HEADER INTEGRAL MEMBRANE PROTEIN PORIN 24-APR-92 2POR 2POR 2 COMPND PORIN (CRYSTAL FORM B) 2POR 3 SOURCE (RHODOBACTER $CAPSULATUS) (STRAIN 37B4) (FORMERLY 2POR 4 SOURCE 2 (RHODOPSEUDOMONAS $CAPSULATA)) 2POR 5 AUTHOR M.S.WEISS,G.E.SCHULZ 2POR 6 REVDAT 1 15-JUL-93 2POR 0 2POR 7 JRNL AUTH M.S.WEISS,G.E.SCHULZ 2POR 8 JRNL TITL STRUCTURE OF PORIN REFINED AT 1.8 ANGSTROMS 2POR 9 JRNL TITL 2 RESOLUTION 2POR 10 JRNL REF J.MOL.BIOL. V. 227 493 1992 2POR 11 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 2POR 12 REMARK 1 2POR 13 REMARK 1 REFERENCE 1 2POR 14 REMARK 1 AUTH M.S.WEISS,U.ABELE,J.WECKESSER,W.WELTE,E.SCHILTZ, 2POR 15 REMARK 1 AUTH 2 G.E.SCHULZ 2POR 16 REMARK 1 TITL MOLECULAR ARCHITECTURE AND ELECTROSTATIC PROPERTIES 2POR 17 REMARK 1 TITL 2 OF A BACTERIAL PORIN 2POR 18 REMARK 1 REF SCIENCE V. 254 1627 1991 2POR 19 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 2POR 20 REMARK 1 REFERENCE 2 2POR 21 REMARK 1 AUTH E.SCHILTZ,A.KREUSCH,U.NESTEL,G.E.SCHULZ 2POR 22 REMARK 1 TITL PRIMARY STRUCTURE OF PORIN FROM RHODOBACTER 2POR 23 REMARK 1 TITL 2 CAPSULATUS 2POR 24 REMARK 1 REF EUR.J.BIOCHEM. V. 199 587 1991 2POR 25 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 2POR 26 REMARK 1 REFERENCE 3 2POR 27 REMARK 1 AUTH M.S.WEISS,A.KREUSCH,E.SCHILTZ,U.NESTEL,W.WELTE, 2POR 28 REMARK 1 AUTH 2 J.WECKESSER,G.E.SCHULZ 2POR 29 REMARK 1 TITL THE STRUCTURE OF PORIN FROM RHODOBACTER CAPSULATUS 2POR 30 REMARK 1 TITL 2 AT 1.8 ANGSTROMS RESOLUTION 2POR 31 REMARK 1 REF /FEBS$ LETT. V. 280 379 1991 2POR 32 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 2POR 33 REMARK 1 REFERENCE 4 2POR 34 REMARK 1 AUTH A.KREUSCH,M.S.WEISS,W.WELTE,J.WECKESSER,G.E.SCHULZ 2POR 35 REMARK 1 TITL CRYSTALS OF AN INTEGRAL MEMBRANE PROTEIN 2POR 36 REMARK 1 TITL 2 DIFFRACTING TO 1.8 ANGSTROMS RESOLUTION 2POR 37 REMARK 1 REF J.MOL.BIOL. V. 217 9 1991 2POR 38 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2POR 39 REMARK 1 REFERENCE 5 2POR 40 REMARK 1 AUTH M.S.WEISS,T.WACKER,J.WECKESSER,W.WELTE,G.E.SCHULZ 2POR 41 REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF PORIN FROM 2POR 42 REMARK 1 TITL 2 RHODOBACTER CAPSULATUS AT 3 ANGSTROMS RESOLUTION 2POR 43 REMARK 1 REF /FEBS$ LETT. V. 267 268 1990 2POR 44 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 2POR 45 REMARK 1 REFERENCE 6 2POR 46 REMARK 1 AUTH M.S.WEISS,T.WACKER,U.NESTEL,D.WOITZIK,J.WECKESSER, 2POR 47 REMARK 1 AUTH 2 W.KREUTZ,W.WELTE,G.E.SCHULZ 2POR 48 REMARK 1 TITL THE STRUCTURE OF PORIN FROM RHODOBACTER CAPSULATUS 2POR 49 REMARK 1 TITL 2 AT 0.6 NM RESOLUTION 2POR 50 REMARK 