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HEADER HYDROLASE 02-DEC-15 5FPQ
TITLE STRUCTURE OF HOMO SAPIENS ACETYLCHOLINESTERASE
TITLE 2 PHOSPHONYLATED BY SARIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 33-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
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, SIGNALING PROTEIN, ACETYLCHOLINESTERASE, SARIN, HI-6, QM,
KEYWDS 2 DENSITY FUNCTIONAL THEORY CALCULATIONS, 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 5FPQ 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) : 45.410
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.35
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.36
REMARK 3 NUMBER OF REFLECTIONS : 81198
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1784
REMARK 3 R VALUE (WORKING SET) : 0.1767
REMARK 3 FREE R VALUE : 0.2103
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 4144
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 45.4177 - 7.4468 0.98 2786 154 0.1788 0.1843
REMARK 3 2 7.4468 - 5.9149 1.00 2676 143 0.1737 0.2029
REMARK 3 3 5.9149 - 5.1684 0.99 2641 131 0.1557 0.2036
REMARK 3 4 5.1684 - 4.6964 0.99 2617 147 0.1344 0.1657
REMARK 3 5 4.6964 - 4.3601 1.00 2594 135 0.1273 0.1452
REMARK 3 6 4.3601 - 4.1032 1.00 2637 130 0.1363 0.1462
REMARK 3 7 4.1032 - 3.8978 1.00 2556 150 0.1444 0.1816
REMARK 3 8 3.8978 - 3.7282 1.00 2580 145 0.1573 0.1795
REMARK 3 9 3.7282 - 3.5847 0.99 2585 132 0.1735 0.2095
REMARK 3 10 3.5847 - 3.4611 0.99 2560 146 0.1935 0.2379
REMARK 3 11 3.4611 - 3.3529 0.99 2562 143 0.1982 0.2162
REMARK 3 12 3.3529 - 3.2571 0.99 2549 143 0.1992 0.2289
REMARK 3 13 3.2571 - 3.1714 1.00 2561 129 0.2072 0.2334
REMARK 3 14 3.1714 - 3.0940 0.99 2556 133 0.2071 0.2543
REMARK 3 15 3.0940 - 3.0237 1.00 2567 119 0.2084 0.2666
REMARK 3 16 3.0237 - 2.9594 0.99 2565 144 0.1987 0.2412
REMARK 3 17 2.9594 - 2.9002 1.00 2544 135 0.2058 0.2730
REMARK 3 18 2.9002 - 2.8454 0.99 2529 148 0.2106 0.2403
REMARK 3 19 2.8454 - 2.7946 0.99 2546 135 0.2008 0.2423
REMARK 3 20 2.7946 - 2.7473 0.99 2485 146 0.1947 0.2216
REMARK 3 21 2.7473 - 2.7030 0.99 2560 137 0.1909 0.2445
REMARK 3 22 2.7030 - 2.6614 0.99 2562 140 0.1862 0.2159
REMARK 3 23 2.6614 - 2.6222 0.99 2490 133 0.1861 0.2370
REMARK 3 24 2.6222 - 2.5853 0.99 2579 138 0.1916 0.2047
REMARK 3 25 2.5853 - 2.5504 0.99 2523 120 0.1908 0.2626
REMARK 3 26 2.5504 - 2.5173 0.99 2504 161 0.2001 0.2592
REMARK 3 27 2.5173 - 2.4858 0.99 2533 127 0.1909 0.2465
REMARK 3 28 2.4858 - 2.4558 0.99 2504 136 0.2077 0.2526
REMARK 3 29 2.4558 - 2.4273 0.99 2548 132 0.2081 0.2579
REMARK 3 30 2.4273 - 2.4000 0.99 2555 132 0.2179 0.2771
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) : 0.25
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.30
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.71
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 8687
REMARK 3 ANGLE : 1.081 11874
REMARK 3 CHIRALITY : 0.079 1256
REMARK 3 PLANARITY : 0.005 1578
REMARK 3 DIHEDRAL : 14.655 3143
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 4 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9177 32.1947 39.1464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1594 T22: 0.2468
REMARK 3 T33: 0.1903 T12: -0.0087
REMARK 3 T13: -0.0496 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 1.4276 L22: 0.7869
REMARK 3 L33: 2.3159 L12: 0.0907
