HEADER OXIDOREDUCTASE 19-APR-95 1BHS TITLE HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: 17BETA-HYDROXYSTEROID DEHYDROGENASE; COMPND 3 CHAIN: NULL; COMPND 4 SYNONYM: TYPE I 17BETA-HYDROXYSTEROID DEHYDROGENASE; COMPND 5 EC: 1.1.1.62 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN KEYWDS SHORT-CHAIN DEHYDROGENASE, STEROID DEHYDROGENASE, ESTROGEN, KEYWDS 2 HUMAN TYPE I 17BETA-HSD, HUMAN PLACENTAL 17BETA-HSD, KEYWDS 3 OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR D.GHOSH REVDAT 1 07-DEC-96 1BHS 0 JRNL AUTH D.GHOSH,V.Z.PLETNEV,D.W.ZHU,Z.WAWRZAK,W.L.DUAX, JRNL AUTH 2 W.PANGBORN,F.LABRIE,S.X.LIN JRNL TITL STRUCTURE OF HUMAN ESTROGENIC 17 JRNL TITL 2 BETA-HYDROXYSTEROID DEHYDROGENASE AT 2.20 A JRNL TITL 3 RESOLUTION JRNL REF STRUCTURE (LONDON) V. 3 503 1995 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.W.ZHU,X.LEE,R.BRETON,D.GHOSH,W.PANGBORN,W.L.DAUX, REMARK 1 AUTH 2 S.X.LIN REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION REMARK 1 TITL 2 ANALYSIS OF THE COMPLEX OF HUMAN PLACENTAL REMARK 1 TITL 3 17 BETA-HYDROXYSTEROID DEHYDROGENASE WITH NADP+ REMARK 1 REF J.MOL.BIOL. V. 234 242 1993 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 13474 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2178 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 49 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39. REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20-0.25 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 PLANAR ANGLE RESTRAINT: 1.46 DEGREES REMARK 4 REMARK 4 1BHS COMPLIES WITH FORMAT V. 2.1, 25-OCT-1996 REMARK 6 REMARK 6 THE REGION 192 - 200 IS VERY POORLY DEFINED IN THE ELECTRON REMARK 6 DENSITY MAPS AND WAS MODELED STEREOCHEMICALLY. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-NOV-1993 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : R-AXIS IIC REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : RIGAKU REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14079 REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 81. REMARK 200 DATA REDUNDANCY : 3.1 REMARK 200 R MERGE (I) : 0.064 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.0 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-X,1/2+Y,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 61.78178 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.52455 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.78178 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.52455 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CAT REMARK 800 SITE_DESCRIPTION: THE TYR-LYS-SER CATALYTIC TRIAD. REMARK 999 REMARK 999 SEQUENCE REMARK 999 1BHS SWS P14061 285 - 327 NOT IN ATOMS LIST REMARK 999 REMARK 999 REFERENCE REMARK 999 REFERENCE: LUU-THE V ET AL.