| content |
HEADER HYDROLASE 27-MAY-19 6RU2
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUCURONOYL ESTERASE,GE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CERRENA UNICOLOR;
SOURCE 3 ORGANISM_TAXID: 90312;
SOURCE 4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: X-33;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA
KEYWDS CE15, ESTERASE, ALPHA/BETA-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.A.ERNST,C.MOSBECH,A.LANGKILDE,P.WESTH,A.MEYER,J.W.AGGER,S.LARSEN
REVDAT 1 18-MAR-20 6RU2 0
JRNL AUTH H.A.ERNST,C.MOSBECH,A.E.LANGKILDE,P.WESTH,A.S.MEYER,
JRNL AUTH 2 J.W.AGGER,S.LARSEN
JRNL TITL THE STRUCTURAL BASIS OF FUNGAL GLUCURONOYL ESTERASE ACTIVITY
JRNL TITL 2 ON NATURAL SUBSTRATES.
JRNL REF NAT COMMUN V. 11 1026 2020
JRNL REFN ESSN 2041-1723
JRNL PMID 32094331
JRNL DOI 10.1038/S41467-020-14833-9
REMARK 2
REMARK 2 RESOLUTION. 1.96 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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 67955
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3380
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 44.5660 - 5.6499 0.99 3005 156 0.1591 0.1622
REMARK 3 2 5.6499 - 4.4859 1.00 2831 159 0.1303 0.1580
REMARK 3 3 4.4859 - 3.9192 0.99 2801 150 0.1280 0.1405
REMARK 3 4 3.9192 - 3.5611 0.99 2759 128 0.1519 0.1992
REMARK 3 5 3.5611 - 3.3059 0.99 2753 145 0.1699 0.1797
REMARK 3 6 3.3059 - 3.1110 0.99 2727 136 0.1798 0.1999
REMARK 3 7 3.1110 - 2.9553 0.99 2702 165 0.1885 0.2075
REMARK 3 8 2.9553 - 2.8267 0.99 2692 142 0.1919 0.2059
REMARK 3 9 2.8267 - 2.7179 0.99 2687 135 0.1877 0.2357
REMARK 3 10 2.7179 - 2.6241 0.98 2682 139 0.1785 0.1940
REMARK 3 11 2.6241 - 2.5420 0.98 2690 128 0.1859 0.2374
REMARK 3 12 2.5420 - 2.4694 0.98 2660 145 0.1815 0.2241
REMARK 3 13 2.4694 - 2.4044 0.98 2653 129 0.1849 0.2006
REMARK 3 14 2.4044 - 2.3457 0.98 2625 153 0.1907 0.2177
REMARK 3 15 2.3457 - 2.2924 0.98 2665 134 0.1999 0.2292
REMARK 3 16 2.2924 - 2.2436 0.98 2651 137 0.1989 0.2445
REMARK 3 17 2.2436 - 2.1987 0.98 2657 137 0.2092 0.2639
REMARK 3 18 2.1987 - 2.1572 0.98 2643 132 0.2088 0.2225
REMARK 3 19 2.1572 - 2.1187 0.98 2631 129 0.2094 0.2505
REMARK 3 20 2.1187 - 2.0828 0.98 2668 135 0.2212 0.2450
REMARK 3 21 2.0828 - 2.0492 0.98 2581 149 0.2277 0.2775
REMARK 3 22 2.0492 - 2.0177 0.97 2615 146 0.2316 0.3056
REMARK 3 23 2.0177 - 1.9880 0.98 2621 138 0.2514 0.2587
REMARK 3 24 1.9880 - 1.9600 0.96 2576 133 0.2595 0.2973
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.24
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3188 7.2775 26.9803
REMARK 3 T TENSOR
REMARK 3 T11: 0.2013 T22: 0.1694
REMARK 3 T33: 0.1403 T12: -0.0091
REMARK 3 T13: -0.0824 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 2.3568 L22: 3.5366
REMARK 3 L33: 2.5509 L12: 0.9823
REMARK 3 L13: -0.8973 L23: -0.7282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0917 S12: -0.3151 S13: 0.0930
REMARK 3 S21: 0.1561 S22: -0.0748 S23: -0.2500
REMARK 3 S31: -0.1376 S32: 0.1422 S33: 0.1080
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6547 3.2464 31.1821
REMARK 3 T TENSOR
REMARK 3 T11: 0.1552 T22: 0.1386
REMARK 3 T33: 0.1364 T12: -0.0053
REMARK 3 T13: -0.0076 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.9139 L22: 2.1789
REMARK 3 L33: 2.7076 L12: 1.0387
REMARK 3 L13: 0.0531 L23: -0.0339
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: -0.2970 S13: -0.0532
REMARK 3 S21: 0.1840 S22: -0.0684 S23: -0.1214
REMARK 3 S31: 0.0791 S32: -0.0683 S33: 0.0253
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1312 6.2186 15.6706
REMARK 3 T TENSOR
REMARK 3 T11: 0.1928 T22: 0.1258
REMARK 3 T33: 0.1346 T12: 0.0086
REMARK 3 T13: -0.0099 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.6695 L22: 0.6698
REMARK 3 L33: 0.3486 L12: -0.0554
REMARK 3 L13: -0.1275 L23: -0.0382
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.0212 S13: -0.0279
REMARK 3 S21: 0.0425 S22: 0.0026 S23: 0.1067
REMARK 3 S31: -0.0203 S32: -0.0390 S33: 0.0029
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9051 5.9613 12.7563
REMARK 3 T TENSOR
REMARK 3 T11: 0.1948 T22: 0.1319
REMARK 3 T33: 0.1419 T12: 0.0034
REMARK 3 T13: -0.0064 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.5626 L22: 0.2768
REMARK 3 L33: 1.0107 L12: -0.1331
