| content |
HEADER HYDROLASE/HYDROLASE INHIBITOR 29-JAN-19 6NTH
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY (S) STEREOISOMER OF A-232
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 HYDROLASE, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BESTER,M.A.GUELTA,J.J.HEIGHT,S.D.PEGAN
REVDAT 1 01-JUL-20 6NTH 0
JRNL AUTH J.J.HEIGHT,S.M.BESTER,M.A.GUELTA,S.Y.BAE,J.CHEUNG,S.D.PEGAN
JRNL TITL INSIGHTS INTO INHIBITION OF HUMAN ACETYLCHOLINESTERASE BY
JRNL TITL 2 NOVICHOK, A-SERIES NERVE AGENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 80756
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4033
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 41.3297 - 7.4234 0.99 2858 153 0.1591 0.1444
REMARK 3 2 7.4234 - 5.8977 1.00 2748 147 0.1557 0.1922
REMARK 3 3 5.8977 - 5.1538 1.00 2751 124 0.1423 0.1664
REMARK 3 4 5.1538 - 4.6833 1.00 2680 155 0.1196 0.1401
REMARK 3 5 4.6833 - 4.3480 0.99 2659 145 0.1098 0.1337
REMARK 3 6 4.3480 - 4.0919 1.00 2661 148 0.1184 0.1501
REMARK 3 7 4.0919 - 3.8871 0.99 2625 142 0.1210 0.1411
REMARK 3 8 3.8871 - 3.7180 1.00 2701 120 0.1279 0.1602
REMARK 3 9 3.7180 - 3.5750 1.00 2619 153 0.1399 0.1588
REMARK 3 10 3.5750 - 3.4517 1.00 2627 132 0.1512 0.1450
REMARK 3 11 3.4517 - 3.3438 1.00 2670 121 0.1503 0.1920
REMARK 3 12 3.3438 - 3.2483 1.00 2622 160 0.1521 0.1800
REMARK 3 13 3.2483 - 3.1628 1.00 2654 124 0.1564 0.1743
REMARK 3 14 3.1628 - 3.0856 1.00 2646 130 0.1558 0.1810
REMARK 3 15 3.0856 - 3.0155 1.00 2576 161 0.1601 0.2114
REMARK 3 16 3.0155 - 2.9514 1.00 2653 108 0.1605 0.1824
REMARK 3 17 2.9514 - 2.8923 1.00 2654 133 0.1758 0.2166
REMARK 3 18 2.8923 - 2.8378 1.00 2629 145 0.1740 0.2058
REMARK 3 19 2.8378 - 2.7871 1.00 2588 145 0.1707 0.1955
REMARK 3 20 2.7871 - 2.7399 1.00 2654 138 0.1705 0.2398
REMARK 3 21 2.7399 - 2.6957 1.00 2621 107 0.1686 0.1993
REMARK 3 22 2.6957 - 2.6542 1.00 2616 157 0.1813 0.2180
REMARK 3 23 2.6542 - 2.6152 1.00 2604 135 0.1821 0.2428
REMARK 3 24 2.6152 - 2.5783 1.00 2557 167 0.1883 0.2570
REMARK 3 25 2.5783 - 2.5435 1.00 2652 136 0.1959 0.2512
REMARK 3 26 2.5435 - 2.5105 1.00 2599 141 0.1973 0.2414
REMARK 3 27 2.5105 - 2.4791 1.00 2628 140 0.2126 0.3024
REMARK 3 28 2.4791 - 2.4492 1.00 2591 126 0.2217 0.2861
REMARK 3 29 2.4492 - 2.4208 0.97 2580 140 0.2312 0.2613
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.004 8757
REMARK 3 ANGLE : 0.672 11992
REMARK 3 CHIRALITY : 0.046 1303
REMARK 3 PLANARITY : 0.005 1571
REMARK 3 DIHEDRAL : 4.297 6968
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 441 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 70.5394 26.3098 20.5421
REMARK 3 T TENSOR
REMARK 3 T11: 0.4245 T22: 0.5671
REMARK 3 T33: 0.4376 T12: -0.0289
REMARK 3 T13: -0.0209 T23: 0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 2.6674 L22: 4.0804
REMARK 3 L33: 2.7627 L12: 2.3067
REMARK 3 L13: -0.0509 L23: 2.2320
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: 0.0528 S13: -0.2129
REMARK 3 S21: -0.2396 S22: -0.1393 S23: -0.1397
REMARK 3 S31: -0.0401 S32: 0.1047 S33: 0.0624
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.7028 42.3920 14.3560
REMARK 3 T TENSOR
REMARK 3 T11: 0.5874 T22: 0.6033
REMARK 3 T33: 0.4653 T12: -0.2214
REMARK 3 T13: -0.0280 T23: 0.1228
REMARK 3 L TENSOR
REMARK 3 L11: 4.0563 L22: 2.9701
REMARK 3 L33: 3.8089 L12: -1.8967
REMARK 3 L13: 1.9412 L23: -0.9222
REMARK 3 S TENSOR
REMARK 3 S11: -0.1935 S12: 0.4706 S13: 0.4636
REMARK 3 S21: -0.1257 S22: -0.0522 S23: -0.3552
REMARK 3 S31: -0.6655 S32: 0.6778 S33: 0.2828
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6181 32.9032 5.2081
REMARK 3 T TENSOR
REMARK 3 T11: 0.5698 T22: 0.5355
REMARK 3 T33: 0.3686 T12: 0.0143
