| 7r02-pdb | HEADER HYDROLASE 01-FEB-22 7R02
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(3-(DIETHYLAMINO)
TITLE 2 PROPYL)-4-METHYL-3-NITROBENZAMIDE
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
KEYWDS HYDROLASE, COMPLEX, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM
REVDAT 1 27-APR-22 7R02 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 89140
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1760
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 28.7100 - 5.4000 0.98 6961 137 0.1679 0.1719
REMARK 3 2 5.4000 - 4.2900 1.00 6842 134 0.1360 0.1272
REMARK 3 3 4.2900 - 3.7500 1.00 6805 130 0.1461 0.1730
REMARK 3 4 3.7500 - 3.4100 1.00 6732 149 0.1661 0.1989
REMARK 3 5 3.4100 - 3.1600 1.00 6721 113 0.1877 0.1981
REMARK 3 6 3.1600 - 2.9800 1.00 6709 154 0.1941 0.2059
REMARK 3 7 2.9800 - 2.8300 1.00 6686 138 0.1921 0.2180
REMARK 3 8 2.8300 - 2.7000 1.00 6683 135 0.1889 0.2302
REMARK 3 9 2.7000 - 2.6000 1.00 6654 149 0.1805 0.1813
REMARK 3 10 2.6000 - 2.5100 1.00 6650 138 0.1816 0.2040
REMARK 3 11 2.5100 - 2.4300 1.00 6642 118 0.1931 0.2373
REMARK 3 12 2.4300 - 2.3600 1.00 6652 133 0.2056 0.2461
REMARK 3 13 2.3600 - 2.3000 1.00 6643 132 0.2206 0.2379
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.59
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4681 12.6796 40.8482
REMARK 3 T TENSOR
REMARK 3 T11: 0.4513 T22: 0.3609
REMARK 3 T33: 0.3135 T12: -0.0199
REMARK 3 T13: -0.0363 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 3.0680 L22: 1.8657
REMARK 3 L33: 4.2354 L12: -0.6490
REMARK 3 L13: -0.7748 L23: -0.8847
REMARK 3 S TENSOR
REMARK 3 S11: -0.1283 S12: -0.4000 S13: -0.0411
REMARK 3 S21: 0.3956 S22: 0.0626 S23: 0.0482
REMARK 3 S31: 0.0050 S32: 0.0524 S33: 0.0633
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5833 10.7922 24.0130
REMARK 3 T TENSOR
REMARK 3 T11: 0.3277 T22: 0.2999
REMARK 3 T33: 0.3212 T12: 0.0110
REMARK 3 T13: -0.0174 T23: 0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 1.5406 L22: 1.0660
REMARK 3 L33: 2.8973 L12: 0.0314
REMARK 3 L13: -0.4656 L23: -0.1635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: -0.1196 S13: -0.0436
REMARK 3 S21: 0.0712 S22: 0.0012 S23: -0.0591
REMARK 3 S31: 0.1712 S32: 0.0657 S33: 0.0628
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1463 17.7018 11.9349
REMARK 3 T TENSOR
REMARK 3 T11: 0.2770 T22: 0.4227
REMARK 3 T33: 0.3717 T12: 0.0173
REMARK 3 T13: 0.0511 T23: 0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 3.8645 L22: 2.8651
REMARK 3 L33: 4.3727 L12: 2.0992
REMARK 3 L13: 1.9989 L23: 1.0647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0951 S12: 0.2355 S13: 0.1846
REMARK 3 S21: -0.1752 S22: -0.0689 S23: -0.3164
REMARK 3 S31: -0.2491 S32: 0.6441 S33: 0.1910
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6078 -1.2967 11.3739
REMARK 3 T TENSOR
REMARK 3 T11: 0.5758 T22: 0.3154
REMARK 3 T33: 0.3492 T12: 0.0188
REMARK 3 T13: 0.0584 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 4.7656 L22: 2.2809
REMARK 3 L33: 2.1940 L12: 0.2076
REMARK 3 L13: 0.7023 L23: 0.9505
REMARK 3 S TENSOR
REMARK 3 S11: -0.1107 S12: 0.0229 S13: -0.7572
REMARK 3 S21: 0.0574 S22: 0.0745 S23: -0.1274
REMARK 3 S31: 0.7629 S32: 0.0795 S33: -0.0076
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2259 21.7301 -3.8994
REMARK 3 T TENSOR
REMARK 3 T11: 0.2966 T22: 0.3910
REMARK 3 T33: 0.3523 T12: -0.0443
REMARK 3 T13: -0.0335 T23: 0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 1.8747 L22: 2.7165
REMARK 3 L33: 5.2371 L12: -0.2033
REMARK 3 L13: -0.1740 L23: -0.2726