REMARK 3 L13: -0.0766 L23: -0.2546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: 0.0407 S13: -0.0340
REMARK 3 S21: -0.0229 S22: -0.0520 S23: -0.0367
REMARK 3 S31: -0.0707 S32: 0.0670 S33: 0.0535
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 408 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7724 -8.1739 13.5124
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.1373
REMARK 3 T33: 0.1780 T12: 0.0190
REMARK 3 T13: -0.0095 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.5257 L22: 0.3692
REMARK 3 L33: 1.6008 L12: 0.2249
REMARK 3 L13: -0.0193 L23: 0.1235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: -0.0006 S13: -0.0861
REMARK 3 S21: 0.0074 S22: -0.0621 S23: -0.0043
REMARK 3 S31: 0.0411 S32: 0.0398 S33: 0.0911
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 409 THROUGH 432 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1915 -15.4537 15.3465
REMARK 3 T TENSOR
REMARK 3 T11: 0.2170 T22: 0.1321
REMARK 3 T33: 0.2156 T12: -0.0056
REMARK 3 T13: -0.0200 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 2.1481 L22: 2.0311
REMARK 3 L33: 2.3305 L12: -0.1566
REMARK 3 L13: -0.3596 L23: -0.1421
REMARK 3 S TENSOR
REMARK 3 S11: 0.0539 S12: 0.0024 S13: -0.2646
REMARK 3 S21: -0.0046 S22: 0.0156 S23: -0.0254
REMARK 3 S31: 0.1568 S32: 0.0265 S33: -0.0670
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 433 THROUGH 459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3763 -8.0365 15.4737
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.1263
REMARK 3 T33: 0.1628 T12: 0.0378
REMARK 3 T13: -0.0103 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.6717 L22: 1.4121
REMARK 3 L33: 2.4991 L12: 0.3011
REMARK 3 L13: 0.6194 L23: -0.5344
REMARK 3 S TENSOR
REMARK 3 S11: 0.1099 S12: 0.0022 S13: -0.1338
REMARK 3 S21: 0.0164 S22: -0.0189 S23: -0.1260
REMARK 3 S31: 0.1494 S32: 0.2494 S33: -0.0979
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7133 -35.0039 30.6828
REMARK 3 T TENSOR
REMARK 3 T11: 0.1855 T22: 0.1746
REMARK 3 T33: 0.1468 T12: -0.0173
REMARK 3 T13: -0.0409 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 2.3139 L22: 2.0161
REMARK 3 L33: 2.5084 L12: 0.9967
REMARK 3 L13: -0.9105 L23: -0.9689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: -0.2711 S13: 0.0607
REMARK 3 S21: 0.0718 S22: -0.0801 S23: -0.0636
REMARK 3 S31: -0.1175 S32: 0.1388 S33: 0.0099
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4141 -37.0671 35.4362
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.1567
REMARK 3 T33: 0.1829 T12: 0.0040
REMARK 3 T13: 0.0008 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 2.1552 L22: 1.4412
REMARK 3 L33: 2.3394 L12: 0.2832
REMARK 3 L13: -0.0747 L23: -0.4179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: -0.1999 S13: 0.0377
REMARK 3 S21: 0.2361 S22: -0.0543 S23: -0.0488
REMARK 3 S31: -0.0524 S32: 0.0120 S33: 0.0489
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6653 -28.8660 23.2246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2000 T22: 0.1839
REMARK 3 T33: 0.2496 T12: 0.0057
REMARK 3 T13: 0.0418 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 2.3739 L22: 0.7054
REMARK 3 L33: 0.8205 L12: -0.2946
REMARK 3 L13: 0.0615 L23: -0.0905
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.1194 S13: -0.1112
REMARK 3 S21: 0.0802 S22: -0.0362 S23: 0.1511
REMARK 3 S31: -0.0764 S32: -0.1639 S33: 0.0270
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3871 -25.8024 19.5481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.2018
REMARK 3 T33: 0.2489 T12: 0.0242
REMARK 3 T13: 0.0249 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 1.3641 L22: 2.1732
REMARK 3 L33: 2.4367 L12: -0.8538
REMARK 3 L13: 0.2458 L23: 1.2717
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: -0.0389 S13: 0.2285
REMARK 3 S21: -0.1225 S22: -0.0198 S23: 0.1066
REMARK 3 S31: -0.1553 S32: -0.1466 S33: -0.0082
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0207 -44.3940 18.8972
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.2293
REMARK 3 T33: 0.2152 T12: -0.0530
REMARK 3 T13: 0.0062 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 1.9494 L22: 1.5723
REMARK 3 L33: 2.7307 L12: -0.4160
REMARK 3 L13: -1.0150 L23: -0.0935
REMARK 3 S TENSOR
REMARK 3 S11: -0.0933 S12: 0.0992 S13: -0.0506
