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HEADER HYDROLASE 21-APR-23 8OTU
TITLE THE CRYSTAL STRUCTURE OF PET44, A PETASE ENZYME FROM ALKALILIMNICOLA
TITLE 2 EHRLICHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALKALILIMNICOLA EHRLICHII;
SOURCE 3 ORGANISM_TAXID: 351052;
SOURCE 4 GENE: CAL65_11960;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PETASE, PET, ENZYME, HYDROLASE, ESTERASE, PLASTIC, DEGRADATION,
KEYWDS 2 BIOTECH, ENZYME EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.COSTANZI,V.APPLEGATE,S.H.J.SMITS
REVDAT 1 06-NOV-24 8OTU 0
JRNL AUTH E.COSTANZI,V.APPLEGATE,S.H.J.SMITS
JRNL TITL THE CRYSTAL STRUCTURE OF PET44, A PETASE ENZYME FROM
JRNL TITL 2 ALKALILIMNICOLA EHRLICHII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 100364
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.150
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5036
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 50.3100 - 4.3500 0.99 3465 173 0.1648 0.1688
REMARK 3 2 4.3500 - 3.4500 1.00 3390 180 0.1261 0.1314
REMARK 3 3 3.4500 - 3.0200 0.99 3326 178 0.1221 0.1630
REMARK 3 4 3.0200 - 2.7400 0.99 3328 173 0.1181 0.1339
REMARK 3 5 2.7400 - 2.5400 0.99 3321 170 0.1162 0.1473
REMARK 3 6 2.5400 - 2.3900 0.99 3311 137 0.1143 0.1358
REMARK 3 7 2.3900 - 2.2700 0.99 3306 175 0.1174 0.1360
REMARK 3 8 2.2700 - 2.1800 0.99 3265 186 0.1202 0.1403
REMARK 3 9 2.1800 - 2.0900 0.99 3319 152 0.1184 0.1187
REMARK 3 10 2.0900 - 2.0200 0.99 3283 171 0.1230 0.1340
REMARK 3 11 2.0200 - 1.9600 0.98 3234 195 0.1234 0.1408
REMARK 3 12 1.9600 - 1.9000 0.98 3243 170 0.1274 0.1536
REMARK 3 13 1.9000 - 1.8500 0.98 3295 154 0.1247 0.1293
REMARK 3 14 1.8500 - 1.8000 0.98 3208 191 0.1244 0.1409
REMARK 3 15 1.8000 - 1.7600 0.98 3236 173 0.1251 0.1616
REMARK 3 16 1.7600 - 1.7300 0.98 3240 173 0.1268 0.1471
REMARK 3 17 1.7300 - 1.6900 0.98 3206 171 0.1313 0.1630
REMARK 3 18 1.6900 - 1.6600 0.97 3249 165 0.1336 0.1301
REMARK 3 19 1.6600 - 1.6300 0.97 3208 167 0.1463 0.1697
REMARK 3 20 1.6300 - 1.6000 0.97 3238 174 0.1493 0.1534
REMARK 3 21 1.6000 - 1.5800 0.97 3161 171 0.1480 0.1706
REMARK 3 22 1.5800 - 1.5500 0.97 3287 138 0.1494 0.1583
REMARK 3 23 1.5500 - 1.5300 0.97 3196 163 0.1515 0.2024
REMARK 3 24 1.5300 - 1.5100 0.97 3177 182 0.1529 0.2090
REMARK 3 25 1.5100 - 1.4900 0.96 3154 178 0.1594 0.1951
REMARK 3 26 1.4900 - 1.4700 0.96 3140 177 0.1643 0.1751
REMARK 3 27 1.4700 - 1.4500 0.94 3069 192 0.1755 0.2247
REMARK 3 28 1.4500 - 1.4300 0.93 3061 164 0.1953 0.1918
REMARK 3 29 1.4300 - 1.4200 0.78 2600 146 0.2377 0.2528
REMARK 3 30 1.4200 - 1.4000 0.56 1812 97 0.2856 0.2859
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.118
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.843
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.37
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 4312
REMARK 3 ANGLE : 1.157 5834
REMARK 3 CHIRALITY : 0.086 609
REMARK 3 PLANARITY : 0.012 778
REMARK 3 DIHEDRAL : 12.335 1555
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4215 -13.5762 37.4458