REMARK 3 T13: -0.0327 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 3.4700 L22: 2.2279
REMARK 3 L33: 2.8041 L12: 1.1125
REMARK 3 L13: 3.0720 L23: 0.9854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: 0.0505 S13: 0.0576
REMARK 3 S21: -0.2684 S22: -0.1330 S23: 0.1320
REMARK 3 S31: -0.3168 S32: 0.1057 S33: 0.0606
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5864 35.9189 57.7726
REMARK 3 T TENSOR
REMARK 3 T11: 0.6083 T22: 0.4963
REMARK 3 T33: 0.3579 T12: -0.1262
REMARK 3 T13: 0.0244 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 3.1493 L22: 7.3329
REMARK 3 L33: 2.6517 L12: -1.9982
REMARK 3 L13: -0.9943 L23: -2.6034
REMARK 3 S TENSOR
REMARK 3 S11: -0.1140 S12: -0.5234 S13: -0.0485
REMARK 3 S21: 1.2320 S22: 0.1174 S23: 0.0018
REMARK 3 S31: 0.0211 S32: -0.2608 S33: 0.0456
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5701 21.2617 43.8628
REMARK 3 T TENSOR
REMARK 3 T11: 0.6021 T22: 0.4510
REMARK 3 T33: 0.4258 T12: -0.0632
REMARK 3 T13: -0.0015 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 2.6757 L22: 0.2975
REMARK 3 L33: 5.3006 L12: -0.7779
REMARK 3 L13: -2.9155 L23: 1.2107
REMARK 3 S TENSOR
REMARK 3 S11: -0.3701 S12: -0.2985 S13: -0.3028
REMARK 3 S21: 0.3866 S22: 0.1104 S23: -0.1889
REMARK 3 S31: 1.0649 S32: 0.4756 S33: 0.2743
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1311 41.3889 41.0155
REMARK 3 T TENSOR
REMARK 3 T11: 0.4416 T22: 0.5139
REMARK 3 T33: 0.3431 T12: -0.1491
REMARK 3 T13: -0.0803 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 2.9979 L22: 3.4793
REMARK 3 L33: 4.0188 L12: 0.8403
REMARK 3 L13: -1.1690 L23: -2.0833
REMARK 3 S TENSOR
REMARK 3 S11: 0.1761 S12: -0.0875 S13: 0.1173
REMARK 3 S21: 0.5204 S22: -0.2454 S23: -0.1999
REMARK 3 S31: -0.2818 S32: 0.3618 S33: 0.0886
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8743 35.2813 40.9999
REMARK 3 T TENSOR
REMARK 3 T11: 0.3502 T22: 0.3238
REMARK 3 T33: 0.3053 T12: -0.1231
REMARK 3 T13: 0.0071 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 3.7248 L22: 3.1297
REMARK 3 L33: 3.9128 L12: -2.0322
REMARK 3 L13: -1.6586 L23: 1.1620
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: -0.1443 S13: -0.0533
REMARK 3 S21: 0.4044 S22: -0.1017 S23: 0.0510
REMARK 3 S31: 0.0110 S32: 0.0743 S33: 0.0618
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 237 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9247 32.2742 34.1567
REMARK 3 T TENSOR
REMARK 3 T11: 0.3310 T22: 0.3677
REMARK 3 T33: 0.4015 T12: -0.1097
REMARK 3 T13: 0.0249 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.6947 L22: 1.2537
REMARK 3 L33: 3.2053 L12: -0.9424
REMARK 3 L13: 0.4481 L23: -0.0867
REMARK 3 S TENSOR
REMARK 3 S11: 0.1411 S12: -0.0413 S13: -0.1857
REMARK 3 S21: 0.1383 S22: -0.0518 S23: 0.3394
REMARK 3 S31: 0.2621 S32: -0.4090 S33: -0.0618
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 238 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4032 27.2327 24.4857
REMARK 3 T TENSOR
REMARK 3 T11: 0.3794 T22: 0.5814
REMARK 3 T33: 0.3765 T12: 0.0370
REMARK 3 T13: 0.0360 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 4.3900 L22: 3.5697
REMARK 3 L33: 3.3870 L12: -1.9934
REMARK 3 L13: 1.4531 L23: -1.1353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0988 S12: 0.1849 S13: -0.0935
REMARK 3 S21: -0.1672 S22: -0.2015 S23: -0.4193
REMARK 3 S31: 0.3158 S32: 0.5409 S33: 0.1242
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 301 THROUGH 341 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7947 37.3026 22.5471
REMARK 3 T TENSOR
REMARK 3 T11: 0.3989 T22: 0.4798
REMARK 3 T33: 0.3004 T12: -0.0743
REMARK 3 T13: -0.0003 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 2.6433 L22: 2.0991