REMARK 3 S21: 0.0296 S22: -0.0016 S23: 0.3088
REMARK 3 S31: 0.1967 S32: -0.5135 S33: 0.0532
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 235 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8012 -23.4699 13.7832
REMARK 3 T TENSOR
REMARK 3 T11: 0.1952 T22: 0.1576
REMARK 3 T33: 0.2196 T12: 0.0241
REMARK 3 T13: -0.0001 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.2742 L22: 1.6430
REMARK 3 L33: 1.4721 L12: 0.6225
REMARK 3 L13: 0.0848 L23: 0.5266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0398 S12: 0.0986 S13: 0.1520
REMARK 3 S21: -0.0872 S22: 0.0484 S23: 0.2008
REMARK 3 S31: -0.1794 S32: -0.0572 S33: -0.0919
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 236 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5010 -36.5951 18.0252
REMARK 3 T TENSOR
REMARK 3 T11: 0.1658 T22: 0.1312
REMARK 3 T33: 0.1436 T12: 0.0016
REMARK 3 T13: 0.0001 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.4300 L22: 0.9189
REMARK 3 L33: 0.7573 L12: 0.2550
REMARK 3 L13: -0.2310 L23: 0.0055
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: -0.0183 S13: -0.0042
REMARK 3 S21: 0.0139 S22: -0.0361 S23: 0.0707
REMARK 3 S31: -0.0125 S32: -0.0314 S33: 0.0488
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 408 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8458 -47.1288 19.3826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.1354
REMARK 3 T33: 0.1698 T12: 0.0030
REMARK 3 T13: -0.0051 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.6404 L22: 0.5148
REMARK 3 L33: 0.8053 L12: 0.3279
REMARK 3 L13: -0.0294 L23: 0.1482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: 0.0098 S13: -0.0307
REMARK 3 S21: 0.0473 S22: -0.0357 S23: 0.0565
REMARK 3 S31: 0.0337 S32: -0.0313 S33: 0.0424
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 409 THROUGH 432 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6075 -55.9619 22.8998
REMARK 3 T TENSOR
REMARK 3 T11: 0.2037 T22: 0.1460
REMARK 3 T33: 0.2582 T12: -0.0474
REMARK 3 T13: 0.0362 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 3.3201 L22: 3.1863
REMARK 3 L33: 2.9874 L12: -0.8733
REMARK 3 L13: -0.5282 L23: 1.4154
REMARK 3 S TENSOR
REMARK 3 S11: -0.1205 S12: -0.0566 S13: -0.4031
REMARK 3 S21: 0.2788 S22: -0.1569 S23: 0.2195
REMARK 3 S31: 0.4499 S32: -0.2018 S33: 0.2593
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 433 THROUGH 459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5292 -51.9814 22.0977
REMARK 3 T TENSOR
REMARK 3 T11: 0.1752 T22: 0.1098
REMARK 3 T33: 0.1746 T12: 0.0138
REMARK 3 T13: -0.0254 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 1.0568 L22: 1.4426
REMARK 3 L33: 3.8646 L12: 0.1781
REMARK 3 L13: -0.0199 L23: 0.5002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0417 S12: -0.0193 S13: -0.0854
REMARK 3 S21: 0.0522 S22: 0.0117 S23: -0.1318
REMARK 3 S31: 0.2210 S32: 0.2321 S33: -0.0410
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 6RU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68208
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 49.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.26100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 1.18300
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: PHASER
REMARK 200 STARTING MODEL: 6RTV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PH 5.5, 17% PEG10000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 131.11950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.22500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.22500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.55975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.22500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.22500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 196.67925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.22500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.22500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.55975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.22500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.22500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 196.67925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 131.11950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 835 LIES ON A SPECIAL POSITION.
