| 5EFZ-pdb | HEADER HYDROLASE 26-OCT-15 5EFZ
TITLE MONOCLINIC STRUCTURE OF THE ACETYL ESTERASE MEKB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: HYDROLASE;
COMPND 5 EC: 2.3.1.-,2.3.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS VERONII;
SOURCE 3 ORGANISM_TAXID: 76761;
SOURCE 4 GENE: MEKB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, ACETYL ESTER HYDROLASE, PSEUDOMONAS VERONII,
KEYWDS 2 TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER,K.NIEFIND
REVDAT 1 16-DEC-15 5EFZ 0
JRNL AUTH C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER,K.NIEFIND
JRNL TITL A NOVEL ESTERASE SUBFAMILY WITH ALPHA/BETA-HYDROLASE FOLD
JRNL TITL 2 SUGGESTED BY STRUCTURES OF TWO BACTERIAL ENZYMES HOMOLOGOUS
JRNL TITL 3 TO L-HOMOSERINE O-ACETYL TRANSFERASES
JRNL REF FEBS LETT. 2015
JRNL REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 201791
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2133
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 46.2952 - 4.4872 0.99 13508 126 0.1655 0.1880
REMARK 3 2 4.4872 - 3.5621 1.00 13352 159 0.1387 0.1676
REMARK 3 3 3.5621 - 3.1119 1.00 13407 132 0.1467 0.1767
REMARK 3 4 3.1119 - 2.8274 1.00 13344 140 0.1501 0.1909
REMARK 3 5 2.8274 - 2.6248 1.00 13323 132 0.1578 0.1843
REMARK 3 6 2.6248 - 2.4700 1.00 13353 151 0.1555 0.2108
REMARK 3 7 2.4700 - 2.3464 1.00 13291 141 0.1587 0.2019
REMARK 3 8 2.3464 - 2.2442 1.00 13382 125 0.1602 0.1980
REMARK 3 9 2.2442 - 2.1578 1.00 13333 142 0.1631 0.1947
REMARK 3 10 2.1578 - 2.0834 1.00 13258 140 0.1676 0.2073
REMARK 3 11 2.0834 - 2.0182 1.00 13303 132 0.1810 0.2074
REMARK 3 12 2.0182 - 1.9605 1.00 13348 155 0.1984 0.2295
REMARK 3 13 1.9605 - 1.9089 1.00 13258 160 0.2141 0.2394
REMARK 3 14 1.9089 - 1.8623 0.99 13190 147 0.2427 0.2909
REMARK 3 15 1.8623 - 1.8200 0.98 13008 151 0.2717 0.3365
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) : 19.590
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 : 0.012 16501
REMARK 3 ANGLE : 1.217 22302
REMARK 3 CHIRALITY : 0.061 2395
REMARK 3 PLANARITY : 0.006 2907
REMARK 3 DIHEDRAL : 13.679 5922
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 34
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1806 93.4241 40.7428
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.3480
REMARK 3 T33: 0.1851 T12: -0.0815
REMARK 3 T13: 0.0315 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 3.1780 L22: 1.8570
REMARK 3 L33: 1.4443 L12: -0.0818
REMARK 3 L13: 0.6826 L23: -0.4938
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.5054 S13: -0.0411
REMARK 3 S21: 0.2873 S22: 0.0449 S23: 0.3244
REMARK 3 S31: 0.0683 S32: -0.3920 S33: -0.0734
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9314 97.7140 25.1692
REMARK 3 T TENSOR
REMARK 3 T11: 0.1334 T22: 0.2666
REMARK 3 T33: 0.1901 T12: -0.0413
REMARK 3 T13: 0.0156 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 5.4260 L22: 1.8832
REMARK 3 L33: 0.8612 L12: 1.7465
REMARK 3 L13: 0.7009 L23: 0.2837
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: -0.0139 S13: 0.3338
REMARK 3 S21: -0.0241 S22: -0.0830 S23: 0.2582
REMARK 3 S31: 0.0524 S32: -0.2920 S33: -0.0044
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1630 88.9680 31.3102
REMARK 3 T TENSOR
