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HEADER HYDROLASE 28-JAN-22 7QYN
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
TITLE 2 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, COMPLEX, REACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM
REVDAT 1 27-APR-22 7QYN 0
JRNL AUTH C.LINDGREN,N.FORSGREN,N.HOSTER,C.AKFUR,E.ARTURSSON,
JRNL AUTH 2 L.EDVINSSON,R.SVENSSON,F.WOREK,F.EKSTROM,A.LINUSSON
JRNL TITL BROAD-SPECTRUM ANTIDOTE DISCOVERY BY UNTANGLING THE
JRNL TITL 2 REACTIVATION MECHANISM OF NERVE AGENT INHIBITED
JRNL TITL 3 ACETYLCHOLINESTERASE.
JRNL REF CHEMISTRY 2022
JRNL REFN ISSN 0947-6539
JRNL PMID 35420233
JRNL DOI 10.1002/CHEM.202200678
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 69463
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1396
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 28.6921 - 5.3754 0.98 7063 139 0.1534 0.1692
REMARK 3 2 5.3754 - 4.2712 1.00 6907 135 0.1277 0.1379
REMARK 3 3 4.2712 - 3.7326 1.00 6850 129 0.1432 0.1818
REMARK 3 4 3.7326 - 3.3919 1.00 6808 151 0.1638 0.2080
REMARK 3 5 3.3919 - 3.1491 1.00 6795 113 0.1872 0.2435
REMARK 3 6 3.1491 - 2.9636 1.00 6755 157 0.1953 0.2195
REMARK 3 7 2.9636 - 2.8154 1.00 6740 139 0.2040 0.2745
REMARK 3 8 2.8154 - 2.6929 1.00 6744 134 0.2119 0.2454
REMARK 3 9 2.6929 - 2.5893 1.00 6708 150 0.2250 0.3099
REMARK 3 10 2.5893 - 2.5000 1.00 6697 149 0.2364 0.2818
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.88
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 : 0.007 8859
REMARK 3 ANGLE : 1.100 12054
REMARK 3 CHIRALITY : 0.042 1292
REMARK 3 PLANARITY : 0.006 1572
REMARK 3 DIHEDRAL : 17.508 3242
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7940 11.0638 29.0937
REMARK 3 T TENSOR
REMARK 3 T11: 0.3090 T22: 0.2919
REMARK 3 T33: 0.3042 T12: 0.0051
REMARK 3 T13: -0.0220 T23: 0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 1.5398 L22: 1.3391
REMARK 3 L33: 3.0957 L12: 0.1290
REMARK 3 L13: -0.2058 L23: -0.0605
REMARK 3 S TENSOR
REMARK 3 S11: -0.0152 S12: -0.1909 S13: -0.0156
REMARK 3 S21: 0.1758 S22: 0.0089 S23: -0.0202
REMARK 3 S31: 0.1319 S32: 0.0006 S33: 0.0068
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 229:324)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2664 9.7619 10.3101
REMARK 3 T TENSOR
REMARK 3 T11: 0.3123 T22: 0.2551
REMARK 3 T33: 0.3113 T12: 0.0983
REMARK 3 T13: 0.0447 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 5.2838 L22: 2.0334
REMARK 3 L33: 3.5857 L12: 1.9425
REMARK 3 L13: 0.8582 L23: 0.5043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1231 S12: 0.2030 S13: -0.2937
REMARK 3 S21: -0.2014 S22: 0.0619 S23: -0.2231
REMARK 3 S31: 0.2311 S32: 0.2685 S33: 0.0490
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 325:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6626 16.7597 6.5454
REMARK 3 T TENSOR
REMARK 3 T11: 0.2535 T22: 0.3185
REMARK 3 T33: 0.3427 T12: -0.0290
REMARK 3 T13: -0.0446 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.5267 L22: 1.0746
REMARK 3 L33: 4.0634 L12: -0.0455
REMARK 3 L13: -0.2257 L23: -0.3402
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: 0.0651 S13: 0.0557
REMARK 3 S21: -0.1354 S22: 0.0554 S23: 0.1753
REMARK 3 S31: 0.0566 S32: -0.4694 S33: -0.0380
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7833 1.1676 13.5914
REMARK 3 T TENSOR
REMARK 3 T11: 0.4107 T22: 0.6459
REMARK 3 T33: 0.5143 T12: -0.2282
REMARK 3 T13: 0.0065 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 7.6979 L22: 9.4201
REMARK 3 L33: 5.4020 L12: -0.9285
REMARK 3 L13: 2.4653 L23: -1.0567
REMARK 3 S TENSOR
REMARK 3 S11: -0.2524 S12: -0.2576 S13: -0.6865
REMARK 3 S21: 0.2956 S22: 0.1615 S23: 1.0369
REMARK 3 S31: 0.5536 S32: -1.5333 S33: 0.1957
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4781 6.2596 -1.1945
REMARK 3 T TENSOR
REMARK 3 T11: 0.4144 T22: 0.5016
REMARK 3 T33: 0.3536 T12: 0.0004
