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HEADER HYDROLASE 18-JUN-13 4BTL
TITLE AROMATIC INTERACTIONS IN ACETYLCHOLINESTERASE-INHIBITOR COMPLEXES
CAVEAT 4BTL NAG A 1544 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 2 4BTL NAG B 1548 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS ACETYLCHOLINESTERASE, HYDROLASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,W.QIAN,C.ENGDAHL,
AUTHOR 2 L.BERG,F.EKSTROM,A.LINUSSON
REVDAT 1 11-SEP-13 4BTL 0
JRNL AUTH C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,
JRNL AUTH 2 C.ENGDAHL,W.QIAN,F.J.EKSTROM,A.LINUSSON
JRNL TITL DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY
JRNL TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS.
JRNL REF J.MED.CHEM. 2013
JRNL REFN ESSN 1520-4804
JRNL PMID 23984975
JRNL DOI 10.1021/JM400990P
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.500
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.813
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.86
REMARK 3 NUMBER OF REFLECTIONS : 68722
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1916
REMARK 3 R VALUE (WORKING SET) : 0.1908
REMARK 3 FREE R VALUE : 0.2316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1384
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 28.8148 - 5.3756 0.99 7093 140 0.1712 0.1988
REMARK 3 2 5.3756 - 4.2712 0.99 6816 131 0.1440 0.1559
REMARK 3 3 4.2712 - 3.7326 0.98 6724 133 0.1581 0.2162
REMARK 3 4 3.7326 - 3.3919 0.99 6730 149 0.1992 0.2435
REMARK 3 5 3.3919 - 3.1491 0.99 6735 115 0.2231 0.2804
REMARK 3 6 3.1491 - 2.9637 0.99 6678 154 0.2235 0.2672
REMARK 3 7 2.9637 - 2.8154 0.99 6640 136 0.2279 0.2714
REMARK 3 8 2.8154 - 2.6929 0.99 6678 131 0.2601 0.3000
REMARK 3 9 2.6929 - 2.5893 0.99 6636 149 0.2620 0.3242
REMARK 3 10 2.5893 - 2.5000 0.99 6608 146 0.2818 0.3357
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 : 0.98
REMARK 3 K_SOL : 0.310
REMARK 3 B_SOL : 40.932
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.37
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.77
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.4814
REMARK 3 B22 (A**2) : 14.3665
REMARK 3 B33 (A**2) : -17.8480
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
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 8896
REMARK 3 ANGLE : 1.094 12115
REMARK 3 CHIRALITY : 0.077 1287
REMARK 3 PLANARITY : 0.005 1576
REMARK 3 DIHEDRAL : 16.667 3284
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6863 12.8063 41.3651
REMARK 3 T TENSOR
REMARK 3 T11: 0.3575 T22: 0.4322
REMARK 3 T33: 0.2012 T12: -0.0103
REMARK 3 T13: -0.0276 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 3.3564 L22: 2.0142
REMARK 3 L33: 4.4758 L12: -1.0457
REMARK 3 L13: 0.0256 L23: -0.5539
REMARK 3 S TENSOR
REMARK 3 S11: -0.1963 S12: -0.1974 S13: 0.1523
REMARK 3 S21: 0.4640 S22: 0.1863 S23: 0.0426
REMARK 3 S31: 0.0118 S32: -0.3499 S33: -0.0156
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 46:111)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2376 17.4367 29.1879
REMARK 3 T TENSOR
REMARK 3 T11: 0.3160 T22: 0.5378
REMARK 3 T33: 0.0865 T12: -0.0161
REMARK 3 T13: -0.0427 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.6208 L22: 0.8516
REMARK 3 L33: 1.8128 L12: -0.1488
REMARK 3 L13: -0.0442 L23: -0.2425
REMARK 3 S TENSOR
REMARK 3 S11: -0.1776 S12: -0.6056 S13: 0.2855
