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HEADER HYDROLASE 25-NOV-15 5FOQ
TITLE ACETYLCHOLINESTERASE IN COMPLEX WITH C7653
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, 1-548;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HEK293F;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE, SIGNALING PROTEIN, QUANTUM CHEMISTRY, DENSITY FUNCTIONAL
KEYWDS 2 THEORY, DRUG DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BERG,B.K.MISHRA,D.C.ANDERSSON,F.EKSTROM,A.LINUSSON
REVDAT 1 02-MAR-16 5FOQ 0
JRNL AUTH L.BERG,B.K.MISHRA,C.D.ANDERSSON,F.EKSTROM,A.LINUSSON
JRNL TITL THE NATURE OF ACTIVATED NON-CLASSICAL HYDROGEN BONDS: A
JRNL TITL 2 CASE STUDY ON ACETYLCHOLINESTERASE-LIGAND COMPLEXES.
JRNL REF CHEMISTRY V. 22 2672 2016
JRNL REFN ISSN 0947-6539
JRNL PMID 26751405
JRNL DOI 10.1002/CHEM.201503973
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.300
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.978
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.33
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.30
REMARK 3 NUMBER OF REFLECTIONS : 88553
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1922
REMARK 3 R VALUE (WORKING SET) : 0.1915
REMARK 3 FREE R VALUE : 0.2219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1746
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 28.9806 - 5.2561 1.00 7697 156 0.1612 0.1786
REMARK 3 2 5.2561 - 4.1759 0.99 7392 147 0.1388 0.1405
REMARK 3 3 4.1759 - 3.6492 0.98 7301 141 0.1645 0.1923
REMARK 3 4 3.6492 - 3.3161 0.99 7259 136 0.1958 0.2389
REMARK 3 5 3.3161 - 3.0787 0.99 7310 146 0.2217 0.2795
REMARK 3 6 3.0787 - 2.8973 0.99 7256 155 0.2297 0.2579
REMARK 3 7 2.8973 - 2.7524 0.99 7249 155 0.2277 0.2875
REMARK 3 8 2.7524 - 2.6326 0.99 7196 152 0.2251 0.2795
REMARK 3 9 2.6326 - 2.5313 0.98 7172 150 0.2396 0.2528
REMARK 3 10 2.5313 - 2.4440 0.97 7097 138 0.2726 0.3187
REMARK 3 11 2.4440 - 2.3677 0.96 7002 134 0.3087 0.3544
REMARK 3 12 2.3677 - 2.3000 0.95 6876 136 0.3471 0.4239
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) : 0.30
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.008 8740
REMARK 3 ANGLE : 1.069 11920
REMARK 3 CHIRALITY : 0.073 1281
REMARK 3 PLANARITY : 0.005 1557
REMARK 3 DIHEDRAL : 15.907 3155
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 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2079 16.2907 33.6435
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.2925
REMARK 3 T33: 0.2705 T12: -0.0027
REMARK 3 T13: -0.0436 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 1.2634 L22: 1.6238
REMARK 3 L33: 2.8461 L12: -0.3036
REMARK 3 L13: -0.5356 L23: -0.7503
REMARK 3 S TENSOR
REMARK 3 S11: -0.1389 S12: -0.2585 S13: 0.0808
REMARK 3 S21: 0.2820 S22: 0.0868 S23: -0.0073
REMARK 3 S31: -0.1313 S32: 0.0560 S33: 0.0516
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6666 12.6553 26.7371
REMARK 3 T TENSOR
REMARK 3 T11: 0.2876 T22: 0.2582
REMARK 3 T33: 0.2121 T12: 0.0255
REMARK 3 T13: -0.0476 T23: 0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 3.7366 L22: 1.1348
REMARK 3 L33: 3.7096 L12: 0.3921
