Header list of 1of9.pdb file
Complete list - 25 20 Bytes
HEADER TOXIN 09-APR-03 1OF9
TITLE SOLUTION STRUCTURE OF THE PORE FORMING TOXIN OF ENTAMOEBA
TITLE 2 HISTOLYTICA (AMOEBAPORE A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PORE-FORMING PEPTIDE AMEOBAPORE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMOEBAPORE A, EH-APP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 5759
KEYWDS PORE FORMING, TOXIN, SAPLIP, AMOEBAPORE A
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR O.HECHT,K.SCHLEINKOFER,H.BRUHN,M.LEIPPE,N.VAN NULAND,
AUTHOR 2 A.J.DINGLEY,J.GROTZINGER
REVDAT 3 24-FEB-09 1OF9 1 VERSN
REVDAT 2 12-JAN-05 1OF9 1 JRNL
REVDAT 1 26-FEB-04 1OF9 0
JRNL AUTH O.HECHT,N.VAN NULAND,K.SCHLEINKOFER,A.J.DINGLEY,
JRNL AUTH 2 H.BRUHN,M.LEIPPE,J.GROTZINGER
JRNL TITL SOLUTION STRUCTURE OF THE PORE-FORMING PROTEIN OF
JRNL TITL 2 ENTAMOEBA HISTOLYTICA
JRNL REF J.BIOL.CHEM. V. 279 17834 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14970207
JRNL DOI 10.1074/JBC.M312978200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OF9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12549.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: 2D H1-SPECTROSCOPY
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 400
REMARK 400 COMPOUND
REMARK 400 FORMS PORES IN THE CYTOPLASMIC MEMBRANE OF HOST CELLS.
REMARK 400 HAS ANTIBACTERIAL ACTIVITY AGAINST M.LUTEUS. CONTAINS
REMARK 400 ONE SAPOSIN DOMAIN.
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 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 LEU A 4 46.77 -147.97
REMARK 500 1 ASN A 6 -31.42 -39.46
REMARK 500 1 CYS A 8 -79.45 -64.77
REMARK 500 1 LEU A 18 -87.85 -52.72
REMARK 500 1 THR A 20 42.41 30.18
REMARK 500 1 THR A 21 -45.97 -176.60
REMARK 500 1 ALA A 24 16.74 95.47
REMARK 500 1 LYS A 37 38.34 -159.74
REMARK 500 1 ALA A 38 -88.76 -107.26
REMARK 500 1 ASP A 63 -70.85 -74.58
REMARK 500 1 LYS A 64 40.07 171.55
REMARK 500 1 ASP A 66 -177.23 -50.30
REMARK 500 1 LYS A 73 -71.10 -51.06
REMARK 500 1 ILE A 74 1.15 -66.45
REMARK 500 1 HIS A 75 81.97 69.13
REMARK 500 2 CYS A 8 -76.93 -68.12
REMARK 500 2 LEU A 18 -89.60 -49.14
REMARK 500 2 THR A 20 22.40 42.62
REMARK 500 2 THR A 21 -41.85 165.12
REMARK 500 2 SER A 32 -35.83 -35.42
REMARK 500 2 LYS A 37 41.41 -159.34
REMARK 500 2 ALA A 38 -98.80 -132.33
REMARK 500 2 LYS A 64 68.75 162.34
REMARK 500 2 ASP A 66 178.09 -47.93
REMARK 500 2 HIS A 75 52.12 33.57
REMARK 500 2 ALA A 76 31.41 -97.87
REMARK 500 3 GLU A 2 -4.60 86.26
REMARK 500 3 LEU A 4 61.61 -174.25
REMARK 500 3 LEU A 7 -87.42 -64.71
REMARK 500 3 CYS A 8 -74.21 -43.82
REMARK 500 3 LEU A 18 -82.21 -46.73
REMARK 500 3 THR A 21 113.60 84.63
REMARK 500 3 LYS A 37 36.99 -170.65
