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HEADER HYDROLASE 02-DEC-15 5FPP
TITLE STRUCTURE OF A PRE-REACTION TERNARY COMPLEX BETWEEN SARIN-
TITLE 2 ACETYLCHOLINESTERASE AND HI-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: SARIN PHOSPHONYLATION PRODUCT COVALENTLY ATTACHED TO
COMPND 9 SER203
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS HYDROLASE, SARIN, HI-6, QM, DENSITY FUNCTIONAL THEORY CALCULATIONS,
KEYWDS 2 MICHAELIS COMPLEX.
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ALLGARDSSON,L.BERG,C.AKFUR,A.HORNBERG,F.WOREK,A.LINUSSON,F.EKSTROM
REVDAT 1 11-MAY-16 5FPP 0
JRNL AUTH A.ALLGARDSSON,L.BERG,C.AKFUR,A.HORNBERG,F.WOREK,A.LINUSSON,
JRNL AUTH 2 F.J.EKSTROM
JRNL TITL STRUCTURE OF A PREREACTION COMPLEX BETWEEN THE NERVE AGENT
JRNL TITL 2 SARIN, ITS BIOLOGICAL TARGET ACETYLCHOLINESTERASE, AND THE
JRNL TITL 3 ANTIDOTE HI-6.
JRNL REF PROC.NATL.ACAD.SCI.USA 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 27140636
JRNL DOI 10.1073/PNAS.1523362113
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.950
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.04
REMARK 3 NUMBER OF REFLECTIONS : 77689
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1763
REMARK 3 R VALUE (WORKING SET) : 0.1756
REMARK 3 FREE R VALUE : 0.2133
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1541
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 28.9520 - 5.3275 0.96 7079 142 0.1621 0.1814
REMARK 3 2 5.3275 - 4.2328 0.97 6996 141 0.1311 0.1653
REMARK 3 3 4.2328 - 3.6990 0.98 6926 134 0.1477 0.1829
REMARK 3 4 3.6990 - 3.3613 0.99 6969 139 0.1741 0.2145
REMARK 3 5 3.3613 - 3.1207 0.99 6943 132 0.1958 0.2425
REMARK 3 6 3.1207 - 2.9369 0.99 6929 154 0.2129 0.2510
REMARK 3 7 2.9369 - 2.7899 0.99 6900 140 0.2182 0.2879
REMARK 3 8 2.7899 - 2.6686 0.99 6923 141 0.2199 0.2718
REMARK 3 9 2.6686 - 2.5659 0.99 6878 151 0.2243 0.2777
REMARK 3 10 2.5659 - 2.4774 0.98 6812 144 0.2392 0.2723
REMARK 3 11 2.4774 - 2.4000 0.97 6793 123 0.2732 0.3321
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) : 0.32
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.00
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 8867
REMARK 3 ANGLE : 1.103 12100
REMARK 3 CHIRALITY : 0.076 1286
REMARK 3 PLANARITY : 0.005 1597
REMARK 3 DIHEDRAL : 15.961 3222
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8717 11.2359 29.1061
REMARK 3 T TENSOR
REMARK 3 T11: 0.2639 T22: 0.2173
REMARK 3 T33: 0.2230 T12: 0.0042
REMARK 3 T13: -0.0257 T23: 0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 1.3884 L22: 1.4015
REMARK 3 L33: 3.0163 L12: 0.0965
REMARK 3 L13: -0.4026 L23: -0.2151
REMARK 3 S TENSOR
REMARK 3 S11: -0.0621 S12: -0.1013 S13: 0.0581
REMARK 3 S21: 0.2088 S22: 0.0545 S23: 0.0101
REMARK 3 S31: 0.0917 S32: -0.0321 S33: 0.0138
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 229:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3703 9.4725 10.3067
REMARK 3 T TENSOR
REMARK 3 T11: 0.3307 T22: 0.2486
REMARK 3 T33: 0.2372 T12: 0.0582
REMARK 3 T13: 0.0274 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.6741 L22: 1.2384
REMARK 3 L33: 2.2876 L12: 1.4805
REMARK 3 L13: 0.4398 L23: -0.0064
REMARK 3 S TENSOR
REMARK 3 S11: -0.1926 S12: 0.3830 S13: -0.2237
REMARK 3 S21: -0.1204 S22: 0.0683 S23: -0.2183
REMARK 3 S31: 0.3278 S32: 0.3210 S33: 0.1134
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 332:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4035 17.1642 6.4542
