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HEADER HYDROLASE 28-AUG-17 5OV9
TITLE CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH CRYSTAL
TITLE 2 VIOLET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 32-574
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS DIMERIC, COMPLEX, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ALLGARDSSON,C.D.ANDERSSON,C.AKFUR,F.WOREK,A.LINUSSON,F.EKSTROM
REVDAT 1 06-SEP-17 5OV9 0
JRNL AUTH A.ALLGARDSSON,C.D.ANDERSSON,C.AKFUR,F.WOREK,A.LINUSSON,
JRNL AUTH 2 F.EKSTROM
JRNL TITL AN UNUSUAL DIMERIC INHIBITOR OF ACETYLCHOLINESTERASE:
JRNL TITL 2 COOPERATIVE BINDING OF CRYSTAL VIOLET
JRNL REF MOLECULES V. 22 1433 2017
JRNL REFN ESSN 1420-3049
JRNL DOI 10.3390/MOLECULES22091433
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 79973
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1585
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 29.1079 - 5.3276 0.95 7255 145 0.1504 0.1829
REMARK 3 2 5.3276 - 4.2329 0.98 7191 147 0.1205 0.1484
REMARK 3 3 4.2329 - 3.6990 0.99 7209 138 0.1332 0.1631
REMARK 3 4 3.6990 - 3.3614 0.99 7222 138 0.1587 0.1857
REMARK 3 5 3.3614 - 3.1207 0.99 7168 146 0.1780 0.1953
REMARK 3 6 3.1207 - 2.9369 0.99 7118 154 0.1884 0.2335
REMARK 3 7 2.9369 - 2.7900 0.99 7096 144 0.1962 0.2826
REMARK 3 8 2.7900 - 2.6686 0.99 7063 151 0.1903 0.2347
REMARK 3 9 2.6686 - 2.5659 0.98 7015 160 0.1923 0.2375
REMARK 3 10 2.5659 - 2.4774 0.98 7033 128 0.2029 0.2766
REMARK 3 11 2.4774 - 2.4000 0.98 7018 134 0.2268 0.2688
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.79
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 : 0.012 8842
REMARK 3 ANGLE : 1.364 12042
REMARK 3 CHIRALITY : 0.056 1274
REMARK 3 PLANARITY : 0.007 1588
REMARK 3 DIHEDRAL : 17.005 3147
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 1 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7303 11.7443 28.5607
REMARK 3 T TENSOR
REMARK 3 T11: 0.2906 T22: 0.2840
REMARK 3 T33: 0.3333 T12: 0.0271
REMARK 3 T13: -0.0023 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 1.1327 L22: 1.0544
REMARK 3 L33: 2.5923 L12: 0.1251
REMARK 3 L13: -0.3533 L23: -0.4370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0537 S12: -0.1471 S13: -0.0153
REMARK 3 S21: 0.1295 S22: 0.0272 S23: -0.0500
REMARK 3 S31: 0.0395 S32: -0.0085 S33: 0.0196
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4008 16.8497 10.1963
REMARK 3 T TENSOR
REMARK 3 T11: 0.3469 T22: 0.4139
REMARK 3 T33: 0.3711 T12: 0.0553
REMARK 3 T13: 0.0402 T23: 0.0878
REMARK 3 L TENSOR
REMARK 3 L11: 2.8035 L22: 2.6553
REMARK 3 L33: 3.8837 L12: 1.5447
REMARK 3 L13: 0.3695 L23: 0.4313
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.2899 S13: 0.0289
REMARK 3 S21: -0.2174 S22: -0.1086 S23: -0.1478
REMARK 3 S31: -0.0591 S32: 0.5084 S33: 0.1060
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5954 4.7637 9.9861
REMARK 3 T TENSOR
REMARK 3 T11: 0.4539 T22: 0.3249
REMARK 3 T33: 0.2864 T12: -0.0401
REMARK 3 T13: 0.0142 T23: -0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 5.0009 L22: 1.5451
REMARK 3 L33: 2.6353 L12: -0.6640
REMARK 3 L13: -0.0056 L23: -0.2320
REMARK 3 S TENSOR
REMARK 3 S11: -0.2147 S12: 0.1333 S13: -0.5953
REMARK 3 S21: -0.0703 S22: 0.1495 S23: -0.0101
REMARK 3 S31: 0.5095 S32: 0.0593 S33: 0.0580
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1110 17.6890 6.5081
REMARK 3 T TENSOR
REMARK 3 T11: 0.3011 T22: 0.3803
REMARK 3 T33: 0.3852 T12: -0.0413
REMARK 3 T13: -0.0494 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.1062 L22: 1.0129