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 79
REMARK 465 ALA A 80
REMARK 465 LEU A 460
REMARK 465 GLU A 461
REMARK 465 GLN A 462
REMARK 465 LYS A 463
REMARK 465 LEU A 464
REMARK 465 ILE A 465
REMARK 465 SER A 466
REMARK 465 GLU A 467
REMARK 465 GLU A 468
REMARK 465 ASP A 469
REMARK 465 LEU A 470
REMARK 465 ASN A 471
REMARK 465 SER A 472
REMARK 465 ALA A 473
REMARK 465 VAL A 474
REMARK 465 ASP A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 HIS A 480
REMARK 465 HIS A 481
REMARK 465 GLY B 79
REMARK 465 ALA B 80
REMARK 465 LEU B 460
REMARK 465 GLU B 461
REMARK 465 GLN B 462
REMARK 465 LYS B 463
REMARK 465 LEU B 464
REMARK 465 ILE B 465
REMARK 465 SER B 466
REMARK 465 GLU B 467
REMARK 465 GLU B 468
REMARK 465 ASP B 469
REMARK 465 LEU B 470
REMARK 465 ASN B 471
REMARK 465 SER B 472
REMARK 465 ALA B 473
REMARK 465 VAL B 474
REMARK 465 ASP B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 HIS B 480
REMARK 465 HIS B 481
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 ASN A 92 97.53 -162.57
REMARK 500 ARG A 109 -30.23 -135.62
REMARK 500 ARG A 109 -35.81 -132.71
REMARK 500 GLU A 129 -21.20 -141.54
REMARK 500 SER A 162 -12.77 85.29
REMARK 500 GLN A 213 45.17 -153.64
REMARK 500 SER A 215 -169.67 -172.13
REMARK 500 SER A 270 -128.75 64.15
REMARK 500 PRO A 343 35.03 -81.35
REMARK 500 SER A 370 67.28 62.99
REMARK 500 SER A 427 49.89 -87.15
REMARK 500 TRP A 449 -31.18 -135.50
REMARK 500 ASN B 92 98.02 -161.97
REMARK 500 GLN B 213 48.53 -148.75
REMARK 500 SER B 215 -177.54 -174.18
REMARK 500 SER B 270 -130.76 63.98
REMARK 500 ASN B 325 -168.16 -160.85
REMARK 500 PRO B 343 30.75 -81.94
REMARK 500 SER B 370 62.65 66.25
REMARK 500 TRP B 449 -32.68 -135.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 506 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 259 O
REMARK 620 2 GOL B 505 O2 90.9
REMARK 620 3 GOL B 505 O3 156.7 65.8
REMARK 620 4 HOH B 797 O 101.0 164.8 102.0
REMARK 620 5 HOH B 681 O 87.2 97.2 95.2 92.8
REMARK 620 6 HOH B 663 O 86.3 84.6 91.5 86.8 173.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN A 504 bound
REMARK 800 to SER A 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN A 502 bound
REMARK 800 to THR A 87
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800 to ASN A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN B 504 bound
REMARK 800 to SER B 86
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN B 502 bound
REMARK 800 to THR B 87
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800 to ASN B 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6RTV RELATED DB: PDB
REMARK 900 6RTV CONTAINS AN INACTIVE S270A VARIANT OF THE SAME PROTEIN
REMARK 900 RELATED ID: 6RU1 RELATED DB: PDB
REMARK 900 6RU1 CONTAINS AN INACTIVE S270A VARIANT OF THE SAME PROTEIN
REMARK 900 COMPLEXED WITH AN ALDOURONIC ACID LIGAND
DBREF1 6RU2 A 79 458 UNP GCE_CERUI
DBREF2 6RU2 A A0A0A7EQR3 95 474
DBREF1 6RU2 B 79 458 UNP GCE_CERUI
DBREF2 6RU2 B A0A0A7EQR3 95 474