REMARK 3 T11: 0.1422 T22: 0.1945
REMARK 3 T33: 0.1839 T12: -0.0748
REMARK 3 T13: -0.0054 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.9365 L22: 0.6944
REMARK 3 L33: 0.6503 L12: 0.1760
REMARK 3 L13: 0.2523 L23: 0.2152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0385 S12: -0.1258 S13: -0.0940
REMARK 3 S21: 0.0507 S22: -0.0224 S23: 0.0112
REMARK 3 S31: 0.1946 S32: -0.2044 S33: -0.0113
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9230 109.4725 31.1271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1362 T22: 0.1522
REMARK 3 T33: 0.2374 T12: -0.0363
REMARK 3 T13: 0.0081 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 1.2988 L22: 2.1010
REMARK 3 L33: 5.8332 L12: -0.2350
REMARK 3 L13: 1.0286 L23: -2.0035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0607 S12: -0.0691 S13: 0.2813
REMARK 3 S21: 0.2318 S22: -0.0164 S23: -0.2263
REMARK 3 S31: -0.5709 S32: 0.2429 S33: 0.0845
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3675 102.5726 36.2695
REMARK 3 T TENSOR
REMARK 3 T11: 0.0809 T22: 0.1842
REMARK 3 T33: 0.1646 T12: -0.0336
REMARK 3 T13: -0.0053 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 2.7088 L22: 2.3127
REMARK 3 L33: 4.1845 L12: 0.5574
REMARK 3 L13: -0.7014 L23: 0.5230
REMARK 3 S TENSOR
REMARK 3 S11: 0.1438 S12: -0.2429 S13: 0.1925
REMARK 3 S21: 0.2130 S22: -0.0718 S23: 0.0851
REMARK 3 S31: -0.1875 S32: -0.1198 S33: -0.0662
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 261 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5746 86.3685 20.0909
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.1461
REMARK 3 T33: 0.1955 T12: -0.0364
REMARK 3 T13: 0.0192 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.6749 L22: 1.4611
REMARK 3 L33: 2.3418 L12: -0.3825
REMARK 3 L13: 1.2999 L23: 0.1936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: 0.0320 S13: -0.2214
REMARK 3 S21: 0.0383 S22: -0.0405 S23: -0.0694
REMARK 3 S31: 0.3087 S32: -0.0746 S33: -0.0333
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1345 90.6032 11.5781
REMARK 3 T TENSOR
REMARK 3 T11: 0.1314 T22: 0.2332
REMARK 3 T33: 0.1515 T12: -0.0550
REMARK 3 T13: 0.0289 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.6895 L22: 5.4024
REMARK 3 L33: 3.5220 L12: -0.2879
REMARK 3 L13: 0.7124 L23: 1.6176
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.2108 S13: -0.1548
REMARK 3 S21: -0.4991 S22: 0.0097 S23: 0.1269
REMARK 3 S31: 0.2213 S32: -0.1545 S33: -0.0372
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5247 98.5708 14.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1049 T22: 0.2444
REMARK 3 T33: 0.1585 T12: -0.0086
REMARK 3 T13: 0.0139 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 4.0270 L22: 4.7440
REMARK 3 L33: 1.2305 L12: 3.4624
REMARK 3 L13: 0.5590 L23: 0.6717
REMARK 3 S TENSOR
REMARK 3 S11: -0.0717 S12: 0.1914 S13: 0.0229
REMARK 3 S21: -0.1852 S22: 0.0659 S23: 0.1116
REMARK 3 S31: -0.0201 S32: -0.2730 S33: -0.0046
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0969 108.4283 13.1208
REMARK 3 T TENSOR
REMARK 3 T11: 0.1326 T22: 0.3073
REMARK 3 T33: 0.2779 T12: -0.0433
REMARK 3 T13: 0.0467 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 1.5855 L22: 1.3573
REMARK 3 L33: 1.9614 L12: 0.3141