REMARK 3 S21: 0.2392 S22: 0.1372 S23: -0.2683
REMARK 3 S31: -0.0088 S32: 0.0108 S33: 0.0387
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 112:190)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6803 9.1452 25.3053
REMARK 3 T TENSOR
REMARK 3 T11: 0.2952 T22: 0.3500
REMARK 3 T33: 0.1915 T12: 0.0105
REMARK 3 T13: -0.0729 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 2.1202 L22: 1.5108
REMARK 3 L33: 4.5819 L12: -0.0705
REMARK 3 L13: -0.9803 L23: -0.0293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0502 S12: -0.1429 S13: -0.1237
REMARK 3 S21: 0.2306 S22: 0.0164 S23: -0.1082
REMARK 3 S31: 0.2384 S32: 0.0222 S33: 0.0388
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 191:240)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5687 2.3017 18.2060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2836 T22: 0.2572
REMARK 3 T33: 0.1420 T12: -0.0193
REMARK 3 T13: -0.0318 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 1.9208 L22: 1.4543
REMARK 3 L33: 6.1995 L12: 0.1204
REMARK 3 L13: -1.9955 L23: -0.6911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: -0.2937 S13: -0.1578
REMARK 3 S21: 0.1265 S22: 0.0662 S23: 0.0147
REMARK 3 S31: 0.4601 S32: -0.4187 S33: -0.0129
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 241:275)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6590 13.0302 11.9151
REMARK 3 T TENSOR
REMARK 3 T11: 0.2807 T22: 0.7831
REMARK 3 T33: 0.2718 T12: 0.0627
REMARK 3 T13: 0.0270 T23: 0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 4.1921 L22: 1.3581
REMARK 3 L33: 6.0583 L12: 1.1728
REMARK 3 L13: 5.0293 L23: 1.5596
REMARK 3 S TENSOR
REMARK 3 S11: -0.1829 S12: 0.3811 S13: -0.0458
REMARK 3 S21: -0.2684 S22: -0.1169 S23: -0.3160
REMARK 3 S31: -0.2438 S32: 1.0155 S33: 0.2767
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 276:318)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0237 11.1903 9.2738
REMARK 3 T TENSOR
REMARK 3 T11: 0.2542 T22: 0.5354
REMARK 3 T33: 0.2114 T12: 0.0905
REMARK 3 T13: 0.0210 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 2.8894 L22: 5.3397
REMARK 3 L33: 3.4607 L12: 2.0110
REMARK 3 L13: 1.0023 L23: 0.9542
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: 0.2888 S13: -0.0627
REMARK 3 S21: 0.2849 S22: 0.0011 S23: -0.3040
REMARK 3 S31: 0.1971 S32: 0.3429 S33: -0.0102
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 319:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8358 17.7976 2.7978
REMARK 3 T TENSOR
REMARK 3 T11: 0.1415 T22: 0.3255
REMARK 3 T33: 0.1702 T12: -0.0412
REMARK 3 T13: -0.0020 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 2.7804 L22: 5.3657
REMARK 3 L33: 4.0594 L12: 0.9321
REMARK 3 L13: -0.7861 L23: -2.0643
REMARK 3 S TENSOR
REMARK 3 S11: -0.0719 S12: 0.3593 S13: 0.0407
REMARK 3 S21: 0.0632 S22: -0.0150 S23: 0.0207
REMARK 3 S31: -0.0323 S32: -0.2159 S33: 0.0966
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 367:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9058 17.7599 -8.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2910 T22: 0.5722
REMARK 3 T33: 0.1769 T12: -0.0384
REMARK 3 T13: 0.0005 T23: 0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 2.3497 L22: 4.4892
REMARK 3 L33: 2.1751 L12: -2.1991
REMARK 3 L13: -0.0237 L23: 0.2870
REMARK 3 S TENSOR
REMARK 3 S11: 0.1964 S12: 0.5959 S13: 0.1494
REMARK 3 S21: -0.3755 S22: -0.1841 S23: 0.1124