REMARK 3 L33: 3.0489 L12: -1.6873
REMARK 3 L13: -0.6091 L23: -0.4726
REMARK 3 S TENSOR
REMARK 3 S11: 0.0660 S12: 0.3528 S13: -0.2753
REMARK 3 S21: -0.0705 S22: -0.2057 S23: 0.3232
REMARK 3 S31: 0.2220 S32: -0.1396 S33: 0.1140
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 342 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5058 53.4139 11.8870
REMARK 3 T TENSOR
REMARK 3 T11: 0.3873 T22: 0.5494
REMARK 3 T33: 0.4054 T12: -0.0744
REMARK 3 T13: 0.0194 T23: 0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 1.6837 L22: 3.4316
REMARK 3 L33: 4.3228 L12: 0.7749
REMARK 3 L13: 1.0702 L23: -1.1431
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.0529 S13: 0.0995
REMARK 3 S21: -0.1927 S22: -0.1600 S23: -0.2542
REMARK 3 S31: -0.4246 S32: 0.5753 S33: 0.1704
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 407 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6177 51.2914 30.8304
REMARK 3 T TENSOR
REMARK 3 T11: 0.3808 T22: 0.3274
REMARK 3 T33: 0.3481 T12: -0.0218
REMARK 3 T13: 0.0213 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 2.6341 L22: 1.8528
REMARK 3 L33: 4.1482 L12: 0.4366
REMARK 3 L13: -0.4159 L23: 0.2314
REMARK 3 S TENSOR
REMARK 3 S11: 0.1537 S12: -0.0432 S13: 0.3048
REMARK 3 S21: 0.1893 S22: -0.1704 S23: 0.0890
REMARK 3 S31: -0.3998 S32: 0.1254 S33: 0.0098
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7906 52.0139 32.8403
REMARK 3 T TENSOR
REMARK 3 T11: 0.3603 T22: 0.4818
REMARK 3 T33: 0.4616 T12: 0.0855
REMARK 3 T13: 0.0697 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 3.7367 L22: 3.3610
REMARK 3 L33: 6.5323 L12: 0.2773
REMARK 3 L13: 1.5867 L23: -0.0677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: -0.0637 S13: 0.2426
REMARK 3 S21: 0.0720 S22: -0.0704 S23: 0.4960
REMARK 3 S31: -0.6768 S32: -0.8199 S33: 0.0703
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9722 49.5949 14.2157
REMARK 3 T TENSOR
REMARK 3 T11: 0.3285 T22: 0.3897
REMARK 3 T33: 0.3689 T12: -0.0138
REMARK 3 T13: -0.0076 T23: 0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 2.2845 L22: 0.7459
REMARK 3 L33: 9.3665 L12: 0.1136
REMARK 3 L13: -1.5441 L23: 0.6216
REMARK 3 S TENSOR
REMARK 3 S11: -0.2094 S12: 0.2714 S13: 0.0614
REMARK 3 S21: 0.1143 S22: -0.0219 S23: 0.2924
REMARK 3 S31: 0.1313 S32: -0.4443 S33: 0.1627
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8604 37.9739 45.9041
REMARK 3 T TENSOR
REMARK 3 T11: 0.5407 T22: 0.4421
REMARK 3 T33: 0.3316 T12: 0.0026
REMARK 3 T13: -0.1344 T23: 0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 5.4476 L22: 2.8194
REMARK 3 L33: 4.5594 L12: 0.5001
REMARK 3 L13: -1.3137 L23: -0.4400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0673 S12: -0.2826 S13: 0.3998
REMARK 3 S21: 0.2517 S22: 0.0033 S23: -0.3332
REMARK 3 S31: -0.5410 S32: 0.5014 S33: 0.0390
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2977 25.3318 38.9283
REMARK 3 T TENSOR
REMARK 3 T11: 0.3861 T22: 0.4455
REMARK 3 T33: 0.3695 T12: -0.0079
REMARK 3 T13: -0.0418 T23: 0.0937
REMARK 3 L TENSOR
REMARK 3 L11: 1.5959 L22: 0.6010
REMARK 3 L33: 2.9037 L12: 0.4156
REMARK 3 L13: 1.4596 L23: -0.3428
REMARK 3 S TENSOR
REMARK 3 S11: 0.0674 S12: -0.3235 S13: -0.1442
REMARK 3 S21: 0.0951 S22: -0.0510 S23: -0.0711
REMARK 3 S31: 0.0013 S32: 0.0097 S33: -0.0151
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5463 33.3318 35.2495
REMARK 3 T TENSOR
REMARK 3 T11: 0.3489 T22: 0.3467
REMARK 3 T33: 0.2539 T12: 0.0251
REMARK 3 T13: -0.0591 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 4.4778 L22: 2.5814
REMARK 3 L33: 3.5071 L12: 1.1573
REMARK 3 L13: 0.3680 L23: 0.0951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1216 S12: -0.2163 S13: 0.0281