REMARK 3 L33: 3.5185 L12: -0.2011
REMARK 3 L13: -0.4089 L23: -0.5376
REMARK 3 S TENSOR
REMARK 3 S11: -0.0483 S12: 0.1004 S13: -0.0085
REMARK 3 S21: -0.1339 S22: 0.0388 S23: 0.1073
REMARK 3 S31: -0.0378 S32: -0.3351 S33: -0.0139
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7970 1.9829 13.8031
REMARK 3 T TENSOR
REMARK 3 T11: 0.4597 T22: 0.5676
REMARK 3 T33: 0.4971 T12: -0.1808
REMARK 3 T13: 0.0305 T23: 0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 4.3401 L22: 2.7214
REMARK 3 L33: 6.6924 L12: 0.2176
REMARK 3 L13: 1.0448 L23: -2.2639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0840 S12: -0.0823 S13: -0.6910
REMARK 3 S21: -0.0136 S22: 0.0242 S23: 0.7599
REMARK 3 S31: 0.8307 S32: -1.2916 S33: -0.0231
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 541 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0366 8.6224 -0.6610
REMARK 3 T TENSOR
REMARK 3 T11: 0.4944 T22: 0.5684
REMARK 3 T33: 0.3416 T12: -0.0424
REMARK 3 T13: -0.1226 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 0.5893 L22: 2.5089
REMARK 3 L33: 1.9633 L12: -0.2920
REMARK 3 L13: 0.0940 L23: 0.7409
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: 0.2849 S13: -0.1620
REMARK 3 S21: -0.3008 S22: -0.0815 S23: 0.1043
REMARK 3 S31: 0.2151 S32: -0.1430 S33: -0.0293
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9715 5.9380 -61.2625
REMARK 3 T TENSOR
REMARK 3 T11: 0.4273 T22: 0.5371
REMARK 3 T33: 0.3989 T12: 0.0834
REMARK 3 T13: -0.0888 T23: -0.1656
REMARK 3 L TENSOR
REMARK 3 L11: 5.0565 L22: 2.0274
REMARK 3 L33: 3.4795 L12: -0.8831
REMARK 3 L13: -1.4774 L23: 0.4610
REMARK 3 S TENSOR
REMARK 3 S11: 0.0958 S12: 0.3614 S13: -0.0162
REMARK 3 S21: -0.2588 S22: -0.2472 S23: 0.3146
REMARK 3 S31: -0.1865 S32: -0.4163 S33: 0.0931
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9446 -4.3623 -52.7334
REMARK 3 T TENSOR
REMARK 3 T11: 0.4490 T22: 0.4614
REMARK 3 T33: 0.3870 T12: -0.0182
REMARK 3 T13: -0.0289 T23: -0.1158
REMARK 3 L TENSOR
REMARK 3 L11: 1.0681 L22: 1.4466
REMARK 3 L33: 2.8776 L12: -0.3854
REMARK 3 L13: 0.5264 L23: 0.1200
REMARK 3 S TENSOR
REMARK 3 S11: 0.1341 S12: 0.1041 S13: -0.2601
REMARK 3 S21: -0.0580 S22: -0.2574 S23: 0.1318
REMARK 3 S31: 0.4618 S32: -0.1604 S33: 0.0242
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2275 4.7000 -50.2457
REMARK 3 T TENSOR
REMARK 3 T11: 0.3180 T22: 0.4907
REMARK 3 T33: 0.4098 T12: 0.0387
REMARK 3 T13: -0.0626 T23: -0.1250
REMARK 3 L TENSOR
REMARK 3 L11: 2.5002 L22: 1.4829
REMARK 3 L33: 1.8241 L12: -0.0830
REMARK 3 L13: 0.1215 L23: 0.7753
REMARK 3 S TENSOR
REMARK 3 S11: 0.1114 S12: 0.2052 S13: -0.0239
REMARK 3 S21: -0.1313 S22: -0.3632 S23: 0.5147
REMARK 3 S31: -0.0457 S32: -0.5546 S33: 0.1394
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 142 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7059 6.8977 -53.5212
REMARK 3 T TENSOR
REMARK 3 T11: 0.3771 T22: 0.3926
REMARK 3 T33: 0.2965 T12: 0.0348
REMARK 3 T13: -0.0039 T23: -0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 3.8439 L22: 3.3972
REMARK 3 L33: 1.8663 L12: -2.1511
REMARK 3 L13: 1.9932 L23: -1.0505
REMARK 3 S TENSOR
REMARK 3 S11: 0.1377 S12: 0.0979 S13: 0.1405
REMARK 3 S21: -0.1940 S22: -0.1458 S23: -0.0592
REMARK 3 S31: -0.0647 S32: 0.1116 S33: 0.0276
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9117 2.9222 -44.6568
REMARK 3 T TENSOR
REMARK 3 T11: 0.3464 T22: 0.4190
REMARK 3 T33: 0.3353 T12: 0.0060
REMARK 3 T13: -0.0217 T23: -0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 1.8555 L22: 2.8219
