Header list of 1cfe.pdb file
Complete list - b 16 2 Bytes
HEADER PATHOGENESIS-RELATED PROTEIN 08-NOV-96 1CFE
TITLE P14A, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PATHOGENESIS-RELATED PROTEIN P14A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1 - 135;
COMPND 5 SYNONYM: PATHOGENESIS-RELATED LEAF PROTEIN 6, ETHYLENE INDUCED
COMPND 6 PROTEIN P1, P14;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM LYCOPERSICUM;
SOURCE 3 ORGANISM_TAXID: 4081;
SOURCE 4 ORGAN: LEAF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PATHOGENESIS-RELATED PROTEIN, PR-1 PROTEINS, PLANT DEFENSE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.FERNANDEZ,T.SZYPERSKI,T.BRUYERE,P.RAMAGE,E.MOSINGER,K.WUTHRICH
REVDAT 3 16-FEB-22 1CFE 1 REMARK
REVDAT 2 24-FEB-09 1CFE 1 VERSN
REVDAT 1 12-NOV-97 1CFE 0
JRNL AUTH C.FERNANDEZ,T.SZYPERSKI,T.BRUYERE,P.RAMAGE,E.MOSINGER,
JRNL AUTH 2 K.WUTHRICH
JRNL TITL NMR SOLUTION STRUCTURE OF THE PATHOGENESIS-RELATED PROTEIN
JRNL TITL 2 P14A.
JRNL REF J.MOL.BIOL. V. 266 576 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9067611
JRNL DOI 10.1006/JMBI.1996.0772
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.NIDERMAN,I.GENETET,T.BRUYERE,R.GEES,A.STINTZI,M.LEGRAND,
REMARK 1 AUTH 2 B.FRITIG,E.MOSINGER
REMARK 1 TITL PATHOGENESIS-RELATED PR-1 PROTEINS ARE ANTIFUNGAL. ISOLATION
REMARK 1 TITL 2 AND CHARACTERIZATION OF THREE 14-KILODALTON PROTEINS OF
REMARK 1 TITL 3 TOMATO AND OF A BASIC PR-1 OF TOBACCO WITH INHIBITORY
REMARK 1 TITL 4 ACTIVITY AGAINST PHYTOPHTHORA INFESTANS
REMARK 1 REF PLANT PHYSIOL. V. 108 17 1995
REMARK 1 REFN ISSN 0032-0889
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.LUCAS,A.CAMACHO HENRIQUEZ,F.LOTTSPEICH,A.HENSCHEN,
REMARK 1 AUTH 2 H.L.SANGER
REMARK 1 TITL AMINO ACID SEQUENCE OF THE PATHOGENESIS-RELATED LEAF PROTEIN
REMARK 1 TITL 2 P14 FROM VIROID-INFECTED TOMATO REVEALS A NEW TYPE OF
REMARK 1 TITL 3 STRUCTURALLY UNFAMILIAR PROTEINS
REMARK 1 REF EMBO J. V. 4 2745 1985
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CFE 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_1000172291.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PAPER *JRNL*
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 4 CYS A 91 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 VAL A 86 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 6 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 8 ARG A 100 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 11 VAL A 86 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 11 CYS A 107 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 12 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 12 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 13 TYR A 7 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 13 CYS A 112 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 13 TYR A 135 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 15 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 15 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 17 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 17 TYR A 80 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 17 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 18 CYS A 91 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 18 TYR A 135 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
