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HEADER HYDROLASE 04-FEB-22 7R2F
TITLE STRUCTURE OF TABUN INHIBITED ACETYLCHOLINESTERASE IN COMPLEX WITH 2-
TITLE 2 ((HYDROXYIMINO)METHYL)-1-(5-(4-METHYL-3-NITROBENZAMIDO)PENTYL)
TITLE 3 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;
COMPND 7 OTHER_DETAILS: TABUN PHOSPHYLATION PRODUCT COVALENTLY ATTACHED TO
COMPND 8 SER203
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: HEK293;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HYDROLASE, COMPLEX, TABUN PHOSPHYLATED, REACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,C.LINDGREN,L.EDVINSSON,A.LINUSSON,F.EKSTROM
REVDAT 1 27-APR-22 7R2F 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 1.8.4_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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 85193
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1688
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 46.1411 - 5.2633 0.91 6950 140 0.1536 0.1985
REMARK 3 2 5.2633 - 4.1785 0.93 6915 141 0.1280 0.1384
REMARK 3 3 4.1785 - 3.6506 0.94 6915 134 0.1465 0.1686
REMARK 3 4 3.6506 - 3.3169 0.95 6926 133 0.1685 0.1915
REMARK 3 5 3.3169 - 3.0792 0.95 6943 140 0.1964 0.2225
REMARK 3 6 3.0792 - 2.8977 0.96 6955 151 0.2053 0.2479
REMARK 3 7 2.8977 - 2.7526 0.96 6966 147 0.2064 0.2524
REMARK 3 8 2.7526 - 2.6328 0.97 6980 145 0.2094 0.2613
REMARK 3 9 2.6328 - 2.5314 0.97 6969 151 0.2138 0.2329
REMARK 3 10 2.5314 - 2.4441 0.97 6973 137 0.2235 0.2745
REMARK 3 11 2.4441 - 2.3677 0.97 7011 135 0.2436 0.3437
REMARK 3 12 2.3677 - 2.3000 0.97 7002 134 0.2715 0.3166
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.57
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 9543
REMARK 3 ANGLE : 1.083 13106
REMARK 3 CHIRALITY : 0.042 1429
REMARK 3 PLANARITY : 0.006 1729
REMARK 3 DIHEDRAL : 16.090 3546
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4649 15.1610 31.5171
REMARK 3 T TENSOR
REMARK 3 T11: 0.4008 T22: 0.3146
REMARK 3 T33: 0.2592 T12: 0.0204
REMARK 3 T13: -0.0243 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 1.8735 L22: 1.3152
REMARK 3 L33: 3.4595 L12: 0.1759
REMARK 3 L13: -0.3549 L23: -0.3324
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: -0.2243 S13: 0.1415
REMARK 3 S21: 0.2208 S22: 0.0642 S23: 0.0470
REMARK 3 S31: -0.1046 S32: -0.0540 S33: 0.0296
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1300 8.7732 16.9109
REMARK 3 T TENSOR
REMARK 3 T11: 0.4077 T22: 0.2602
REMARK 3 T33: 0.2652 T12: 0.0881
REMARK 3 T13: 0.0012 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 2.5215 L22: 1.2765
REMARK 3 L33: 3.0575 L12: 0.8687
REMARK 3 L13: -0.4461 L23: -0.8013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0979 S12: 0.1042 S13: -0.1377
REMARK 3 S21: -0.0989 S22: 0.0084 S23: -0.1473
REMARK 3 S31: 0.3659 S32: 0.2160 S33: 0.1124
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7316 3.9920 10.4732
REMARK 3 T TENSOR
REMARK 3 T11: 0.5467 T22: 0.3890
REMARK 3 T33: 0.2689 T12: -0.0386
REMARK 3 T13: 0.0207 T23: -0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 5.7543 L22: 1.4279
REMARK 3 L33: 4.3644 L12: -0.2446
REMARK 3 L13: 0.2998 L23: -1.9788
REMARK 3 S TENSOR
REMARK 3 S11: -0.1291 S12: -0.0100 S13: -0.7268
REMARK 3 S21: -0.2045 S22: 0.2219 S23: 0.1357
REMARK 3 S31: 0.5997 S32: -0.1709 S33: -0.0782
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 342 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4946 17.1667 6.3195
REMARK 3 T TENSOR
REMARK 3 T11: 0.3047 T22: 0.4183
REMARK 3 T33: 0.3252 T12: -0.0432
REMARK 3 T13: -0.0697 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.2246 L22: 1.2343
REMARK 3 L33: 5.1434 L12: -0.2348
REMARK 3 L13: -0.4384 L23: -0.4414
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.1435 S13: 0.0584
REMARK 3 S21: -0.1522 S22: 0.0493 S23: 0.1509
REMARK 3 S31: 0.0116 S32: -0.4962 S33: -0.0354
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1928 1.2082 13.5952
REMARK 3 T TENSOR
REMARK 3 T11: 0.5880 T22: 0.6711
REMARK 3 T33: 0.4872 T12: -0.2794
REMARK 3 T13: 0.0133 T23: 0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 8.3204 L22: 5.1542
REMARK 3 L33: 8.0356 L12: -2.3600
REMARK 3 L13: 0.5802 L23: -1.6400
REMARK 3 S TENSOR
REMARK 3 S11: -0.3106 S12: 0.0484 S13: -0.8123
REMARK 3 S21: 0.1961 S22: 0.0841 S23: 0.8564