REMARK 3 L33: 2.4200 L12: -1.0717
REMARK 3 L13: 0.0766 L23: 0.8249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0835 S12: -0.0598 S13: 0.0062
REMARK 3 S21: 0.0995 S22: 0.0412 S23: -0.2203
REMARK 3 S31: 0.2494 S32: 0.3455 S33: -0.1001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3815 -0.6722 -26.4705
REMARK 3 T TENSOR
REMARK 3 T11: 0.5157 T22: 0.3426
REMARK 3 T33: 0.3831 T12: -0.0492
REMARK 3 T13: 0.0234 T23: -0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 1.9269 L22: 2.9231
REMARK 3 L33: 3.5707 L12: -1.1252
REMARK 3 L13: 1.0804 L23: -0.1990
REMARK 3 S TENSOR
REMARK 3 S11: 0.2093 S12: -0.1500 S13: -0.2985
REMARK 3 S21: 0.3759 S22: -0.0227 S23: 0.1546
REMARK 3 S31: 0.6491 S32: -0.1104 S33: -0.1852
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 367 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7313 -1.4066 -16.4868
REMARK 3 T TENSOR
REMARK 3 T11: 0.6834 T22: 0.4516
REMARK 3 T33: 0.4202 T12: -0.0624
REMARK 3 T13: -0.0463 T23: -0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 5.4093 L22: 2.2963
REMARK 3 L33: 4.6901 L12: 2.0956
REMARK 3 L13: -0.8269 L23: -0.6749
REMARK 3 S TENSOR
REMARK 3 S11: 0.1742 S12: -0.5945 S13: -0.1599
REMARK 3 S21: 0.3029 S22: -0.0538 S23: 0.0413
REMARK 3 S31: 0.5169 S32: -0.0113 S33: -0.1343
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1549 8.7259 -33.0225
REMARK 3 T TENSOR
REMARK 3 T11: 0.3697 T22: 0.4729
REMARK 3 T33: 0.4046 T12: -0.0480
REMARK 3 T13: 0.0593 T23: -0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 2.1618 L22: 2.7177
REMARK 3 L33: 2.7897 L12: 0.1673
REMARK 3 L13: 0.1595 L23: 0.2432
REMARK 3 S TENSOR
REMARK 3 S11: 0.1373 S12: -0.0915 S13: 0.0067
REMARK 3 S21: 0.1276 S22: -0.1685 S23: 0.4334
REMARK 3 S31: 0.2132 S32: -0.4482 S33: 0.0367
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3907 22.6412 -28.6755
REMARK 3 T TENSOR
REMARK 3 T11: 0.4667 T22: 0.4483
REMARK 3 T33: 0.4996 T12: 0.0278
REMARK 3 T13: 0.0286 T23: -0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 3.2453 L22: 6.0013
REMARK 3 L33: 6.3927 L12: 2.7223
REMARK 3 L13: 0.3601 L23: -0.8784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: -0.3365 S13: 0.4495
REMARK 3 S21: 0.1385 S22: 0.1068 S23: 0.4116
REMARK 3 S31: -0.4693 S32: -0.3998 S33: 0.0489
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 541 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0100 10.6096 -21.3183
REMARK 3 T TENSOR
REMARK 3 T11: 0.5837 T22: 0.5382
REMARK 3 T33: 0.2463 T12: -0.0534
REMARK 3 T13: 0.0680 T23: -0.0594
REMARK 3 L TENSOR
REMARK 3 L11: 1.4890 L22: 2.0030
REMARK 3 L33: 0.9705 L12: -0.1054
REMARK 3 L13: 1.2039 L23: -0.1280
REMARK 3 S TENSOR
REMARK 3 S11: -0.2416 S12: 0.2226 S13: 0.4304
REMARK 3 S21: 0.3872 S22: 0.0048 S23: 0.0147
REMARK 3 S31: -0.0880 S32: 0.2930 S33: 0.2896
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TLS WAS USED IN REFINEMENT
REMARK 4
REMARK 4 5OV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006279.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.038050
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.106
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.04764
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.49410
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) POLYETHYLENE GLYCOL 750
REMARK 280 MONOMETHYLETHER, 100 MM HEPES, PH 7.1, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.81500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.94500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.81500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.94500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 PRO A 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ALA A 542
