GLU A 29 OE2 0.109
REMARK 500 12 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 13 GLU A 5 CD GLU A 5 OE2 0.107
REMARK 500 13 GLU A 29 CD GLU A 29 OE2 0.105
REMARK 500 13 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 14 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 14 GLU A 29 CD GLU A 29 OE2 0.111
REMARK 500 14 CYS A 51 C CYS A 51 OXT 0.132
REMARK 500 15 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 15 GLU A 29 CD GLU A 29 OE2 0.107
REMARK 500 15 CYS A 51 C CYS A 51 OXT 0.131
REMARK 500 16 GLU A 5 CD GLU A 5 OE2 0.107
REMARK 500 16 GLU A 29 CD GLU A 29 OE2 0.109
REMARK 500 16 CYS A 51 C CYS A 51 OXT 0.133
REMARK 500 17 GLU A 5 CD GLU A 5 OE2 0.108
REMARK 500 17 GLU A 29 CD GLU A 29 OE2 0.107
REMARK 500
REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS.
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 10 -72.53 -84.10
REMARK 500 1 ASN A 17 107.57 -168.21
REMARK 500 1 LEU A 28 -71.61 -75.01
REMARK 500 1 ALA A 31 165.30 -43.52
REMARK 500 1 ARG A 32 -74.54 -86.86
REMARK 500 1 TYR A 38 -123.57 -83.22
REMARK 500 1 VAL A 39 154.25 69.24
REMARK 500 2 THR A 10 -68.23 -109.71
REMARK 500 2 TRP A 11 73.47 -64.79
REMARK 500 2 ASN A 17 136.75 -170.79
REMARK 500 2 ALA A 31 156.16 -44.79
REMARK 500 2 TYR A 38 -123.56 -82.02
REMARK 500 2 VAL A 39 153.07 68.87
REMARK 500 3 THR A 10 -70.38 -142.16
REMARK 500 3 TRP A 11 81.43 -68.85
REMARK 500 3 ASN A 17 134.25 -170.81
REMARK 500 3 ALA A 31 156.63 -38.98
REMARK 500 3 ALA A 42 81.56 -172.68
REMARK 500 3 HIS A 43 117.24 87.97
REMARK 500 4 LEU A 28 -76.24 -69.96
REMARK 500 4 ALA A 31 -164.79 -48.53
REMARK 500 4 ARG A 32 -53.72 -132.35
REMARK 500 4 ALA A 42 65.68 -163.60
REMARK 500 4 HIS A 43 135.43 92.71
REMARK 500 5 ASN A 17 132.56 -171.71
REMARK 500 5 LEU A 28 -70.14 -71.46
REMARK 500 5 ALA A 31 160.30 -44.66
REMARK 500 5 ARG A 32 -78.80 -83.50
REMARK 500 6 PRO A 7 -77.75 -73.20
REMARK 500 6 THR A 10 -96.31 -86.09
REMARK 500 6 TRP A 11 91.91 -68.32
REMARK 500 6 SER A 12 63.96 -105.15
REMARK 500 6 CYS A 15 -56.11 -120.32
REMARK 500 6 ASN A 17 106.83 -165.62
REMARK 500 6 ALA A 31 163.77 -47.08
REMARK 500 6 ARG A 32 -72.89 -88.00
REMARK 500 6 HIS A 43 154.48 75.97
REMARK 500 7 PRO A 7 -160.98 -76.95
REMARK 500 7 SER A 8 83.29 -59.54
REMARK 500 7 THR A 10 -58.31 -156.21
REMARK 500 7 ALA A 31 161.31 -42.28
REMARK 500 7 ARG A 32 -76.61 -82.75
REMARK 500 7 SER A 35 100.48 -178.31
REMARK 500 7 PHE A 40 150.09 -41.41
REMARK 500 8 SER A 8 -69.41 -24.65
REMARK 500 8 THR A 10 -72.60 -83.74
REMARK 500 8 TRP A 11 77.32 -65.63
REMARK 500 8 ASN A 17 131.47 -172.35
REMARK 500 8 SER A 35 133.23 -171.56
REMARK 500 8 ALA A 42 55.93 -161.00
REMARK 500
REMARK 500 THIS ENTRY HAS 119 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 TYR A 38 0.17 SIDE CHAIN
REMARK 500 2 ARG A 32 0.12 SIDE CHAIN
REMARK 500 2 TYR A 38 0.17 SIDE CHAIN
REMARK 500 2 TYR A 48 0.07 SIDE CHAIN
REMARK 500 3 ARG A 6 0.10 SIDE CHAIN
REMARK 500 3 ARG A 32 0.09 SIDE CHAIN
REMARK 500 3 TYR A 38 0.10 SIDE CHAIN