1 REF /FEBS$ LETT. V. 256 143 1989 2POR 51 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 2POR 52 REMARK 1 REFERENCE 7 2POR 53 REMARK 1 AUTH U.NESTEL,T.WACKER,D.WOITZIK,J.WECKESSER,W.KREUTZ, 2POR 54 REMARK 1 AUTH 2 W.WELTE 2POR 55 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF 2POR 56 REMARK 1 TITL 2 PORIN FROM RHODOBACTER CAPSULATUS 2POR 57 REMARK 1 REF /FEBS$ LETT. V. 242 405 1989 2POR 58 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 2POR 59 REMARK 2 2POR 60 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 2POR 61 REMARK 3 2POR 62 REMARK 3 REFINEMENT. MOLECULAR DYNAMICS REFINEMENT BY THE METHOD OF 2POR 63 REMARK 3 A. BRUNGER, J. KURIYAN, AND M. KARPLUS (PROGRAM *XPLOR*). 2POR 64 REMARK 3 THE R VALUE IS 0.186 FOR ALL 42851 REFLECTIONS IN THE 2POR 65 REMARK 3 RESOLUTION RANGE 10 TO 1.8 ANGSTROMS. THE RMS DEVIATION 2POR 66 REMARK 3 FROM IDEALITY OF THE BOND LENGTHS IS 0.015 ANGSTROMS. THE 2POR 67 REMARK 3 RMS DEVIATION FROM IDEALITY OF THE BOND ANGLES IS 2.8 2POR 68 REMARK 3 DEGREES. 2POR 69 REMARK 4 2POR 70 REMARK 4 PORIN IS A TRIMER CONSISTING OF THREE IDENTICAL SUBUNITS. 2POR 71 REMARK 4 THE SUBUNITS ARE RELATED THROUGH CRYSTALLOGRAPHIC SYMMETRY 2POR 72 REMARK 4 OPERATIONS. THE TRIMER AXIS IS AT X=0.0, Y=0.0. THE MODEL 2POR 73 REMARK 4 HAS BEEN SHIFTED SUCH THAT THE LOWEST Z COORDINATE IN THE 2POR 74 REMARK 4 COORDINATE SET IS ZERO. 2POR 75 REMARK 5 2POR 76 REMARK 5 IN ADDITION TO THE PEPTIDE CHAIN OF 301 AMINO ACIDS, THE 2POR 77 REMARK 5 FINAL MODEL CONTAINS 3 CALCIUM IONS, 274 SOLVENT MOLECULES 2POR 78 REMARK 5 MODELED AS WATER AND FOUR MOLECULES MODELED AS THE 2POR 79 REMARK 5 DETERGENT N-OCTYLTETRAOXYETHYLENE. 240 OF THE 274 SOLVENT 2POR 80 REMARK 5 MOLECULES ARE DIRECTLY OR INDIRECTLY COORDINATED TO A 2POR 81 REMARK 5 PROTEIN ATOM, AND ARE THEREFORE WATER AND LABELED "HOH". 2POR 82 REMARK 5 34 ARE AT THE NONPOLAR OUTER SURFACE OF THE MOLECULE AND 2POR 83 REMARK 5 CONSTITUTE PREFERRED POSITIONS OF DETERGENT FRAGMENTS 2POR 84 REMARK 5 RATHER THAN WATER MOLECULES. THESE ARE MODELED AS WATER 2POR 85 REMARK 5 MOLECULES. THE NUMBERING STARTS AT RESIDUE NUMBER 302 FOR 2POR 86 REMARK 5 IONS, 305 FOR WATER MOLECULES, 545 FOR DETERGENT MOLECULES 2POR 87 REMARK 5 AND 549 FOR THE DETERGENT FRAGMENTS MODELED AS WATER. 2POR 88 REMARK 5 THE *FORMUL* RECORD FOR *HOH* INCLUDES ALL THE SOLVENT 2POR 89 REMARK 5 FRAGMENTS MODELED AS WATER. 2POR 90 REMARK 6 2POR 91 REMARK 6 THE SHEET PRESENTED AS *S1* ON SHEET RECORDS BELOW IS 2POR 92 REMARK 6 ACTUALLY A SIXTEEN-STRANDED BETA-BARREL. THIS IS 2POR 93 REMARK 6 REPRESENTED AS A SEVENTEEN-STRANDED SHEET IN WHICH THE 2POR 94 REMARK 6 FIRST AND LAST STRANDS ARE IDENTICAL. 