REMARK 3 S31: 0.1995 S32: 0.0823 S33: -0.0483
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 407:486)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2744 13.6266 16.1449
REMARK 3 T TENSOR
REMARK 3 T11: 0.2162 T22: 0.5877
REMARK 3 T33: 0.1996 T12: -0.0312
REMARK 3 T13: -0.0143 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.6117 L22: 3.8991
REMARK 3 L33: 2.9673 L12: 0.2352
REMARK 3 L13: 0.2520 L23: 0.9212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: 0.0960 S13: 0.0387
REMARK 3 S21: 0.0343 S22: 0.0502 S23: 0.3303
REMARK 3 S31: 0.0822 S32: -0.7082 S33: -0.0200
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9515 1.0249 13.4346
REMARK 3 T TENSOR
REMARK 3 T11: 0.3491 T22: 0.8708
REMARK 3 T33: 0.4386 T12: -0.2109
REMARK 3 T13: 0.0054 T23: 0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 3.8904 L22: 8.5862
REMARK 3 L33: 2.2005 L12: -1.2593
REMARK 3 L13: -1.3768 L23: -1.0978
REMARK 3 S TENSOR
REMARK 3 S11: -0.1928 S12: 0.1179 S13: -0.8077
REMARK 3 S21: 0.1903 S22: -0.0112 S23: 1.1903
REMARK 3 S31: 0.5189 S32: -1.3949 S33: 0.2081
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 514:542)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6121 6.0928 -1.3185
REMARK 3 T TENSOR
REMARK 3 T11: 0.3530 T22: 0.9403
REMARK 3 T33: 0.1373 T12: -0.0390
REMARK 3 T13: -0.2290 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.6128 L22: 1.9024
REMARK 3 L33: 5.7747 L12: -0.4651
REMARK 3 L13: -1.5947 L23: 0.9710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0643 S12: -0.0693 S13: -0.0767
REMARK 3 S21: -0.5329 S22: -0.0958 S23: 0.3582
REMARK 3 S31: 0.5451 S32: 0.1252 S33: -0.0078
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 4:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7200 6.2561 -61.8018
REMARK 3 T TENSOR
REMARK 3 T11: 0.3883 T22: 0.6680
REMARK 3 T33: 0.2274 T12: 0.0320
REMARK 3 T13: -0.0840 T23: -0.1321
REMARK 3 L TENSOR
REMARK 3 L11: 2.5209 L22: 1.9497
REMARK 3 L33: 4.6081 L12: -0.2451
REMARK 3 L13: 0.6691 L23: -0.2434
REMARK 3 S TENSOR
REMARK 3 S11: 0.2128 S12: 0.6037 S13: 0.1243
REMARK 3 S21: -0.3903 S22: -0.1992 S23: 0.2829
REMARK 3 S31: -0.2285 S32: -0.8365 S33: -0.0160
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 46:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3722 -4.1337 -53.1468
REMARK 3 T TENSOR
REMARK 3 T11: 0.5816 T22: 0.6655
REMARK 3 T33: 0.2496 T12: -0.0786
REMARK 3 T13: -0.0998 T23: -0.1322
REMARK 3 L TENSOR
REMARK 3 L11: 0.5961 L22: 1.4661
REMARK 3 L33: 2.1416 L12: -0.4311
REMARK 3 L13: 0.5452 L23: 0.2354
REMARK 3 S TENSOR
REMARK 3 S11: 0.3075 S12: 0.3687 S13: -0.1366
REMARK 3 S21: -0.1650 S22: -0.2686 S23: 0.1251
REMARK 3 S31: 0.8846 S32: -0.0882 S33: -0.1083
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 87:170)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1067 4.1348 -51.0720
REMARK 3 T TENSOR
REMARK 3 T11: 0.3406 T22: 0.5852
REMARK 3 T33: 0.1375 T12: 0.0171
REMARK 3 T13: -0.0656 T23: -0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 1.4967 L22: 1.3072
REMARK 3 L33: 2.7230 L12: 0.2003
REMARK 3 L13: 0.0504 L23: 0.6660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0471 S12: 0.3549 S13: -0.1714
REMARK 3 S21: -0.2539 S22: -0.1392 S23: 0.1503
REMARK 3 S31: 0.1874 S32: -0.1915 S33: 0.0321
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 171:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5512 3.0263 -47.4148
