Header list of 1beg.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNAL 26-NOV-96 1BEG
TITLE STRUCTURE OF FUNGAL ELICITOR, NMR, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-ELICITIN CRYPTOGEIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHYTOPHTHORA CRYPTOGEA;
SOURCE 3 ORGANISM_TAXID: 4786;
SOURCE 4 STRAIN: ISOLATE ANTIBES 52;
SOURCE 5 OTHER_DETAILS: PROTEIN SECRETED IN THE CULTURE FILTRATE
KEYWDS FUNGAL ELICITOR, SIGNALLING PROTEIN, FUNGAL TOXIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.FEFEU,S.BOUAZIZ,J.-C.HUET,J.-C.PERNOLLET,E.GUITTET
REVDAT 4 16-FEB-22 1BEG 1 REMARK
REVDAT 3 24-FEB-09 1BEG 1 VERSN
REVDAT 2 01-APR-03 1BEG 1 JRNL
REVDAT 1 03-DEC-97 1BEG 0
JRNL AUTH S.FEFEU,S.BOUAZIZ,J.C.HUET,J.C.PERNOLLET,E.GUITTET
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF BETA CRYPTOGEIN, A
JRNL TITL 2 BETA ELICITIN SECRETED BY A PHYTOPATHOGENIC FUNGUS
JRNL TITL 3 PHYTOPHTHORA CRYPTOGEA.
JRNL REF PROTEIN SCI. V. 6 2279 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9385630
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.TERCE-LAFORGUE,J.-C.HUET,J.-C.PERNOLLET
REMARK 1 TITL BIOSYNTHESIS AND SECRETION OF CRYPTOGEIN, A PROTEIN ELICITOR
REMARK 1 TITL 2 SECRETED BY PHYTOPHTHORA CRYPTOGEA
REMARK 1 REF PLANT PHYSIOL. V. 98 936 1992
REMARK 1 REFN ISSN 0032-0889
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SET OF IDEAL BOND LENGTHS AND ANGLES
REMARK 3 USED DURING REFINEMENT: CRYPTO_NMR_PARALLHDG.PRO EFFECTIVE
REMARK 3 RESOLUTION: 1.86A
REMARK 4
REMARK 4 1BEG 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_1000171658.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-18
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LEU A 98 O
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 3 TYR A 12 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 TYR A 33 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 TYR A 33 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 TYR A 87 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 TYR A 12 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 TYR A 33 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 12 TYR A 12 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 15 TYR A 33 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 16 TYR A 33 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 18 TYR A 12 CB - CG - CD2 ANGL. DEV. = -4.3 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 ALA A 2 150.26 72.86
REMARK 500 1 ALA A 5 -120.40 46.62
REMARK 500 1 LYS A 39 51.82 -109.17
REMARK 500 1 THR A 54 -73.29 73.53
REMARK 500 1 ASN A 67 94.82 65.30
REMARK 500 1 PRO A 76 40.53 -78.33
REMARK 500 1 THR A 77 -45.83 -161.29
REMARK 500 1 VAL A 84 -47.60 77.76
REMARK 500 1 ALA A 88 -71.46 -40.45
REMARK 500 2 ALA A 5 -97.88 43.69
REMARK 500 2 LEU A 19 -117.97 -84.46
REMARK 500 2 SER A 20 41.84 29.88
REMARK 500 2 SER A 31 -51.39 -120.21
REMARK 500 2 TYR A 33 -61.37 -102.03
REMARK 500 2 SER A 34 85.18 71.76
REMARK 500 2 ALA A 40 179.91 166.16
REMARK 500 2 LEU A 41 113.91 -13.07
REMARK 500 2 PRO A 42 -173.78 -67.84
REMARK 500 2 ASN A 67 78.00 62.66
REMARK 500 2 ASN A 83 -71.58 -95.65
REMARK 500 2 VAL A 84 -37.29 157.60
REMARK 500 3 THR A 4 -96.73 -115.06
REMARK 500 3 LEU A 19 -65.47 -136.40
REMARK 500 3 SER A 20 51.85 -99.22
REMARK 500 3 TYR A 33 102.96 -51.81
REMARK 500 3 ASN A 67 86.99 65.73
REMARK 500 3 CYS A 71 149.05 -178.56
REMARK 500 4 THR A 4 -95.79 -116.16
REMARK 500 4 ALA A 5 -65.47 -120.92
REMARK 500 4 SER A 31 -65.87 -102.89
REMARK 500 4 THR A 37 -51.23 -121.68
REMARK 500 4 LYS A 39 -57.85 -122.70
REMARK 500 4 SER A 53 44.09 -147.32
REMARK 500 4 THR A 54 -75.18 39.24
REMARK 500 4 ASN A 67 80.05 61.11
REMARK 500 4 CYS A 71 143.11 -178.13
REMARK 500 5 ALA A 2 -73.06 65.69
REMARK 500 5 SER A 23 -60.77 -105.94
REMARK 500 5 ASP A 30 -76.08 -79.59
REMARK 500 5 SER A 31 74.54 -174.27
REMARK 500 5 TYR A 33 143.17 72.49
REMARK 500 5 ALA A 52 -105.33 -85.80
REMARK 500 5 SER A 53 -152.09 36.33
REMARK 500 5 THR A 54 -61.23 -149.59
REMARK 500 5 ASN A 67 97.14 52.96
REMARK 500 5 THR A 77 -42.60 -149.45
REMARK 500 6 ALA A 5 -96.31 41.91
REMARK 500 6 THR A 14 -72.24 -66.94
REMARK 500 6 ILE A 18 -110.40 -77.76
REMARK 500 6 LEU A 19 -43.38 65.74
REMARK 500
REMARK 500 THIS ENTRY HAS 175 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BEG A 1 98 UNP P15570 ELIB_PHYCR 21 118
SEQRES 1 A 98 THR ALA CYS THR ALA THR GLN GLN THR ALA ALA TYR LYS
SEQRES 2 A 98 THR LEU VAL SER ILE LEU SER ASP ALA SER PHE ASN GLN
SEQRES 3 A 98 CYS SER THR ASP SER GLY TYR SER MET LEU THR ALA LYS
SEQRES 4 A 98 ALA LEU PRO THR THR ALA GLN TYR LYS LEU MET CYS ALA
SEQRES 5 A 98 SER THR ALA CYS ASN THR MET ILE LYS LYS ILE VAL THR
SEQRES 6 A 98 LEU ASN PRO PRO ASN CYS ASP LEU THR VAL PRO THR SER
SEQRES 7 A 98 GLY LEU VAL LEU ASN VAL TYR SER TYR ALA ASN GLY PHE
SEQRES 8 A 98 SER ASN LYS CYS SER SER LEU
HELIX 1 1 THR A 6 LEU A 19 1 14
HELIX 2 2 ALA A 22 SER A 31 1 10
HELIX 3 3 MET A 35 THR A 37 5 3
HELIX 4 4 THR A 44 ALA A 52 1 9
HELIX 5 5 ALA A 55 LEU A 66 1 12
HELIX 6 6 TYR A 85 SER A 96 1 12
SHEET 1 A 2 LEU A 73 THR A 74 0
SHEET 2 A 2 VAL A 81 LEU A 82 -1 O LEU A 82 N LEU A 73
SSBOND 1 CYS A 3 CYS A 71 1555 1555 2.02
SSBOND 2 CYS A 27 CYS A 56 1555 1555 2.02
SSBOND 3 CYS A 51 CYS A 95 1555 1555 2.02
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