REMARK 500 3 ALA A 38 -89.35 -111.21
REMARK 500 3 LYS A 64 42.37 166.92
REMARK 500 3 ASP A 66 -177.92 -50.37
REMARK 500 4 GLU A 2 85.65 -166.43
REMARK 500 4 ILE A 3 -70.77 -44.83
REMARK 500 4 CYS A 5 -71.80 -65.78
REMARK 500 4 LEU A 18 -87.80 -51.57
REMARK 500 4 THR A 21 -21.73 88.69
REMARK 500 4 LYS A 37 65.77 -170.34
REMARK 500 4 ALA A 38 -88.16 -144.94
REMARK 500 4 ILE A 61 -36.35 -38.82
REMARK 500 4 LYS A 64 81.10 159.91
REMARK 500 4 ASP A 66 -178.96 -50.23
REMARK 500 5 GLU A 2 89.95 60.88
REMARK 500 5 LEU A 4 33.25 -171.14
REMARK 500 5 CYS A 8 -76.14 -82.67
REMARK 500 5 LEU A 18 -77.65 -36.26
REMARK 500 5 THR A 21 111.88 83.27
REMARK 500 5 LYS A 37 40.33 -172.25
REMARK 500 5 ALA A 38 -91.07 -110.09
REMARK 500 5 LYS A 64 41.79 170.56
REMARK 500 5 ASP A 66 -179.15 -48.60
REMARK 500 5 ALA A 76 43.37 -88.36
REMARK 500 6 GLU A 2 56.53 -146.58
REMARK 500 6 ILE A 3 -70.91 -41.03
REMARK 500 6 CYS A 5 -73.42 -62.98
REMARK 500 6 ASN A 6 -32.33 -39.63
REMARK 500 6 CYS A 8 -78.78 -66.40
REMARK 500 6 LEU A 18 -88.29 -46.01
REMARK 500 6 THR A 20 51.75 24.54
REMARK 500 6 THR A 21 -52.36 179.48
REMARK 500 6 ALA A 24 -26.33 158.01
REMARK 500 6 LYS A 37 39.05 -174.32
REMARK 500 6 ALA A 38 -97.29 -103.84
REMARK 500 6 LYS A 64 44.72 159.69
REMARK 500 6 ASP A 66 -179.57 -49.92
REMARK 500 6 HIS A 75 83.98 65.30
REMARK 500 7 GLU A 2 43.30 -153.65
REMARK 500 7 ILE A 3 -81.22 -58.47
REMARK 500 7 LEU A 7 -79.84 -67.71
REMARK 500 7 LEU A 18 -88.33 -53.06
REMARK 500 7 THR A 20 39.49 31.63
REMARK 500 7 THR A 21 -38.22 -178.52
REMARK 500 7 ALA A 24 21.65 95.39
REMARK 500 7 LYS A 37 39.20 -174.71
REMARK 500 7 ALA A 38 -91.54 -105.64
REMARK 500 7 ILE A 61 -31.68 -38.38
REMARK 500 7 LYS A 64 81.08 160.02
REMARK 500 7 ASP A 66 177.23 -48.51
REMARK 500 7 HIS A 75 45.60 38.41
REMARK 500 8 GLU A 2 64.33 -171.93
REMARK 500 8 LEU A 4 43.88 -152.66
REMARK 500 8 CYS A 8 -82.75 -65.40
REMARK 500 8 LEU A 18 -88.95 -57.06
REMARK 500 8 THR A 20 24.19 41.12
REMARK 500 8 THR A 21 -42.25 163.78
REMARK 500 8 LYS A 37 49.04 -83.91
REMARK 500 8 ALA A 38 -97.92 -117.56
REMARK 500 8 LYS A 64 64.50 157.48
REMARK 500 8 ASP A 66 178.13 -49.04
REMARK 500 8 HIS A 75 50.13 32.17
REMARK 500 9 GLU A 2 40.15 78.54
REMARK 500 9 LEU A 4 48.10 -149.92
REMARK 500 9 LEU A 7 -72.90 -64.35
REMARK 500 9 LEU A 18 -90.77 -50.02
REMARK 500 9 THR A 20 37.26 34.04
REMARK 500 9 THR A 21 -40.12 -179.69
REMARK 500 9 ALA A 24 27.52 89.32
REMARK 500 9 LYS A 37 48.71 -86.17
REMARK 500 9 ALA A 38 -104.65 -116.20
REMARK 500 9 LYS A 64 58.59 159.45
REMARK 500 9 ASP A 66 178.91 -48.50
REMARK 500 10 GLU A 2 -75.35 -39.41
REMARK 500 10 ILE A 3 -34.70 -36.56
REMARK 500 10 CYS A 5 -40.91 -162.98
REMARK 500 10 ASN A 6 -33.37 -36.63