REMARK 500 3 PHE A 49 0.09 SIDE CHAIN
REMARK 500 4 TYR A 38 0.15 SIDE CHAIN
REMARK 500 5 ARG A 32 0.08 SIDE CHAIN
REMARK 500 5 TYR A 38 0.14 SIDE CHAIN
REMARK 500 6 TYR A 38 0.15 SIDE CHAIN
REMARK 500 6 PHE A 49 0.10 SIDE CHAIN
REMARK 500 7 TYR A 38 0.11 SIDE CHAIN
REMARK 500 7 TYR A 48 0.08 SIDE CHAIN
REMARK 500 8 ARG A 6 0.20 SIDE CHAIN
REMARK 500 8 ARG A 32 0.09 SIDE CHAIN
REMARK 500 8 TYR A 38 0.18 SIDE CHAIN
REMARK 500 8 PHE A 49 0.13 SIDE CHAIN
REMARK 500 9 TYR A 38 0.09 SIDE CHAIN
REMARK 500 9 PHE A 49 0.13 SIDE CHAIN
REMARK 500 10 ARG A 32 0.08 SIDE CHAIN
REMARK 500 10 TYR A 38 0.17 SIDE CHAIN
REMARK 500 10 TYR A 48 0.07 SIDE CHAIN
REMARK 500 11 ARG A 32 0.08 SIDE CHAIN
REMARK 500 11 TYR A 38 0.13 SIDE CHAIN
REMARK 500 11 TYR A 48 0.07 SIDE CHAIN
REMARK 500 12 TYR A 38 0.15 SIDE CHAIN
REMARK 500 14 ARG A 32 0.09 SIDE CHAIN
REMARK 500 14 TYR A 38 0.16 SIDE CHAIN
REMARK 500 14 TYR A 48 0.07 SIDE CHAIN
REMARK 500 15 ARG A 32 0.10 SIDE CHAIN
REMARK 500 15 TYR A 38 0.18 SIDE CHAIN
REMARK 500 16 TYR A 38 0.09 SIDE CHAIN
REMARK 500 17 ARG A 32 0.11 SIDE CHAIN
REMARK 500 17 TYR A 38 0.16 SIDE CHAIN
REMARK 500 17 TYR A 48 0.08 SIDE CHAIN
REMARK 500 18 ARG A 32 0.10 SIDE CHAIN
REMARK 500 18 TYR A 38 0.16 SIDE CHAIN
REMARK 500 18 PHE A 49 0.09 SIDE CHAIN
REMARK 500 19 ARG A 32 0.11 SIDE CHAIN
REMARK 500 19 TYR A 38 0.17 SIDE CHAIN
REMARK 500 20 TYR A 38 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AYJ A 2 51 UNP P30231 AFP1_SINAL 2 51
SEQRES 1 A 51 PCA LYS LEU CYS GLU ARG PRO SER GLY THR TRP SER GLY
SEQRES 2 A 51 VAL CYS GLY ASN ASN ASN ALA CYS LYS ASN GLN CYS ILE
SEQRES 3 A 51 ASN LEU GLU LYS ALA ARG HIS GLY SER CYS ASN TYR VAL
SEQRES 4 A 51 PHE PRO ALA HIS LYS CYS ILE CYS TYR PHE PRO CYS
MODRES 1AYJ PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA C5 H7 N O3
HELIX 1 1 ASN A 18 LEU A 28 1 11
SHEET 1 A 3 CYS A 4 PRO A 7 0
SHEET 2 A 3 LYS A 44 PHE A 49 -1 N PHE A 49 O CYS A 4
SHEET 3 A 3 HIS A 33 ASN A 37 -1 N ASN A 37 O LYS A 44
SSBOND 1 CYS A 4 CYS A 51 1555 1555 2.07
SSBOND 2 CYS A 15 CYS A 36 1555 1555 2.07
SSBOND 3 CYS A 21 CYS A 45 1555 1555 2.08
SSBOND 4 CYS A 25 CYS A 47 1555 1555 2.07
LINK C PCA A 1 N LYS A 2 1555 1555 1.34
CISPEP 1 PHE A 40 PRO A 41 1 -9.98
CISPEP 2 PHE A 40 PRO A 41 2 -10.39
CISPEP 3 PHE A 40 PRO A 41 3 0.80
CISPEP 4 PHE A 40 PRO A 41 4 -8.96
CISPEP 5 PHE A 40 PRO A 41 5 -10.45
CISPEP 6 PHE A 40 PRO A 41 6 -8.23
CISPEP 7 PHE A 40 PRO A 41 7 -5.78
CISPEP 8 PHE A 40 PRO A 41 8 -10.34
CISPEP 9 PHE A 40 PRO A 41 9 -10.59
CISPEP 10 PHE A 40 PRO A 41 10 -10.80
CISPEP 11 PHE A 40 PRO A 41 11 -10.34
CISPEP 12 PHE A 40 PRO A 41 12 -10.71
CISPEP 13 PHE A 40 PRO A 41 13 -10.37
CISPEP 14 PHE A 40 PRO A 41 14 -10.22
CISPEP 15 PHE A 40 PRO A 41 15 -10.65
CISPEP 16 PHE A 40 PRO A 41 16 6.06
CISPEP 17 PHE A 40 PRO A 41 17 -10.70
CISPEP 18 PHE A 40 PRO A 41 18 -10.66
CISPEP 19 PHE A 40 PRO A 41 19 -10.66
CISPEP 20 PHE A 40 PRO A 41 20 6.88
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 - c 25 2 Bytes