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HEADER HYDROLASE 05-MAY-20 6WUZ
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY GB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS NERVE AGENT, ACETYLCHOLINESTERASE, TABUN, GA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.MCGUIRE,S.M.BESTER,S.D.PEGAN,J.J.HEIGHT
REVDAT 1 24-FEB-21 6WUZ 0
JRNL AUTH J.R.MCGUIRE,S.M.BESTER,M.A.GUELTA,J.CHEUNG,C.LANGLEY,
JRNL AUTH 2 M.D.WINEMILLER,S.Y.BAE,V.FUNK,J.M.MYSLINSKI,S.D.PEGAN,
JRNL AUTH 3 J.J.HEIGHT
JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO THE INHIBITION OF
JRNL TITL 2 HUMAN ACETYLCHOLINESTERASE BY G-SERIES NERVE AGENTS AND
JRNL TITL 3 SUBSEQUENT REACTIVATION BY HI-6.
JRNL REF CHEM.RES.TOXICOL. 2021
JRNL REFN ISSN 0893-228X
JRNL PMID 33538594
JRNL DOI 10.1021/ACS.CHEMRESTOX.0C00406
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 95232
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 4730
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 41.1750 - 6.9898 0.99 3366 168 0.1845 0.1757
REMARK 3 2 6.9898 - 5.5523 1.00 3266 154 0.1765 0.1844
REMARK 3 3 5.5523 - 4.8517 1.00 3203 171 0.1495 0.1790
REMARK 3 4 4.8517 - 4.4087 1.00 3157 168 0.1271 0.1588
REMARK 3 5 4.4087 - 4.0930 1.00 3177 151 0.1303 0.1391
REMARK 3 6 4.0930 - 3.8519 1.00 3138 173 0.1371 0.1358
REMARK 3 7 3.8519 - 3.6591 1.00 3130 173 0.1461 0.1789
REMARK 3 8 3.6591 - 3.4999 1.00 3053 192 0.1647 0.1956
REMARK 3 9 3.4999 - 3.3652 1.00 3148 176 0.1734 0.1950
REMARK 3 10 3.3652 - 3.2492 1.00 3096 192 0.1674 0.1889
REMARK 3 11 3.2492 - 3.1476 1.00 3135 138 0.1800 0.2323
REMARK 3 12 3.1476 - 3.0577 1.00 3107 184 0.1750 0.2224
REMARK 3 13 3.0577 - 2.9772 1.00 3102 157 0.1810 0.2216
REMARK 3 14 2.9772 - 2.9046 1.00 3097 167 0.1836 0.1961
REMARK 3 15 2.9046 - 2.8385 1.00 3080 148 0.1828 0.2048
REMARK 3 16 2.8385 - 2.7782 1.00 3120 170 0.1800 0.2024
REMARK 3 17 2.7782 - 2.7226 1.00 3115 150 0.1804 0.2109
REMARK 3 18 2.7226 - 2.6712 1.00 3088 154 0.1780 0.1936
REMARK 3 19 2.6712 - 2.6235 1.00 3051 173 0.1792 0.2396
REMARK 3 20 2.6235 - 2.5791 1.00 3146 150 0.1785 0.1936
REMARK 3 21 2.5791 - 2.5375 1.00 3071 187 0.1782 0.1956
REMARK 3 22 2.5375 - 2.4984 1.00 3074 153 0.1773 0.1857
REMARK 3 23 2.4984 - 2.4617 1.00 3099 151 0.1885 0.2584
REMARK 3 24 2.4617 - 2.4270 0.99 3028 155 0.1907 0.2322
REMARK 3 25 2.4270 - 2.3942 0.95 2918 133 0.1998 0.2497
REMARK 3 26 2.3942 - 2.3631 0.88 2800 124 0.2100 0.2493
REMARK 3 27 2.3631 - 2.3336 0.87 2625 145 0.2147 0.2321
REMARK 3 28 2.3336 - 2.3055 0.79 2460 128 0.2162 0.2613
REMARK 3 29 2.3055 - 2.2787 0.80 2421 116 0.2266 0.2218
REMARK 3 30 2.2787 - 2.2531 0.72 2231 129 0.2336 0.2633
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.82
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 : 0.005 8772
REMARK 3 ANGLE : 0.816 12004
REMARK 3 CHIRALITY : 0.048 1300
REMARK 3 PLANARITY : 0.005 1572
REMARK 3 DIHEDRAL : 5.146 6969
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8784 55.0355 381.1002
REMARK 3 T TENSOR
REMARK 3 T11: 0.4797 T22: 0.3548
REMARK 3 T33: 0.2118 T12: -0.0956
REMARK 3 T13: -0.0221 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 2.3709 L22: 5.3657
REMARK 3 L33: 1.5969 L12: -2.3406
REMARK 3 L13: 0.4302 L23: 1.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.2690 S12: -0.4383 S13: 0.0946
REMARK 3 S21: 0.8745 S22: 0.2520 S23: -0.1864
REMARK 3 S31: -0.0990 S32: 0.2678 S33: 0.0575
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6629 59.5680 365.7196
REMARK 3 T TENSOR
REMARK 3 T11: 0.2289 T22: 0.2766
REMARK 3 T33: 0.1986 T12: -0.0704
REMARK 3 T13: 0.0503 T23: -0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 1.5264 L22: 0.7109
REMARK 3 L33: 1.6994 L12: -0.1315
REMARK 3 L13: 0.4742 L23: 0.2993
