HEADER OXIDOREDUCTASE 15-OCT-93 2TMD 2TMD 2 COMPND TRIMETHYLAMINE DEHYDROGENASE (E.C.1.5.99.7) 2TMD 3 SOURCE METHYLOTROPHIC BACTERIUM W=3= A=1= 2TMD 4 AUTHOR F.S.MATHEWS,L.W.LIM,S.WHITE 2TMD 5 REVDAT 1 31-JAN-94 2TMD 0 2TMD 6 REMARK 1 2TMD 7 REMARK 1 REFERENCE 1 2TMD 8 REMARK 1 AUTH M.J.BARBER,P.J.NEAME,L.W.LIM,S.WHITE,F.S.MATHEWS 2TMD 9 REMARK 1 TITL CORRELATION OF X-RAY DEDUCED AND EXPERIMENTAL 2TMD 10 REMARK 1 TITL 2 AMINO ACID SEQUENCES OF TRIMETHYLAMINE 2TMD 11 REMARK 1 TITL 3 DEHYDROGENASE 2TMD 12 REMARK 1 REF J.BIOL.CHEM. V. 267 6611 1992 2TMD 13 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 2TMD 14 REMARK 1 REFERENCE 2 2TMD 15 REMARK 1 AUTH H.D.BELLAMY,L.W.LIM,F.S.MATHEWS,W.R.DUNHAM 2TMD 16 REMARK 1 TITL STUDIES OF CRYSTALLINE TRIMETHYLAMINE 2TMD 17 REMARK 1 TITL 2 DEHYDROGENASE IN THREE OXIDATION STATES AND IN 2TMD 18 REMARK 1 TITL 3 THE PRESENCE OF SUBSTRATE AND INHIBITOR 2TMD 19 REMARK 1 REF J.BIOL.CHEM. V. 264 11887 1989 2TMD 20 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 2TMD 21 REMARK 1 REFERENCE 3 2TMD 22 REMARK 1 AUTH L.W.LIM,F.S.MATHEWS,D.J.STEENKAMP 2TMD 23 REMARK 1 TITL IDENTIFICATION OF ADP IN THE IRON-SULFUR 2TMD 24 REMARK 1 TITL 2 FLAVOPROTEIN TRIMETHYLAMINE DEHYDROGENASE 2TMD 25 REMARK 1 REF J.BIOL.CHEM. V. 263 3075 1988 2TMD 26 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 2TMD 27 REMARK 1 REFERENCE 4 2TMD 28 REMARK 1 AUTH L.W.LIM,N.SHAMALA,F.S.MATHEWS,D.J.STEENKAMP, 2TMD 29 REMARK 1 AUTH 2 R.HAMLIN,N.H.XUONG 2TMD 30 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE IRON-SULFUR 2TMD 31 REMARK 1 TITL 2 FLAVOPROTEIN TRIMETHYLAMINE DEHYDROGENASE AT 2.4 2TMD 32 REMARK 1 TITL 3 ANGSTROMS RESOLUTION 2TMD 33 REMARK 1 REF J.BIOL.CHEM. V. 261 15140 1986 2TMD 34 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 2TMD 35 REMARK 2 2TMD 36 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 2TMD 37 REMARK 3 2TMD 38 REMARK 3 REFINEMENT. 