REMARK 3 L13: 0.5150 L23: -0.0428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: -0.1097 S13: -0.0389
REMARK 3 S21: 0.0675 S22: 0.0131 S23: -0.0556
REMARK 3 S31: -0.1586 S32: 0.1993 S33: -0.0038
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0673 35.8377 37.0123
REMARK 3 T TENSOR
REMARK 3 T11: 0.1948 T22: 0.2712
REMARK 3 T33: 0.1733 T12: 0.0369
REMARK 3 T13: -0.0182 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 2.4735 L22: 2.4525
REMARK 3 L33: 1.4212 L12: 1.1463
REMARK 3 L13: 0.5004 L23: 0.1491
REMARK 3 S TENSOR
REMARK 3 S11: -0.0573 S12: -0.1476 S13: 0.0178
REMARK 3 S21: 0.0901 S22: 0.0295 S23: 0.1616
REMARK 3 S31: -0.3305 S32: -0.2472 S33: 0.0032
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9071 33.6105 27.1921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: 0.2665
REMARK 3 T33: 0.1925 T12: 0.0515
REMARK 3 T13: -0.0312 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.3232 L22: 0.7857
REMARK 3 L33: 1.5654 L12: 0.3381
REMARK 3 L13: 0.1483 L23: -0.5353
REMARK 3 S TENSOR
REMARK 3 S11: -0.0932 S12: 0.1613 S13: 0.0258
REMARK 3 S21: 0.0655 S22: 0.1439 S23: 0.0739
REMARK 3 S31: -0.2348 S32: -0.2431 S33: -0.0259
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.7174 27.0438 28.6871
REMARK 3 T TENSOR
REMARK 3 T11: 0.1916 T22: 0.3805
REMARK 3 T33: 0.2404 T12: 0.0279
REMARK 3 T13: -0.0331 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 1.2290 L22: 0.5492
REMARK 3 L33: 1.6769 L12: 0.7828
REMARK 3 L13: -0.3695 L23: -0.6775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0867 S12: -0.0182 S13: 0.0129
REMARK 3 S21: -0.0871 S22: 0.0808 S23: 0.0295
REMARK 3 S31: 0.0175 S32: -0.4922 S33: 0.0859
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.6208 22.5201 11.1382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2132 T22: 0.2961
REMARK 3 T33: 0.2481 T12: 0.0227
REMARK 3 T13: -0.0208 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.4963 L22: 0.0726
REMARK 3 L33: 1.4960 L12: 0.2025
REMARK 3 L13: 0.6730 L23: 0.2528
REMARK 3 S TENSOR
REMARK 3 S11: 0.0888 S12: -0.0221 S13: -0.1497
REMARK 3 S21: -0.0741 S22: -0.0458 S23: -0.0589
REMARK 3 S31: 0.1033 S32: 0.1642 S33: -0.0201
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.7767 42.2931 13.6956
REMARK 3 T TENSOR
REMARK 3 T11: 0.3072 T22: 0.3572
REMARK 3 T33: 0.2557 T12: -0.1894
REMARK 3 T13: -0.0467 T23: 0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 1.5383 L22: 0.7785
REMARK 3 L33: 0.9383 L12: -0.4632
REMARK 3 L13: 1.0612 L23: -0.2941
REMARK 3 S TENSOR
REMARK 3 S11: -0.1697 S12: 0.4215 S13: 0.2059
REMARK 3 S21: -0.1949 S22: -0.0051 S23: -0.0913
REMARK 3 S31: -0.3745 S32: 0.3598 S33: 0.0348
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4319 32.4997 5.0517
REMARK 3 T TENSOR
REMARK 3 T11: 0.2714 T22: 0.3233
REMARK 3 T33: 0.2027 T12: -0.0299
REMARK 3 T13: -0.0398 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.6742 L22: 0.7774
REMARK 3 L33: 1.3115 L12: 0.4072
REMARK 3 L13: 0.9004 L23: 0.2791
REMARK 3 S TENSOR
REMARK 3 S11: 0.1811 S12: -0.0186 S13: -0.1643
REMARK 3 S21: -0.0421 S22: -0.1855 S23: -0.0527
REMARK 3 S31: -0.1788 S32: 0.1649 S33: 0.0684
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.2755 35.3433 57.6287
REMARK 3 T TENSOR
REMARK 3 T11: 0.3751 T22: 0.2602
REMARK 3 T33: 0.1958 T12: -0.0913
REMARK 3 T13: 0.0321 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.8447 L22: 4.6571
REMARK 3 L33: 0.2132 L12: -0.2202
REMARK 3 L13: -0.3156 L23: -0.1174