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.2908 S13: 0.1599
REMARK 3 S21: -0.1963 S22: 0.0448 S23: 0.0557
REMARK 3 S31: -0.2500 S32: 0.1141 S33: 0.0357
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 383 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4993 15.0600 10.9870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2198 T22: 0.3723
REMARK 3 T33: 0.3332 T12: -0.0453
REMARK 3 T13: -0.0310 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.1716 L22: 1.2248
REMARK 3 L33: 4.4496 L12: -0.0768
REMARK 3 L13: -0.1448 L23: -0.5187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0391 S12: 0.0615 S13: -0.0315
REMARK 3 S21: -0.0453 S22: 0.0483 S23: 0.2287
REMARK 3 S31: 0.0571 S32: -0.6153 S33: -0.0247
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0544 1.1410 13.5715
REMARK 3 T TENSOR
REMARK 3 T11: 0.4956 T22: 0.6384
REMARK 3 T33: 0.5265 T12: -0.2964
REMARK 3 T13: 0.0081 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 6.6154 L22: 9.0675
REMARK 3 L33: 5.3179 L12: -1.6819
REMARK 3 L13: 0.9371 L23: -1.9038
REMARK 3 S TENSOR
REMARK 3 S11: -0.1729 S12: -0.0563 S13: -0.7043
REMARK 3 S21: 0.4451 S22: -0.0297 S23: 1.0750
REMARK 3 S31: 0.7856 S32: -1.6084 S33: 0.2760
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2431 6.2604 -1.5392
REMARK 3 T TENSOR
REMARK 3 T11: 0.4676 T22: 0.5650
REMARK 3 T33: 0.3345 T12: -0.0244
REMARK 3 T13: -0.1256 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 9.1061 L22: 3.7762
REMARK 3 L33: 4.9757 L12: -3.6254
REMARK 3 L13: -5.7248 L23: 3.3480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0805 S12: 0.0401 S13: -0.3287
REMARK 3 S21: -0.3338 S22: -0.1429 S23: 0.1881
REMARK 3 S31: 0.0440 S32: -0.1275 S33: 0.0528
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0140 6.0047 -61.8142
REMARK 3 T TENSOR
REMARK 3 T11: 0.4932 T22: 0.5839
REMARK 3 T33: 0.4306 T12: 0.0337
REMARK 3 T13: -0.1233 T23: -0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 5.4635 L22: 1.9660
REMARK 3 L33: 5.0045 L12: -1.2352
REMARK 3 L13: -2.9721 L23: 0.7673
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: 0.3714 S13: 0.1194
REMARK 3 S21: -0.3460 S22: -0.1431 S23: 0.3431
REMARK 3 S31: -0.1699 S32: -0.8155 S33: 0.0182
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4628 1.0096 -51.6660
REMARK 3 T TENSOR
REMARK 3 T11: 0.3527 T22: 0.4269
REMARK 3 T33: 0.3497 T12: -0.0390
REMARK 3 T13: -0.0633 T23: -0.1059
REMARK 3 L TENSOR
REMARK 3 L11: 1.2279 L22: 1.7822
REMARK 3 L33: 3.6910 L12: -0.2943
REMARK 3 L13: 0.1133 L23: 0.4167
REMARK 3 S TENSOR
REMARK 3 S11: 0.1074 S12: 0.1690 S13: -0.1856
REMARK 3 S21: -0.0921 S22: -0.1563 S23: 0.2994
REMARK 3 S31: 0.3461 S32: -0.3868 S33: 0.0351
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3288 6.8437 -54.1065
REMARK 3 T TENSOR
REMARK 3 T11: 0.3845 T22: 0.4483
REMARK 3 T33: 0.2611 T12: 0.0033
REMARK 3 T13: -0.0255 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 5.0488 L22: 4.2914
REMARK 3 L33: 3.1096 L12: -3.1586
REMARK 3 L13: 1.5952 L23: -0.4107
REMARK 3 S TENSOR
REMARK 3 S11: 0.1261 S12: 0.5369 S13: 0.0391
REMARK 3 S21: -0.1041 S22: -0.1530 S23: -0.0623
REMARK 3 S31: -0.0686 S32: 0.3725 S33: 0.0221
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9927 8.6608 -44.1062
REMARK 3 T TENSOR
REMARK 3 T11: 0.3118 T22: 0.3697
REMARK 3 T33: 0.2618 T12: -0.0342
REMARK 3 T13: -0.0185 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 2.2646 L22: 2.4812
REMARK 3 L33: 3.3891 L12: -1.0783
REMARK 3 L13: 0.1975 L23: 0.4472
REMARK 3 S TENSOR
REMARK 3 S11: 0.0806 S12: 0.1060 S13: 0.0744
REMARK 3 S21: 0.0772 S22: -0.0070 S23: -0.1915