(1989) MOL. ENDOCRINOL. 3, REMARK 999 1301-1309. DBREF 1BHS 1 284 SWS P14061 DHB1_HUMAN 1 284 SEQRES 1 327 ALA ARG THR VAL VAL LEU ILE THR GLY CYS SER SER GLY SEQRES 2 327 ILE GLY LEU HIS LEU ALA VAL ARG LEU ALA SER ASP PRO SEQRES 3 327 SER GLN SER PHE LYS VAL TYR ALA THR LEU ARG ASP LEU SEQRES 4 327 LYS THR GLN GLY ARG LEU TRP GLU ALA ALA ARG ALA LEU SEQRES 5 327 ALA CYS PRO PRO GLY SER LEU GLU THR LEU GLN LEU ASP SEQRES 6 327 VAL ARG ASP SER LYS SER VAL ALA ALA ALA ARG GLU ARG SEQRES 7 327 VAL THR GLU GLY ARG VAL ASP VAL LEU VAL CYS ASN ALA SEQRES 8 327 GLY LEU GLY LEU LEU GLY PRO LEU GLU ALA LEU GLY GLU SEQRES 9 327 ASP ALA VAL ALA SER VAL LEU ASP VAL ASN VAL VAL GLY SEQRES 10 327 THR VAL ARG MET LEU GLN ALA PHE LEU PRO ASP MET LYS SEQRES 11 327 ARG ARG GLY SER GLY ARG VAL LEU VAL THR GLY SER VAL SEQRES 12 327 GLY GLY LEU MET GLY LEU PRO PHE ASN ASP VAL TYR CYS SEQRES 13 327 ALA SER LYS PHE ALA LEU GLU GLY LEU CYS GLU SER LEU SEQRES 14 327 ALA VAL LEU LEU LEU PRO PHE GLY VAL HIS LEU SER LEU SEQRES 15 327 ILE GLU CYS GLY PRO VAL HIS THR ALA PHE MET GLU LYS SEQRES 16 327 VAL LEU GLY SER PRO GLU GLU VAL LEU ASP ARG THR ASP SEQRES 17 327 ILE HIS THR PHE HIS ARG PHE TYR GLN TYR LEU ALA HIS SEQRES 18 327 SER LYS GLN VAL PHE ARG GLU ALA ALA GLN ASN PRO GLU SEQRES 19 327 GLU VAL ALA GLU VAL PHE LEU THR ALA LEU ARG ALA PRO SEQRES 20 327 LYS PRO THR LEU ARG TYR PHE THR THR GLU ARG PHE LEU SEQRES 21 327 PRO LEU LEU ARG MET ARG LEU ASP ASP PRO SER GLY SER SEQRES 22 327 ASN TYR VAL THR ALA MET HIS ARG GLU VAL PHE GLY ASP SEQRES 23 327 VAL PRO ALA LYS ALA GLU ALA GLY ALA GLU ALA GLY GLY SEQRES 24 327 GLY ALA GLY PRO GLY ALA GLU ASP GLU ALA GLY ARG SER SEQRES 25 327 ALA VAL GLY ASP PRO GLU LEU GLY ASP PRO PRO ALA ALA SEQRES 26 327 PRO GLN FORMUL 2 HOH *49(H2 O1) HELIX 1 1 GLY 13 ALA 23 1 11 HELIX 2 2 LEU 39 THR 41 5 3 HELIX 3 3 GLY 43 ALA 51 1 9 HELIX 4 4 SER 69 ARG 78 1 10 HELIX 5 5 LEU 99 ALA 101 5 3 HELIX 6 6 GLU 104 ASN 114 1 11 HELIX 7 7 VAL 116 ARG 132 1 17 HELIX 8 8 VAL 143 GLY 145 5 3 HELIX 9 9 ASP 153 PHE 176 1 24 HELIX 10 10 ALA 191 GLU 194 1 4 HELIX 11 11 GLU 201 ARG 206 1 6 HELIX 12 12 ILE 209 ALA 229 1 21 HELIX 13 13 PRO 233 ARG 245 1 13 HELIX 14 14 LEU 260 ASP 268 1 9 HELIX 15 15 SER 273 GLU 282 1 10 SHEET 1 A 7 ARG 252 PHE 254 0 SHEET 2 A 7 VAL 178 GLU 184 1 N LEU 182 O TYR 253 SHEET 3 A 7 GLY 135 THR 140 1 N GLY 135 O HIS 179 SHEET 4 A 7 VAL 86 CYS 89 1 N LEU 87 O ARG 136 SHEET 5 A 7 THR 3 ILE 7 1 N LEU 6 O VAL 86 SHEET 6 A 7 PHE 30 LEU 36 1 N LYS 31 O THR 3 SHEET 7 A 7 LEU 59 GLN 63 1 N GLU 60 O VAL 32 SITE 1 CAT 3 TYR 155 LYS 159 SER 142 CRYST1 123.560 45.050 61.330 90.00 99.02 90.00 C 1 2 1 4 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 0.008093 0.000000 0.001285 0.00000 