2TMD 39 REMARK 3 PROGRAM X-PLOR 2TMD 40 REMARK 3 AUTHORS BRUNGER 2TMD 41 REMARK 3 R VALUE 0.154 2TMD 42 REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 2TMD 43 REMARK 3 RMSD BOND ANGLES 1.281 DEGREES 2TMD 44 REMARK 3 2TMD 45 REMARK 3 RESOLUTION RANGE 10.0 - 2.4 ANGSTROMS 2TMD 46 REMARK 4 2TMD 47 REMARK 4 THE SHEETS PRESENTED AS *AA* AND *AB* ON SHEET RECORDS 2TMD 48 REMARK 4 BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THESE ARE 2TMD 49 REMARK 4 REPRESENTED BY NINE-STRANDED SHEETS IN WHICH THE FIRST 2TMD 50 REMARK 4 AND LAST STRANDS ARE IDENTICAL. 2TMD 51 REMARK 5 2TMD 52 REMARK 5 THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. THE 2TMD 53 REMARK 5 TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 2TMD 54 REMARK 5 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO 2TMD 55 REMARK 5 CHAIN *A*. 2TMD 56 SEQRES 1 A 729 ALA ARG ASP PRO LYS HIS ASP ILE LEU PHE GLU PRO ILE 2TMD 57 SEQRES 2 A 729 GLN ILE GLY PRO LYS THR LEU ARG ASN ARG PHE TYR GLN 2TMD 58 SEQRES 3 A 729 VAL PRO HIS CYS ILE GLY ALA GLY SER ASP LYS PRO GLY 2TMD 59 SEQRES 4 A 729 PHE GLN SER ALA HIS ARG SER VAL LYS ALA GLU GLY GLY 2TMD 60 SEQRES 5 A 729 TRP ALA ALA LEU ASN THR GLU TYR CYS SER ILE ASN PRO 2TMD 61 SEQRES 6 A 729 GLU SER ASP ASP THR HIS ARG LEU SER ALA ARG ILE TRP 2TMD 62 SEQRES 7 A 729 ASP GLU GLY ASP VAL ARG ASN LEU LYS ALA MET THR ASP 2TMD 63 SEQRES 8 A 729 GLU VAL HIS LYS TYR GLY ALA LEU ALA GLY VAL GLU LEU 2TMD 64 SEQRES 9 A 729 TRP TYR GLY GLY ALA HIS ALA PRO ASN MET GLU SER ARG 2TMD 65 SEQRES 10 A 729 ALA THR PRO ARG GLY PRO SER GLN TYR ALA SER GLU PHE 2TMD 66 SEQRES 11 A 729 GLU THR LEU SER TYR CYS LYS GLU MET ASP LEU SER ASP 2TMD 67 SEQRES 12 A 729 ILE ALA GLN VAL GLN GLN PHE TYR VAL ASP ALA ALA LYS 2TMD 68 SEQRES 13 A 729 ARG SER ARG ASP ALA GLY PHE ASP ILE VAL TYR VAL TYR 2TMD 69 SEQRES 14 A 729 GLY ALA HIS SER TYR LEU PRO LEU GLN PHE LEU ASN PRO 2TMD 70 SEQRES 15 A 729 TYR TYR ASN LYS ARG THR ASP LYS TYR GLY GLY SER LEU 2TMD 71 SEQRES 16 A 729 GLU ASN ARG ALA ARG PHE TRP LEU GLU THR LEU GLU LYS 2TMD 72 SEQRES 17 A 729 VAL LYS HIS ALA VAL GLY SER ASP CYS ALA ILE ALA THR 2TMD 73 SEQRES 18 A 729 ARG PHE GLY VAL ASP THR VAL TYR GLY PRO GLY GLN ILE 2TMD 74 SEQRES 19 A 729 GLU ALA GLU VAL ASP GLY GLN LYS PHE VAL GLU MET ALA 2TMD 75 SEQRES 20 A 729 ASP