REMARK 3 S31: -0.1426 S32: 0.3472 S33: -0.0549
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0560 -9.8181 -47.7004
REMARK 3 T TENSOR
REMARK 3 T11: 0.5755 T22: 0.5406
REMARK 3 T33: 0.4645 T12: 0.1644
REMARK 3 T13: -0.1387 T23: -0.0987
REMARK 3 L TENSOR
REMARK 3 L11: 1.7085 L22: 4.0286
REMARK 3 L33: 5.3661 L12: -1.3191
REMARK 3 L13: -0.1343 L23: 1.4932
REMARK 3 S TENSOR
REMARK 3 S11: 0.1362 S12: 0.0905 S13: -0.2898
REMARK 3 S21: 0.1611 S22: -0.0034 S23: -0.1545
REMARK 3 S31: 0.8006 S32: 0.7894 S33: -0.1416
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 298 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2735 14.3867 -40.2684
REMARK 3 T TENSOR
REMARK 3 T11: 0.3961 T22: 0.4297
REMARK 3 T33: 0.4258 T12: -0.0786
REMARK 3 T13: -0.0594 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 4.5813 L22: 1.2427
REMARK 3 L33: 4.3620 L12: -2.2370
REMARK 3 L13: -1.4711 L23: 0.7216
REMARK 3 S TENSOR
REMARK 3 S11: 0.1746 S12: 0.3398 S13: 0.6656
REMARK 3 S21: 0.0788 S22: -0.0884 S23: -0.4213
REMARK 3 S31: -0.4362 S32: 0.4349 S33: -0.0738
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1621 1.9477 -26.6855
REMARK 3 T TENSOR
REMARK 3 T11: 0.4642 T22: 0.3671
REMARK 3 T33: 0.3385 T12: -0.0879
REMARK 3 T13: 0.0204 T23: -0.0694
REMARK 3 L TENSOR
REMARK 3 L11: 1.7132 L22: 1.7028
REMARK 3 L33: 3.2135 L12: -0.3810
REMARK 3 L13: 0.9831 L23: -0.1434
REMARK 3 S TENSOR
REMARK 3 S11: 0.1926 S12: -0.1810 S13: -0.2404
REMARK 3 S21: 0.2435 S22: -0.1045 S23: 0.1923
REMARK 3 S31: 0.4977 S32: -0.2954 S33: -0.0922
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9492 22.4832 -28.7797
REMARK 3 T TENSOR
REMARK 3 T11: 0.4940 T22: 0.3415
REMARK 3 T33: 0.4212 T12: 0.0192
REMARK 3 T13: 0.0104 T23: -0.1041
REMARK 3 L TENSOR
REMARK 3 L11: 7.6967 L22: 4.5025
REMARK 3 L33: 5.5162 L12: -1.2363
REMARK 3 L13: 0.5151 L23: -3.1977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: -0.4090 S13: 0.8090
REMARK 3 S21: -0.0086 S22: 0.0159 S23: 0.4135
REMARK 3 S31: -0.4673 S32: -0.4849 S33: -0.0339
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2033 11.1954 -21.6106
REMARK 3 T TENSOR
REMARK 3 T11: 0.4807 T22: 0.3593
REMARK 3 T33: 0.2503 T12: -0.0657
REMARK 3 T13: 0.0225 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 9.2903 L22: 1.8443
REMARK 3 L33: 4.1647 L12: -1.1145
REMARK 3 L13: 4.7154 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: 0.3432 S13: -0.4468
REMARK 3 S21: 0.0970 S22: 0.0301 S23: -0.0431
REMARK 3 S31: 0.0873 S32: 0.3307 S33: -0.1042
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 7R02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-13
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) : 1.03763
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 : 89430
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.6000
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) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
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 (%): 70.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
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 39.42600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.61650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.55250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.61650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.42600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.55250
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 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
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 NE CZ NH1 NH2