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: -0.1048 S13: 0.0016
REMARK 3 S21: 0.2659 S22: -0.1276 S23: 0.1295
REMARK 3 S31: 0.0524 S32: -0.3492 S33: 0.1062
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9959 52.3965 367.6335
REMARK 3 T TENSOR
REMARK 3 T11: 0.2647 T22: 0.2204
REMARK 3 T33: 0.1844 T12: -0.0966
REMARK 3 T13: -0.0110 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 1.5186 L22: 2.4626
REMARK 3 L33: 2.3384 L12: -0.7700
REMARK 3 L13: -0.1449 L23: -0.3608
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: -0.2081 S13: -0.0932
REMARK 3 S21: 0.4014 S22: -0.0660 S23: -0.0140
REMARK 3 S31: 0.1715 S32: -0.1057 S33: 0.0601
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.3977 64.1043 359.9752
REMARK 3 T TENSOR
REMARK 3 T11: 0.1861 T22: 0.1597
REMARK 3 T33: 0.2274 T12: -0.0657
REMARK 3 T13: 0.0168 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 4.8783 L22: 1.1147
REMARK 3 L33: 3.7631 L12: -1.5560
REMARK 3 L13: 2.8574 L23: -0.8443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0604 S12: 0.1953 S13: 0.3239
REMARK 3 S21: 0.1272 S22: -0.1359 S23: -0.1555
REMARK 3 S31: -0.2233 S32: 0.1692 S33: 0.0930
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9583 57.3197 355.9574
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.2457
REMARK 3 T33: 0.2591 T12: -0.0527
REMARK 3 T13: -0.0176 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.3282 L22: 1.9637
REMARK 3 L33: 3.6383 L12: -0.6736
REMARK 3 L13: 0.0049 L23: 0.0588
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: -0.0392 S13: 0.1554
REMARK 3 S21: 0.0747 S22: -0.0704 S23: -0.3509
REMARK 3 S31: -0.1818 S32: 0.4122 S33: -0.0240
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 254 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2244 61.5295 343.5774
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.3583
REMARK 3 T33: 0.2022 T12: 0.0066
REMARK 3 T13: -0.0086 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.8947 L22: 3.5742
REMARK 3 L33: 2.3500 L12: -1.5606
REMARK 3 L13: -0.0111 L23: -0.4312
REMARK 3 S TENSOR
REMARK 3 S11: 0.1997 S12: 0.4965 S13: 0.1562
REMARK 3 S21: -0.2077 S22: -0.2997 S23: -0.0104
REMARK 3 S31: -0.1409 S32: -0.3956 S33: 0.0800
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0130 63.3027 349.4984
REMARK 3 T TENSOR
REMARK 3 T11: 0.2011 T22: 0.3922
REMARK 3 T33: 0.2578 T12: 0.0051
REMARK 3 T13: -0.0158 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 3.3743 L22: 3.2292
REMARK 3 L33: 1.9102 L12: -2.5693
REMARK 3 L13: -1.3908 L23: 1.7282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0719 S12: 0.2185 S13: 0.0517
REMARK 3 S21: -0.1913 S22: -0.2409 S23: 0.2406
REMARK 3 S31: -0.1143 S32: -0.3380 S33: 0.2136
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5751 59.0525 345.2995
REMARK 3 T TENSOR
REMARK 3 T11: 0.2582 T22: 0.4092
REMARK 3 T33: 0.2818 T12: -0.0630
REMARK 3 T13: 0.0103 T23: 0.0837
REMARK 3 L TENSOR
REMARK 3 L11: 2.1455 L22: 1.6154
REMARK 3 L33: 0.8050 L12: -0.6687
REMARK 3 L13: -0.3714 L23: -0.2014
REMARK 3 S TENSOR
REMARK 3 S11: 0.1928 S12: 0.3076 S13: 0.4461
REMARK 3 S21: -0.0250 S22: -0.2407 S23: -0.4182
REMARK 3 S31: -0.2285 S32: 0.2084 S33: 0.0355
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8908 38.9218 344.3743
REMARK 3 T TENSOR
REMARK 3 T11: 0.2383 T22: 0.2516
REMARK 3 T33: 0.2397 T12: -0.0353
REMARK 3 T13: 0.0285 T23: -0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 0.9062 L22: 0.7548
REMARK 3 L33: 3.2328 L12: 0.4292
REMARK 3 L13: 0.7160 L23: 0.3440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0853 S12: 0.0369 S13: -0.1467
REMARK 3 S21: 0.0471 S22: -0.1144 S23: 0.0248
REMARK 3 S31: 0.3739 S32: -0.3249 S33: 0.0205