2POR 95 REMARK 7 2POR 96 REMARK 7 THE CRYSTALS HAVE FORM *B* AS DESCRIBED IN THE *JRNL* 2POR 97 REMARK 7 REFERENCE. 2POR 98 SEQRES 1 301 GLU VAL LYS LEU SER GLY ASP ALA ARG MET GLY VAL MET 2POR 99 SEQRES 2 301 TYR ASN GLY ASP ASP TRP ASN PHE SER SER ARG SER ARG 2POR 100 SEQRES 3 301 VAL LEU PHE THR MET SER GLY THR THR ASP SER GLY LEU 2POR 101 SEQRES 4 301 GLU PHE GLY ALA SER PHE LYS ALA HIS GLU SER VAL GLY 2POR 102 SEQRES 5 301 ALA GLU THR GLY GLU ASP GLY THR VAL PHE LEU SER GLY 2POR 103 SEQRES 6 301 ALA PHE GLY LYS ILE GLU MET GLY ASP ALA LEU GLY ALA 2POR 104 SEQRES 7 301 SER GLU ALA LEU PHE GLY ASP LEU TYR GLU VAL GLY TYR 2POR 105 SEQRES 8 301 THR ASP LEU ASP ASP ARG GLY GLY ASN ASP ILE PRO TYR 2POR 106 SEQRES 9 301 LEU THR GLY ASP GLU ARG LEU THR ALA GLU ASP ASN PRO 2POR 107 SEQRES 10 301 VAL LEU LEU TYR THR TYR SER ALA GLY ALA PHE SER VAL 2POR 108 SEQRES 11 301 ALA ALA SER MET SER ASP GLY LYS VAL GLY GLU THR SER 2POR 109 SEQRES 12 301 GLU ASP ASP ALA GLN GLU MET ALA VAL ALA ALA ALA TYR 2POR 110 SEQRES 13 301 THR PHE GLY ASN TYR THR VAL GLY LEU GLY TYR GLU LYS 2POR 111 SEQRES 14 301 ILE ASP SER PRO ASP THR ALA LEU MET ALA ASP MET GLU 2POR 112 SEQRES 15 301 GLN LEU GLU LEU ALA ALA ILE ALA LYS PHE GLY ALA THR 2POR 113 SEQRES 16 301 ASN VAL LYS ALA TYR TYR ALA ASP GLY GLU LEU ASP ARG 2POR 114 SEQRES 17 301 ASP PHE ALA ARG ALA VAL PHE ASP LEU THR PRO VAL ALA 2POR 115 SEQRES 18 301 ALA ALA ALA THR ALA VAL ASP HIS LYS ALA TYR GLY LEU 2POR 116 SEQRES 19 301 SER VAL ASP SER THR PHE GLY ALA THR THR VAL GLY GLY 2POR 117 SEQRES 20 301 TYR VAL GLN VAL LEU ASP ILE ASP THR ILE ASP ASP VAL 2POR 118 SEQRES 21 301 THR TYR TYR GLY LEU GLY ALA SER TYR ASP LEU GLY GLY 2POR 119 SEQRES 22 301 GLY ALA SER ILE VAL GLY GLY ILE ALA ASP ASN ASP LEU 2POR 120 SEQRES 23 301 PRO ASN SER ASP MET VAL ALA ASP LEU GLY VAL LYS PHE 2POR 121 SEQRES 24 301 LYS PHE 2POR 122 FTNOTE 1 2POR 123 FTNOTE 1 THE SIDECHAIN CG, SD, AND CE ATOMS OF RESIDUE MET 13 AND 2POR 124 FTNOTE 1 THE SIDECHAIN OF RESIDUE SER 50 HAVE BEEN MODELED WITH TWO 2POR 125 FTNOTE 1 ALTERNATE CONFORMATIONS. 2POR 126 FTNOTE 2 2POR 127 FTNOTE 2 THE CG1 AND CG2 ATOMS OF RESIDUE VAL 152 HAVE BEEN MODELED 2POR 128 FTNOTE 2 WITH THREE ALTERNATE CONFORMATIONS. 2POR 129 FTNOTE 3 2POR 130 FTNOTE 3 RESIDUE 545 HAS NOT BEEN UNAMBIGUOUSLY IDENTIFIED. IT HAS 2POR 131 FTNOTE 3 BEEN MODELED AS A DETERGENT N-OCTYLTETRAOXYETHYLENE. 