SER LEU VAL ASP MET TRP ASP ILE THR ILE GLY ASP 2TMD 76 SEQRES 21 A 729 ILE ALA GLU TRP GLY GLU ASP ALA GLY PRO SER ARG PHE 2TMD 77 SEQRES 22 A 729 TYR GLN GLN GLY HIS THR ILE PRO TRP VAL LYS LEU VAL 2TMD 78 SEQRES 23 A 729 LYS GLN VAL SER LYS LYS PRO VAL LEU GLY VAL GLY ARG 2TMD 79 SEQRES 24 A 729 TYR THR ASP PRO GLU LYS MET ILE GLU ILE VAL THR LYS 2TMD 80 SEQRES 25 A 729 GLY TYR ALA ASP ILE ILE GLY CYS ALA ARG PRO SER ILE 2TMD 81 SEQRES 26 A 729 ALA ASP PRO PHE LEU PRO GLN LYS VAL GLU GLN GLY ARG 2TMD 82 SEQRES 27 A 729 TYR ASP ASP ILE ARG VAL CYS ILE GLY CYS ASN VAL CYS 2TMD 83 SEQRES 28 A 729 ILE SER ARG TRP GLU ILE GLY GLY PRO PRO MET ILE CYS 2TMD 84 SEQRES 29 A 729 THR GLN ASN ALA THR ALA GLY GLU GLU TYR ARG ARG GLY 2TMD 85 SEQRES 30 A 729 TRP HIS PRO GLU LYS PHE ARG GLN THR LYS ASN LYS ASP 2TMD 86 SEQRES 31 A 729 SER VAL LEU ILE VAL GLY ALA GLY PRO SER GLY SER GLU 2TMD 87 SEQRES 32 A 729 ALA ALA ARG VAL LEU MET GLU SER GLY TYR THR VAL HIS 2TMD 88 SEQRES 33 A 729 LEU THR ASP THR ALA GLU LYS ILE GLY GLY HIS LEU ASN 2TMD 89 SEQRES 34 A 729 GLN VAL ALA ALA LEU PRO GLY LEU GLY GLU TRP SER TYR 2TMD 90 SEQRES 35 A 729 HIS ARG ASP TYR ARG GLU THR GLN ILE THR LYS LEU LEU 2TMD 91 SEQRES 36 A 729 LYS LYS ASN LYS GLU SER GLN LEU ALA LEU GLY GLN LYS 2TMD 92 SEQRES 37 A 729 PRO MET THR ALA ASP ASP VAL LEU GLN TYR GLY ALA ASP 2TMD 93 SEQRES 38 A 729 LYS VAL ILE ILE ALA THR GLY ALA ARG TRP ASN THR ASP 2TMD 94 SEQRES 39 A 729 GLY THR ASN CYS LEU THR HIS ASP PRO ILE PRO GLY ALA 2TMD 95 SEQRES 40 A 729 ASP ALA SER LEU PRO ASP GLN LEU THR PRO GLU GLN VAL 2TMD 96 SEQRES 41 A 729 MET ASP GLY LYS LYS LYS ILE GLY LYS ARG VAL VAL ILE 2TMD 97 SEQRES 42 A 729 LEU ASN ALA ASP THR TYR PHE MET ALA PRO SER LEU ALA 2TMD 98 SEQRES 43 A 729 GLU LYS LEU ALA THR ALA GLY HIS GLU VAL THR ILE VAL 2TMD 99 SEQRES 44 A 729 SER GLY VAL HIS LEU ALA ASN TYR MET HIS PHE THR LEU 2TMD 100 SEQRES 45 A 729 GLU TYR PRO ASN MET MET ARG ARG LEU HIS GLU LEU HIS 2TMD 101 SEQRES 46 A 729 VAL GLU GLU LEU GLY ASP HIS PHE CYS SER ARG ILE GLU 2TMD 102 SEQRES 47 A 729 PRO GLY ARG MET GLU ILE TYR ASN ILE TRP GLY ASP GLY 2TMD 