REMARK 3 T TENSOR
REMARK 3 T11: 0.2151 T22: 0.1527
REMARK 3 T33: 0.1858 T12: 0.0007
REMARK 3 T13: 0.0041 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 0.1070 L22: 0.1382
REMARK 3 L33: 0.2503 L12: 0.0049
REMARK 3 L13: -0.0473 L23: -0.0566
REMARK 3 S TENSOR
REMARK 3 S11: 0.1117 S12: -0.1995 S13: 0.1894
REMARK 3 S21: 0.1016 S22: -0.0846 S23: -0.0653
REMARK 3 S31: -0.1259 S32: 0.0588 S33: -0.0018
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1080 -33.2981 35.6079
REMARK 3 T TENSOR
REMARK 3 T11: 0.2522 T22: 0.1703
REMARK 3 T33: 0.1854 T12: -0.0186
REMARK 3 T13: -0.0016 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.3804 L22: 0.2391
REMARK 3 L33: 0.2701 L12: 0.0821
REMARK 3 L13: 0.1226 L23: -0.0396
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.1537 S13: -0.1583
REMARK 3 S21: 0.2641 S22: -0.0839 S23: 0.0029
REMARK 3 S31: 0.2161 S32: -0.2695 S33: 0.0046
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1385 -29.3907 23.2295
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.1567
REMARK 3 T33: 0.1380 T12: 0.0208
REMARK 3 T13: -0.0060 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 1.1095 L22: 0.6441
REMARK 3 L33: 0.7920 L12: 0.1890
REMARK 3 L13: -0.2502 L23: -0.0568
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: 0.1541 S13: -0.0674
REMARK 3 S21: 0.0054 S22: -0.0419 S23: 0.0013
REMARK 3 S31: 0.0952 S32: -0.1620 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5199 -20.4751 12.2120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1672 T22: 0.2533
REMARK 3 T33: 0.1739 T12: 0.0545
REMARK 3 T13: 0.0210 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 0.0978 L22: 0.1735
REMARK 3 L33: 0.0949 L12: 0.0368
REMARK 3 L13: 0.0975 L23: -0.0355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: 0.4004 S13: 0.2483
REMARK 3 S21: -0.0441 S22: -0.0512 S23: -0.1142
REMARK 3 S31: -0.0213 S32: -0.0538 S33: -0.0029
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1652 -16.9612 19.8568
REMARK 3 T TENSOR
REMARK 3 T11: 0.1704 T22: 0.1661
REMARK 3 T33: 0.1724 T12: 0.0530
REMARK 3 T13: 0.0081 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.4443 L22: 0.2956
REMARK 3 L33: 0.3037 L12: 0.3350
REMARK 3 L13: -0.1531 L23: 0.0554
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: 0.1264 S13: 0.1570
REMARK 3 S21: 0.0146 S22: -0.0391 S23: -0.0740
REMARK 3 S31: -0.0783 S32: -0.0145 S33: 0.0195
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 276 THROUGH 305 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1342 -7.7426 22.8208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2784 T22: 0.1686
REMARK 3 T33: 0.2918 T12: 0.0478
REMARK 3 T13: 0.0497 T23: 0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 0.0734 L22: 0.0556
REMARK 3 L33: 0.2088 L12: -0.0596
REMARK 3 L13: -0.0663 L23: 0.1508
REMARK 3 S TENSOR
REMARK 3 S11: 0.2597 S12: 0.1507 S13: 0.4054
REMARK 3 S21: 0.0245 S22: -0.0721 S23: -0.0244
REMARK 3 S31: -0.3899 S32: -0.0782 S33: -0.0862