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8228 39.0310 356.2910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1875 T22: 0.2571
REMARK 3 T33: 0.2719 T12: 0.0539
REMARK 3 T13: -0.0311 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 2.3677 L22: 1.8909
REMARK 3 L33: 5.5964 L12: 0.1353
REMARK 3 L13: -0.5563 L23: -0.3459
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.0511 S13: -0.2298
REMARK 3 S21: 0.0591 S22: -0.0837 S23: -0.2405
REMARK 3 S31: 0.4323 S32: 0.5476 S33: 0.0943
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4919 41.6860 337.4681
REMARK 3 T TENSOR
REMARK 3 T11: 0.2427 T22: 0.2723
REMARK 3 T33: 0.2342 T12: 0.0096
REMARK 3 T13: 0.0013 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 1.2957 L22: 1.0405
REMARK 3 L33: 8.7821 L12: 0.5596
REMARK 3 L13: 0.4572 L23: -1.0117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0509 S12: 0.1535 S13: -0.0473
REMARK 3 S21: -0.2216 S22: -0.0669 S23: -0.1793
REMARK 3 S31: 0.1963 S32: 0.0939 S33: 0.1237
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1837 53.2791 368.9989
REMARK 3 T TENSOR
REMARK 3 T11: 0.4135 T22: 0.3511
REMARK 3 T33: 0.2417 T12: 0.0153
REMARK 3 T13: 0.0972 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 3.4513 L22: 2.8425
REMARK 3 L33: 3.5687 L12: 1.0701
REMARK 3 L13: 0.1351 L23: -0.3248
REMARK 3 S TENSOR
REMARK 3 S11: 0.2052 S12: -0.3751 S13: -0.2528
REMARK 3 S21: 0.3254 S22: -0.0837 S23: 0.2674
REMARK 3 S31: 0.5452 S32: -0.4820 S33: -0.1127
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5556 65.7877 362.0676
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.3102
REMARK 3 T33: 0.2714 T12: 0.0064
REMARK 3 T13: 0.0394 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 1.3650 L22: 0.6031
REMARK 3 L33: 3.5138 L12: 0.7238
REMARK 3 L13: -1.1528 L23: -0.1185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: -0.2478 S13: 0.1241
REMARK 3 S21: 0.1036 S22: 0.0361 S23: 0.0541
REMARK 3 S31: -0.0846 S32: -0.0954 S33: -0.0695
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8713 57.1338 357.9984
REMARK 3 T TENSOR
REMARK 3 T11: 0.2080 T22: 0.2912
REMARK 3 T33: 0.1680 T12: -0.0284
REMARK 3 T13: 0.0520 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 3.0119 L22: 1.7663
REMARK 3 L33: 2.6920 L12: 0.2145
REMARK 3 L13: -0.9195 L23: -0.3305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0943 S12: -0.1188 S13: 0.0705
REMARK 3 S21: 0.0574 S22: 0.0438 S23: 0.2848
REMARK 3 S31: 0.2853 S32: -0.4333 S33: 0.0181
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4073 54.9800 360.3526
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.2869
REMARK 3 T33: 0.1664 T12: 0.0896
REMARK 3 T13: 0.0420 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 4.9038 L22: 4.8039
REMARK 3 L33: 2.4155 L12: 3.9105
REMARK 3 L13: -0.8085 L23: -0.1138
REMARK 3 S TENSOR
REMARK 3 S11: -0.0184 S12: -0.2421 S13: -0.1599
REMARK 3 S21: 0.1089 S22: -0.0625 S23: -0.1665
REMARK 3 S31: 0.4099 S32: 0.3561 S33: 0.0526
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5118 56.6616 350.6048
REMARK 3 T TENSOR
REMARK 3 T11: 0.2076 T22: 0.2856
REMARK 3 T33: 0.2046 T12: 0.0595
REMARK 3 T13: 0.0312 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 1.4695 L22: 1.3860
REMARK 3 L33: 2.3942 L12: 0.6033
REMARK 3 L13: -0.3561 L23: 0.6182
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: 0.0032 S13: -0.1069
REMARK 3 S21: 0.0488 S22: 0.0949 S23: -0.1705
REMARK 3 S31: 0.3228 S32: 0.2138 S33: 0.0057
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7223 73.9005 358.0921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2582 T22: 0.4269
REMARK 3 T33: 0.3197 T12: -0.0227
REMARK 3 T13: 0.0420 T23: -0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 1.0916 L22: 1.9367