REMARK 465 THR A 543
REMARK 465 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 ALA B 542
REMARK 465 THR B 543
REMARK 465 ALA B 544
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 1 CG CD OE1 OE2
REMARK 470 GLU A 4 CG CD OE1 OE2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 SER A 495 OG
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 494 CG OD1 OD2
REMARK 470 SER B 495 OG
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 LEU B 540 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1009 O HOH A 1010 2.15
REMARK 500 O HOH A 936 O HOH A 993 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 47 -7.35 78.13
REMARK 500 ALA A 62 51.07 -118.07
REMARK 500 PHE A 158 -5.82 -140.60
REMARK 500 SER A 203 -122.27 57.57
REMARK 500 ASP A 306 -83.90 -141.86
REMARK 500 ASP A 323 51.18 -111.26
REMARK 500 HIS A 387 59.17 -148.78
REMARK 500 VAL A 407 -60.21 -135.38
REMARK 500 PHE B 47 -0.64 76.62
REMARK 500 ARG B 107 141.27 -39.14
REMARK 500 PHE B 158 -0.21 -141.08
REMARK 500 SER B 203 -121.41 53.23
REMARK 500 ASP B 306 -88.13 -126.18
REMARK 500 ASP B 323 43.53 -105.24
REMARK 500 VAL B 407 -63.36 -128.22
REMARK 500 PRO B 492 6.11 -67.73
REMARK 500 ARG B 493 -53.05 -158.16
REMARK 500 ASP B 494 173.01 -58.90
REMARK 500 LYS B 496 73.78 57.94
REMARK 500 SER B 497 -145.33 -149.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1011 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B 932 DISTANCE = 6.19 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PE4 B 607
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAG B 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG0 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG0 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETX A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETX A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVI A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVI A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVI B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVI B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AE3 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PE4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ETX B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 350
DBREF 5OV9 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5OV9 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 5OV9 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 5OV9 PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
HET NAG A 601 14
HET PG0 A 602 8
HET PG0 A 603 8
HET ETX A 604 6
HET ETX A 605 6
HET EDO A 606 4
HET EDO A 607 4
HET CVI A 608 28
HET CVI A 609 28
HET NAG B 601 14
HET CVI B 602 28
HET CVI B 603 28
HET PEG B 604 7
HET PGE B 605 10
HET AE3 B 606 9
HET PE4 B 607 23
HET ETX B 608 6
HET EDO B 609 4
HET EDO B 610 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM ETX 2-ETHOXYETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CVI CRYSTAL VIOLET
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM AE3 2-(2-ETHOXYETHOXY)ETHANOL
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PG0 PEG 6000
HETSYN EDO ETHYLENE GLYCOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 PG0 2(C5 H12 O3)
FORMUL 6 ETX 3(C4 H10 O2)
FORMUL 8 EDO 4(C2 H6 O2)
FORMUL 10 CVI 4(C25 H30 N3 1+)
FORMUL 15 PEG C4 H10 O3
FORMUL 16 PGE C6 H14 O4