REMARK 3 T TENSOR
REMARK 3 T11: 0.1963 T22: 0.2917
REMARK 3 T33: 0.2674 T12: -0.0209
REMARK 3 T13: -0.0427 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.0908 L22: 1.1775
REMARK 3 L33: 4.0783 L12: 0.0951
REMARK 3 L13: -0.2018 L23: -0.7397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: 0.1164 S13: 0.0214
REMARK 3 S21: -0.0413 S22: 0.0363 S23: 0.1892
REMARK 3 S31: -0.0771 S32: -0.4659 S33: -0.0675
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9739 0.9793 13.7388
REMARK 3 T TENSOR
REMARK 3 T11: 0.4297 T22: 0.6000
REMARK 3 T33: 0.5000 T12: -0.2721
REMARK 3 T13: 0.0010 T23: 0.0819
REMARK 3 L TENSOR
REMARK 3 L11: 3.8619 L22: 8.0186
REMARK 3 L33: 3.1970 L12: -0.6572
REMARK 3 L13: 1.8778 L23: -1.3387
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: -0.0944 S13: -0.6848
REMARK 3 S21: 0.2626 S22: 0.1273 S23: 0.9049
REMARK 3 S31: 0.5871 S32: -1.2217 S33: 0.0908
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 514:548)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3567 6.5767 -2.0484
REMARK 3 T TENSOR
REMARK 3 T11: 0.3757 T22: 0.3232
REMARK 3 T33: 0.2754 T12: -0.0629
REMARK 3 T13: -0.0999 T23: 0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 3.5322 L22: 2.6792
REMARK 3 L33: 7.1168 L12: -2.2915
REMARK 3 L13: -0.7665 L23: 2.3523
REMARK 3 S TENSOR
REMARK 3 S11: 0.1535 S12: 0.5940 S13: -0.2056
REMARK 3 S21: -0.3554 S22: -0.2797 S23: 0.2213
REMARK 3 S31: -0.1152 S32: -0.0433 S33: 0.1152
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 5:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3828 6.3470 -61.6128
REMARK 3 T TENSOR
REMARK 3 T11: 0.3611 T22: 0.3881
REMARK 3 T33: 0.3375 T12: 0.0233
REMARK 3 T13: -0.0984 T23: -0.1383
REMARK 3 L TENSOR
REMARK 3 L11: 5.6968 L22: 2.0292
REMARK 3 L33: 6.2394 L12: -1.1688
REMARK 3 L13: -1.9621 L23: 0.6789
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.5519 S13: 0.0424
REMARK 3 S21: -0.2481 S22: -0.1570 S23: 0.3111
REMARK 3 S31: -0.1522 S32: -0.7618 S33: 0.0528
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 46:158)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3161 1.5916 -51.7302
REMARK 3 T TENSOR
REMARK 3 T11: 0.3324 T22: 0.3331
REMARK 3 T33: 0.2779 T12: -0.0153
REMARK 3 T13: -0.0652 T23: -0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 1.3612 L22: 1.5944
REMARK 3 L33: 3.6153 L12: -0.1184
REMARK 3 L13: 0.1712 L23: 0.5456
REMARK 3 S TENSOR
REMARK 3 S11: 0.1164 S12: 0.1260 S13: -0.1948
REMARK 3 S21: -0.0951 S22: -0.1281 S23: 0.1894
REMARK 3 S31: 0.4578 S32: -0.2331 S33: -0.0001
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 159:191)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0964 8.9240 -55.7360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3733 T22: 0.4063
REMARK 3 T33: 0.2529 T12: -0.0033
REMARK 3 T13: -0.0374 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 4.7418 L22: 8.4533
REMARK 3 L33: 3.9842 L12: -6.3231
REMARK 3 L13: 3.6663 L23: -3.9254
REMARK 3 S TENSOR
REMARK 3 S11: 0.2139 S12: 0.1549 S13: 0.0171
REMARK 3 S21: -0.2873 S22: -0.1010 S23: -0.1936
REMARK 3 S31: -0.2358 S32: 0.4092 S33: -0.0929
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 192:298)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1055 1.4204 -45.1536
REMARK 3 T TENSOR
REMARK 3 T11: 0.3342 T22: 0.3623
REMARK 3 T33: 0.2493 T12: 0.0475