REMARK 3 L33: 7.5375 L12: 0.3951
REMARK 3 L13: 0.7302 L23: 0.5069
REMARK 3 S TENSOR
REMARK 3 S11: 0.0198 S12: -0.1227 S13: 0.2873
REMARK 3 S21: 0.0525 S22: -0.0674 S23: -0.1068
REMARK 3 S31: -0.3628 S32: 0.6695 S33: 0.0833
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5546 51.3630 345.0213
REMARK 3 T TENSOR
REMARK 3 T11: 0.3390 T22: 0.4165
REMARK 3 T33: 0.3458 T12: 0.0786
REMARK 3 T13: 0.0968 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 2.4108 L22: 1.2860
REMARK 3 L33: 2.0150 L12: 1.1593
REMARK 3 L13: 0.8206 L23: 0.6142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0867 S12: 0.0703 S13: -0.5727
REMARK 3 S21: 0.0737 S22: 0.1653 S23: -0.3619
REMARK 3 S31: 0.4874 S32: 0.4966 S33: -0.0862
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3974 75.4004 332.6203
REMARK 3 T TENSOR
REMARK 3 T11: 0.2567 T22: 0.2308
REMARK 3 T33: 0.2108 T12: 0.0490
REMARK 3 T13: 0.0212 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 3.3199 L22: 2.6457
REMARK 3 L33: 4.1540 L12: 0.3391
REMARK 3 L13: -1.3754 L23: -0.4273
REMARK 3 S TENSOR
REMARK 3 S11: 0.1238 S12: -0.0485 S13: 0.2134
REMARK 3 S21: 0.0270 S22: 0.0125 S23: 0.1340
REMARK 3 S31: -0.4252 S32: -0.1003 S33: -0.1581
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4569 63.7152 331.8599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2196 T22: 0.3269
REMARK 3 T33: 0.1999 T12: 0.0021
REMARK 3 T13: 0.0122 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 1.5314 L22: 1.5424
REMARK 3 L33: 2.7074 L12: 0.2048
REMARK 3 L13: -0.8496 L23: -0.8269
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.2384 S13: 0.0581
REMARK 3 S21: -0.0959 S22: 0.0176 S23: 0.0685
REMARK 3 S31: 0.0005 S32: -0.2668 S33: -0.0243
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7800 64.8973 343.7061
REMARK 3 T TENSOR
REMARK 3 T11: 0.2539 T22: 0.4485
REMARK 3 T33: 0.2755 T12: -0.0277
REMARK 3 T13: -0.0149 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 2.4658 L22: 4.0064
REMARK 3 L33: 2.7652 L12: 1.9184
REMARK 3 L13: -0.0546 L23: -2.0603
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.0861 S13: 0.2083
REMARK 3 S21: -0.1420 S22: -0.0702 S23: 0.1765
REMARK 3 S31: 0.0331 S32: -0.3883 S33: -0.0300
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8088 48.9583 337.5267
REMARK 3 T TENSOR
REMARK 3 T11: 0.3507 T22: 0.4250
REMARK 3 T33: 0.2998 T12: -0.1669
REMARK 3 T13: 0.0175 T23: -0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 2.3995 L22: 2.0422
REMARK 3 L33: 2.7608 L12: -0.8532
REMARK 3 L13: -1.4883 L23: 0.9029
REMARK 3 S TENSOR
REMARK 3 S11: -0.1935 S12: 0.4253 S13: -0.3059
REMARK 3 S21: -0.0777 S22: 0.0217 S23: 0.2298
REMARK 3 S31: 0.4282 S32: -0.4969 S33: 0.1722
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0966 58.2988 328.4215
REMARK 3 T TENSOR
REMARK 3 T11: 0.3120 T22: 0.3035
REMARK 3 T33: 0.1866 T12: -0.0070
REMARK 3 T13: 0.0388 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 4.6092 L22: 1.9702
REMARK 3 L33: 3.6943 L12: 1.4989
REMARK 3 L13: -3.8481 L23: -0.9198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: -0.1545 S13: 0.1028
REMARK 3 S21: -0.0631 S22: -0.1233 S23: -0.0287
REMARK 3 S31: 0.4269 S32: -0.1562 S33: 0.1199
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 6WUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1000249037.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-16
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 : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95341
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.17.1-3660
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, KNO3, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 107.77000
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 215.54000