SEQADV 6RU2 GLY A 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU A 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU A 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLN A 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LYS A 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU A 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ILE A 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 SER A 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU A 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU A 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASP A 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU A 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASN A 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 SER A 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ALA A 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 VAL A 474 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASP A 475 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 476 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 477 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 478 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 479 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 480 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS A 481 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLY B 459 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU B 460 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU B 461 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLN B 462 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LYS B 463 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU B 464 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ILE B 465 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 SER B 466 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU B 467 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 GLU B 468 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASP B 469 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 LEU B 470 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASN B 471 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 SER B 472 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ALA B 473 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 VAL B 474 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 ASP B 475 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 476 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 477 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 478 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 479 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 480 UNP A0A0A7EQR EXPRESSION TAG
SEQADV 6RU2 HIS B 481 UNP A0A0A7EQR EXPRESSION TAG
SEQRES 1 A 403 GLY ALA CYS GLY ALA ILE ALA SER THR VAL PRO ASN TYR
SEQRES 2 A 403 ASN ASN ALA LYS LEU PRO ASP PRO PHE THR PHE ALA ASN
SEQRES 3 A 403 GLY THR ALA LEU ARG THR LYS ALA ASP TRP SER CYS ARG
SEQRES 4 A 403 ARG ALA GLU ILE SER ALA LEU ILE GLN ASN TYR GLU ALA