REMARK 3 S31: 0.9600 S32: -1.6415 S33: 0.2999
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5343 6.3853 -0.5849
REMARK 3 T TENSOR
REMARK 3 T11: 0.5776 T22: 0.7465
REMARK 3 T33: 0.3718 T12: -0.0314
REMARK 3 T13: -0.1496 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 4.3875 L22: 3.0430
REMARK 3 L33: 3.5827 L12: -1.7549
REMARK 3 L13: -3.4991 L23: 2.2930
REMARK 3 S TENSOR
REMARK 3 S11: -0.1719 S12: 0.3988 S13: -0.2773
REMARK 3 S21: -0.3022 S22: 0.0038 S23: 0.2045
REMARK 3 S31: 0.3919 S32: -0.3590 S33: 0.1455
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4838 1.3783 -56.9918
REMARK 3 T TENSOR
REMARK 3 T11: 0.4843 T22: 0.5490
REMARK 3 T33: 0.3549 T12: -0.0189
REMARK 3 T13: -0.0769 T23: -0.1365
REMARK 3 L TENSOR
REMARK 3 L11: 1.4526 L22: 1.5890
REMARK 3 L33: 4.1016 L12: -0.3956
REMARK 3 L13: -0.1389 L23: 0.5406
REMARK 3 S TENSOR
REMARK 3 S11: 0.1372 S12: 0.2901 S13: -0.1524
REMARK 3 S21: -0.1377 S22: -0.2342 S23: 0.2920
REMARK 3 S31: 0.2789 S32: -0.4863 S33: 0.0964
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6944 3.1533 -47.9666
REMARK 3 T TENSOR
REMARK 3 T11: 0.4467 T22: 0.4460
REMARK 3 T33: 0.2789 T12: 0.0118
REMARK 3 T13: -0.0445 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.9389 L22: 2.3961
REMARK 3 L33: 3.6026 L12: -0.6777
REMARK 3 L13: -0.0609 L23: 0.9392
REMARK 3 S TENSOR
REMARK 3 S11: 0.1149 S12: 0.0771 S13: -0.0699
REMARK 3 S21: 0.0663 S22: -0.0331 S23: -0.1316
REMARK 3 S31: 0.1824 S32: 0.3282 S33: -0.0942
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8149 10.6707 -36.8494
REMARK 3 T TENSOR
REMARK 3 T11: 0.4519 T22: 0.4117
REMARK 3 T33: 0.3069 T12: -0.0688
REMARK 3 T13: -0.0918 T23: -0.1098
REMARK 3 L TENSOR
REMARK 3 L11: 3.8625 L22: 1.3652
REMARK 3 L33: 6.2097 L12: -1.5424
REMARK 3 L13: -1.2737 L23: -0.8305
REMARK 3 S TENSOR
REMARK 3 S11: 0.1161 S12: 0.2202 S13: 0.1954
REMARK 3 S21: 0.1947 S22: -0.0053 S23: -0.2477
REMARK 3 S31: 0.0387 S32: 0.3168 S33: -0.0921
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4061 -0.0931 -22.2128
REMARK 3 T TENSOR
REMARK 3 T11: 0.7369 T22: 0.4396
REMARK 3 T33: 0.3539 T12: -0.0621
REMARK 3 T13: -0.0503 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 2.0177 L22: 1.9221
REMARK 3 L33: 2.8680 L12: -0.2429
REMARK 3 L13: 0.5827 L23: -0.2829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2435 S12: -0.3286 S13: -0.3625
REMARK 3 S21: 0.5562 S22: -0.1027 S23: -0.0128
REMARK 3 S31: 0.6567 S32: 0.0181 S33: -0.1557
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2473 11.3241 -33.4828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3879 T22: 0.5446
REMARK 3 T33: 0.3538 T12: 0.0099
REMARK 3 T13: 0.0435 T23: -0.1144
REMARK 3 L TENSOR
REMARK 3 L11: 2.9335 L22: 5.2972
REMARK 3 L33: 5.2839 L12: 1.2916
REMARK 3 L13: 0.6587 L23: 0.1289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0257 S13: 0.1023
REMARK 3 S21: -0.0292 S22: -0.1590 S23: 0.6771
REMARK 3 S31: 0.0381 S32: -0.8668 S33: 0.1634
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2142 11.3273 -21.9909
REMARK 3 T TENSOR
REMARK 3 T11: 0.6313 T22: 0.4425
REMARK 3 T33: 0.2327 T12: -0.0754
REMARK 3 T13: 0.0217 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 8.9113 L22: 1.8698
REMARK 3 L33: 6.1967 L12: -0.6518
REMARK 3 L13: 7.2320 L23: -0.6926
REMARK 3 S TENSOR
REMARK 3 S11: 0.0748 S12: 0.2425 S13: -0.3269
REMARK 3 S21: 0.3240 S22: -0.0724 S23: -0.0263
REMARK 3 S31: 0.1433 S32: 0.3961 S33: 0.0045
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 7R2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292120754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-15
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 : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85474
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.7000
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-30 % /W7V) 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 39.41300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.78450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.37750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.78450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.41300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.37750
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 THR A 543
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 GLN A 7 CG CD OE1 NE2