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 215.54000
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 107.77000
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: 4960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E
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, C
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 646.62000
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 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ARG A 493
REMARK 465 ASP A 494
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 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 ARG B 493
REMARK 465 ASP B 494
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 OG SER B 203 P1 UCJ B 602 1.26
REMARK 500 ND2 ASN A 350 C2 NAG C 1 2.05
REMARK 500 ND2 ASN B 265 O5 NAG E 1 2.12
REMARK 500 OG SER A 203 C1 UCJ A 601 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 PRO B 492 C - N - CA ANGL. DEV. = 9.2 DEGREES
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 -3.13 77.00
REMARK 500 ALA A 167 72.33 -153.94
REMARK 500 SER A 203 -118.14 61.58
REMARK 500 ASP A 306 -80.70 -99.20
REMARK 500 VAL A 407 -59.88 -129.29
REMARK 500 PHE B 47 -3.06 74.27
REMARK 500 CYS B 96 10.37 -143.55
REMARK 500 SER B 203 -118.33 61.09
REMARK 500 ASP B 306 -79.94 -97.31
REMARK 500 ASN B 350 -168.42 -107.31
REMARK 500 VAL B 407 -63.96 -126.62
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 UCJ B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6WUV RELATED DB: PDB
REMARK 900 RELATED ID: 6WUY RELATED DB: PDB
DBREF 6WUZ A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6WUZ 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 SER 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 SER 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
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET FUC D 3 10
HET NAG E 1 14
HET NAG E 2 14
HET FUC E 3 10
HET UCJ A 601 7
HET 7PE B 601 21
HET UCJ B 602 7
HET NAG B 603 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM UCJ PROPAN-2-YL HYDROGEN (S)-METHYLPHOSPHONATE
HETNAM 7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)
HETNAM 2 7PE ETHOXY)ETHANOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN 7PE POLYETHYLENE GLYCOL FRAGMENT
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 3 FUC 3(C6 H12 O5)
FORMUL 6 UCJ 2(C4 H11 O3 P)
FORMUL 7 7PE C14 H30 O7
FORMUL 10 HOH *794(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 HIS A 284 1 8
HELIX 14 AB5 GLU A 285 LEU A 289 5 5
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 ALA A 542 1 9
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 GLY B 240 VAL B 255 1 16
HELIX 38 AE2 ASN B 265 THR B 275 1 11
HELIX 39 AE3 PRO B 277 HIS B 284 1 8
HELIX 40 AE4 GLU B 285 LEU B 289 5 5
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 PHE B 535 SER B 541 1 7
SHEET 1 AA1 3 LEU A 9 THR A 11 0
SHEET 2 AA1 3 ARG A 16 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA511 ILE B 20 LEU B 22 0
SHEET 2 AA511 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK OG SER A 203 P1 UCJ A 601 1555 1555 1.41
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN B 265 C1 NAG E 1 1555 1555 1.42
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN B 464 C1 NAG B 603 1555 1555 1.50
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.42
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -3.73
CISPEP 2 TYR B 105 PRO B 106 0 3.28
CISPEP 3 CYS B 257 PRO B 258 0 -2.59
CRYST1 104.944 104.944 323.310 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 0.009529 0.005502 0.000000 0.00000
SCALE2 0.000000 0.011003 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003093 0.00000
TER 4189 ALA A 542
TER 8335 ALA B 542
MASTER 681 0 13 52 32 0 0 6 9205 2 180 84
END |