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: -0.3892 S13: -0.0599
REMARK 3 S21: 0.4001 S22: -0.0539 S23: 0.0728
REMARK 3 S31: 0.1244 S32: -0.1321 S33: 0.1286
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.0381 20.8749 44.0790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2930 T22: 0.2358
REMARK 3 T33: 0.2031 T12: -0.0280
REMARK 3 T13: -0.0126 T23: 0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 0.7453 L22: 0.0446
REMARK 3 L33: 0.9885 L12: -0.1043
REMARK 3 L13: -0.8429 L23: 0.1559
REMARK 3 S TENSOR
REMARK 3 S11: -0.2026 S12: -0.2898 S13: -0.3495
REMARK 3 S21: 0.2537 S22: -0.0052 S23: 0.0888
REMARK 3 S31: 0.3401 S32: 0.3050 S33: 0.1250
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 119.1159 40.9072 40.9541
REMARK 3 T TENSOR
REMARK 3 T11: 0.2745 T22: 0.3186
REMARK 3 T33: 0.2521 T12: -0.1208
REMARK 3 T13: -0.0466 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 1.0200 L22: 0.9259
REMARK 3 L33: 0.6468 L12: 0.1299
REMARK 3 L13: -0.3508 L23: -0.4434
REMARK 3 S TENSOR
REMARK 3 S11: 0.0408 S12: -0.2012 S13: 0.0694
REMARK 3 S21: 0.1691 S22: -0.1372 S23: -0.0647
REMARK 3 S31: -0.1905 S32: 0.3095 S33: 0.0541
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 107.7817 34.8396 40.8791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: 0.1976
REMARK 3 T33: 0.1860 T12: -0.0794
REMARK 3 T13: 0.0161 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.4669 L22: 1.4824
REMARK 3 L33: 1.2341 L12: -0.5767
REMARK 3 L13: -0.3649 L23: 0.4698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0277 S12: -0.1518 S13: -0.0885
REMARK 3 S21: 0.2868 S22: -0.0716 S23: 0.0599
REMARK 3 S31: -0.0148 S32: 0.0580 S33: 0.0982
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.7373 29.6781 29.1656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1350 T22: 0.2246
REMARK 3 T33: 0.2373 T12: -0.0660
REMARK 3 T13: -0.0073 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.7522 L22: 1.0383
REMARK 3 L33: 1.2084 L12: -0.3082
REMARK 3 L13: -0.1669 L23: -0.1438
REMARK 3 S TENSOR
REMARK 3 S11: 0.1375 S12: 0.1698 S13: -0.0090
REMARK 3 S21: -0.0164 S22: -0.1572 S23: 0.0318
REMARK 3 S31: 0.0383 S32: 0.0968 S33: 0.0160
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.0289 37.0343 22.1610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1816 T22: 0.2987
REMARK 3 T33: 0.2374 T12: -0.0455
REMARK 3 T13: -0.0049 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 0.7787 L22: 0.6041
REMARK 3 L33: 0.9233 L12: -0.5510
REMARK 3 L13: -0.1050 L23: -0.2303
REMARK 3 S TENSOR
REMARK 3 S11: 0.1470 S12: 0.1682 S13: -0.0537
REMARK 3 S21: 0.0499 S22: -0.1292 S23: 0.1194
REMARK 3 S31: 0.0670 S32: 0.0282 S33: -0.0295
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 117.3368 53.0670 11.7117
REMARK 3 T TENSOR
REMARK 3 T11: 0.2448 T22: 0.2933
REMARK 3 T33: 0.2326 T12: -0.0579
REMARK 3 T13: -0.0230 T23: 0.0675
REMARK 3 L TENSOR
REMARK 3 L11: 0.8298 L22: 0.5894
REMARK 3 L33: 1.4332 L12: 0.0134
REMARK 3 L13: 0.6803 L23: -0.3674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: -0.0790 S13: -0.0262
REMARK 3 S21: -0.0133 S22: -0.1704 S23: -0.2292
REMARK 3 S31: -0.1521 S32: 0.3548 S33: 0.1097
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.4376 50.9172 30.8354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2306 T22: 0.1917
REMARK 3 T33: 0.2180 T12: -0.0529
REMARK 3 T13: -0.0214 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.9111 L22: 0.4327