REMARK 3 T13: -0.1504 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 4.9755 L22: 2.7617
REMARK 3 L33: 6.6670 L12: -1.8453
REMARK 3 L13: -4.8216 L23: 2.9065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: 0.0498 S13: -0.3530
REMARK 3 S21: -0.2721 S22: -0.0813 S23: 0.2356
REMARK 3 S31: 0.2600 S32: -0.0826 S33: 0.0850
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6257 6.3158 -62.0337
REMARK 3 T TENSOR
REMARK 3 T11: 0.4934 T22: 0.5372
REMARK 3 T33: 0.4172 T12: 0.0102
REMARK 3 T13: -0.1023 T23: -0.1356
REMARK 3 L TENSOR
REMARK 3 L11: 8.9210 L22: 2.4542
REMARK 3 L33: 4.7964 L12: -2.4251
REMARK 3 L13: -2.5183 L23: 0.5073
REMARK 3 S TENSOR
REMARK 3 S11: 0.1272 S12: 0.5106 S13: 0.0816
REMARK 3 S21: -0.3084 S22: -0.1675 S23: 0.2787
REMARK 3 S31: -0.2817 S32: -0.8066 S33: 0.0002
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 46:71)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1501 0.3718 -61.7611
REMARK 3 T TENSOR
REMARK 3 T11: 0.4293 T22: 0.4972
REMARK 3 T33: 0.2961 T12: -0.0077
REMARK 3 T13: -0.0530 T23: -0.0921
REMARK 3 L TENSOR
REMARK 3 L11: 1.2622 L22: 1.4924
REMARK 3 L33: 3.5043 L12: -1.0420
REMARK 3 L13: 1.5372 L23: -0.7667
REMARK 3 S TENSOR
REMARK 3 S11: 0.1283 S12: 0.2224 S13: -0.2738
REMARK 3 S21: -0.3710 S22: -0.1909 S23: 0.0923
REMARK 3 S31: 0.3238 S32: -0.2593 S33: 0.0114
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 72:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0554 1.5872 -48.6782
REMARK 3 T TENSOR
REMARK 3 T11: 0.3526 T22: 0.4235
REMARK 3 T33: 0.3473 T12: -0.0341
REMARK 3 T13: -0.0461 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 1.8333 L22: 2.0593
REMARK 3 L33: 3.0938 L12: -0.1491
REMARK 3 L13: -0.2292 L23: 0.6637
REMARK 3 S TENSOR
REMARK 3 S11: 0.1940 S12: 0.2186 S13: -0.2066
REMARK 3 S21: -0.0466 S22: -0.2507 S23: 0.3199
REMARK 3 S31: 0.2885 S32: -0.4922 S33: 0.0433
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 159:240)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3037 11.5423 -48.9488
REMARK 3 T TENSOR
REMARK 3 T11: 0.3683 T22: 0.3141
REMARK 3 T33: 0.2734 T12: -0.0399
REMARK 3 T13: -0.0275 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 3.8650 L22: 3.3772
REMARK 3 L33: 2.8627 L12: -1.9697
REMARK 3 L13: 0.3567 L23: -0.5356
REMARK 3 S TENSOR
REMARK 3 S11: 0.1146 S12: 0.3639 S13: 0.0897
REMARK 3 S21: -0.1445 S22: -0.0871 S23: -0.1096
REMARK 3 S31: -0.3371 S32: 0.1211 S33: -0.0366
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 241:297)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4497 -9.0938 -46.6936
REMARK 3 T TENSOR
REMARK 3 T11: 0.5140 T22: 0.5253
REMARK 3 T33: 0.4820 T12: 0.1258
REMARK 3 T13: -0.1320 T23: -0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 1.2583 L22: 3.7425
REMARK 3 L33: 7.9466 L12: -1.2153
REMARK 3 L13: -0.4706 L23: 3.5428
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: 0.0892 S13: -0.1971
REMARK 3 S21: 0.2973 S22: 0.0759 S23: -0.2318
REMARK 3 S31: 0.7810 S32: 0.9238 S33: -0.1037
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 298:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3569 14.3341 -40.4084
REMARK 3 T TENSOR
REMARK 3 T11: 0.3841 T22: 0.4340
REMARK 3 T33: 0.4545 T12: -0.0668
REMARK 3 T13: -0.0769 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 4.5736 L22: 2.1698
REMARK 3 L33: 4.4625 L12: -2.0405
REMARK 3 L13: -2.1898 L23: 1.6490
REMARK 3 S TENSOR
REMARK 3 S11: 0.2696 S12: 0.0687 S13: 0.6571
REMARK 3 S21: 0.0718 S22: -0.0478 S23: -0.5788
REMARK 3 S31: -0.6426 S32: 0.5750 S33: -0.2309
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 332:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2655 -6.2416 -21.9715
REMARK 3 T TENSOR
REMARK 3 T11: 0.7431 T22: 0.3359
REMARK 3 T33: 0.3492 T12: 0.0266
REMARK 3 T13: -0.0575 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 6.4549 L22: 6.9398
REMARK 3 L33: 2.7499 L12: 3.1866
REMARK 3 L13: 0.8229 L23: 0.1915
REMARK 3 S TENSOR