REMARK 3 T13: -0.0605 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 2.3638 L22: 3.2079
REMARK 3 L33: 3.2961 L12: -1.3846
REMARK 3 L13: -0.1103 L23: 1.3069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: 0.0389 S13: -0.1469
REMARK 3 S21: 0.1139 S22: 0.0847 S23: -0.2489
REMARK 3 S31: 0.4399 S32: 0.5313 S33: -0.1661
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 299:331)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5921 14.8574 -39.8306
REMARK 3 T TENSOR
REMARK 3 T11: 0.2899 T22: 0.4019
REMARK 3 T33: 0.3718 T12: -0.0223
REMARK 3 T13: -0.0950 T23: -0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 5.1128 L22: 1.5616
REMARK 3 L33: 5.0297 L12: -1.5874
REMARK 3 L13: -1.7758 L23: 2.1952
REMARK 3 S TENSOR
REMARK 3 S11: 0.2599 S12: 0.0838 S13: 0.7178
REMARK 3 S21: 0.0037 S22: 0.0653 S23: -0.5209
REMARK 3 S31: -0.5001 S32: 0.6874 S33: -0.3079
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 332:382)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8477 -6.1588 -22.0526
REMARK 3 T TENSOR
REMARK 3 T11: 0.6922 T22: 0.2904
REMARK 3 T33: 0.3230 T12: 0.0109
REMARK 3 T13: -0.0924 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 7.4156 L22: 5.2243
REMARK 3 L33: 2.6897 L12: 2.0091
REMARK 3 L13: 0.3087 L23: -1.0110
REMARK 3 S TENSOR
REMARK 3 S11: 0.3441 S12: -0.0180 S13: -0.7174
REMARK 3 S21: 0.2180 S22: -0.0276 S23: -0.0813
REMARK 3 S31: 0.9475 S32: 0.1173 S33: -0.3314
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 383:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5652 6.0966 -29.4041
REMARK 3 T TENSOR
REMARK 3 T11: 0.3401 T22: 0.3072
REMARK 3 T33: 0.2848 T12: -0.0705
REMARK 3 T13: 0.0136 T23: -0.1044
REMARK 3 L TENSOR
REMARK 3 L11: 2.4513 L22: 2.1835
REMARK 3 L33: 3.9890 L12: -0.4092
REMARK 3 L13: 1.3427 L23: -0.7797
REMARK 3 S TENSOR
REMARK 3 S11: 0.2227 S12: -0.2085 S13: -0.2112
REMARK 3 S21: 0.2218 S22: -0.0906 S23: 0.3080
REMARK 3 S31: 0.2664 S32: -0.3866 S33: -0.1486
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2799 22.6124 -28.7967
REMARK 3 T TENSOR
REMARK 3 T11: 0.4537 T22: 0.3507
REMARK 3 T33: 0.3680 T12: 0.0462
REMARK 3 T13: 0.0210 T23: -0.1231
REMARK 3 L TENSOR
REMARK 3 L11: 5.6116 L22: 8.9770
REMARK 3 L33: 2.6601 L12: 2.2670
REMARK 3 L13: 2.0295 L23: -2.7004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0803 S12: -0.5201 S13: 0.9030
REMARK 3 S21: 0.1608 S22: 0.1169 S23: 0.9942
REMARK 3 S31: -0.3886 S32: -0.4547 S33: -0.0100
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 514:544)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6094 11.2404 -21.7206
REMARK 3 T TENSOR
REMARK 3 T11: 0.4141 T22: 0.3668
REMARK 3 T33: 0.1817 T12: -0.0586
REMARK 3 T13: 0.0006 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 9.1329 L22: 1.9414
REMARK 3 L33: 4.7414 L12: -1.1544
REMARK 3 L13: 5.0580 L23: -0.4308
REMARK 3 S TENSOR
REMARK 3 S11: -0.0204 S12: 0.1725 S13: -0.3969
REMARK 3 S21: 0.2661 S22: 0.0161 S23: -0.0415
REMARK 3 S31: 0.1128 S32: 0.5171 S33: 0.0176
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SOME REGIONS OF THE CATALYTIC SITE IS
REMARK 3 DISORDERED. THE REFINEMENT INCLUDED AN INTEGRATED METHODOLOGY
REMARK 3 CYCLING BETWEEN A CONVENTIONAL CRYSTALLOGRAPHIC REFINEMENT AND A
REMARK 3 QUANTUM CHEMICAL CLUSTER APPROACH USING IMPLICIT DISPERSION-
REMARK 3 CORRECTED DENSITY FUNCTIONAL THEORY (DFT) CALCULATIONS
REMARK 4
REMARK 4 5FPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-15.