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 62 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.6141 -4.1737 15.1043
REMARK 3 T TENSOR
REMARK 3 T11: 0.1806 T22: 0.2266
REMARK 3 T33: 0.1997 T12: 0.0321
REMARK 3 T13: 0.0150 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.1642 L22: 0.1103
REMARK 3 L33: 0.1565 L12: -0.1205
REMARK 3 L13: 0.1213 L23: 0.0472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: 0.0804 S13: 0.1184
REMARK 3 S21: -0.0037 S22: 0.0434 S23: 0.0844
REMARK 3 S31: -0.0480 S32: -0.0966 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 63 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.6947 -14.0848 1.7886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2007 T22: 0.2908
REMARK 3 T33: 0.1844 T12: 0.0428
REMARK 3 T13: -0.0190 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.1761 L22: 0.3525
REMARK 3 L33: 0.2862 L12: 0.1673
REMARK 3 L13: -0.0117 L23: -0.1190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0240 S12: 0.3886 S13: 0.0034
REMARK 3 S21: -0.0802 S22: -0.0250 S23: 0.0882
REMARK 3 S31: 0.0409 S32: 0.0551 S33: 0.0334
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.1135 -19.3275 9.3454
REMARK 3 T TENSOR
REMARK 3 T11: 0.1766 T22: 0.2097
REMARK 3 T33: 0.1999 T12: 0.0550
REMARK 3 T13: -0.0138 T23: -0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 0.3541 L22: 0.3539
REMARK 3 L33: 0.5070 L12: 0.1191
REMARK 3 L13: 0.2831 L23: -0.1430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: 0.2287 S13: -0.1190
REMARK 3 S21: -0.0295 S22: -0.0409 S23: -0.0116
REMARK 3 S31: 0.1047 S32: 0.0929 S33: -0.0007
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 165 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8018 -6.1272 -1.4598
REMARK 3 T TENSOR
REMARK 3 T11: 0.1935 T22: 0.3274
REMARK 3 T33: 0.2029 T12: 0.0033
REMARK 3 T13: 0.0135 T23: 0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.0157 L22: 0.0141
REMARK 3 L33: 0.0288 L12: -0.0143
REMARK 3 L13: 0.0271 L23: -0.0193
REMARK 3 S TENSOR
REMARK 3 S11: 0.0794 S12: 0.2533 S13: 0.0348
REMARK 3 S21: -0.0248 S22: 0.0104 S23: -0.0752
REMARK 3 S31: -0.0752 S32: 0.1742 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 166 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.9432 -15.5431 19.6377
REMARK 3 T TENSOR
REMARK 3 T11: 0.1722 T22: 0.2277
REMARK 3 T33: 0.2239 T12: 0.0539
REMARK 3 T13: -0.0225 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.2220 L22: 0.1351
REMARK 3 L33: 0.1430 L12: -0.2292
REMARK 3 L13: 0.0602 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: 0.0397 S13: -0.0040
REMARK 3 S21: -0.0005 S22: 0.0144 S23: -0.1309
REMARK 3 S31: 0.0584 S32: 0.2387 S33: 0.0125
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 209 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.2245 -20.7739 28.2791
REMARK 3 T TENSOR
REMARK 3 T11: 0.2195 T22: 0.2050
REMARK 3 T33: 0.2160 T12: 0.0689
REMARK 3 T13: -0.0012 T23: 0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 0.1573 L22: 0.0804
REMARK 3 L33: 0.1396 L12: -0.0042
REMARK 3 L13: 0.0423 L23: 0.0990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0591 S12: -0.1668 S13: -0.0553