SCALE2 0.000000 0.022198 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016509 0.00000 ATOM 991 N GLY 135 16.015 4.028 19.781 1.00 29.12 N ATOM 992 CA GLY 135 16.226 3.261 18.572 1.00 27.21 C ATOM 993 C GLY 135 15.902 4.176 17.419 1.00 25.67 C ATOM 994 O GLY 135 15.261 5.220 17.607 1.00 25.98 O ATOM 995 N ARG 136 16.418 3.848 16.245 1.00 23.94 N ATOM 996 CA ARG 136 16.151 4.653 15.071 1.00 26.70 C ATOM 997 C ARG 136 15.848 3.696 13.956 1.00 25.01 C ATOM 998 O ARG 136 16.428 2.622 13.887 1.00 27.79 O ATOM 999 CB ARG 136 17.331 5.559 14.722 1.00 30.80 C ATOM 1000 CG ARG 136 16.974 6.655 13.706 1.00 40.64 C ATOM 1001 CD ARG 136 17.687 7.973 14.025 1.00 52.23 C ATOM 1002 NE ARG 136 17.718 8.241 15.472 1.00 58.65 N ATOM 1003 CZ ARG 136 18.291 9.302 16.044 1.00 57.69 C ATOM 1004 NH1 ARG 136 18.855 10.240 15.302 1.00 53.71 N ATOM 1005 NH2 ARG 136 18.270 9.441 17.365 1.00 61.63 N ATOM 1006 N VAL 137 14.866 4.049 13.141 1.00 27.89 N ATOM 1007 CA VAL 137 14.439 3.222 12.029 1.00 25.55 C ATOM 1008 C VAL 137 14.458 4.128 10.840 1.00 22.92 C ATOM 1009 O VAL 137 13.927 5.228 10.901 1.00 24.48 O ATOM 1010 CB VAL 137 12.993 2.734 12.220 1.00 28.32 C ATOM 1011 CG1 VAL 137 12.519 1.959 10.988 1.00 24.68 C ATOM 1012 CG2 VAL 137 12.893 1.883 13.471 1.00 30.53 C ATOM 1013 N LEU 138 15.144 3.714 9.791 1.00 22.35 N ATOM 1014 CA LEU 138 15.189 4.511 8.585 1.00 21.76 C ATOM 1015 C LEU 138 14.542 3.669 7.507 1.00 15.69 C ATOM 1016 O LEU 138 14.864 2.503 7.353 1.00 19.89 O ATOM 1017 CB LEU 138 16.625 4.857 8.197 1.00 25.03 C ATOM 1018 CG LEU 138 17.429 5.825 9.057 1.00 24.97 C ATOM 1019 CD1 LEU 138 18.747 6.010 8.372 1.00 22.47 C ATOM 1020 CD2 LEU 138 16.735 7.162 9.190 1.00 19.73 C ATOM 1021 N VAL 139 13.620 4.260 6.767 1.00 19.20 N ATOM 1022 CA VAL 139 12.910 3.536 5.742 1.00 18.21 C ATOM 1023 C VAL 139 13.239 4.188 4.428 1.00 21.81 C ATOM 1024 O VAL 139 13.189 5.411 4.316 1.00 22.39 O ATOM 1025 CB VAL 139 11.385 3.591 5.986 1.00 21.07 C ATOM 1026 CG1 VAL 139 10.661 2.639 5.048 1.00 16.69 C ATOM 1027 CG2 VAL 139 11.069 3.240 7.434 1.00 18.48 C ATOM 1028 N THR 140 13.643 3.374 3.458 1.00 21.20 N ATOM 1029 CA THR 140 13.978 3.863 2.140 1.00 17.97 C ATOM 1030 C THR 140 12.677 4.153 1.392 1.00 23.75 C ATOM 1031 O THR 140 11.892 3.242 1.101 1.00 27.70 O ATOM 1032 CB THR 140 14.835 2.818 1.367 1.00 13.14 C ATOM 1033 OG1 THR 140 16.044 2.582 2.087 1.00 21.74 O ATOM 1034 CG2 THR 140 15.198 3.300 -0.029 1.00 11.87 C ATOM 1299 N VAL 178 11.849 6.438 20.296 1.00 37.56 N ATOM 1300 CA VAL 178 12.414 5.798 19.116 1.00 37.04 C ATOM 1301 C VAL 178 12.010 6.615 17.881 1.00 37.61 C ATOM 1302 O VAL 178 10.894 7.116 17.822 1.00 36.82 O ATOM 1303 CB VAL 178 12.096 4.269 19.040 1.00 33.11 C ATOM 1304 CG1 VAL 178 11.480 3.767 