2POR 132 FTNOTE 4 2POR 133 FTNOTE 4 THIRTY FOUR DETERGENT FRAGMENTS HAVE BEEN MODELED AS WATERS 2POR 134 FTNOTE 4 (SEE REMARK 5) 2POR 135 HET CA 302 1 CALCIUM 2POR 136 HET CA 303 1 CALCIUM 2POR 137 HET CA 304 1 CALCIUM 2POR 138 HET OTE 545 21 N-OCTYLTETRAOXYETHYLENE 2POR 139 HET OTE 546 21 N-OCTYLTETRAOXYETHYLENE 2POR 140 HET OTE 547 21 N-OCTYLTETRAOXYETHYLENE 2POR 141 HET OTE 548 21 N-OCTYLTETRAOXYETHYLENE 2POR 142 FORMUL 2 CA 3(CA1 ++) 2POR 143 FORMUL 3 OTE 4(C16 H34 O5) 2POR 144 FORMUL 4 HOH *274(H2 O1) 2POR 145 HELIX 1 H1 SER 50 GLU 54 1 2POR 146 HELIX 2 H2 GLY 77 PHE 83 1 2POR 147 HELIX 3 H3 ARG 208 VAL 214 1 2POR 148 SHEET 1 S117 GLU 1 ASN 15 0 2POR 149 SHEET 2 S117 ASP 18 THR 35 -1 O ASP 18 N ASN 15 2POR 150 SHEET 3 S117 LEU 39 LYS 46 -1 O LEU 39 N THR 35 2POR 151 SHEET 4 S117 GLY 59 GLY 65 -1 N THR 60 O SER 44 2POR 152 SHEET 5 S117 GLY 68 ASP 74 -1 N GLY 68 O GLY 65 2POR 153 SHEET 6 S117 VAL 118 ALA 125 -1 N VAL 118 O GLY 73 2POR 154 SHEET 7 S117 PHE 128 SER 135 -1 N PHE 128 O ALA 125 2POR 155 SHEET 8 S117 GLN 148 PHE 158 -1 O GLU 149 N SER 135 2POR 156 SHEET 9 S117 TYR 161 ASP 171 -1 N TYR 161 O PHE 158 2POR 157 SHEET 10 S117 MET 181 PHE 192 -1 N MET 181 O ILE 170 2POR 158 SHEET 11 S117 THR 195 LEU 206 -1 N THR 195 O PHE 192 2POR 159 SHEET 12 S117 VAL 227 PHE 240 -1 N VAL 227 O LEU 206 2POR 160 SHEET 13 S117 THR 243 ILE 254 -1 N THR 243 O PHE 240 2POR 161 SHEET 14 S117 ASP 258 LEU 271 -1 N ASP 258 O ILE 254 2POR 162 SHEET 15 S117 ALA 275 ASP 285 -1 O ALA 275 N LEU 271 2POR 163 SHEET 16 S117 VAL 292 PHE 301 -1 N VAL 292 O ALA 282 2POR 164 SHEET 17 S117 GLU 1 ASN 15 1 N GLY 6 0 PHE 301 2POR 165 TURN 1 TN1 ASN 15 ASP 18 2POR 166 TURN 2 TN2 THR 35 GLY 38 2POR 167 TURN 3 TN3 LYS 46 GLU 49 2POR 168 TURN 4 TN4 GLY 65 GLY 68 2POR 169 TURN 5 TN5 GLY 90 ASP 93 2POR 170 TURN 6 TN6 ASP 95 GLY 98 2POR 171 TURN 7 TN7 GLY 107 ARG 110 2POR 172 TURN 8 TN8 ALA 113 ASN 116 2POR 173 TURN 9 TN9 ALA 125 PHE 128 2POR 174 TURN 10 T10 VAL 139 THR 142 2POR 175 TURN 11 T11 PHE 158 TYR 161 2POR 176 TURN 12 T12 ASP 174 LEU 177 2POR 177 TURN 13 T13 PHE 192 THR 195 2POR 178 TURN 14 T14 PHE 240 THR 243 2POR 179 TURN 15 T15 ILE 254 ILE 257 2POR 180 TURN 16 T16 GLY 272 ALA 275 2POR 181 TURN 17 T17 LEU 286 SER 289 2POR 182 CRYST1 92.300 92.300 146.200 90.00 90.00 120.00 R 3 9 2POR 183 ORIGX1 1.000000 0.000000 0.000000 0.00000 2POR 184 ORIGX2 0.000000 1.000000 0.000000 0.00000 2POR 185 ORIGX3 0.000000 0.000000 1.000000 0.00000 2POR 186 SCALE1 0.010834 0.006255 0.000000 0.00000 2POR 187 SCALE2 0.000000 0.012510 0.000000 0.00000 2POR 188 SCALE3 0.000000 0.000000 0.006840 0.00000 2POR 189