REMARK 3 S21: 0.0970 S22: 0.0467 S23: -0.1068
REMARK 3 S31: 0.0868 S32: 0.1237 S33: 0.0181
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 227 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5822 -12.0013 29.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.2164 T22: 0.2595
REMARK 3 T33: 0.2260 T12: 0.0567
REMARK 3 T13: -0.0261 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.0695 L22: 0.0343
REMARK 3 L33: 0.0738 L12: -0.0491
REMARK 3 L13: 0.0149 L23: 0.0297
REMARK 3 S TENSOR
REMARK 3 S11: -0.1118 S12: -0.4267 S13: 0.0297
REMARK 3 S21: 0.2436 S22: 0.1180 S23: -0.0675
REMARK 3 S31: -0.0013 S32: 0.0741 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 246 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.7658 -24.2060 24.5215
REMARK 3 T TENSOR
REMARK 3 T11: 0.2547 T22: 0.2032
REMARK 3 T33: 0.3037 T12: 0.0120
REMARK 3 T13: 0.0171 T23: 0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 0.0109 L22: 0.0293
REMARK 3 L33: 0.0050 L12: 0.0200
REMARK 3 L13: -0.0149 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: -0.1002 S12: -0.1097 S13: -0.4602
REMARK 3 S21: 0.1777 S22: 0.0936 S23: 0.2553
REMARK 3 S31: 0.2793 S32: -0.0554 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 260 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8904 -8.6176 20.5009
REMARK 3 T TENSOR
REMARK 3 T11: 0.1694 T22: 0.1922
REMARK 3 T33: 0.1912 T12: 0.0321
REMARK 3 T13: 0.0007 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.0803 L22: 0.0765
REMARK 3 L33: 0.0512 L12: -0.0435
REMARK 3 L13: 0.0713 L23: -0.0065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0054 S12: -0.0165 S13: -0.0513
REMARK 3 S21: 0.0818 S22: 0.0730 S23: 0.0135
REMARK 3 S31: 0.0153 S32: -0.0197 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 276 THROUGH 307 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.1462 -5.1742 28.7144
REMARK 3 T TENSOR
REMARK 3 T11: 0.2242 T22: 0.2395
REMARK 3 T33: 0.1892 T12: 0.0627
REMARK 3 T13: -0.0081 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.3003 L22: 0.2029
REMARK 3 L33: 0.1576 L12: -0.2805
REMARK 3 L13: 0.0343 L23: -0.0154
REMARK 3 S TENSOR
REMARK 3 S11: -0.1153 S12: -0.1485 S13: 0.0796
REMARK 3 S21: 0.1625 S22: 0.1581 S23: -0.0511
REMARK 3 S31: -0.1113 S32: -0.1025 S33: 0.0004
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8OTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1292129515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100380
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 57.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 10% (W/V) PEG
REMARK 280 8000, 10% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 285K
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 70.56650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.83000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.56650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.83000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 597 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ILE A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 ARG A 7