103 SEQRES 48 A 729 SER LYS ARG THR TYR ARG GLY PRO GLY VAL SER PRO ARG 2TMD 104 SEQRES 49 A 729 ASP ALA ASN THR SER HIS ARG TRP ILE GLU PHE ASP SER 2TMD 105 SEQRES 50 A 729 LEU VAL LEU VAL THR GLY ARG HIS SER GLU CYS THR LEU 2TMD 106 SEQRES 51 A 729 TRP ASN GLU LEU LYS ALA ARG GLU SER GLU TRP ALA GLU 2TMD 107 SEQRES 52 A 729 ASN ASP ILE LYS GLY ILE TYR LEU ILE GLY ASP ALA GLU 2TMD 108 SEQRES 53 A 729 ALA PRO ARG LEU ILE ALA ASP ALA THR PHE THR GLY HIS 2TMD 109 SEQRES 54 A 729 ARG VAL ALA ARG GLU ILE GLU GLU ALA ASN PRO GLN ILE 2TMD 110 SEQRES 55 A 729 ALA ILE PRO TYR LYS ARG GLU THR ILE ALA TRP GLY THR 2TMD 111 SEQRES 56 A 729 PRO HIS MET PRO GLY GLY ASN PHE LYS ILE GLU TYR LYS 2TMD 112 SEQRES 57 A 729 VAL 2TMD 113 SEQRES 1 B 729 ALA ARG ASP PRO LYS HIS ASP ILE LEU PHE GLU PRO ILE 2TMD 114 SEQRES 2 B 729 GLN ILE GLY PRO LYS THR LEU ARG ASN ARG PHE TYR GLN 2TMD 115 SEQRES 3 B 729 VAL PRO HIS CYS ILE GLY ALA GLY SER ASP LYS PRO GLY 2TMD 116 SEQRES 4 B 729 PHE GLN SER ALA HIS ARG SER VAL LYS ALA GLU GLY GLY 2TMD 117 SEQRES 5 B 729 TRP ALA ALA LEU ASN THR GLU TYR CYS SER ILE ASN PRO 2TMD 118 SEQRES 6 B 729 GLU SER ASP ASP THR HIS ARG LEU SER ALA ARG ILE TRP 2TMD 119 SEQRES 7 B 729 ASP GLU GLY ASP VAL ARG ASN LEU LYS ALA MET THR ASP 2TMD 120 SEQRES 8 B 729 GLU VAL HIS LYS TYR GLY ALA LEU ALA GLY VAL GLU LEU 2TMD 121 SEQRES 9 B 729 TRP TYR GLY GLY ALA HIS ALA PRO ASN MET GLU SER ARG 2TMD 122 SEQRES 10 B 729 ALA THR PRO ARG GLY PRO SER GLN TYR ALA SER GLU PHE 2TMD 123 SEQRES 11 B 729 GLU THR LEU SER TYR CYS LYS GLU MET ASP LEU SER ASP 2TMD 124 SEQRES 12 B 729 ILE ALA GLN VAL GLN GLN PHE TYR VAL ASP ALA ALA LYS 2TMD 125 SEQRES 13 B 729 ARG SER ARG ASP ALA GLY PHE ASP ILE VAL TYR VAL TYR 2TMD 126 SEQRES 14 B 729 GLY ALA HIS SER TYR LEU PRO LEU GLN PHE LEU ASN PRO 2TMD 127 SEQRES 15 B 729 TYR TYR ASN LYS ARG THR ASP LYS TYR GLY GLY SER LEU 2TMD 128 SEQRES 16 B 729 GLU ASN ARG ALA ARG PHE TRP LEU GLU THR LEU GLU LYS 2TMD 129 SEQRES 17 B 729 VAL LYS HIS ALA VAL GLY SER ASP CYS ALA ILE ALA THR 2TMD 130 SEQRES 18 B 729 ARG PHE GLY VAL ASP THR VAL TYR GLY PRO GLY GLN ILE 2TMD 131 SEQRES 