REMARK 3 L13: -2.1497 L23: 0.1283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0771 S12: -0.3800 S13: -0.0008
REMARK 3 S21: 0.1778 S22: 0.0488 S23: -0.0207
REMARK 3 S31: 0.2444 S32: 0.1393 S33: 0.0430
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5314 2.8376 26.3217
REMARK 3 T TENSOR
REMARK 3 T11: 0.3682 T22: 0.2354
REMARK 3 T33: 0.2979 T12: 0.0120
REMARK 3 T13: 0.0071 T23: 0.0859
REMARK 3 L TENSOR
REMARK 3 L11: 2.1681 L22: 0.9286
REMARK 3 L33: 2.3772 L12: -0.3845
REMARK 3 L13: -0.3396 L23: 1.1465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: -0.1985 S13: -0.2964
REMARK 3 S21: 0.1715 S22: 0.1353 S23: 0.0179
REMARK 3 S31: 0.5206 S32: -0.2561 S33: -0.0781
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9735 8.3644 11.5652
REMARK 3 T TENSOR
REMARK 3 T11: 0.3054 T22: 0.2210
REMARK 3 T33: 0.2623 T12: 0.0826
REMARK 3 T13: 0.0203 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 3.3671 L22: 1.1694
REMARK 3 L33: 3.0252 L12: 0.2731
REMARK 3 L13: 0.1512 L23: -0.2862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0539 S12: 0.2098 S13: -0.2941
REMARK 3 S21: -0.0879 S22: -0.0434 S23: -0.1687
REMARK 3 S31: 0.4067 S32: 0.2650 S33: 0.1127
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3600 20.0854 -3.5902
REMARK 3 T TENSOR
REMARK 3 T11: 0.2753 T22: 0.3609
REMARK 3 T33: 0.2886 T12: -0.0076
REMARK 3 T13: -0.0292 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.4224 L22: 2.9652
REMARK 3 L33: 3.3864 L12: 0.0278
REMARK 3 L13: -0.2869 L23: -1.3261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0640 S12: 0.2737 S13: 0.0552
REMARK 3 S21: -0.1377 S22: -0.0973 S23: 0.1068
REMARK 3 S31: -0.0236 S32: -0.1126 S33: 0.0188
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3961 13.7803 16.3594
REMARK 3 T TENSOR
REMARK 3 T11: 0.2010 T22: 0.3887
REMARK 3 T33: 0.3248 T12: -0.0545
REMARK 3 T13: -0.0252 T23: 0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 2.2568 L22: 2.8358
REMARK 3 L33: 3.6091 L12: -0.1796
REMARK 3 L13: -0.2060 L23: 0.4085
REMARK 3 S TENSOR
REMARK 3 S11: -0.0347 S12: -0.0717 S13: -0.1058
REMARK 3 S21: -0.0118 S22: 0.0558 S23: 0.3643
REMARK 3 S31: 0.1286 S32: -0.6700 S33: -0.0377
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9061 1.1665 14.2887
REMARK 3 T TENSOR
REMARK 3 T11: 0.4361 T22: 0.5842
REMARK 3 T33: 0.4755 T12: -0.2290
REMARK 3 T13: -0.0028 T23: 0.0868
REMARK 3 L TENSOR
REMARK 3 L11: 4.3630 L22: 7.4416
REMARK 3 L33: 4.4860 L12: 0.7919
REMARK 3 L13: 1.1634 L23: -3.0153
REMARK 3 S TENSOR
REMARK 3 S11: -0.0098 S12: -0.0514 S13: -0.4395
REMARK 3 S21: 0.2420 S22: 0.2445 S23: 0.6756
REMARK 3 S31: 0.4520 S32: -1.5197 S33: -0.1749
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6233 6.0635 -1.1400
REMARK 3 T TENSOR
REMARK 3 T11: 0.3721 T22: 0.3590
REMARK 3 T33: 0.2966 T12: -0.0631
REMARK 3 T13: -0.1202 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.5591 L22: 2.9812
REMARK 3 L33: 9.3460 L12: -1.1333
REMARK 3 L13: -2.3108 L23: 2.5255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: -0.1550 S13: -0.0152
REMARK 3 S21: -0.3874 S22: -0.0572 S23: 0.3031
REMARK 3 S31: 0.3322 S32: 0.2168 S33: 0.1564
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8581 6.1165 -61.5990