REMARK 3 L33: 0.8573 L12: -0.2574
REMARK 3 L13: -0.3250 L23: 0.0366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0811 S12: 0.0314 S13: 0.2179
REMARK 3 S21: 0.1587 S22: -0.1105 S23: 0.0368
REMARK 3 S31: -0.1381 S32: 0.0002 S33: 0.0147
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 91.7471 52.0273 32.7954
REMARK 3 T TENSOR
REMARK 3 T11: 0.1801 T22: 0.2287
REMARK 3 T33: 0.2828 T12: 0.0370
REMARK 3 T13: 0.0181 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 1.2272 L22: 0.8746
REMARK 3 L33: 2.2707 L12: 0.1994
REMARK 3 L13: 0.3867 L23: 0.0539
REMARK 3 S TENSOR
REMARK 3 S11: 0.0168 S12: -0.0160 S13: 0.1811
REMARK 3 S21: 0.0475 S22: -0.0234 S23: 0.1732
REMARK 3 S31: -0.2453 S32: -0.3891 S33: 0.0088
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.9717 49.3503 14.2716
REMARK 3 T TENSOR
REMARK 3 T11: 0.1849 T22: 0.1689
REMARK 3 T33: 0.1728 T12: 0.0545
REMARK 3 T13: -0.0181 T23: 0.0559
REMARK 3 L TENSOR
REMARK 3 L11: 0.7930 L22: 0.2752
REMARK 3 L33: 1.8051 L12: 0.3654
REMARK 3 L13: -0.2341 L23: -0.3901
REMARK 3 S TENSOR
REMARK 3 S11: -0.2108 S12: 0.0836 S13: -0.0662
REMARK 3 S21: -0.1316 S22: 0.0135 S23: 0.3926
REMARK 3 S31: -0.2084 S32: 0.0801 S33: 0.0423
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 5FPQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-15.
REMARK 100 THE PDBE ID CODE IS EBI-65684.
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 : 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) : 0.919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 47.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.9
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.20
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.1
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.90
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 4EY4
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 107.75000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 215.50000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 215.50000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 107.75000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 52.43450
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -90.81922
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 104.86900
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 THR A 543
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 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 ALA B 497
REMARK 465 THR B 543
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 OH5 1PE A 1543 O HOH A 2041 2.16
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 PRO A 25 30.38 -65.51
REMARK 500 PHE A 47 -4.70 78.14
REMARK 500 ALA A 167 76.39 -150.44
REMARK 500 SER A 196 65.23 -117.31
REMARK 500 ASP A 306 -86.77 -91.90
REMARK 500 HIS A 387 54.93 -142.66
REMARK 500 VAL A 407 -63.22 -131.45
REMARK 500 ASN A 464 50.67 -116.43
REMARK 500 ASP A 514 -160.88 -164.84
REMARK 500 PHE B 47 -6.98 77.24
REMARK 500 ALA B 62 50.01 -113.45
REMARK 500 ALA B 167 72.03 -150.85
REMARK 500 ASP B 306 -91.19 -95.25
REMARK 500 VAL B 407 -60.60 -131.20
REMARK 500 ASP B 514 -153.05 -156.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 264 ASN A 265 136.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND ARE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE): THESE HAVE BEEN REPOSITIONED
REMARK 525 BY APPLYING THE SYMMETRY TRANSFORMATION INDICATED.