19 B 729 GLU ALA GLU VAL ASP GLY GLN LYS PHE VAL GLU MET ALA 2TMD 132 SEQRES 20 B 729 ASP SER LEU VAL ASP MET TRP ASP ILE THR ILE GLY ASP 2TMD 133 SEQRES 21 B 729 ILE ALA GLU TRP GLY GLU ASP ALA GLY PRO SER ARG PHE 2TMD 134 SEQRES 22 B 729 TYR GLN GLN GLY HIS THR ILE PRO TRP VAL LYS LEU VAL 2TMD 135 SEQRES 23 B 729 LYS GLN VAL SER LYS LYS PRO VAL LEU GLY VAL GLY ARG 2TMD 136 SEQRES 24 B 729 TYR THR ASP PRO GLU LYS MET ILE GLU ILE VAL THR LYS 2TMD 137 SEQRES 25 B 729 GLY TYR ALA ASP ILE ILE GLY CYS ALA ARG PRO SER ILE 2TMD 138 SEQRES 26 B 729 ALA ASP PRO PHE LEU PRO GLN LYS VAL GLU GLN GLY ARG 2TMD 139 SEQRES 27 B 729 TYR ASP ASP ILE ARG VAL CYS ILE GLY CYS ASN VAL CYS 2TMD 140 SEQRES 28 B 729 ILE SER ARG TRP GLU ILE GLY GLY PRO PRO MET ILE CYS 2TMD 141 SEQRES 29 B 729 THR GLN ASN ALA THR ALA GLY GLU GLU TYR ARG ARG GLY 2TMD 142 SEQRES 30 B 729 TRP HIS PRO GLU LYS PHE ARG GLN THR LYS ASN LYS ASP 2TMD 143 SEQRES 31 B 729 SER VAL LEU ILE VAL GLY ALA GLY PRO SER GLY SER GLU 2TMD 144 SEQRES 32 B 729 ALA ALA ARG VAL LEU MET GLU SER GLY TYR THR VAL HIS 2TMD 145 SEQRES 33 B 729 LEU THR ASP THR ALA GLU LYS ILE GLY GLY HIS LEU ASN 2TMD 146 SEQRES 34 B 729 GLN VAL ALA ALA LEU PRO GLY LEU GLY GLU TRP SER TYR 2TMD 147 SEQRES 35 B 729 HIS ARG ASP TYR ARG GLU THR GLN ILE THR LYS LEU LEU 2TMD 148 SEQRES 36 B 729 LYS LYS ASN LYS GLU SER GLN LEU ALA LEU GLY GLN LYS 2TMD 149 SEQRES 37 B 729 PRO MET THR ALA ASP ASP VAL LEU GLN TYR GLY ALA ASP 2TMD 150 SEQRES 38 B 729 LYS VAL ILE ILE ALA THR GLY ALA ARG TRP ASN THR ASP 2TMD 151 SEQRES 39 B 729 GLY THR ASN CYS LEU THR HIS ASP PRO ILE PRO GLY ALA 2TMD 152 SEQRES 40 B 729 ASP ALA SER LEU PRO ASP GLN LEU THR PRO GLU GLN VAL 2TMD 153 SEQRES 41 B 729 MET ASP GLY LYS LYS LYS ILE GLY LYS ARG VAL VAL ILE 2TMD 154 SEQRES 42 B 729 LEU ASN ALA ASP THR TYR PHE MET ALA PRO SER LEU ALA 2TMD 155 SEQRES 43 B 729 GLU LYS LEU ALA THR ALA GLY HIS GLU VAL THR ILE VAL 2TMD 156 SEQRES 44 B 729 SER GLY VAL HIS LEU ALA ASN TYR MET HIS PHE THR LEU 2TMD 157 SEQRES 45 B 729 GLU TYR PRO ASN MET MET ARG ARG LEU HIS GLU LEU HIS 2TMD 158 SEQRES 46 B 729 VAL GLU GLU LEU