REMARK 3 T TENSOR
REMARK 3 T11: 0.4383 T22: 0.5968
REMARK 3 T33: 0.3801 T12: 0.0493
REMARK 3 T13: -0.1148 T23: -0.1611
REMARK 3 L TENSOR
REMARK 3 L11: 2.1254 L22: 1.7971
REMARK 3 L33: 4.2535 L12: -0.1555
REMARK 3 L13: -1.1798 L23: -0.2955
REMARK 3 S TENSOR
REMARK 3 S11: 0.1484 S12: 0.7317 S13: 0.0708
REMARK 3 S21: -0.3574 S22: -0.1618 S23: 0.2863
REMARK 3 S31: -0.2538 S32: -0.9077 S33: 0.0430
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3588 1.1284 -51.4004
REMARK 3 T TENSOR
REMARK 3 T11: 0.3680 T22: 0.4443
REMARK 3 T33: 0.3350 T12: -0.0198
REMARK 3 T13: -0.0623 T23: -0.1160
REMARK 3 L TENSOR
REMARK 3 L11: 1.1158 L22: 1.4739
REMARK 3 L33: 3.5972 L12: -0.3521
REMARK 3 L13: 0.2719 L23: 0.5360
REMARK 3 S TENSOR
REMARK 3 S11: 0.1131 S12: 0.2416 S13: -0.2234
REMARK 3 S21: -0.1306 S22: -0.1454 S23: 0.2726
REMARK 3 S31: 0.4705 S32: -0.3344 S33: 0.0194
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9672 8.5866 -55.3622
REMARK 3 T TENSOR
REMARK 3 T11: 0.3655 T22: 0.4904
REMARK 3 T33: 0.3140 T12: 0.0288
REMARK 3 T13: -0.0063 T23: -0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 7.5839 L22: 4.4122
REMARK 3 L33: 3.2626 L12: -4.5906
REMARK 3 L13: 1.8109 L23: -1.5267
REMARK 3 S TENSOR
REMARK 3 S11: 0.5022 S12: 0.5129 S13: -0.2299
REMARK 3 S21: -0.4780 S22: -0.3042 S23: 0.0559
REMARK 3 S31: -0.1835 S32: 0.1995 S33: -0.1947
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6941 1.5193 -45.1846
REMARK 3 T TENSOR
REMARK 3 T11: 0.3029 T22: 0.4169
REMARK 3 T33: 0.2735 T12: 0.0425
REMARK 3 T13: -0.0469 T23: -0.0748
REMARK 3 L TENSOR
REMARK 3 L11: 1.7497 L22: 2.3110
REMARK 3 L33: 3.1732 L12: -0.8507
REMARK 3 L13: 0.0420 L23: 0.7250
REMARK 3 S TENSOR
REMARK 3 S11: 0.1629 S12: 0.1127 S13: -0.1812
REMARK 3 S21: 0.0954 S22: 0.0133 S23: -0.1813
REMARK 3 S31: 0.3259 S32: 0.4808 S33: -0.1705
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 298 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2584 14.1798 -40.0425
REMARK 3 T TENSOR
REMARK 3 T11: 0.3231 T22: 0.4333
REMARK 3 T33: 0.3505 T12: -0.0418
REMARK 3 T13: -0.0584 T23: -0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 5.1651 L22: 1.4210
REMARK 3 L33: 5.0637 L12: -1.7018
REMARK 3 L13: -2.3262 L23: 1.8363
REMARK 3 S TENSOR
REMARK 3 S11: 0.2637 S12: 0.3699 S13: 0.6489
REMARK 3 S21: -0.0246 S22: 0.1067 S23: -0.3611
REMARK 3 S31: -0.2382 S32: 0.5934 S33: -0.3591
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7502 1.9736 -26.7863
REMARK 3 T TENSOR
REMARK 3 T11: 0.3956 T22: 0.3329
REMARK 3 T33: 0.3081 T12: -0.0708
REMARK 3 T13: 0.0198 T23: -0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 1.8521 L22: 1.4196
REMARK 3 L33: 2.7533 L12: -0.2086
REMARK 3 L13: 0.7463 L23: 0.2309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1788 S12: -0.1291 S13: -0.2899
REMARK 3 S21: 0.2358 S22: -0.0942 S23: 0.1943
REMARK 3 S31: 0.4827 S32: -0.2216 S33: -0.0989
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0633 22.3808 -28.7326
REMARK 3 T TENSOR
REMARK 3 T11: 0.3733 T22: 0.3291
REMARK 3 T33: 0.3072 T12: 0.0347
REMARK 3 T13: -0.0174 T23: -0.0864
REMARK 3 L TENSOR
REMARK 3 L11: 7.5906 L22: 4.5257
REMARK 3 L33: 7.7307 L12: 2.0646