REMARK 465 LYS A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 PHE A 13
REMARK 465 ALA A 14
REMARK 465 PHE A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 MET A 19
REMARK 465 LEU A 20
REMARK 465 LEU A 21
REMARK 465 SER A 22
REMARK 465 THR A 23
REMARK 465 SER A 24
REMARK 465 VAL A 25
REMARK 465 TRP A 26
REMARK 465 SER A 27
REMARK 465 MET A 28
REMARK 465 ASN A 29
REMARK 465 PRO A 30
REMARK 465 GLY A 31
REMARK 465 ASP A 32
REMARK 465 VAL A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 35
REMARK 465 THR A 36
REMARK 465 CYS A 37
REMARK 465 GLU A 38
REMARK 465 GLY A 39
REMARK 465 ASP A 40
REMARK 465 CYS A 41
REMARK 465 VAL A 306
REMARK 465 ASP A 307
REMARK 465 LYS A 308
REMARK 465 LEU A 309
REMARK 465 ALA A 310
REMARK 465 ALA A 311
REMARK 465 ALA A 312
REMARK 465 LEU A 313
REMARK 465 GLU A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ILE B 4
REMARK 465 ILE B 5
REMARK 465 LYS B 6
REMARK 465 ARG B 7
REMARK 465 LYS B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 PHE B 13
REMARK 465 ALA B 14
REMARK 465 PHE B 15
REMARK 465 SER B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 MET B 19
REMARK 465 LEU B 20
REMARK 465 LEU B 21
REMARK 465 SER B 22
REMARK 465 THR B 23
REMARK 465 SER B 24
REMARK 465 VAL B 25
REMARK 465 TRP B 26
REMARK 465 SER B 27
REMARK 465 MET B 28
REMARK 465 ASN B 29
REMARK 465 PRO B 30
REMARK 465 GLY B 31
REMARK 465 ASP B 32
REMARK 465 VAL B 33
REMARK 465 PRO B 34
REMARK 465 ASP B 35
REMARK 465 THR B 36
REMARK 465 CYS B 37
REMARK 465 GLU B 38
REMARK 465 GLY B 39
REMARK 465 ASP B 40
REMARK 465 CYS B 41
REMARK 465 LYS B 308
REMARK 465 LEU B 309
REMARK 465 ALA B 310
REMARK 465 ALA B 311
REMARK 465 ALA B 312
REMARK 465 LEU B 313
REMARK 465 GLU B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
REMARK 465 HIS B 319
REMARK 465 HIS B 320
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 SER A 172 -125.67 59.96
REMARK 500 HIS A 226 -91.12 -129.09
REMARK 500 SER B 172 -124.24 63.52
REMARK 500 HIS B 226 -87.09 -129.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 70 O
REMARK 620 2 VAL A 72 O 99.0
REMARK 620 3 PHE A 75 O 108.8 87.4
REMARK 620 4 EDO A 415 O2 94.7 162.2 77.4
REMARK 620 5 HOH A 585 O 163.9 92.1 83.2 77.2
REMARK 620 6 HOH A 675 O 91.8 83.4 158.5 107.6 77.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 153 O
REMARK 620 2 GLU B 291 O 61.8
REMARK 620 3 ASP B 293 O 57.7 4.5
REMARK 620 4 ILE B 296 O 58.1 3.7 1.6
REMARK 620 5 HOH B 605 O 58.8 5.9 3.5 4.9
REMARK 620 6 HOH B 665 O 61.7 4.2 4.7 5.4 3.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 70 O
REMARK 620 2 VAL B 72 O 98.0
REMARK 620 3 PHE B 75 O 110.4 87.3
REMARK 620 4 HOH B 560 O 166.6 88.0 81.7
REMARK 620 5 HOH B 652 O 91.1 170.5 87.0 83.6
REMARK 620 6 HOH B 683 O 91.3 87.2 158.1 77.0 95.3
REMARK 620 N 1 2 3 4 5
DBREF1 8OTU A 1 305 UNP A0A3E0WVY1_9GAMM
DBREF2 8OTU A A0A3E0WVY1 1 305
DBREF1 8OTU B 1 305 UNP A0A3E0WVY1_9GAMM
DBREF2 8OTU B A0A3E0WVY1 1 305