REMARK 470 GLN A 322 CG CD OE1 NE2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
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 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 -5.25 75.94
REMARK 500 PHE A 158 -2.84 -140.67
REMARK 500 ALA A 167 70.83 -152.04
REMARK 500 SER A 203 -120.43 54.79
REMARK 500 ASP A 306 -87.16 -125.44
REMARK 500 VAL A 407 -60.61 -128.71
REMARK 500 HIS A 447 121.00 -39.70
REMARK 500 ARG A 493 -94.28 -83.30
REMARK 500 ASP A 494 85.90 -39.75
REMARK 500 PHE B 47 -1.41 74.19
REMARK 500 SER B 203 -123.32 56.79
REMARK 500 ASP B 306 -85.26 -132.41
REMARK 500 VAL B 407 -58.97 -125.91
REMARK 500 HIS B 447 117.07 -39.99
REMARK 500 SER B 497 59.64 -104.23
REMARK 500
REMARK 500 REMARK: NULL
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 PG0 B 609
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7QYN RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 2-((HYDROXYIMINO)
REMARK 900 METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)PYRIDINIUM
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: 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 7R02 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7R02 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 I62 A 601 21
HET NAG A 602 14
HET NAG A 603 14
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 EDO A 609 4
HET I62 B 601 21
HET NAG B 602 14
HET NAG B 603 14
HET PG0 B 604 8
HET PG0 B 605 8
HET PG0 B 606 8
HET PG0 B 607 8
HET PG0 B 608 8
HET PG0 B 609 6
HET 9YU B 610 23
HETNAM I62 ~{N}-[(~{E})-3-(DIETHYLAMINO)PROP-2-ENYL]-4-METHYL-3-
HETNAM 2 I62 NITRO-BENZAMIDE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 9YU 2-[2-[2-[2-[2-[2-(2-METHOXYETHOXY)
HETNAM 2 9YU ETHOXY]ETHOXY]ETHOXY]ETHOXY]ETHOXY]ETHANOL
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
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 I62 2( 1+)
FORMUL 4 NAG 4(C8 H15 N O6)
FORMUL 6 PG0 11(C5 H12 O3)
FORMUL 11 EDO C2 H6 O2
FORMUL 21 9YU C15 H32 O8
FORMUL 22 HOH *346(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 SER A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 TRP A 286 1 10
HELIX 14 AB5 HIS A 287 LEU A 289 5 3
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 THR A 543 1 10
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 GLY B 143 1 9
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 ASN B 265 THR B 275 1 11
HELIX 39 AE3 PRO B 277 TRP B 286 1 10
HELIX 40 AE4 THR B 311 GLY B 319 1 9
HELIX 41 AE5 GLY B 335 VAL B 340 1 6
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASN B 464 5 9
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 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 TRP A 117 O VAL A 147
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 VAL B 29 N LEU B 22
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 LEU B 146 N TRP B 102
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 2.10
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.08
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.02
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A 603 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.46
LINK ND2 ASN B 464 C1 NAG B 603 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -7.08
CISPEP 2 TYR B 105 PRO B 106 0 2.35
CRYST1 78.852 111.105 227.233 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 0.012682 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004401 0.00000
TER 4238 THR A 543
TER 8471 THR B 543
MASTER 546 0 19 51 32 0 0 6 8896 2 227 84
END
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