REMARK 3 L13: 1.6210 L23: -1.3305
REMARK 3 S TENSOR
REMARK 3 S11: 0.0032 S12: -0.4173 S13: 0.7768
REMARK 3 S21: -0.0677 S22: 0.0409 S23: 0.3890
REMARK 3 S31: -0.0290 S32: -0.6876 S33: 0.0034
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3093 11.3368 -21.5192
REMARK 3 T TENSOR
REMARK 3 T11: 0.4374 T22: 0.4403
REMARK 3 T33: 0.2263 T12: -0.0703
REMARK 3 T13: 0.0138 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 8.5400 L22: 2.1492
REMARK 3 L33: 4.7000 L12: -0.6449
REMARK 3 L13: 3.1353 L23: -0.1288
REMARK 3 S TENSOR
REMARK 3 S11: 0.1485 S12: -0.1843 S13: -0.2681
REMARK 3 S21: 0.0970 S22: -0.0790 S23: -0.0410
REMARK 3 S31: 0.0136 S32: 0.6292 S33: -0.0877
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 5FOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-15.
REMARK 100 THE PDBE ID CODE IS EBI-65631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04
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 : 89319
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 29.70
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.41
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
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 39.51000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.51000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.88500
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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 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 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 165 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 ALA B 544 CA C O CB
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 -13.11 78.38
REMARK 500 CYS A 96 -0.04 -148.61
REMARK 500 ALA A 167 72.34 -152.38
REMARK 500 SER A 203 -123.02 50.14
REMARK 500 ASP A 306 -86.07 -132.85
REMARK 500 ASP A 323 58.09 -107.72
REMARK 500 HIS A 387 59.29 -145.22
REMARK 500 VAL A 407 -63.39 -124.44
REMARK 500 ARG A 525 52.49 37.34
REMARK 500 SER A 541 49.95 -80.30
REMARK 500 PHE B 47 -3.82 69.90
REMARK 500 PRO B 55 150.95 -48.76
REMARK 500 ALA B 62 60.08 -112.71
REMARK 500 CYS B 96 12.07 -142.97
REMARK 500 SER B 203 -121.48 50.60
REMARK 500 ASP B 306 -82.32 -120.08
REMARK 500 GLN B 322 -79.47 -37.98
REMARK 500 LEU B 324 128.73 -170.66
REMARK 500 VAL B 407 -60.89 -124.25
REMARK 500 LYS B 496 116.42 69.24
REMARK 500 SER B 497 -54.54 -148.28
REMARK 500 ASN B 514 -168.00 -164.72
REMARK 500 ALA B 542 -76.32 -123.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GC8 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GC8 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P15 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 601 BOUND TO ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 701 BOUND TO ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 601 BOUND TO ASN B 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FPP RELATED DB: PDB
REMARK 900 STRUCTURE OF A PRE-REACTION TERNAY COMPLEX BETWEEN
REMARK 900 SARIN-ACETYLCHOLINESTERASE AND HI-6
REMARK 900 RELATED ID: 5FPQ RELATED DB: PDB
REMARK 900 STRUCTURE OF HOMO SAPIENS ACETYLCHOLINESTERASE
REMARK 900 PHOSPHONYLATED BY SARIN.