REMARK 3 T TENSOR
REMARK 3 T11: 0.3068 T22: 0.5758
REMARK 3 T33: 0.1774 T12: 0.0369
REMARK 3 T13: -0.0514 T23: -0.0605
REMARK 3 L TENSOR
REMARK 3 L11: 1.0428 L22: 1.6383
REMARK 3 L33: 3.0652 L12: -0.3647
REMARK 3 L13: -0.0236 L23: 0.8992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0819 S12: 0.0437 S13: -0.0903
REMARK 3 S21: -0.0315 S22: 0.0839 S23: -0.1370
REMARK 3 S31: 0.2902 S32: 0.3901 S33: -0.1604
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 301:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0447 10.6142 -36.8734
REMARK 3 T TENSOR
REMARK 3 T11: 0.2215 T22: 0.4106
REMARK 3 T33: 0.1435 T12: -0.0578
REMARK 3 T13: -0.0746 T23: -0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 2.3490 L22: 2.2175
REMARK 3 L33: 4.9620 L12: -1.5951
REMARK 3 L13: -0.5991 L23: -0.0777
REMARK 3 S TENSOR
REMARK 3 S11: 0.1947 S12: 0.2382 S13: 0.2469
REMARK 3 S21: 0.0636 S22: -0.0659 S23: -0.2586
REMARK 3 S31: -0.0837 S32: 0.4682 S33: -0.1375
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 342:406)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2142 -5.3040 -18.5396
REMARK 3 T TENSOR
REMARK 3 T11: 0.6423 T22: 0.4029
REMARK 3 T33: 0.2484 T12: 0.0074
REMARK 3 T13: -0.1154 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 3.9030 L22: 1.9413
REMARK 3 L33: 5.6079 L12: 1.2148
REMARK 3 L13: 0.6400 L23: 0.2721
REMARK 3 S TENSOR
REMARK 3 S11: 0.2206 S12: -0.8224 S13: -0.2722
REMARK 3 S21: 0.4139 S22: -0.0307 S23: -0.0285
REMARK 3 S31: 0.9059 S32: 0.0979 S33: -0.1577
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 407:486)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4239 8.3091 -33.3972
REMARK 3 T TENSOR
REMARK 3 T11: 0.2872 T22: 0.5820
REMARK 3 T33: 0.2036 T12: 0.0060
REMARK 3 T13: 0.0012 T23: -0.0764
REMARK 3 L TENSOR
REMARK 3 L11: 1.1420 L22: 4.2293
REMARK 3 L33: 3.5151 L12: 0.7659
REMARK 3 L13: -0.2668 L23: 0.3582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0390 S12: -0.0222 S13: -0.0369
REMARK 3 S21: 0.1103 S22: -0.0387 S23: 0.2565
REMARK 3 S31: 0.1963 S32: -0.3665 S33: -0.0072
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 487:513)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9888 22.2256 -28.8968
REMARK 3 T TENSOR
REMARK 3 T11: 0.4229 T22: 0.7462
REMARK 3 T33: 0.3008 T12: 0.0891
REMARK 3 T13: 0.0761 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 3.4287 L22: 7.9371
REMARK 3 L33: 2.6602 L12: 1.4033
REMARK 3 L13: 1.5610 L23: -2.7497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: -0.5027 S13: 0.6404
REMARK 3 S21: 0.4943 S22: 0.3791 S23: 0.9116
REMARK 3 S31: -0.4337 S32: -1.0682 S33: -0.3772
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 514:543)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2780 11.2396 -21.7828
REMARK 3 T TENSOR
REMARK 3 T11: 0.4628 T22: 0.7597
REMARK 3 T33: -0.0153 T12: -0.0568
REMARK 3 T13: -0.0042 T23: -0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 1.7041 L22: 1.8700
REMARK 3 L33: 5.2563 L12: 0.1026
REMARK 3 L13: 2.9799 L23: -0.1108
REMARK 3 S TENSOR
REMARK 3 S11: 0.2122 S12: -0.1128 S13: -0.1586
REMARK 3 S21: 0.2656 S22: -0.2214 S23: 0.1544
REMARK 3 S31: 0.1765 S32: 0.6188 S33: 0.0823
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 258-264 WERE EXCLUDED FROM THE
REMARK 3 MODEL DUE TO LACK OF ELECTRON DENSITY.