REMARK 500 10 LEU A 7 -73.61 -50.88
REMARK 500 10 CYS A 8 -70.88 -87.74
REMARK 500 10 LEU A 18 -82.15 -39.02
REMARK 500 10 THR A 21 113.79 84.13
REMARK 500 10 ALA A 24 -0.96 78.11
REMARK 500 10 LYS A 37 40.04 -179.79
REMARK 500 10 ALA A 38 -95.56 -104.37
REMARK 500 10 LYS A 64 68.12 159.81
REMARK 500 10 ASP A 66 -178.26 -50.16
REMARK 500 10 LYS A 73 -72.86 -51.25
REMARK 500 10 HIS A 75 70.61 66.97
REMARK 500 10 ALA A 76 -89.65 -101.98
REMARK 500 11 GLU A 2 32.62 -171.16
REMARK 500 11 LEU A 4 36.94 -151.40
REMARK 500 11 CYS A 5 -72.78 -70.72
REMARK 500 11 LEU A 7 -70.61 -65.63
REMARK 500 11 LEU A 18 -90.65 -53.03
REMARK 500 11 THR A 20 25.71 39.79
REMARK 500 11 THR A 21 -41.50 162.70
REMARK 500 11 LYS A 37 39.51 -174.37
REMARK 500 11 ALA A 38 -97.41 -113.40
REMARK 500 11 LYS A 64 44.97 161.28
REMARK 500 11 ASP A 66 179.34 -49.51
REMARK 500 12 GLU A 2 58.72 -99.99
REMARK 500 12 LEU A 4 55.43 -173.47
REMARK 500 12 CYS A 8 -77.93 -66.06
REMARK 500 12 LEU A 18 -89.86 -56.43
REMARK 500 12 THR A 20 91.12 36.40
REMARK 500 12 THR A 21 -21.43 88.96
REMARK 500 12 LYS A 37 48.02 -86.58
REMARK 500 12 ALA A 38 -103.44 -118.70
REMARK 500 12 LYS A 64 43.18 163.41
REMARK 500 12 ASP A 66 -178.03 -50.90
REMARK 500 12 LYS A 73 -70.29 -50.43
REMARK 500 12 HIS A 75 94.47 68.62
REMARK 500 12 ALA A 76 22.79 -153.24
REMARK 500 13 GLU A 2 -7.76 90.30
REMARK 500 13 LEU A 4 64.93 176.32
REMARK 500 13 CYS A 8 -76.59 -76.40
REMARK 500 13 LEU A 18 -83.23 -40.18
REMARK 500 13 THR A 20 103.55 32.53
REMARK 500 13 THR A 21 -6.49 87.33
REMARK 500 13 ALA A 24 13.20 88.42
REMARK 500 13 LYS A 37 40.39 -170.26
REMARK 500 13 ALA A 38 -89.10 -129.54
REMARK 500 13 LYS A 64 40.40 170.69
REMARK 500 13 ASP A 66 179.62 -49.12
REMARK 500 13 ALA A 76 -128.42 -76.78
REMARK 500 14 GLU A 2 57.84 -172.11
REMARK 500 14 LEU A 4 43.70 -155.22
REMARK 500 14 CYS A 8 -76.18 -54.78
REMARK 500 14 LEU A 18 -81.59 -34.76
REMARK 500 14 THR A 21 114.69 83.79
REMARK 500 14 ALA A 24 -0.81 78.38
REMARK 500 14 LYS A 37 49.46 -165.60
REMARK 500 14 ALA A 38 -87.68 -126.31
REMARK 500 14 LYS A 64 44.01 161.75
REMARK 500 14 ASP A 66 179.29 -48.67
REMARK 500 14 HIS A 75 74.69 61.72
REMARK 500 15 GLU A 2 69.06 -173.09
REMARK 500 15 LEU A 4 34.25 -166.17
REMARK 500 15 CYS A 5 -70.58 -71.15
REMARK 500 15 LEU A 7 -84.19 -66.05
REMARK 500 15 CYS A 8 -74.52 -43.27
REMARK 500 15 LEU A 18 -88.40 -45.51
REMARK 500 15 THR A 20 92.47 34.80
REMARK 500 15 THR A 21 -8.83 86.36
REMARK 500 15 LYS A 37 53.04 -92.18
REMARK 500 15 ALA A 38 -101.69 -135.74
REMARK 500 15 LYS A 64 44.39 160.73
REMARK 500 15 ASP A 66 178.10 -48.69
REMARK 500 16 GLU A 2 53.04 78.92
REMARK 500 16 ILE A 3 -82.44 -42.72
REMARK 500 16 CYS A 5 -73.05 -65.28
REMARK 500 16 LEU A 18 -85.36 -47.50