REMARK 525
REMARK 525 M RES CSSEQI ORIGINAL COORDINATES SYMMETRY TRANS. DIST.
REMARK 525 X Y Z
REMARK 525 HOH D 113 127.565 21.434 39.207 001 455 3.41
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A1543
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: 5FPP RELATED DB: PDB
REMARK 900 STRUCTURE OF A PRE-REACTION TERNAY COMPLEX BETWEEN
REMARK 900 SARIN-ACETYLCHOLINESTERASE AND HI-6
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 OTHER_DETAILS: SARIN PHOSPHONYLATION PRODUCT COVALENTLY ATTACHED TO
REMARK 999 SER203D
DBREF 5FPQ A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 5FPQ B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
MODRES 5FPQ SGB A 203 SER MODIFIED SERINE
MODRES 5FPQ SGB B 203 SER MODIFIED SERINE
HET SGB A 203 13
HET SGB B 203 13
HET 1PE A1543 38
HETNAM SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-
HETNAM 2 SGB SERINE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 SGB 2(C7 H16 N O5 P)
FORMUL 4 1PE C10 H22 O6
FORMUL 5 HOH *113(H2 O)
HELIX 1 1 ASP A 5 GLU A 7 5 3
HELIX 2 2 MET 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 ARG A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 VAL A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 ALA A 204 LEU A 214 1 11
HELIX 10 10 SER A 215 GLY A 220 1 6
HELIX 11 11 GLY A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 THR A 275 1 11
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
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 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 ARG A 534 1 10
HELIX 26 26 PHE A 535 SER A 541 1 7
HELIX 27 27 ASP B 5 GLU B 7 5 3
HELIX 28 28 MET B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 ARG B 143 1 9
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 VAL B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 ALA B 204 LEU B 214 1 11
HELIX 36 36 SER B 215 GLY B 220 1 6
HELIX 37 37 MET B 241 VAL B 255 1 15
HELIX 38 38 ASN B 265 THR B 275 1 11
HELIX 39 39 PRO B 277 ASN B 283 1 7
HELIX 40 40 HIS B 284 LEU B 289 5 6
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 VAL B 340 1 6
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 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 ARG B 534 ALA B 542 1 9
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 VAL A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 LEU A 22 0
SHEET 2 AB11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
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 GLY A 201 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 VAL 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 VAL B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 LEU B 22 0
SHEET 2 BB11 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
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 GLY B 201 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 VAL B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 BD 2 VAL B 239 GLY B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.07
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.08
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
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 C GLU B 202 N SGB B 203 1555 1555 1.35
LINK C SGB B 203 N ALA B 204 1555 1555 1.34
CISPEP 1 TYR A 105 PRO A 106 0 2.77
CISPEP 2 TYR B 105 PRO B 106 0 1.48
SITE 1 AC1 6 MET A 241 ASP A 304 GLY A 305 ASP A 306
SITE 2 AC1 6 HOH A2041 ASN B 283
CRYST1 104.869 104.869 323.250 90.00 90.00 120.00 P 31 2 1 12
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 0.009536 0.005505 0.000000 0.00000
SCALE2 0.000000 0.011011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003094 0.00000
TER 4205 ALA A 542
TER 8402 ALA B 542
MASTER 613 0 3 52 34 0 2 6 8551 2 61 84
END |