SEQRES 5 A 403 GLY THR LEU PRO PRO LYS PRO PRO VAL VAL THR ALA SER
SEQRES 6 A 403 PHE SER LYS SER GLY ASN THR GLY THR LEU ALA ILE THR
SEQRES 7 A 403 ALA GLY LEU SER ASN SER GLN THR ILE LYS PHE SER PRO
SEQRES 8 A 403 THR ILE SER TYR PRO SER GLY THR PRO PRO ALA ASN GLY
SEQRES 9 A 403 TRP PRO LEU ILE ILE ALA TYR GLU GLY GLY SER ILE PRO
SEQRES 10 A 403 ILE PRO ALA GLY VAL ALA THR LEU THR TYR SER ASN SER
SEQRES 11 A 403 ASP MET ALA GLN GLN ASN SER ALA SER SER ARG GLY GLN
SEQRES 12 A 403 GLY LEU PHE TYR GLN LEU TYR GLY SER THR HIS SER ALA
SEQRES 13 A 403 SER ALA MET THR ALA TRP VAL TRP GLY VAL SER ARG ILE
SEQRES 14 A 403 ILE ASP ALA LEU GLU MET THR PRO THR ALA GLN ILE ASN
SEQRES 15 A 403 THR GLN ARG ILE GLY VAL THR GLY CYS SER ARG ASP GLY
SEQRES 16 A 403 LYS GLY ALA LEU MET ALA GLY ALA PHE GLU GLU ARG ILE
SEQRES 17 A 403 ALA LEU THR ILE PRO GLN GLU SER GLY SER GLY GLY ASP
SEQRES 18 A 403 ALA CYS TRP ARG LEU SER LYS TYR GLU ILE ASP ASN GLY
SEQRES 19 A 403 ASN GLN VAL GLN ASP ALA VAL GLU ILE VAL GLY GLU ASN
SEQRES 20 A 403 VAL TRP PHE SER THR ASN PHE ASN ASN TYR VAL GLN LYS
SEQRES 21 A 403 LEU PRO THR VAL PRO GLU ASP HIS HIS LEU LEU ALA ALA
SEQRES 22 A 403 MET VAL ALA PRO ARG ALA MET ILE SER PHE GLU ASN THR
SEQRES 23 A 403 ASP TYR LEU TRP LEU SER PRO MET SER SER PHE GLY CYS
SEQRES 24 A 403 MET THR ALA ALA HIS THR VAL TRP GLN GLY LEU GLY ILE
SEQRES 25 A 403 ALA ASP SER HIS GLY PHE ALA GLN VAL GLY GLY HIS ALA
SEQRES 26 A 403 HIS CYS ALA TRP PRO SER SER LEU THR PRO GLN LEU ASN
SEQRES 27 A 403 ALA PHE ILE ASN ARG PHE LEU LEU ASP GLN SER ALA THR
SEQRES 28 A 403 THR ASN VAL PHE THR THR ASN ASN GLN PHE GLY LYS VAL
SEQRES 29 A 403 GLN TRP ASN ALA ALA ASN TRP ILE THR TRP THR THR PRO
SEQRES 30 A 403 THR LEU THR GLY LEU GLU GLN LYS LEU ILE SER GLU GLU
SEQRES 31 A 403 ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 403 GLY ALA CYS GLY ALA ILE ALA SER THR VAL PRO ASN TYR
SEQRES 2 B 403 ASN ASN ALA LYS LEU PRO ASP PRO PHE THR PHE ALA ASN
SEQRES 3 B 403 GLY THR ALA LEU ARG THR LYS ALA ASP TRP SER CYS ARG
SEQRES 4 B 403 ARG ALA GLU ILE SER ALA LEU ILE GLN ASN TYR GLU ALA
SEQRES 5 B 403 GLY THR LEU PRO PRO LYS PRO PRO VAL VAL THR ALA SER
SEQRES 6 B 403 PHE SER LYS SER GLY ASN THR GLY THR LEU ALA ILE THR
SEQRES 7 B 403 ALA GLY LEU SER ASN SER GLN THR ILE LYS PHE SER PRO
SEQRES 8 B 403 THR ILE SER TYR PRO SER GLY THR PRO PRO ALA ASN GLY
SEQRES 9 B 403 TRP PRO LEU ILE ILE ALA TYR GLU GLY GLY SER ILE PRO
SEQRES 10 B 403 ILE PRO ALA GLY VAL ALA THR LEU THR TYR SER ASN SER
SEQRES 11 B 403 ASP MET ALA GLN GLN ASN SER ALA SER SER ARG GLY GLN
SEQRES 12 B 403 GLY LEU PHE TYR GLN LEU TYR GLY SER THR HIS SER ALA
SEQRES 13 B 403 SER ALA MET THR ALA TRP VAL TRP GLY VAL SER ARG ILE
SEQRES 14 B 403 ILE ASP ALA LEU GLU MET THR PRO THR ALA GLN ILE ASN
SEQRES 15 B 403 THR GLN ARG ILE GLY VAL THR GLY CYS SER ARG ASP GLY
SEQRES 16 B 403 LYS GLY ALA LEU MET ALA GLY ALA PHE GLU GLU ARG ILE
SEQRES 17 B 403 ALA LEU THR ILE PRO GLN GLU SER GLY SER GLY GLY ASP