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ASP B 323 CG OD1 OD2
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 -7.00 74.70
REMARK 500 ALA A 62 50.97 -116.25
REMARK 500 SUN A 203 -124.03 59.17
REMARK 500 VAL A 303 89.63 -68.15
REMARK 500 ASP A 306 -83.85 -131.37
REMARK 500 VAL A 407 -64.75 -130.31
REMARK 500 ARG A 493 30.42 -79.72
REMARK 500 ASP A 494 97.24 -162.77
REMARK 500 SER A 541 45.67 -85.75
REMARK 500 PHE B 47 -0.45 71.92
REMARK 500 ALA B 62 53.22 -119.93
REMARK 500 PHE B 158 -0.12 -142.69
REMARK 500 ALA B 167 75.41 -154.11
REMARK 500 ASN B 170 19.14 56.64
REMARK 500 SUN B 203 -120.31 61.64
REMARK 500 ASP B 306 -84.24 -129.14
REMARK 500 VAL B 407 -61.21 -123.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 851 DISTANCE = 6.09 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 I1X A 603
REMARK 610 PG0 A 605
REMARK 610 PG0 A 607
REMARK 610 I1X B 601
REMARK 610 7PG B 610
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: 7R02 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH N-(3-(DIETHYLAMINO)PROPYL)-4-
REMARK 900 METHYL-3-NITROBENZAMIDE
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 7R2F A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7R2F 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 SUN 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 SUN 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
MODRES 7R2F SUN A 203 SER MODIFIED RESIDUE
MODRES 7R2F SUN B 203 SER MODIFIED RESIDUE
HET SUN A 203 14
HET SUN B 203 14
HET NAG A 601 14
HET NAG A 602 14
HET I1X A 603 16
HET PG0 A 604 8
HET PG0 A 605 7
HET PG0 A 606 8
HET PG0 A 607 6
HET PG0 A 608 8
HET PG0 A 609 8
HET I1X B 601 18
HET PG0 B 602 8
HET PG0 B 603 8
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 8
HET 7PG B 610 23
HETNAM SUN O-[(R)-(DIMETHYLAMINO)(ETHOXY)PHOSPHORYL]-L-SERINE
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 7PG 2,5,8,11,14,17,20,23-OCTAOXAPENTACOSAN-25-OL
HETSYN SUN TABUN CONJUGATED SERINE
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 1 SUN 2(C7 H17 N2 O5 P)
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 5 I1X 2(C19 H23 N4 O4 1+)
FORMUL 6 PG0 14(C5 H12 O3)
FORMUL 21 7PG C17 H36 O9
FORMUL 22 HOH *252(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 SUN 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 ARG A 274 1 9
HELIX 13 AB4 PRO A 277 ASP A 283 1 7
HELIX 14 AB5 HIS A 284 LEU A 289 5 6
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASN A 464 5 9
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 SER A 541 1 8
HELIX 27 AC9 ASP B 5 GLN B 7 5 3
HELIX 28 AD1 VAL B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 GLU B 142 1 8
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 ILE B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SUN B 203 SER B 215 1 13
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 SER B 240 VAL B 255 1 16
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 ASP B 283 1 7
HELIX 40 AE4 HIS B 284 VAL B 288 5 5
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 343 1 9
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASN B 464 5 9
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 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 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 VAL A 226 N LEU A 199
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 VAL B 226 N LEU B 199
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 TYR B 426 N VAL B 328
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 2.06
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 2.07
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.11
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.07
LINK C GLU A 202 N SUN A 203 1555 1555 1.33
LINK C SUN A 203 N ALA A 204 1555 1555 1.33
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A 602 1555 1555 1.45
LINK C GLU B 202 N SUN B 203 1555 1555 1.33
LINK C SUN B 203 N ALA B 204 1555 1555 1.34
CISPEP 1 TYR A 105 PRO A 106 0 -6.74
CISPEP 2 TYR B 105 PRO B 106 0 4.13
CISPEP 3 SER B 497 PRO B 498 0 -8.93
CRYST1 78.826 110.755 227.569 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 0.012686 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004394 0.00000
TER 4529 ALA A 542
TER 9032 THR B 543
MASTER 491 0 21 52 32 0 0 6 8784 2 240 84
END |