REMARK 3 S21: 0.0607 S22: 0.0245 S23: -0.0617
REMARK 3 S31: -0.2871 S32: 0.2146 S33: 0.0579
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8246 31.4464 30.4895
REMARK 3 T TENSOR
REMARK 3 T11: 0.3714 T22: 0.4900
REMARK 3 T33: 0.3296 T12: 0.0874
REMARK 3 T13: -0.0307 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 2.6627 L22: 1.8026
REMARK 3 L33: 2.7509 L12: 0.9360
REMARK 3 L13: 0.2654 L23: -0.1044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0261 S12: -0.1734 S13: 0.0222
REMARK 3 S21: 0.1094 S22: -0.0031 S23: 0.1982
REMARK 3 S31: -0.2339 S32: -0.4796 S33: 0.0132
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0828 17.7718 11.9892
REMARK 3 T TENSOR
REMARK 3 T11: 0.4240 T22: 0.4330
REMARK 3 T33: 0.4124 T12: 0.0784
REMARK 3 T13: -0.0213 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.5524 L22: 2.5920
REMARK 3 L33: 1.9571 L12: 0.5866
REMARK 3 L13: 0.9301 L23: 0.6857
REMARK 3 S TENSOR
REMARK 3 S11: 0.1460 S12: 0.1468 S13: -0.3086
REMARK 3 S21: 0.0841 S22: -0.0327 S23: -0.1702
REMARK 3 S31: 0.3741 S32: 0.1709 S33: -0.0957
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 367 THROUGH 406 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4794 18.7954 3.4765
REMARK 3 T TENSOR
REMARK 3 T11: 0.4439 T22: 0.4502
REMARK 3 T33: 0.3740 T12: 0.0340
REMARK 3 T13: -0.0371 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 3.3272 L22: 3.3332
REMARK 3 L33: 6.3239 L12: -1.5710
REMARK 3 L13: -0.2211 L23: 1.6354
REMARK 3 S TENSOR
REMARK 3 S11: 0.1000 S12: 0.2633 S13: -0.1366
REMARK 3 S21: -0.1535 S22: -0.1301 S23: -0.0962
REMARK 3 S31: 0.2786 S32: -0.0788 S33: -0.0185
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.5272 34.5772 13.6007
REMARK 3 T TENSOR
REMARK 3 T11: 0.4007 T22: 0.4243
REMARK 3 T33: 0.2757 T12: -0.0689
REMARK 3 T13: -0.0636 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 3.6299 L22: 6.0440
REMARK 3 L33: 3.3847 L12: -2.7312
REMARK 3 L13: 0.3911 L23: -0.8908
REMARK 3 S TENSOR
REMARK 3 S11: -0.2169 S12: 0.1938 S13: 0.2257
REMARK 3 S21: 0.1472 S22: 0.1243 S23: -0.2639
REMARK 3 S31: -0.3995 S32: 0.1777 S33: 0.1061
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 6NTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000239398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-16
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 : 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) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80880
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.31200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-21% POLYETHYLENE GLYCOL 3350 (PEG)
REMARK 280 AND 0.17- 0.21M POTASSIUM NITRATE, PH 7, VAPOR DIFFUSION,
REMARK 280 SITTING 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 108.07367
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 216.14733
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 216.14733
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 108.07367
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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 25.0 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 0.00000
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 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
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 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
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 A 203 P09 L0S A 608 1.23
REMARK 500 OG SER B 203 P09 L0S B 605 1.24
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 -1.84 71.74
REMARK 500 SER A 203 -129.35 58.05
REMARK 500 ASP A 306 -77.03 -105.56
REMARK 500 VAL A 407 -63.07 -126.87
REMARK 500 PHE B 47 -1.58 75.17