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 ASN A 2 -1.52 -149.29
REMARK 500 1 PRO A 22 -157.52 -81.52
REMARK 500 1 ALA A 27 -52.34 62.47
REMARK 500 1 ASP A 43 -61.26 -103.67
REMARK 500 1 CYS A 44 -13.73 106.29
REMARK 500 1 SER A 49 -87.93 42.56
REMARK 500 1 ASP A 61 39.23 -76.57
REMARK 500 1 GLU A 74 27.73 -72.01
REMARK 500 1 LYS A 90 81.53 49.09
REMARK 500 1 ARG A 92 61.29 -106.07
REMARK 500 1 HIS A 93 -70.43 -165.87
REMARK 500 1 TRP A 99 103.52 -44.33
REMARK 500 1 ASN A 114 29.85 -167.22
REMARK 500 2 SER A 3 174.31 64.41
REMARK 500 2 CYS A 44 46.65 79.27
REMARK 500 2 HIS A 48 140.40 61.91
REMARK 500 2 ALA A 51 64.09 37.99
REMARK 500 2 GLU A 74 42.47 -76.67
REMARK 500 2 ASN A 79 -104.35 -152.67
REMARK 500 2 TYR A 80 -32.75 177.70
REMARK 500 2 ASN A 83 40.52 38.42
REMARK 500 2 GLN A 84 -135.79 -156.32
REMARK 500 2 HIS A 93 -52.16 -135.16
REMARK 500 2 TRP A 99 103.80 -34.20
REMARK 500 2 TRP A 116 -111.40 45.67
REMARK 500 2 GLN A 132 -38.50 -139.94
REMARK 500 2 ARG A 133 135.60 85.81
REMARK 500 3 SER A 3 164.80 167.16
REMARK 500 3 HIS A 48 51.27 -92.53
REMARK 500 3 ASP A 61 44.95 -157.00
REMARK 500 3 GLU A 74 31.07 -71.91
REMARK 500 3 PRO A 76 20.33 -74.64
REMARK 500 3 SER A 77 -35.37 -133.77
REMARK 500 3 ASN A 79 -154.74 -151.16
REMARK 500 3 TYR A 80 -145.32 -126.77
REMARK 500 3 ALA A 81 -51.35 83.48
REMARK 500 3 CYS A 91 47.20 -100.99
REMARK 500 3 ARG A 92 72.33 -113.86
REMARK 500 3 HIS A 93 -49.04 -155.51
REMARK 500 3 TRP A 99 98.47 -59.55
REMARK 500 3 ASN A 101 44.43 -88.76
REMARK 500 4 PRO A 22 -162.68 -67.27
REMARK 500 4 ASP A 61 70.42 24.07
REMARK 500 4 THR A 63 -108.31 34.09
REMARK 500 4 TYR A 80 -140.61 -77.20
REMARK 500 4 ALA A 81 -54.14 83.35
REMARK 500 4 ASN A 83 60.17 79.44
REMARK 500 4 LYS A 90 43.51 -91.23
REMARK 500 4 CYS A 91 33.39 -93.17
REMARK 500 4 ARG A 92 44.15 -81.21
REMARK 500
REMARK 500 THIS ENTRY HAS 289 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 7 0.15 SIDE CHAIN
REMARK 500 1 TYR A 36 0.07 SIDE CHAIN
REMARK 500 1 ARG A 40 0.12 SIDE CHAIN
REMARK 500 1 ARG A 65 0.14 SIDE CHAIN
REMARK 500 1 TYR A 78 0.08 SIDE CHAIN
REMARK 500 1 TYR A 80 0.17 SIDE CHAIN
REMARK 500 1 ARG A 92 0.09 SIDE CHAIN
REMARK 500 1 TYR A 94 0.07 SIDE CHAIN
REMARK 500 1 ARG A 133 0.08 SIDE CHAIN
REMARK 500 2 TYR A 7 0.15 SIDE CHAIN
REMARK 500 2 ARG A 15 0.17 SIDE CHAIN
REMARK 500 2 TYR A 80 0.07 SIDE CHAIN
REMARK 500 2 PHE A 118 0.11 SIDE CHAIN
REMARK 500 2 TYR A 135 0.09 SIDE CHAIN
REMARK 500 3 ARG A 15 0.16 SIDE CHAIN
REMARK 500 3 TYR A 36 0.07 SIDE CHAIN
REMARK 500 3 TYR A 78 0.16 SIDE CHAIN
REMARK 500 3 TYR A 80 0.13 SIDE CHAIN
REMARK 500 3 ARG A 100 0.11 SIDE CHAIN
REMARK 500 3 ARG A 104 0.12 SIDE CHAIN
REMARK 500 3 ARG A 109 0.10 SIDE CHAIN
REMARK 500 3 TYR A 135 0.09 SIDE CHAIN
REMARK 500 4 TYR A 7 0.11 SIDE CHAIN
REMARK 500 4 ARG A 32 0.08 SIDE CHAIN
REMARK 500 4 TYR A 36 0.16 SIDE CHAIN
REMARK 500 4 ARG A 75 0.15 SIDE CHAIN