SEQRES 18 B 403 ALA CYS TRP ARG LEU SER LYS TYR GLU ILE ASP ASN GLY
SEQRES 19 B 403 ASN GLN VAL GLN ASP ALA VAL GLU ILE VAL GLY GLU ASN
SEQRES 20 B 403 VAL TRP PHE SER THR ASN PHE ASN ASN TYR VAL GLN LYS
SEQRES 21 B 403 LEU PRO THR VAL PRO GLU ASP HIS HIS LEU LEU ALA ALA
SEQRES 22 B 403 MET VAL ALA PRO ARG ALA MET ILE SER PHE GLU ASN THR
SEQRES 23 B 403 ASP TYR LEU TRP LEU SER PRO MET SER SER PHE GLY CYS
SEQRES 24 B 403 MET THR ALA ALA HIS THR VAL TRP GLN GLY LEU GLY ILE
SEQRES 25 B 403 ALA ASP SER HIS GLY PHE ALA GLN VAL GLY GLY HIS ALA
SEQRES 26 B 403 HIS CYS ALA TRP PRO SER SER LEU THR PRO GLN LEU ASN
SEQRES 27 B 403 ALA PHE ILE ASN ARG PHE LEU LEU ASP GLN SER ALA THR
SEQRES 28 B 403 THR ASN VAL PHE THR THR ASN ASN GLN PHE GLY LYS VAL
SEQRES 29 B 403 GLN TRP ASN ALA ALA ASN TRP ILE THR TRP THR THR PRO
SEQRES 30 B 403 THR LEU THR GLY LEU GLU GLN LYS LEU ILE SER GLU GLU
SEQRES 31 B 403 ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
HET NAG A 501 14
HET MAN A 502 22
HET EDO A 503 10
HET MAN A 504 22
HET NAG B 501 14
HET MAN B 502 22
HET EDO B 503 10
HET MAN B 504 22
HET GOL B 505 14
HET NA B 506 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 MAN 4(C6 H12 O6)
FORMUL 5 EDO 2(C2 H6 O2)
FORMUL 11 GOL C3 H8 O3
FORMUL 12 NA NA 1+
FORMUL 13 HOH *542(H2 O)
HELIX 1 AA1 THR A 110 GLU A 129 1 20
HELIX 2 AA2 SER A 206 ALA A 211 1 6
HELIX 3 AA3 SER A 215 ARG A 219 5 5
HELIX 4 AA4 GLY A 222 GLY A 229 1 8
HELIX 5 AA5 SER A 235 MET A 253 1 19
HELIX 6 AA6 THR A 254 ALA A 257 5 4
HELIX 7 AA7 SER A 270 GLU A 283 1 14
HELIX 8 AA8 CYS A 301 ASN A 311 1 11
HELIX 9 AA9 ASP A 317 ASN A 325 1 9
HELIX 10 AB1 SER A 329 TYR A 335 5 7
HELIX 11 AB2 LYS A 338 VAL A 342 5 5
HELIX 12 AB3 ASP A 345 MET A 352 1 8
HELIX 13 AB4 TYR A 366 LEU A 369 5 4
HELIX 14 AB5 SER A 370 LEU A 388 1 19
HELIX 15 AB6 ILE A 390 ASP A 392 5 3
HELIX 16 AB7 PRO A 408 SER A 410 5 3
HELIX 17 AB8 LEU A 411 LEU A 423 1 13
HELIX 18 AB9 ASN A 445 TRP A 449 5 5
HELIX 19 AC1 THR B 110 GLU B 129 1 20
HELIX 20 AC2 SER B 206 ALA B 211 1 6
HELIX 21 AC3 SER B 215 ARG B 219 5 5
HELIX 22 AC4 GLY B 222 GLY B 229 1 8
HELIX 23 AC5 SER B 235 MET B 253 1 19
HELIX 24 AC6 THR B 254 ALA B 257 5 4
HELIX 25 AC7 SER B 270 GLU B 283 1 14
HELIX 26 AC8 CYS B 301 ASN B 311 1 11
HELIX 27 AC9 ASP B 317 ASN B 325 1 9
HELIX 28 AD1 SER B 329 TYR B 335 5 7
HELIX 29 AD2 LYS B 338 VAL B 342 5 5
HELIX 30 AD3 ASP B 345 MET B 352 1 8
HELIX 31 AD4 TYR B 366 LEU B 369 5 4
HELIX 32 AD5 SER B 370 LEU B 388 1 19
HELIX 33 AD6 ILE B 390 ASP B 392 5 3
HELIX 34 AD7 PRO B 408 SER B 410 5 3
HELIX 35 AD8 LEU B 411 LEU B 423 1 13
HELIX 36 AD9 ASN B 445 TRP B 449 5 5
SHEET 1 AA1 3 VAL A 139 SER A 147 0
SHEET 2 AA1 3 THR A 150 GLY A 158 -1 O THR A 152 N SER A 145
SHEET 3 AA1 3 THR A 164 PHE A 167 -1 O PHE A 167 N ILE A 155
SHEET 1 AA210 VAL A 139 SER A 147 0
SHEET 2 AA210 THR A 150 GLY A 158 -1 O THR A 152 N SER A 145
SHEET 3 AA210 THR A 170 SER A 172 -1 O ILE A 171 N GLY A 151