DBREF 5FOQ A 1 548 PDB 5FOQ 5FOQ 1 548
DBREF 5FOQ B 1 548 PDB 5FOQ 5FOQ 1 548
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
MODRES 5FOQ ASN A 350 ASN GLYCOSYLATION SITE
MODRES 5FOQ ASN A 464 ASN GLYCOSYLATION SITE
MODRES 5FOQ ASN B 350 ASN GLYCOSYLATION SITE
HET NAG A 601 14
HET NAG A 701 14
HET GC8 A1543 26
HET PG0 A1544 20
HET PG0 A1545 20
HET NAG B 601 14
HET GC8 B1544 26
HET PG0 B1545 20
HET PG0 B1546 20
HET P15 B1547 48
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GC8 2-(2,4-DICHLOROPHENOXY)-N-[4-(1-PIPERIDINYLMETHYL)
HETNAM 2 GC8 PHENYL]ACETAMIDE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETSYN PG0 PEG 6000
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 GC8 2(C20 H22 CL2 N2 O2)
FORMUL 6 PG0 4(C5 H12 O3)
FORMUL 12 P15 C13 H28 O7
FORMUL 13 HOH *298(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 215 SER A 220 1 6
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 THR A 275 1 11
HELIX 12 12 PRO A 277 HIS A 284 1 8
HELIX 13 13 GLU A 285 LEU A 289 5 5
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 GLY A 342 5 8
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 SER A 541 1 17
HELIX 26 26 ASP B 5 GLN B 7 5 3
HELIX 27 27 VAL B 42 ARG B 46 5 5
HELIX 28 28 PHE B 80 MET B 85 1 6
HELIX 29 29 LEU B 130 ASP B 134 5 5
HELIX 30 30 GLY B 135 GLY B 143 1 9
HELIX 31 31 VAL B 153 LEU B 159 1 7
HELIX 32 32 ASN B 170 ILE B 187 1 18
HELIX 33 33 ALA B 188 PHE B 190 5 3
HELIX 34 34 SER B 203 LEU B 214 1 12
HELIX 35 35 SER B 215 PHE B 222 5 8
HELIX 36 36 ALA B 241 VAL B 255 1 15
HELIX 37 37 ASN B 265 THR B 275 1 11
HELIX 38 38 PRO B 277 ASP B 283 1 7
HELIX 39 39 HIS B 284 LEU B 289 5 6
HELIX 40 40 THR B 311 GLY B 319 1 9
HELIX 41 41 GLY B 335 VAL B 340 1 6
HELIX 42 42 SER B 355 VAL B 367 1 13
HELIX 43 43 SER B 371 THR B 383 1 13
HELIX 44 44 ASP B 390 VAL B 407 1 18
HELIX 45 45 VAL B 407 GLN B 421 1 15
HELIX 46 46 PRO B 440 GLY B 444 5 5
HELIX 47 47 GLU B 450 PHE B 455 1 6
HELIX 48 48 GLY B 456 ASP B 460 5 5
HELIX 49 49 ASP B 460 ASN B 464 5 5
HELIX 50 50 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 ARG B 534 THR B 543 1 10
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
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 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A 701 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -1.41
CISPEP 2 TYR B 105 PRO B 106 0 1.30
CISPEP 3 SER B 497 PRO B 498 0 -10.73
SITE 1 AC1 11 TYR A 72 ASP A 74 GLY A 120 GLY A 121
SITE 2 AC1 11 TYR A 124 GLU A 202 TRP A 286 TYR A 337
SITE 3 AC1 11 PHE A 338 TYR A 341 HOH A2121
SITE 1 AC2 3 ASP A 304 GLY A 305 SER A 309
SITE 1 AC3 3 ARG A 525 THR A 528 GLN B 527
SITE 1 AC4 11 TYR B 72 ASP B 74 GLY B 121 TYR B 124
SITE 2 AC4 11 GLU B 202 TRP B 286 TYR B 337 PHE B 338
SITE 3 AC4 11 TYR B 341 HIS B 447 HOH B2066
SITE 1 AC5 2 TYR B 382 P15 B1547
SITE 1 AC6 2 ASP B 304 SER B 309
SITE 1 AC7 8 LEU A 380 GLN A 527 PHE A 531 PHE A 535
SITE 2 AC7 8 LEU B 380 HIS B 381 THR B 528 PG0 B1545
SITE 1 AC8 4 GLY A 345 SER A 347 ASN A 350 LEU A 353
SITE 1 AC9 1 ASN A 464
SITE 1 BC1 3 ASN B 350 LEU B 353 HOH B2111
CRYST1 79.020 111.770 227.090 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 0.012655 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004404 0.00000
TER 4177 ALA A 542
TER 8338 ALA B 544
MASTER 587 0 10 52 34 0 15 6 8853 2 237 86
END |