FORMUL 17 AE3 C6 H14 O3
FORMUL 18 PE4 C16 H34 O8
FORMUL 22 HOH *543(H2 O)
HELIX 1 AA1 ASP A 5 GLN A 7 5 3
HELIX 2 AA2 VAL A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 GLY A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 ILE A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 SER A 220 1 6
HELIX 11 AB2 ALA A 241 VAL A 255 1 15
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASN A 464 5 9
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 SER A 541 1 8
HELIX 27 AC9 ASP B 5 GLN B 7 5 3
HELIX 28 AD1 VAL B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 GLU B 142 1 8
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 ILE B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 SER B 240 VAL B 255 1 16
HELIX 38 AE2 ASP B 266 ARG B 276 1 11
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASN B 464 5 9
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 2 VAL A 239 SER A 240 0
SHEET 2 AA4 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 AA5 3 LEU B 9 VAL B 12 0
SHEET 2 AA5 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA5 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA611 ILE B 20 ALA B 24 0
SHEET 2 AA611 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA611 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA611 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA611 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA611 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA611 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA611 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA611 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA611 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA611 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.14
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.47
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.46
CISPEP 1 TYR A 105 PRO A 106 0 -6.53
CISPEP 2 TYR B 105 PRO B 106 0 5.12
CISPEP 3 SER B 495 LYS B 496 0 10.68
CISPEP 4 LYS B 496 SER B 497 0 11.91
CISPEP 5 SER B 497 PRO B 498 0 -15.50
SITE 1 AC1 5 TRP A 286 LEU A 289 CVI A 609 HOH A 761
SITE 2 AC1 5 HOH A 969
SITE 1 AC2 5 HIS A 381 HIS A 393 THR A 528 HOH A 850
SITE 2 AC2 5 GLN B 527
SITE 1 AC3 3 VAL A 303 ASP A 304 SER A 309
SITE 1 AC4 2 SER A 57 VAL A 59
SITE 1 AC5 3 GLN A 140 VAL A 141 HOH A 906
SITE 1 AC6 1 ASP A 333
SITE 1 AC7 7 ASP A 74 THR A 75 LEU A 76 VAL A 340
SITE 2 AC7 7 TYR A 341 CVI A 609 HOH A 925
SITE 1 AC8 6 TYR A 72 ASP A 283 TRP A 286 TYR A 341
SITE 2 AC8 6 PG0 A 602 CVI A 608
SITE 1 AC9 8 TYR B 72 ASP B 74 THR B 75 LEU B 76
SITE 2 AC9 8 THR B 83 VAL B 340 TYR B 341 CVI B 603
SITE 1 AD1 8 TYR B 72 GLN B 279 ASP B 283 TRP B 286
SITE 2 AD1 8 HIS B 287 TYR B 341 CVI B 602 PGE B 605
SITE 1 AD2 1 ASP B 304
SITE 1 AD3 7 TRP B 286 LEU B 289 GLN B 291 GLU B 292
SITE 2 AD3 7 SER B 293 CVI B 603 HOH B 822
SITE 1 AD4 3 GLN A 527 HIS B 381 HOH B 883
SITE 1 AD5 8 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 AD5 8 LEU B 380 HIS B 381 GLN B 527 PHE B 535
SITE 1 AD6 2 LYS B 332 ASP B 333
SITE 1 AD7 1 ALA B 370
SITE 1 AD8 1 ARG B 11
SITE 1 AD9 3 SER A 347 ASN A 350 HOH A 723
SITE 1 AE1 3 ASN B 350 SER B 352 LEU B 353
CRYST1 79.630 113.890 226.670 90.00 90.00 90.00 P 21 21 21 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 0.012558 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004412 0.00000
TER 4185 SER A 541
TER 8350 SER B 541
MASTER 660 0 19 52 32 0 27 6 9064 2 253 86
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