SEQADV 8OTU VAL A 306 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ASP A 307 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LYS A 308 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LEU A 309 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA A 310 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA A 311 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA A 312 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LEU A 313 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU GLU A 314 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 315 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 316 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 317 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 318 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 319 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS A 320 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU VAL B 306 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ASP B 307 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LYS B 308 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LEU B 309 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA B 310 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA B 311 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU ALA B 312 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU LEU B 313 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU GLU B 314 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 315 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 316 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 317 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 318 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 319 UNP A0A3E0WVY EXPRESSION TAG
SEQADV 8OTU HIS B 320 UNP A0A3E0WVY EXPRESSION TAG
SEQRES 1 A 320 MET SER SER ILE ILE LYS ARG LYS LEU ALA SER LEU PHE
SEQRES 2 A 320 ALA PHE SER ALA ALA MET LEU LEU SER THR SER VAL TRP
SEQRES 3 A 320 SER MET ASN PRO GLY ASP VAL PRO ASP THR CYS GLU GLY
SEQRES 4 A 320 ASP CYS GLY TYR ALA ARG GLY PRO ASP PRO THR GLU SER
SEQRES 5 A 320 PHE LEU GLU ALA ASP SER GLY PRO TYR THR ILE ALA THR
SEQRES 6 A 320 SER ASN VAL SER SER LEU VAL ARG GLY PHE GLY GLY GLY
SEQRES 7 A 320 THR ILE TYR TYR PRO VAL ASN ALA GLU GLY THR MET ALA
SEQRES 8 A 320 ALA ILE VAL VAL ILE PRO GLY TYR MET SER TYR GLN SER
SEQRES 9 A 320 SER ILE SER PHE TRP GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 10 A 320 PHE VAL VAL MET THR ILE ASP THR ASN ARG ILE SER ASP
SEQRES 11 A 320 GLN PRO PRO SER ARG ARG ASP GLN ILE GLU ALA ALA LEU
SEQRES 12 A 320 GLU TYR LEU VAL ASP GLN SER ASN SER SER ARG SER PRO
SEQRES 13 A 320 ILE ASN GLY MET VAL ASP PRO ASN ARG LEU GLY ALA VAL
SEQRES 14 A 320 GLY TRP SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA
SEQRES 15 A 320 ALA ASP ASP GLY ILE GLN ALA ALA ILE GLY LEU ALA PRO
SEQRES 16 A 320 TRP ASN THR SER SER LEU GLY PHE ARG SER ILE GLU THR
SEQRES 17 A 320 PRO THR LEU ILE PHE ALA CYS GLU ARG ASP SER ILE ALA
SEQRES 18 A 320 PRO VAL ARG SER HIS ALA SER PRO PHE TYR ASN ALA ILE