REMARK 500 ALA B 62 52.51 -110.31
REMARK 500 ALA B 167 75.46 -152.55
REMARK 500 SER B 203 -118.97 56.67
REMARK 500 ASP B 306 -83.91 -101.41
REMARK 500 VAL B 407 -60.40 -127.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1012 DISTANCE = 5.82 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 L0S A 608
REMARK 610 L0S B 605
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L0S A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L0S B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 605 through NAG A 607 bound to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800 602 through NAG A 604 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800 601 through NAG B 603 bound to ASN B 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NTG RELATED DB: PDB
DBREF 6NTH A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 6NTH 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 A 601 14
HET FUC A 602 10
HET NAG A 603 14
HET NAG A 604 14
HET FUC A 605 10
HET NAG A 606 14
HET NAG A 607 14
HET L0S A 608 12
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET L0S B 605 12
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM L0S METHYL (R)-N-[(1E)-1-(DIETHYLAMINO)ETHYLIDENE]-P-
HETNAM 2 L0S METHYLPHOSPHONAMIDATE
HETSYN L0S A-232
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 4 FUC 3(C6 H12 O5)
FORMUL 6 L0S 2(C8 H19 N2 O2 P)
FORMUL 10 HOH *587(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 ASN A 265 THR A 275 1 11
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 PHE A 535 SER A 541 1 7
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 ASP B 266 THR B 275 1 10
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 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O 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 VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
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 THR B 103 N SER B 30
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 SER B 196 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O 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 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.04
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 265 C1 NAG A 606 1555 1555 1.43
LINK ND2 ASN A 350 C1 NAG A 603 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN B 265 C1 NAG B 604 1555 1555 1.44
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.44
LINK C1 FUC A 602 O6 NAG A 603 1555 1555 1.44
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.45
LINK C1 FUC A 605 O6 NAG A 606 1555 1555 1.44
LINK O4 NAG A 606 C1 NAG A 607 1555 1555 1.44
LINK C1 FUC B 601 O6 NAG B 602 1555 1555 1.44
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 0.75
CISPEP 2 CYS A 257 PRO A 258 0 -9.71
CISPEP 3 TYR B 105 PRO B 106 0 -3.98
CISPEP 4 CYS B 257 PRO B 258 0 -2.87
SITE 1 AC1 12 TRP A 86 GLY A 121 GLY A 122 TYR A 133
SITE 2 AC1 12 GLU A 202 SER A 203 ALA A 204 PHE A 295
SITE 3 AC1 12 PHE A 297 TYR A 337 PHE A 338 HIS A 447
SITE 1 AC2 11 TRP B 86 GLY B 121 GLY B 122 TYR B 133
SITE 2 AC2 11 GLU B 202 SER B 203 ALA B 204 PHE B 295
SITE 3 AC2 11 PHE B 297 PHE B 338 HIS B 447
SITE 1 AC3 1 ASN A 265
SITE 1 AC4 6 PRO A 344 GLY A 345 SER A 347 ASP A 349
SITE 2 AC4 6 ASN A 350 HOH A 811
SITE 1 AC5 2 SER A 462 ASN A 464
SITE 1 AC6 1 ASN B 265
SITE 1 AC7 4 PRO B 344 GLY B 345 SER B 347 ASN B 350
CRYST1 105.646 105.646 324.221 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 0.009466 0.005465 0.000000 0.00000
SCALE2 0.000000 0.010930 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003084 0.00000
TER 4167 ALA A 542
TER 8321 ALA B 542
MASTER 671 0 13 52 32 0 12 6 9025 2 183 84
END |