REMARK 500 16 THR A 20 35.15 34.39
REMARK 500 16 THR A 21 -40.69 -179.52
REMARK 500 16 ALA A 24 11.58 90.58
REMARK 500 16 ALA A 38 -103.74 -115.08
REMARK 500 16 LYS A 64 71.26 158.43
REMARK 500 16 ASP A 66 178.22 -48.78
REMARK 500 17 GLU A 2 36.39 179.06
REMARK 500 17 CYS A 5 -74.56 -63.92
REMARK 500 17 LEU A 18 -93.88 -48.34
REMARK 500 17 THR A 20 43.42 35.84
REMARK 500 17 THR A 21 -46.85 -174.55
REMARK 500 17 ALA A 38 -102.33 -121.31
REMARK 500 17 ASP A 63 -71.51 -74.92
REMARK 500 17 LYS A 64 39.24 172.49
REMARK 500 17 ASP A 66 -179.72 -50.53
REMARK 500 17 HIS A 75 42.68 34.09
REMARK 500 18 GLU A 2 28.10 46.82
REMARK 500 18 LEU A 4 54.28 179.11
REMARK 500 18 LEU A 7 -76.89 -63.68
REMARK 500 18 LEU A 18 -92.37 -51.75
REMARK 500 18 THR A 20 39.64 31.98
REMARK 500 18 THR A 21 -38.96 -177.11
REMARK 500 18 ALA A 24 30.30 93.19
REMARK 500 18 LYS A 37 39.02 -176.56
REMARK 500 18 ALA A 38 -92.58 -116.03
REMARK 500 18 LYS A 64 38.93 172.75
REMARK 500 18 ASP A 66 -177.74 -50.17
REMARK 500 18 LYS A 73 -71.34 -50.28
REMARK 500 19 GLU A 2 95.90 178.03
REMARK 500 19 LEU A 4 36.17 -168.42
REMARK 500 19 CYS A 5 -71.88 -54.73
REMARK 500 19 LEU A 7 -76.78 -62.82
REMARK 500 19 LEU A 18 -92.43 -54.21
REMARK 500 19 THR A 20 39.40 31.31
REMARK 500 19 THR A 21 -47.35 -134.90
REMARK 500 19 ASN A 36 -30.61 -39.16
REMARK 500 19 ALA A 38 -107.95 -123.19
REMARK 500 19 ILE A 61 -34.22 -38.51
REMARK 500 19 LYS A 64 82.14 160.87
REMARK 500 19 ASP A 66 178.08 -48.42
REMARK 500 19 ALA A 76 -101.27 -53.68
REMARK 500 20 LEU A 4 55.47 176.54
REMARK 500 20 LEU A 18 -85.05 -44.81
REMARK 500 20 THR A 20 38.31 32.87
REMARK 500 20 THR A 21 -41.34 176.82
REMARK 500 20 ALA A 24 14.35 89.76
REMARK 500 20 LYS A 37 45.90 -164.81
REMARK 500 20 ALA A 38 -100.79 -114.56
REMARK 500 20 LYS A 64 41.87 164.44
REMARK 500 20 ASP A 66 -179.40 -49.94
REMARK 500 20 HIS A 75 42.84 33.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OF9 A 1 77 UNP P34095 PFPA_ENTHI 22 98
SEQRES 1 A 77 GLY GLU ILE LEU CYS ASN LEU CYS THR GLY LEU ILE ASN
SEQRES 2 A 77 THR LEU GLU ASN LEU LEU THR THR LYS GLY ALA ASP LYS
SEQRES 3 A 77 VAL LYS ASP TYR ILE SER SER LEU CYS ASN LYS ALA SER
SEQRES 4 A 77 GLY PHE ILE ALA THR LEU CYS THR LYS VAL LEU ASP PHE
SEQRES 5 A 77 GLY ILE ASP LYS LEU ILE GLN LEU ILE GLU ASP LYS VAL
SEQRES 6 A 77 ASP ALA ASN ALA ILE CYS ALA LYS ILE HIS ALA CYS
HELIX 1 1 LEU A 4 LEU A 19 1 16
HELIX 2 2 ALA A 24 ASN A 36 1 13
HELIX 3 3 ILE A 42 GLY A 53 1 12
HELIX 4 4 GLY A 53 LYS A 64 1 12
HELIX 5 5 ASP A 66 HIS A 75 1 10
SSBOND 1 CYS A 5 CYS A 77 1555 1555 2.12
SSBOND 2 CYS A 8 CYS A 71 1555 1555 2.18
SSBOND 3 CYS A 35 CYS A 46 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 - 25 20 Bytes