REMARK 100 THE PDBE ID CODE IS EBI-65683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.039
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MARMOSAIC 225)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77695
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 29.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.7
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.0
REMARK 200 R MERGE FOR SHELL (I) : 0.68
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 39.41250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.77800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.77600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.77800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.41250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.77600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLU B 4
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 THR A 543 OG1 CG2
REMARK 470 THR A 545 OG1 CG2
REMARK 470 GLU A 546 CG CD OE1 OE2
REMARK 470 PRO A 548 CG CD
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
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 O3 HI6 B 1545 O HOH B 2194 2.12
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 -4.15 78.19
REMARK 500 PRO A 104 151.66 -49.20
REMARK 500 ALA A 167 68.51 -156.43
REMARK 500 SGB A 203 -121.87 62.31
REMARK 500 ASP A 306 -86.18 -132.56
REMARK 500 VAL A 407 -61.47 -128.05
REMARK 500 HIS A 447 122.45 -39.38
REMARK 500 THR A 543 136.86 -174.70
REMARK 500 GLU A 546 -139.52 -153.33
REMARK 500 ALA A 547 -134.79 155.16
REMARK 500 CYS B 96 10.09 -145.47
REMARK 500 PHE B 158 -4.41 -140.49
REMARK 500 ALA B 167 70.83 -151.51
REMARK 500 SGB B 203 -122.73 55.36
REMARK 500 ASP B 306 -84.37 -122.53
REMARK 500 VAL B 407 -59.76 -122.97
REMARK 500 HIS B 447 119.71 -38.18
REMARK 500 ARG B 493 -6.89 -145.45
REMARK 500 SER B 495 -150.52 -75.62
REMARK 500 LYS B 496 120.40 61.66
REMARK 500 SER B 497 156.24 -45.55
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 HI6 B 1545
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE3 A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE3 B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 601 BOUND TO ASN A 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FOQ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH C7653
REMARK 900 RELATED ID: 5FPQ RELATED DB: PDB
REMARK 900 STRUCTURE OF HOMO SAPIENS ACETYLCHOLINESTERASE
REMARK 900 PHOSPHONYLATED BY SARIN.