GLY ASP HIS PHE CYS SER ARG ILE GLU 2TMD 159 SEQRES 47 B 729 PRO GLY ARG MET GLU ILE TYR ASN ILE TRP GLY ASP GLY 2TMD 160 SEQRES 48 B 729 SER LYS ARG THR TYR ARG GLY PRO GLY VAL SER PRO ARG 2TMD 161 SEQRES 49 B 729 ASP ALA ASN THR SER HIS ARG TRP ILE GLU PHE ASP SER 2TMD 162 SEQRES 50 B 729 LEU VAL LEU VAL THR GLY ARG HIS SER GLU CYS THR LEU 2TMD 163 SEQRES 51 B 729 TRP ASN GLU LEU LYS ALA ARG GLU SER GLU TRP ALA GLU 2TMD 164 SEQRES 52 B 729 ASN ASP ILE LYS GLY ILE TYR LEU ILE GLY ASP ALA GLU 2TMD 165 SEQRES 53 B 729 ALA PRO ARG LEU ILE ALA ASP ALA THR PHE THR GLY HIS 2TMD 166 SEQRES 54 B 729 ARG VAL ALA ARG GLU ILE GLU GLU ALA ASN PRO GLN ILE 2TMD 167 SEQRES 55 B 729 ALA ILE PRO TYR LYS ARG GLU THR ILE ALA TRP GLY THR 2TMD 168 SEQRES 56 B 729 PRO HIS MET PRO GLY GLY ASN PHE LYS ILE GLU TYR LYS 2TMD 169 SEQRES 57 B 729 VAL 2TMD 170 FTNOTE 1 2TMD 171 FTNOTE 1 THR A 70 - HIS A 71 OMEGA = 17.29 2TMD 172 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2TMD 173 FTNOTE 2 2TMD 174 FTNOTE 2 THR B 70 - HIS B 71 OMEGA = 16.18 2TMD 175 FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2TMD 176 HET FS4 A 801 8 IRON/SULFUR CLUSTER 2TMD 177 HET FMN A 802 31 FLAVIN MONONUCLEOTIDE PROSTHETIC GROUP 2TMD 178 HET ADP A 803 27 ADENOSINE DIPHOSPHATE 2TMD 179 HET FS4 B 801 8 IRON/SULFUR CLUSTER 2TMD 180 HET FMN B 802 31 FLAVIN MONONUCLEOTIDE PROSTHETIC GROUP 2TMD 181 HET ADP B 803 27 ADENOSINE DIPHOSPHATE 2TMD 182 FORMUL 3 FS4 2(FE4 S4) 2TMD 183 FORMUL 4 FMN 2(C17 H21 N4 O9 P1) 2TMD 184 FORMUL 5 ADP 2(C10 H15 N5 O10 P2) 2TMD 185 FORMUL 6 HOH *581(H2 O1) 2TMD 186 HELIX 1 AA PRO A 4 PHE A 10 5 2TMD 187 HELIX 2 A1 PRO A 38 GLU A 50 1 2TMD 188 HELIX 3 A2 GLU A 80 LYS A 95 1 2TMD 189 HELIX 4 AU1 GLY A 108 HIS A 110 5 NOT IDENTIFIED 2TMD 190 HELIX 5 A3 LEU A 141 ALA A 161 1 2TMD 191 HELIX 6 AB LEU A 175 LEU A 180 1 2TMD 192 HELIX 7 A4 LEU A 195 VAL A 213 1 2TMD 193 HELIX 8 A5 ASP A 239 LEU A 250 1 2TMD 194 HELIX 9 AC GLU A 263 GLU A 266 5 2TMD 195 HELIX 10 A6 THR A 279 LYS A 287 1 2TMD 196 HELIX 11 A7 PRO A 303 LYS A 312 1 2TMD 197 HELIX 12 AD PRO A 323 ALA A 326 1 2TMD 198 HELIX 13 A8 LEU A 