20.336 1.00 28.26 C ATOM 1305 CG2 VAL 178 11.306 3.925 17.831 1.00 30.40 C ATOM 1306 N HIS 179 12.958 6.832 16.958 1.00 40.42 N ATOM 1307 CA HIS 179 12.731 7.659 15.755 1.00 39.71 C ATOM 1308 C HIS 179 12.633 6.923 14.424 1.00 33.18 C ATOM 1309 O HIS 179 13.491 6.134 14.090 1.00 37.42 O ATOM 1310 CB HIS 179 13.813 8.730 15.641 1.00 39.51 C ATOM 1311 CG HIS 179 14.094 9.437 16.928 1.00 46.80 C ATOM 1312 ND1 HIS 179 13.369 10.531 17.355 1.00 45.45 N ATOM 1313 CD2 HIS 179 15.029 9.207 17.883 1.00 47.75 C ATOM 1314 CE1 HIS 179 13.846 10.944 18.515 1.00 46.52 C ATOM 1315 NE2 HIS 179 14.853 10.158 18.857 1.00 47.72 N ATOM 1316 N LEU 180 11.622 7.278 13.640 1.00 31.10 N ATOM 1317 CA LEU 180 11.341 6.674 12.345 1.00 26.01 C ATOM 1318 C LEU 180 11.463 7.783 11.311 1.00 29.13 C ATOM 1319 O LEU 180 10.878 8.855 11.493 1.00 29.26 O ATOM 1320 CB LEU 180 9.899 6.179 12.354 1.00 29.93 C ATOM 1321 CG LEU 180 9.202 5.305 11.311 1.00 35.00 C ATOM 1322 CD1 LEU 180 9.702 5.597 9.922 1.00 36.80 C ATOM 1323 CD2 LEU 180 9.391 3.848 11.654 1.00 38.35 C ATOM 1324 N SER 181 12.231 7.538 10.249 1.00 26.89 N ATOM 1325 CA SER 181 12.405 8.505 9.157 1.00 22.36 C ATOM 1326 C SER 181 12.339 7.785 7.815 1.00 23.24 C ATOM 1327 O SER 181 12.727 6.621 7.697 1.00 24.53 O ATOM 1328 CB SER 181 13.752 9.241 9.235 1.00 19.64 C ATOM 1329 OG SER 181 13.784 10.169 10.293 1.00 20.87 O ATOM 1330 N LEU 182 11.797 8.483 6.825 1.00 22.71 N ATOM 1331 CA LEU 182 11.682 8.014 5.460 1.00 19.15 C ATOM 1332 C LEU 182 12.682 8.882 4.683 1.00 19.80 C ATOM 1333 O LEU 182 12.717 10.108 4.865 1.00 19.50 O ATOM 1334 CB LEU 182 10.265 8.293 4.940 1.00 14.70 C ATOM 1335 CG LEU 182 9.187 7.366 5.481 1.00 15.99 C ATOM 1336 CD1 LEU 182 7.898 8.106 5.619 1.00 9.14 C ATOM 1337 CD2 LEU 182 9.036 6.203 4.543 1.00 18.04 C ATOM 1338 N ILE 183 13.553 8.253 3.898 1.00 19.56 N ATOM 1339 CA ILE 183 14.512 9.001 3.069 1.00 23.20 C ATOM 1340 C ILE 183 13.946 8.924 1.652 1.00 21.26 C ATOM 1341 O ILE 183 13.919 7.860 1.034 1.00 22.64 O ATOM 1342 CB ILE 183 15.950 8.404 3.121 1.00 21.57 C ATOM 1343 CG1 ILE 183 16.413 8.246 4.578 1.00 23.31 C ATOM 1344 CG2 ILE 183 16.908 9.300 2.376 1.00 15.11 C ATOM 1345 CD1 ILE 183 16.503 9.533 5.363 1.00 26.10 C ATOM 1346 N GLU 184 13.395 10.037 1.190 1.00 21.68 N ATOM 1347 CA GLU 184 12.770 10.095 -0.120 1.00 21.35 C ATOM 1348 C GLU 184 13.761 10.215 -1.251 1.00 21.80 C ATOM 1349 O GLU 184 14.227 11.308 -1.557 1.00 22.95 O ATOM 1350 CB GLU 184 11.762 11.256 -0.189 1.00 26.03 C ATOM 1351 CG GLU 184 10.774 11.347 0.992 1.00 25.53 C ATOM 1352 CD GLU 184 9.790 10.172 1.085 1.00 28.33 C ATOM 1353 OE1 GLU 184 9.948 9.185 0.341 1.00 26.78 O ATOM 1354 OE2 GLU 184 8.853 10.234 1.915 1.00 25.04 O MASTER 201 0 0 15 7 0 1 6 2227 1 0 26 END .