DBREF 5FPP A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5FPP B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 5FPP ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 5FPP THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 5FPP GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 5FPP ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 5FPP PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 5FPP ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 5FPP THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 5FPP GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 5FPP ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 5FPP PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
MODRES 5FPP SGB A 203 SER SARIN-SERINE
MODRES 5FPP SGB B 203 SER SARIN-SERINE
HET SGB A 203 13
HET SGB B 203 13
HET NAG A 601 14
HET CO3 A1549 4
HET P6G A1550 19
HET AE3 A1551 9
HET HI6 A1552 42
HET HI6 B1545 36
HET AE3 B1546 9
HET CO3 B1547 4
HETNAM SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CO3 CARBONATE ION
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM AE3 2-(2-ETHOXYETHOXY)ETHANOL
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
HETSYN P6G POLYETHYLENE GLYCOL PEG400
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN 2 HI6 PYRIDINIUM DIMETHYLETHER
FORMUL 1 SGB 2(C7 H16 N O5 P)
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 CO3 2(C O3 2-)
FORMUL 5 P6G C12 H26 O7
FORMUL 6 AE3 2(C6 H14 O3)
FORMUL 7 HI6 2(C14 H16 N4 O3 2+)
FORMUL 11 HOH *457(H2 O)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLY A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SGB A 203 SER A 215 1 13
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 THR A 275 1 11
HELIX 13 13 PRO A 277 TRP A 286 1 10
HELIX 14 14 HIS A 287 LEU A 289 5 3
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 343 1 9
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 ASP A 460 ASN A 464 5 5
HELIX 25 25 THR A 466 GLY A 487 1 22
HELIX 26 26 ARG A 525 ARG A 534 1 10
HELIX 27 27 ARG A 534 ALA A 542 1 9
HELIX 28 28 ASP B 5 GLN B 7 5 3
HELIX 29 29 VAL B 42 ARG B 46 5 5
HELIX 30 30 PHE B 80 MET B 85 1 6
HELIX 31 31 LEU B 130 ASP B 134 5 5
HELIX 32 32 GLY B 135 GLY B 143 1 9
HELIX 33 33 VAL B 153 LEU B 159 1 7
HELIX 34 34 ASN B 170 ILE B 187 1 18
HELIX 35 35 ALA B 188 PHE B 190 5 3
HELIX 36 36 SGB B 203 SER B 215 1 13
HELIX 37 37 SER B 215 SER B 220 1 6
HELIX 38 38 SER B 240 VAL B 255 1 16
HELIX 39 39 ASN B 265 ARG B 276 1 12
HELIX 40 40 PRO B 277 TRP B 286 1 10
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 VAL B 343 1 9
HELIX 43 43 SER B 355 VAL B 367 1 13
HELIX 44 44 SER B 371 THR B 383 1 13
HELIX 45 45 ASP B 390 VAL B 407 1 18
HELIX 46 46 VAL B 407 GLN B 421 1 15
HELIX 47 47 PRO B 440 GLY B 444 5 5
HELIX 48 48 GLU B 450 PHE B 455 1 6
HELIX 49 49 GLY B 456 ASP B 460 5 5
HELIX 50 50 ASP B 460 ASN B 464 5 5
HELIX 51 51 THR B 466 GLY B 487 1 22
HELIX 52 52 ARG B 525 ARG B 534 1 10
HELIX 53 53 ARG B 534 THR B 543 1 10
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.02
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK C GLU A 202 N SGB A 203 1555 1555 1.34
LINK C SGB A 203 N ALA A 204 1555 1555 1.34
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.47
LINK C GLU B 202 N SGB B 203 1555 1555 1.34
LINK C SGB B 203 N ALA B 204 1555 1555 1.34
CISPEP 1 TYR A 105 PRO A 106 0 -3.56
CISPEP 2 THR A 545 GLU A 546 0 -1.21
CISPEP 3 TYR B 105 PRO B 106 0 6.86
CISPEP 4 SER B 497 PRO B 498 0 2.14
SITE 1 AC1 1 TRP A 286
SITE 1 AC2 10 HIS A 381 GLN A 527 PHE A 535 HOH A2214
SITE 2 AC2 10 HOH A2263 ALA B 377 LEU B 380 HIS B 381
SITE 3 AC2 10 GLN B 527 PHE B 535
SITE 1 AC3 4 HIS A 393 ASP A 404 ARG A 525 THR A 528
SITE 1 AC4 10 ASP A 74 TYR A 124 SGB A 203 TRP A 286
SITE 2 AC4 10 ARG A 296 PHE A 297 SER A 298 TYR A 337
SITE 3 AC4 10 PHE A 338 TYR A 341
SITE 1 AC5 9 TRP B 86 TYR B 124 GLU B 202 SGB B 203
SITE 2 AC5 9 PHE B 295 TYR B 337 PHE B 338 TYR B 341
SITE 3 AC5 9 HOH B2194
SITE 1 AC6 1 GLN A 527
SITE 1 AC7 2 TRP B 286 HOH B2123
SITE 1 AC8 5 SER A 347 ASN A 350 HOH A2200 HOH A2202
SITE 2 AC8 5 HOH A2207
CRYST1 78.825 111.552 227.556 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 0.008964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004395 0.00000
TER 4278 PRO A 548
TER 8469 ALA B 544
MASTER 559 0 10 53 32 0 15 6 9061 2 180 86
END |