REMARK 3 S11: 0.4268 S12: -0.1425 S13: -0.5940
REMARK 3 S21: 0.5146 S22: -0.1214 S23: -0.1566
REMARK 3 S31: 0.8168 S32: 0.1060 S33: -0.3124
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 383:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7060 5.8656 -29.4107
REMARK 3 T TENSOR
REMARK 3 T11: 0.3653 T22: 0.3732
REMARK 3 T33: 0.3201 T12: -0.0553
REMARK 3 T13: 0.0341 T23: -0.1115
REMARK 3 L TENSOR
REMARK 3 L11: 2.0641 L22: 2.7999
REMARK 3 L33: 3.8096 L12: -0.1083
REMARK 3 L13: 0.5081 L23: -0.2420
REMARK 3 S TENSOR
REMARK 3 S11: 0.1559 S12: -0.1947 S13: -0.1111
REMARK 3 S21: 0.2509 S22: -0.1250 S23: 0.2438
REMARK 3 S31: 0.2105 S32: -0.4847 S33: -0.0496
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0318 22.4255 -28.9380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5086 T22: 0.4069
REMARK 3 T33: 0.4078 T12: 0.0635
REMARK 3 T13: -0.0446 T23: -0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 8.9405 L22: 4.7865
REMARK 3 L33: 6.2358 L12: -1.2527
REMARK 3 L13: -0.3731 L23: -2.1245
REMARK 3 S TENSOR
REMARK 3 S11: 0.4106 S12: -0.3870 S13: 0.7560
REMARK 3 S21: -0.2632 S22: -0.2513 S23: 0.4796
REMARK 3 S31: -0.4383 S32: -0.7148 S33: -0.1239
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1823 11.2749 -21.7890
REMARK 3 T TENSOR
REMARK 3 T11: 0.5236 T22: 0.3450
REMARK 3 T33: 0.2558 T12: -0.0610
REMARK 3 T13: 0.0126 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 8.7134 L22: 1.7104
REMARK 3 L33: 5.3632 L12: 0.2319
REMARK 3 L13: 6.7596 L23: 0.2378
REMARK 3 S TENSOR
REMARK 3 S11: 0.1086 S12: 0.3616 S13: -0.1658
REMARK 3 S21: 0.2377 S22: -0.1083 S23: -0.0912
REMARK 3 S31: -0.0092 S32: 0.2478 S33: -0.0206
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 7QYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-12
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 : MAX II
REMARK 200 BEAMLINE : I911-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04088
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69672
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.55300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
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 (%): 70.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-30 % (W/V) PEG750MME 0.1 M HEPES PH
REMARK 280 6.9-7.1, VAPOR DIFFUSION, HANGING 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 39.29750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.95500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.38200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.95500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.29750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.38200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 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 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 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 CG CD CE NZ
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 OD2 ASP B 390 ND1 HIS B 393 2.19
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 -3.85 71.84
REMARK 500 ALA A 167 71.18 -155.29
REMARK 500 SER A 203 -120.07 55.10
REMARK 500 ASP A 306 -86.60 -127.31
REMARK 500 VAL A 407 -62.75 -126.50
REMARK 500 ARG A 493 30.81 -80.74
REMARK 500 SER A 495 -38.11 -134.32
REMARK 500 ARG A 525 52.97 38.95
REMARK 500 PRO B 55 156.63 -48.04
REMARK 500 CYS B 96 11.78 -146.80
REMARK 500 ALA B 167 68.48 -156.28
REMARK 500 SER B 203 -122.63 49.81
REMARK 500 ASP B 306 -79.04 -135.60
REMARK 500 VAL B 407 -62.93 -123.83
REMARK 500 ASN B 514 -165.77 -163.22
REMARK 500 ARG B 525 60.96 31.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7R0A RELATED DB: PDB
REMARK 900 SARIN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
REMARK 900 PYRIDINIUM
REMARK 900 RELATED ID: 7R2F RELATED DB: PDB
REMARK 900 TABUN-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-
REMARK 900 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