REMARK 4
REMARK 4 4BTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-13.
REMARK 100 THE PDBE ID CODE IS EBI-57320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9805
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
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 : 69367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 29.05
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.5
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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 (%): 41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-31 %(W/V) PEG750MME, 0.1 M
REMARK 280 HEPES PH 7.0-7.1
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 39.33550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.55600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.41200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.55600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.33550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.41200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.9 KCAL/MOL
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 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 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 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 GLU B 268 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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 O HOH A 2149 O HOH A 2152 2.00
REMARK 500 O HOH B 2121 O HOH B 2125 2.09
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 -4.33 68.63
REMARK 500 CYS A 96 8.22 -156.00
REMARK 500 PHE A 123 14.79 58.31
REMARK 500 ALA A 167 75.75 -157.73
REMARK 500 SER A 203 -122.00 56.33
REMARK 500 ASP A 306 -83.13 -128.58
REMARK 500 SER A 371 173.67 -58.16
REMARK 500 HIS A 387 59.00 -140.17
REMARK 500 VAL A 407 -66.06 -129.60
REMARK 500 LEU A 518 118.32 -39.48
REMARK 500 ARG A 525 51.76 38.91
REMARK 500 PRO B 41 47.66 -75.79
REMARK 500 PRO B 55 153.04 -46.43
REMARK 500 ALA B 62 54.78 -116.11
REMARK 500 PHE B 123 19.92 59.61
REMARK 500 ALA B 167 65.47 -167.18
REMARK 500 SER B 203 -121.02 59.20
REMARK 500 ASP B 306 -83.42 -123.38
REMARK 500 ASP B 323 30.36 -98.42
REMARK 500 VAL B 407 -67.05 -120.10
REMARK 500 LYS B 496 166.70 64.05
REMARK 500 SER B 497 102.50 62.85
REMARK 500 ASN B 514 -166.97 -164.30
REMARK 500 ALA B 542 57.39 -105.94
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 PE3 A 1545
REMARK 610 PE3 A 1546
REMARK 610 PE3 A 1550
REMARK 610 PE3 A 1552
REMARK 610 PE3 A 1553
REMARK 610 PE3 B 1545
REMARK 610 PE3 B 1547
REMARK 610 PE3 B 1550
REMARK 610 PE3 B 1551
REMARK 610 PE3 B 1553
REMARK 610 PE3 B 1555
REMARK 610 5GZ A 1549
REMARK 610 5GZ B 1552
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GZ B1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 A1553
DBREF 4BTL A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4BTL B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET 5GZ A1543 28
HET NAG A1544 14
HET PE3 A1545 5
HET PE3 A1546 7
HET NAG A1547 14
HET EDO A1548 4
HET 5GZ A1549 22
HET PE3 A1550 4
HET EDO A1551 4
HET 5GZ B1544 28
HET PE3 B1545 7
HET NAG B1546 14
HET PE3 B1547 10
HET NAG B1548 14
HET EDO B1549 4
HET PE3 B1550 4
HET PE3 B1551 7
HET 5GZ B1552 23
HET PE3 B1553 7
HET EDO B1554 4
HET PE3 B1555 22
HET PE3 A1552 7
HET PE3 A1553 10
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-
HETNAM 2 PE3 TRIDECAOXAHENTETRACONTANE-1,41-DIOL
HETNAM 5GZ 4-(2-CHLORO-6-NITROPHENOXY)-N-[2-