330 GLU A 335 1 2TMD 199 HELIX 14 AU2 TYR A 339 ILE A 342 5 NOT IDENTIFIED 2TMD 200 HELIX 15 AE VAL A 350 ILE A 357 1 2TMD 201 HELIX 16 AF GLU A 373 ARG A 376 1 2TMD 202 HELIX 17 A9 SER A 400 GLU A 410 1 2TMD 203 HELIX 18 AG LEU A 428 VAL A 431 1 2TMD 204 HELIX 19 A10 GLY A 438 LEU A 455 1 2TMD 205 HELIX 20 A11 ALA A 472 LEU A 476 1 2TMD 206 HELIX 21 A12 PRO A 517 ASP A 522 1 2TMD 207 HELIX 22 A13 MET A 541 THR A 551 1 2TMD 208 HELIX 23 AH TYR A 567 PHE A 570 1 2TMD 209 HELIX 24 A14 TYR A 574 GLU A 583 1 2TMD 210 HELIX 25 A15 THR A 649 ALA A 656 1 2TMD 211 HELIX 26 A16 ILE A 681 ARG A 693 1 2TMD 212 HELIX 27 BA PRO B 4 PHE B 10 5 2TMD 213 HELIX 28 B1 PRO B 38 GLU B 50 1 2TMD 214 HELIX 29 B2 GLU B 80 LYS B 95 1 2TMD 215 HELIX 30 BU1 GLY B 108 HIS B 110 5 NOT IDENTIFIED 2TMD 216 HELIX 31 B3 LEU B 141 ALA B 161 1 2TMD 217 HELIX 32 BB LEU B 175 LEU B 180 1 2TMD 218 HELIX 33 B4 LEU B 195 VAL B 213 1 2TMD 219 HELIX 34 B5 ASP B 239 LEU B 250 1 2TMD 220 HELIX 35 BC GLU B 263 GLU B 266 5 2TMD 221 HELIX 36 B6 THR B 279 LYS B 287 1 2TMD 222 HELIX 37 B7 PRO B 303 LYS B 312 1 2TMD 223 HELIX 38 BD PRO B 323 ALA B 326 1 2TMD 224 HELIX 39 B8 LEU B 330 GLU B 335 1 2TMD 225 HELIX 40 BU2 TYR B 339 ILE B 342 5 NOT IDENTIFIED 2TMD 226 HELIX 41 BE VAL B 350 ILE B 357 1 2TMD 227 HELIX 42 BF GLU B 373 ARG B 376 1 2TMD 228 HELIX 43 B9 SER B 400 GLU B 410 1 2TMD 229 HELIX 44 BG LEU B 428 VAL B 431 1 2TMD 230 HELIX 45 B10 GLY B 438 LEU B 455 1 2TMD 231 HELIX 46 B11 ALA B 472 LEU B 476 1 2TMD 232 HELIX 47 B12 PRO B 517 ASP B 522 1 2TMD 233 HELIX 48 B13 MET B 541 THR B 551 1 2TMD 234 HELIX 49 BH TYR B 567 PHE B 570 1 2TMD 235 HELIX 50 B14 TYR B 574 GLU B 583 1 2TMD 236 HELIX 51 B15 THR B 649 ALA B 656 1 2TMD 237 HELIX 52 B16 ILE B 681 ARG B 693 1 2TMD 238 SHEET 1 AA 9 PHE A 24 GLN A 26 0 2TMD 239 SHEET 2 AA 9 ALA A 55 SER A 62 1 2TMD 240 SHEET 3 AA 9 LEU A 99 TRP A 105 1 2TMD 241 SHEET 4 AA 9 ASP A 164 GLY A 170 1 2TMD 242 SHEET 5 AA 9 ALA A 218 ASP A 226 1 2TMD 243 SHEET 6 AA 9 MET A 253 ILE A 258 1 2TMD 244 SHEET 7 AA 9 VAL A 294 GLY A 296 1 2TMD 245 SHEET 8 AA 9 ILE A 318 CYS A 320 1 2TMD 246 SHEET 