REMARK 900 PYRIDINIUM
REMARK 900 RELATED ID: 7R3C RELATED DB: PDB
REMARK 900 VX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
REMARK 900 RELATED ID: 7R02 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH N-(3-(DIETHYLAMINO)PROPYL)-4-
REMARK 900 METHYL-3-NITROBENZAMIDE
REMARK 900 RELATED ID: 7R4E RELATED DB: PDB
REMARK 900 RVX-INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
DBREF 7QYN A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7QYN B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET NAG A 601 14
HET NAG A 602 14
HET I1X A 603 27
HET PG0 A 604 8
HET PG0 A 605 8
HET PG0 A 606 8
HET PG0 A 607 8
HET PG0 A 608 8
HET PG0 A 609 8
HET PG0 A 610 8
HET NAG B 601 14
HET NAG B 602 14
HET I1X B 603 27
HET PG0 B 604 8
HET PG0 B 605 8
HET PG0 B 606 8
HET PG0 B 607 8
HET TOE B 608 11
HET TOE B 609 11
HET P15 B 610 20
HET CL B 611 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM I1X 4-METHYL-3-NITRO-~{N}-[(2~{E},4~{E})-5-[2-
HETNAM 2 I1X [(OXIDANYLAMINO)METHYL]PYRIDIN-1-YL]PENTA-2,4-
HETNAM 3 I1X DIENYL]BENZAMIDE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN PG0 PEG 6000
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 I1X 2(C19 H23 N4 O4 1+)
FORMUL 6 PG0 11(C5 H12 O3)
FORMUL 20 TOE 2(C7 H16 O4)
FORMUL 22 P15 C13 H28 O7
FORMUL 23 CL CL 1-
FORMUL 24 HOH *288(H2 O)
HELIX 1 AA1 VAL A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 GLY A 143 1 9
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 ILE A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 LEU A 214 1 12
HELIX 9 AA9 SER A 215 SER A 220 1 6
HELIX 10 AB1 SER A 240 VAL A 255 1 16
HELIX 11 AB2 ASP A 266 THR A 275 1 10
HELIX 12 AB3 PRO A 277 TRP A 286 1 10
HELIX 13 AB4 HIS A 287 LEU A 289 5 3
HELIX 14 AB5 THR A 311 THR A 318 1 8
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASN A 464 5 9
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ALA A 542 1 18
HELIX 25 AC7 ASP B 5 GLN B 7 5 3
HELIX 26 AC8 VAL B 42 ARG B 46 5 5
HELIX 27 AC9 PHE B 80 MET B 85 1 6
HELIX 28 AD1 LEU B 130 ASP B 134 5 5
HELIX 29 AD2 GLY B 135 GLY B 143 1 9
HELIX 30 AD3 VAL B 153 LEU B 159 1 7
HELIX 31 AD4 ASN B 170 ILE B 187 1 18
HELIX 32 AD5 ALA B 188 PHE B 190 5 3
HELIX 33 AD6 SER B 203 LEU B 214 1 12
HELIX 34 AD7 SER B 215 SER B 220 1 6
HELIX 35 AD8 SER B 240 VAL B 255 1 16
HELIX 36 AD9 ASP B 266 THR B 275 1 10
HELIX 37 AE1 PRO B 277 TRP B 286 1 10
HELIX 38 AE2 THR B 311 GLY B 319 1 9
HELIX 39 AE3 GLY B 335 VAL B 340 1 6
HELIX 40 AE4 SER B 355 VAL B 367 1 13
HELIX 41 AE5 SER B 371 THR B 383 1 13
HELIX 42 AE6 ASP B 390 VAL B 407 1 18
HELIX 43 AE7 VAL B 407 GLN B 421 1 15
HELIX 44 AE8 PRO B 440 GLY B 444 5 5
HELIX 45 AE9 GLU B 450 PHE B 455 1 6
HELIX 46 AF1 GLY B 456 ASN B 464 5 9
HELIX 47 AF2 THR B 466 GLY B 487 1 22
HELIX 48 AF3 ARG B 525 ARG B 534 1 10
HELIX 49 AF4 ARG B 534 THR B 543 1 10
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 ALA A 31 N ILE A 20
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 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O SER A 196 N VAL A 114
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 PHE A 430 N VAL A 330
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 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA511 ILE B 20 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O ALA B 31 N ILE B 20
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.02
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.02
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.46
LINK ND2 ASN B 464 C1 NAG B 602 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -5.48
CISPEP 2 TYR B 105 PRO B 106 0 6.67
CISPEP 3 SER B 497 PRO B 498 0 13.29
CRYST1 78.595 110.764 227.910 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 0.012723 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004388 0.00000
TER 4196 THR A 543
TER 8370 THR B 543
MASTER 517 0 21 49 32 0 0 6 8862 2 256 84
END |