HETNAM 2 5GZ (DIETHYLAMINO)ETHYL]BENZENESULFONAMIDE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
HETSYN PE3 POLYETHYLENE GLYCOL
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 6 5GZ 4(C18 H22 CL N3 O5 S)
FORMUL 8 PE3 11(C28 H58 O15)
FORMUL 8 NAG 4(C8 H15 N O6)
FORMUL 9 HOH *318(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 LEU A 216 PHE A 222 5 7
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 THR A 275 1 11
HELIX 12 12 PRO A 277 HIS A 284 1 8
HELIX 13 13 GLU A 285 LEU A 289 5 5
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 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 GLN B 7 5 3
HELIX 28 28 VAL 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 GLY B 143 1 9
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 ILE B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 SER B 215 1 13
HELIX 36 36 SER B 215 SER B 220 1 6
HELIX 37 37 ALA B 241 GLY B 256 1 16
HELIX 38 38 GLY B 264 THR B 275 1 12
HELIX 39 39 PRO B 277 TRP B 286 1 10
HELIX 40 40 HIS B 287 LEU B 289 5 3
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 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 PHE B 535 SER B 541 1 7
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
SHEET 1 BD 2 VAL B 239 SER 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 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 350 C1 NAG A1544 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A1547 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B1548 1555 1555 1.45
LINK ND2 ASN B 464 C1 NAG B1546 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -4.18
CISPEP 2 TYR B 105 PRO B 106 0 5.53
SITE 1 AC1 19 ASP A 74 TRP A 86 GLY A 120 GLY A 121
SITE 2 AC1 19 GLY A 122 TYR A 124 GLU A 202 TRP A 286
SITE 3 AC1 19 SER A 293 ILE A 294 PHE A 295 TYR A 337
SITE 4 AC1 19 PHE A 338 TYR A 341 HIS A 447 PE3 A1546
SITE 5 AC1 19 5GZ A1549 HOH A2060 HOH A2110
SITE 1 AC2 2 GLY A 345 ASN A 350
SITE 1 AC3 1 HIS A 381
SITE 1 AC4 3 TYR A 72 5GZ A1543 5GZ A1549
SITE 1 AC5 1 ASN A 464
SITE 1 AC6 2 GLU A 81 MET A 85
SITE 1 AC7 8 TRP A 286 HIS A 287 LEU A 289 GLN A 291
SITE 2 AC7 8 SER A 293 5GZ A1543 PE3 A1546 HOH A2110
SITE 1 AC8 1 ASP A 5
SITE 1 AC9 19 ASP B 74 TRP B 86 GLY B 120 GLY B 121
SITE 2 AC9 19 GLY B 122 TYR B 124 GLU B 202 TRP B 286
SITE 3 AC9 19 SER B 293 ILE B 294 PHE B 295 PHE B 297
SITE 4 AC9 19 TYR B 337 PHE B 338 TYR B 341 HIS B 447
SITE 5 AC9 19 5GZ B1552 HOH B2059 HOH B2101
SITE 1 BC1 4 TRP B 286 TYR B 341 5GZ B1552 HOH B2148
SITE 1 BC2 2 SER B 462 ASN B 464
SITE 1 BC3 4 GLN A 527 HIS B 381 TYR B 382 PE3 B1555
SITE 1 BC4 4 GLY B 345 SER B 347 ASN B 350 LEU B 353
SITE 1 BC5 5 THR B 112 GLU B 142 GLY B 143 ALA B 144
SITE 2 BC5 5 ARG B 485
SITE 1 BC6 3 ARG B 224 GLN B 325 THR B 486
SITE 1 BC7 4 ASP B 333 ASP B 396 LEU B 441 TRP B 442
SITE 1 BC8 7 TRP B 286 HIS B 287 LEU B 289 GLU B 292
SITE 2 BC8 7 SER B 293 5GZ B1544 PE3 B1545
SITE 1 BC9 2 ASP B 304 SER B 309
SITE 1 CC1 1 ARG B 417
SITE 1 CC2 9 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 CC2 9 ALA B 377 LEU B 380 HIS B 381 PHE B 531
SITE 3 CC2 9 PE3 B1547
SITE 1 CC3 2 ASP A 304 GLY A 305
SITE 1 CC4 1 ASP A 333
CRYST1 78.671 110.824 227.112 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 0.012711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009023 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004403 0.00000
TER 4210 ALA A 542
TER 8382 THR B 543
MASTER 697 0 23 53 34 0 35 6 8961 2 279 84
END |