SEQRES 19 A 320 PRO SER SER THR ASP LYS ALA TYR PHE GLU ILE SER GLY
SEQRES 20 A 320 GLY ASN HIS TYR CYS ALA ASN GLY SER ASN ARG TYR ASP
SEQRES 21 A 320 ALA LEU LEU GLY LYS TYR GLY VAL ALA TRP MET LYS LEU
SEQRES 22 A 320 HIS LEU ASP GLN ASP GLN ARG TYR ALA PRO PHE LEU CYS
SEQRES 23 A 320 GLY PRO ASN HIS GLU ARG ASP ARG GLN ILE SER GLU HIS
SEQRES 24 A 320 ARG SER THR CYS PRO PHE VAL ASP LYS LEU ALA ALA ALA
SEQRES 25 A 320 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 320 MET SER SER ILE ILE LYS ARG LYS LEU ALA SER LEU PHE
SEQRES 2 B 320 ALA PHE SER ALA ALA MET LEU LEU SER THR SER VAL TRP
SEQRES 3 B 320 SER MET ASN PRO GLY ASP VAL PRO ASP THR CYS GLU GLY
SEQRES 4 B 320 ASP CYS GLY TYR ALA ARG GLY PRO ASP PRO THR GLU SER
SEQRES 5 B 320 PHE LEU GLU ALA ASP SER GLY PRO TYR THR ILE ALA THR
SEQRES 6 B 320 SER ASN VAL SER SER LEU VAL ARG GLY PHE GLY GLY GLY
SEQRES 7 B 320 THR ILE TYR TYR PRO VAL ASN ALA GLU GLY THR MET ALA
SEQRES 8 B 320 ALA ILE VAL VAL ILE PRO GLY TYR MET SER TYR GLN SER
SEQRES 9 B 320 SER ILE SER PHE TRP GLY PRO ARG LEU ALA SER HIS GLY
SEQRES 10 B 320 PHE VAL VAL MET THR ILE ASP THR ASN ARG ILE SER ASP
SEQRES 11 B 320 GLN PRO PRO SER ARG ARG ASP GLN ILE GLU ALA ALA LEU
SEQRES 12 B 320 GLU TYR LEU VAL ASP GLN SER ASN SER SER ARG SER PRO
SEQRES 13 B 320 ILE ASN GLY MET VAL ASP PRO ASN ARG LEU GLY ALA VAL
SEQRES 14 B 320 GLY TRP SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA
SEQRES 15 B 320 ALA ASP ASP GLY ILE GLN ALA ALA ILE GLY LEU ALA PRO
SEQRES 16 B 320 TRP ASN THR SER SER LEU GLY PHE ARG SER ILE GLU THR
SEQRES 17 B 320 PRO THR LEU ILE PHE ALA CYS GLU ARG ASP SER ILE ALA
SEQRES 18 B 320 PRO VAL ARG SER HIS ALA SER PRO PHE TYR ASN ALA ILE
SEQRES 19 B 320 PRO SER SER THR ASP LYS ALA TYR PHE GLU ILE SER GLY
SEQRES 20 B 320 GLY ASN HIS TYR CYS ALA ASN GLY SER ASN ARG TYR ASP
SEQRES 21 B 320 ALA LEU LEU GLY LYS TYR GLY VAL ALA TRP MET LYS LEU
SEQRES 22 B 320 HIS LEU ASP GLN ASP GLN ARG TYR ALA PRO PHE LEU CYS
SEQRES 23 B 320 GLY PRO ASN HIS GLU ARG ASP ARG GLN ILE SER GLU HIS
SEQRES 24 B 320 ARG SER THR CYS PRO PHE VAL ASP LYS LEU ALA ALA ALA
SEQRES 25 B 320 LEU GLU HIS HIS HIS HIS HIS HIS
HET NA A 401 1
HET EDO A 402 10
HET EDO A 403 10
HET EDO A 404 10
HET EDO A 405 10
HET EDO A 406 10
HET EDO A 407 10
HET EDO A 408 10
HET EDO A 409 10
HET EDO A 410 10
HET EDO A 411 10
HET EDO A 412 10
HET EDO A 413 10
HET EDO A 414 10
HET EDO A 415 10
HET EDO A 416 10
HET EDO A 417 10
HET CL A 418 1
HET CL A 419 1
HET NA B 401 1
HET NA B 402 1
HET EDO B 403 10
HET EDO B 404 10
HET EDO B 405 10
HET EDO B 406 10
HET EDO B 407 10
HET EDO B 408 10
HET EDO B 409 10
HET EDO B 410 10
HET EDO B 411 10
HET CL B 412 1
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NA 3(NA 1+)
FORMUL 4 EDO 25(C2 H6 O2)
FORMUL 20 CL 3(CL 1-)
FORMUL 34 HOH *477(H2 O)
HELIX 1 AA1 THR A 50 ALA A 56 1 7
HELIX 2 AA2 TYR A 102 SER A 107 5 6
HELIX 3 AA3 PHE A 108 SER A 115 1 8
HELIX 4 AA4 GLN A 131 ASN A 151 1 21
HELIX 5 AA5 SER A 172 ASP A 184 1 13
HELIX 6 AA6 SER A 200 ARG A 204 5 5