9 AA 9 PHE A 24 GLN A 26 1 2TMD 247 SHEET 1 BA 5 GLN A 462 ALA A 464 0 2TMD 248 SHEET 2 BA 5 THR A 414 THR A 418 1 2TMD 249 SHEET 3 BA 5 SER A 391 VAL A 395 1 2TMD 250 SHEET 4 BA 5 LYS A 482 ILE A 485 1 2TMD 251 SHEET 5 BA 5 GLY A 668 LEU A 671 1 2TMD 252 SHEET 1 CA 5 GLN A 514 LEU A 515 0 2TMD 253 SHEET 2 CA 5 SER A 637 VAL A 641 1 2TMD 254 SHEET 3 CA 5 ARG A 530 ASN A 535 1 2TMD 255 SHEET 4 CA 5 GLU A 555 SER A 560 1 2TMD 256 SHEET 5 CA 5 GLU A 587 GLY A 590 1 2TMD 257 SHEET 1 DA 3 HIS A 592 GLU A 598 0 2TMD 258 SHEET 2 DA 3 ARG A 601 ASN A 606 -1 2TMD 259 SHEET 3 DA 3 ARG A 631 GLU A 634 -1 2TMD 260 SHEET 1 AB 9 PHE B 24 GLN B 26 0 2TMD 261 SHEET 2 AB 9 ALA B 55 SER B 62 1 2TMD 262 SHEET 3 AB 9 LEU B 99 TRP B 105 1 2TMD 263 SHEET 4 AB 9 ASP B 164 GLY B 170 1 2TMD 264 SHEET 5 AB 9 ALA B 218 ASP B 226 1 2TMD 265 SHEET 6 AB 9 MET B 253 ILE B 258 1 2TMD 266 SHEET 7 AB 9 VAL B 294 GLY B 296 1 2TMD 267 SHEET 8 AB 9 ILE B 318 CYS B 320 1 2TMD 268 SHEET 9 AB 9 PHE B 24 GLN B 26 1 2TMD 269 SHEET 1 BB 5 GLN B 462 ALA B 464 0 2TMD 270 SHEET 2 BB 5 THR B 414 THR B 418 1 2TMD 271 SHEET 3 BB 5 SER B 391 VAL B 395 1 2TMD 272 SHEET 4 BB 5 LYS B 482 ILE B 485 1 2TMD 273 SHEET 5 BB 5 GLY B 668 LEU B 671 1 2TMD 274 SHEET 1 CB 5 GLN B 514 LEU B 515 0 2TMD 275 SHEET 2 CB 5 SER B 637 VAL B 641 1 2TMD 276 SHEET 3 CB 5 ARG B 530 ASN B 535 1 2TMD 277 SHEET 4 CB 5 GLU B 555 SER B 560 1 2TMD 278 SHEET 5 CB 5 GLU B 587 GLY B 590 1 2TMD 279 SHEET 1 DB 3 HIS B 592 GLU B 598 0 2TMD 280 SHEET 2 DB 3 ARG B 601 ASN B 606 -1 2TMD 281 SHEET 3 DB 3 ARG B 631 GLU B 634 -1 2TMD 282 CRYST1 147.750 71.950 83.820 90.00 97.69 90.00 P 21 2 2TMD 283 ORIGX1 1.000000 0.000000 0.000000 0.00000 2TMD 284 ORIGX2 0.000000 1.000000 0.000000 0.00000 2TMD 285 ORIGX3 0.000000 0.000000 1.000000 0.00000 2TMD 286 SCALE1 0.006768 0.000000 0.000914 0.00000 2TMD 287 SCALE2 0.000000 0.013899 0.000000 0.00000 2TMD 288 SCALE3 0.000000 0.000000 0.012039 0.00000 2TMD 289 MTRIX1 1 -0.971338 0.217797 0.095224 66.47540 2TMD 290 MTRIX2 1 0.210859 0.604543 0.768158 -15.99959 2TMD 291 MTRIX3 1 0.109736 0.766219 -0.633140 14.45649 2TMD 292