REMARK 500 4 TYR A 80 0.08 SIDE CHAIN
REMARK 500 4 ARG A 104 0.09 SIDE CHAIN
REMARK 500 4 ARG A 109 0.09 SIDE CHAIN
REMARK 500 5 TYR A 7 0.08 SIDE CHAIN
REMARK 500 5 TYR A 36 0.07 SIDE CHAIN
REMARK 500 5 ARG A 40 0.10 SIDE CHAIN
REMARK 500 5 ARG A 75 0.09 SIDE CHAIN
REMARK 500 5 TYR A 78 0.10 SIDE CHAIN
REMARK 500 5 ARG A 104 0.09 SIDE CHAIN
REMARK 500 5 ARG A 133 0.11 SIDE CHAIN
REMARK 500 6 ARG A 40 0.17 SIDE CHAIN
REMARK 500 6 TYR A 78 0.14 SIDE CHAIN
REMARK 500 6 ARG A 92 0.15 SIDE CHAIN
REMARK 500 6 ARG A 109 0.15 SIDE CHAIN
REMARK 500 6 ARG A 111 0.11 SIDE CHAIN
REMARK 500 6 PHE A 118 0.12 SIDE CHAIN
REMARK 500 6 TYR A 135 0.16 SIDE CHAIN
REMARK 500 7 TYR A 80 0.11 SIDE CHAIN
REMARK 500 7 ARG A 100 0.09 SIDE CHAIN
REMARK 500 7 ARG A 104 0.14 SIDE CHAIN
REMARK 500 7 ARG A 109 0.10 SIDE CHAIN
REMARK 500 7 ARG A 133 0.08 SIDE CHAIN
REMARK 500 7 TYR A 135 0.07 SIDE CHAIN
REMARK 500 8 ARG A 32 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 134 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CFE A 1 135 UNP P04284 PR06_LYCES 25 159
SEQRES 1 A 135 GLN ASN SER PRO GLN ASP TYR LEU ALA VAL HIS ASN ASP
SEQRES 2 A 135 ALA ARG ALA GLN VAL GLY VAL GLY PRO MET SER TRP ASP
SEQRES 3 A 135 ALA ASN LEU ALA SER ARG ALA GLN ASN TYR ALA ASN SER
SEQRES 4 A 135 ARG ALA GLY ASP CYS ASN LEU ILE HIS SER GLY ALA GLY
SEQRES 5 A 135 GLU ASN LEU ALA LYS GLY GLY GLY ASP PHE THR GLY ARG
SEQRES 6 A 135 ALA ALA VAL GLN LEU TRP VAL SER GLU ARG PRO SER TYR
SEQRES 7 A 135 ASN TYR ALA THR ASN GLN CYS VAL GLY GLY LYS LYS CYS
SEQRES 8 A 135 ARG HIS TYR THR GLN VAL VAL TRP ARG ASN SER VAL ARG
SEQRES 9 A 135 LEU GLY CYS GLY ARG ALA ARG CYS ASN ASN GLY TRP TRP
SEQRES 10 A 135 PHE ILE SER CYS ASN TYR ASP PRO VAL GLY ASN TRP ILE
SEQRES 11 A 135 GLY GLN ARG PRO TYR
HELIX 1 H1 PRO A 4 GLN A 17 1 14
HELIX 2 H2 ALA A 27 ARG A 40 1 14
HELIX 3 H3 GLY A 64 VAL A 72 1 9
HELIX 4 310 SER A 73 ARG A 75 5 3
HELIX 5 H4 HIS A 93 VAL A 98 1 6
SHEET 1 B 4 SER A 24 TRP A 25 0
SHEET 2 B 4 ARG A 104 ARG A 111 1 N LEU A 105 O SER A 24
SHEET 3 B 4 TRP A 117 ASP A 124 -1 N SER A 120 O GLY A 108
SHEET 4 B 4 GLU A 53 GLY A 58 -1 N ALA A 56 O ILE A 119
SSBOND 1 CYS A 44 CYS A 112 1555 1555 2.10
SSBOND 2 CYS A 85 CYS A 91 1555 1555 2.08
SSBOND 3 CYS A 107 CYS A 121 1555 1555 2.07
CISPEP 1 ASP A 124 PRO A 125 1 -19.62
CISPEP 2 ASP A 124 PRO A 125 2 -6.35
CISPEP 3 ASP A 124 PRO A 125 3 -10.29
CISPEP 4 ASP A 124 PRO A 125 4 -20.57
CISPEP 5 ASP A 124 PRO A 125 5 -13.19
CISPEP 6 ASP A 124 PRO A 125 6 -21.05
CISPEP 7 ASP A 124 PRO A 125 7 -16.34
CISPEP 8 ASP A 124 PRO A 125 8 -17.68
CISPEP 9 ASP A 124 PRO A 125 9 -11.01
CISPEP 10 ASP A 124 PRO A 125 10 -20.34
CISPEP 11 ASP A 124 PRO A 125 11 -13.34
CISPEP 12 ASP A 124 PRO A 125 12 -17.19
CISPEP 13 ASP A 124 PRO A 125 13 -13.49
CISPEP 14 ASP A 124 PRO A 125 14 -11.99
CISPEP 15 ASP A 124 PRO A 125 15 -15.08
CISPEP 16 ASP A 124 PRO A 125 16 -9.50
CISPEP 17 ASP A 124 PRO A 125 17 -20.09
CISPEP 18 ASP A 124 PRO A 125 18 -16.74
CISPEP 19 ASP A 124 PRO A 125 19 -17.93
CISPEP 20 ASP A 124 PRO A 125 20 -16.40
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