HELIX 7 AA7 HIS A 226 ILE A 234 1 9
HELIX 8 AA8 TYR A 251 GLY A 255 5 5
HELIX 9 AA9 TYR A 259 ASP A 276 1 18
HELIX 10 AB1 ASP A 278 ARG A 280 5 3
HELIX 11 AB2 TYR A 281 CYS A 286 1 6
HELIX 12 AB3 ASN A 289 ASP A 293 5 5
HELIX 13 AB4 THR B 50 ALA B 56 1 7
HELIX 14 AB5 TYR B 102 SER B 107 5 6
HELIX 15 AB6 PHE B 108 SER B 115 1 8
HELIX 16 AB7 GLN B 131 ASN B 151 1 21
HELIX 17 AB8 SER B 172 ASP B 184 1 13
HELIX 18 AB9 SER B 200 ARG B 204 5 5
HELIX 19 AC1 HIS B 226 ILE B 234 1 9
HELIX 20 AC2 TYR B 251 GLY B 255 5 5
HELIX 21 AC3 TYR B 259 ASP B 276 1 18
HELIX 22 AC4 ASP B 278 LEU B 285 5 8
HELIX 23 AC5 ASN B 289 ASP B 293 5 5
SHEET 1 AA1 9 ILE A 63 VAL A 68 0
SHEET 2 AA1 9 GLY A 78 PRO A 83 -1 O GLY A 78 N VAL A 68
SHEET 3 AA1 9 VAL A 119 ILE A 123 -1 O VAL A 120 N TYR A 81
SHEET 4 AA1 9 MET A 90 ILE A 96 1 N VAL A 95 O ILE A 123
SHEET 5 AA1 9 VAL A 161 TRP A 171 1 O ASP A 162 N MET A 90
SHEET 6 AA1 9 ALA A 189 LEU A 193 1 O LEU A 193 N GLY A 170
SHEET 7 AA1 9 THR A 210 CYS A 215 1 O PHE A 213 N GLY A 192
SHEET 8 AA1 9 LYS A 240 ILE A 245 1 O ILE A 245 N ALA A 214
SHEET 9 AA1 9 ILE A 296 SER A 301 -1 O GLU A 298 N GLU A 244
SHEET 1 AA2 9 ILE B 63 VAL B 68 0
SHEET 2 AA2 9 GLY B 78 PRO B 83 -1 O GLY B 78 N VAL B 68
SHEET 3 AA2 9 VAL B 119 ILE B 123 -1 O VAL B 120 N TYR B 81
SHEET 4 AA2 9 MET B 90 ILE B 96 1 N VAL B 95 O ILE B 123
SHEET 5 AA2 9 VAL B 161 TRP B 171 1 O ASP B 162 N MET B 90
SHEET 6 AA2 9 ALA B 189 LEU B 193 1 O LEU B 193 N GLY B 170
SHEET 7 AA2 9 THR B 210 CYS B 215 1 O PHE B 213 N GLY B 192
SHEET 8 AA2 9 LYS B 240 ILE B 245 1 O ILE B 245 N ALA B 214
SHEET 9 AA2 9 ILE B 296 SER B 301 -1 O GLU B 298 N GLU B 244
SSBOND 1 CYS A 215 CYS A 252 1555 1555 2.03
SSBOND 2 CYS A 286 CYS A 303 1555 1555 2.05
SSBOND 3 CYS B 215 CYS B 252 1555 1555 2.05
SSBOND 4 CYS B 286 CYS B 303 1555 1555 2.05
LINK O SER A 70 NA NA A 401 1555 1555 2.28
LINK O VAL A 72 NA NA A 401 1555 1555 2.25
LINK O PHE A 75 NA NA A 401 1555 1555 2.33
LINK O SER A 153 NA NA B 402 1555 4446 2.29
LINK NA NA A 401 O2 EDO A 415 1555 1555 2.44
LINK NA NA A 401 O HOH A 585 1555 1555 2.67
LINK NA NA A 401 O HOH A 675 1555 1555 2.37
LINK O SER B 70 NA NA B 401 1555 1555 2.32
LINK O VAL B 72 NA NA B 401 1555 1555 2.25
LINK O PHE B 75 NA NA B 401 1555 1555 2.31
LINK O GLU B 291 NA NA B 402 1555 1555 2.24
LINK O ASP B 293 NA NA B 402 1555 1555 2.48
LINK O ILE B 296 NA NA B 402 1555 1555 2.32
LINK NA NA B 401 O HOH B 560 1555 1555 2.65
LINK NA NA B 401 O HOH B 652 1555 1555 2.36
LINK NA NA B 401 O HOH B 683 1555 1555 2.41
LINK NA NA B 402 O HOH B 605 1555 1555 2.50
LINK NA NA B 402 O HOH B 665 1555 1555 2.55
CISPEP 1 CYS A 303 PRO A 304 0 -0.70
CISPEP 2 CYS B 303 PRO B 304 0 -4.71
CRYST1 141.133 45.660 84.187 90.00 97.83 90.00 C 1 2 1 8
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 0.007086 0.000000 0.000974 0.00000
SCALE2 0.000000 0.021901 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011990 0.00000
TER 4020 PHE A 305
TER 8031 ASP B 307
MASTER 647 0 31 23 18 0 0 6 4624 2 280 50
END |