SHEET 4 AA210 ALA A 201 TYR A 205 -1 O THR A 202 N SER A 172
SHEET 5 AA210 TRP A 183 TYR A 189 1 N ALA A 188 O LEU A 203
SHEET 6 AA210 ILE A 259 CYS A 269 1 O GLY A 265 N ILE A 187
SHEET 7 AA210 LEU A 288 GLN A 292 1 O GLN A 292 N GLY A 268
SHEET 8 AA210 ALA A 357 ASN A 363 1 O PHE A 361 N PRO A 291
SHEET 9 AA210 HIS A 394 VAL A 399 1 O GLY A 395 N MET A 358
SHEET 10 AA210 PHE A 433 THR A 434 1 O THR A 434 N PHE A 396
SHEET 1 AA3 3 VAL B 139 SER B 147 0
SHEET 2 AA3 3 THR B 150 SER B 160 -1 O THR B 156 N THR B 141
SHEET 3 AA3 3 GLN B 163 PHE B 167 -1 O PHE B 167 N ILE B 155
SHEET 1 AA410 VAL B 139 SER B 147 0
SHEET 2 AA410 THR B 150 SER B 160 -1 O THR B 156 N THR B 141
SHEET 3 AA410 THR B 170 SER B 172 -1 O ILE B 171 N GLY B 151
SHEET 4 AA410 ALA B 201 TYR B 205 -1 O THR B 202 N SER B 172
SHEET 5 AA410 TRP B 183 TYR B 189 1 N ALA B 188 O LEU B 203
SHEET 6 AA410 ILE B 259 CYS B 269 1 O GLY B 265 N ILE B 187
SHEET 7 AA410 LEU B 288 GLN B 292 1 O GLN B 292 N GLY B 268
SHEET 8 AA410 ALA B 357 ASN B 363 1 O ILE B 359 N THR B 289
SHEET 9 AA410 HIS B 394 VAL B 399 1 O GLY B 395 N MET B 358
SHEET 10 AA410 PHE B 433 THR B 434 1 O THR B 434 N PHE B 396
SSBOND 1 CYS A 81 CYS A 116 1555 1555 2.05
SSBOND 2 CYS A 269 CYS A 405 1555 1555 2.05
SSBOND 3 CYS A 301 CYS A 377 1555 1555 2.06
SSBOND 4 CYS B 81 CYS B 116 1555 1555 2.04
SSBOND 5 CYS B 269 CYS B 405 1555 1555 2.05
SSBOND 6 CYS B 301 CYS B 377 1555 1555 2.07
LINK OG SER A 86 C1 MAN A 504 1555 1555 1.44
LINK OG1 THR A 87 C1 MAN A 502 1555 1555 1.45
LINK ND2 ASN A 104 C1 NAG A 501 1555 1555 1.43
LINK OG SER B 86 C1 MAN B 504 1555 1555 1.44
LINK OG1 THR B 87 C1 MAN B 502 1555 1555 1.45
LINK ND2 ASN B 104 C1 NAG B 501 1555 1555 1.44
LINK O ILE B 259 NA NA B 506 1555 1555 2.38
LINK O2 GOL B 505 NA NA B 506 1555 1555 2.75
LINK O3 GOL B 505 NA NA B 506 1555 1555 2.61
LINK NA NA B 506 O HOH B 797 1555 1555 2.31
LINK NA NA B 506 O HOH B 681 1555 1555 2.49
LINK NA NA B 506 O HOH B 663 1555 1555 2.64
CISPEP 1 ALA A 354 PRO A 355 0 4.45
CISPEP 2 ALA B 354 PRO B 355 0 4.27
SITE 1 AC1 4 LYS A 274 GLN A 316 GLU A 324 TRP A 368
SITE 1 AC2 4 LYS B 274 GLN B 316 GLU B 324 TRP B 368
SITE 1 AC3 8 GLU A 252 GLU B 252 PRO B 255 ILE B 259
SITE 2 AC3 8 THR B 261 NA B 506 HOH B 686 HOH B 787
SITE 1 AC4 5 ILE B 259 GOL B 505 HOH B 663 HOH B 681
SITE 2 AC4 5 HOH B 797
SITE 1 AC5 2 ILE A 84 SER A 86
SITE 1 AC6 5 THR A 87 ASN A 127 TYR A 128 TYR A 335
SITE 2 AC6 5 HOH A 774
SITE 1 AC7 7 CYS A 81 PHE A 102 ASN A 104 THR A 106
SITE 2 AC7 7 HOH A 608 HOH A 638 ASN B 92
SITE 1 AC8 2 ILE B 84 SER B 86
SITE 1 AC9 6 SER A 427 THR B 87 ASN B 127 TYR B 128
SITE 2 AC9 6 TYR B 335 HOH B 779
SITE 1 AD1 6 ASN A 92 CYS B 81 PHE B 102 ASN B 104
SITE 2 AD1 6 THR B 106 HOH B 636
CRYST1 84.450 84.450 262.239 90.00 90.00 90.00 P 41 21 2 16
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 0.011841 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003813 0.00000
TER 2890 GLY A 459
TER 5766 GLY B 459
MASTER 658 0 10 36 26 0 16 6 6343 2 174 62
END |