REMARK 3 L13: -0.8107 L23: -0.6903
REMARK 3 S TENSOR
REMARK 3 S11: -0.0251 S12: 0.2094 S13: 0.0329
REMARK 3 S21: -0.0414 S22: 0.0062 S23: -0.2344
REMARK 3 S31: 0.0298 S32: 0.3303 S33: 0.0320
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 81 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5508 115.2424 14.4061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1834 T22: 0.2056
REMARK 3 T33: 0.2378 T12: -0.0749
REMARK 3 T13: 0.0491 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.1694 L22: 1.1329
REMARK 3 L33: 0.9394 L12: 0.1222
REMARK 3 L13: 0.1030 L23: -0.0521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: 0.1873 S13: 0.2712
REMARK 3 S21: -0.0934 S22: 0.0413 S23: -0.0554
REMARK 3 S31: -0.1964 S32: 0.2268 S33: -0.0285
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0166 96.9529 28.1273
REMARK 3 T TENSOR
REMARK 3 T11: 0.1040 T22: 0.1178
REMARK 3 T33: 0.1479 T12: -0.0190
REMARK 3 T13: 0.0307 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.3686 L22: 5.5202
REMARK 3 L33: 4.2097 L12: 1.7865
REMARK 3 L13: 1.1449 L23: 3.5821
REMARK 3 S TENSOR
REMARK 3 S11: 0.1248 S12: -0.1239 S13: -0.1039
REMARK 3 S21: 0.3592 S22: -0.0497 S23: -0.0633
REMARK 3 S31: 0.2718 S32: 0.0021 S33: -0.0799
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 241 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0789 112.9670 19.4306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1364 T22: 0.1228
REMARK 3 T33: 0.2062 T12: -0.0402
REMARK 3 T13: 0.0508 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 1.9905 L22: 1.1580
REMARK 3 L33: 3.3760 L12: -0.2075
REMARK 3 L13: 0.9526 L23: -0.5860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.0697 S13: 0.2711
REMARK 3 S21: 0.0456 S22: 0.0184 S23: 0.0397
REMARK 3 S31: -0.4023 S32: 0.1254 S33: 0.0178
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 281 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4670 104.2264 3.9435
REMARK 3 T TENSOR
REMARK 3 T11: 0.1488 T22: 0.1859
REMARK 3 T33: 0.1312 T12: -0.0415
REMARK 3 T13: 0.0029 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.5754 L22: 3.6058
REMARK 3 L33: 3.2380 L12: 0.0255
REMARK 3 L13: -0.7218 L23: -1.3522
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: 0.4005 S13: 0.0426
REMARK 3 S21: -0.2790 S22: 0.0513 S23: 0.0528
REMARK 3 S31: -0.0788 S32: 0.0410 S33: -0.0391
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 10 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.1123 81.0870 45.0769
REMARK 3 T TENSOR
REMARK 3 T11: 0.3838 T22: 0.1613
REMARK 3 T33: 0.2747 T12: -0.0211
REMARK 3 T13: -0.0625 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 5.7189 L22: 0.8596
REMARK 3 L33: 6.9893 L12: -2.1270
REMARK 3 L13: -5.0998 L23: 2.1379
REMARK 3 S TENSOR
REMARK 3 S11: -0.1078 S12: 0.2455 S13: 0.2265
REMARK 3 S21: -0.2600 S22: 0.0565 S23: -0.0104
REMARK 3 S31: -0.3277 S32: -0.2219 S33: 0.0474
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 33 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2275 76.3383 60.1798
REMARK 3 T TENSOR
REMARK 3 T11: 0.2765 T22: 0.1633
REMARK 3 T33: 0.2010 T12: 0.0624
REMARK 3 T13: -0.0249 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.6770 L22: 1.9904
REMARK 3 L33: 2.8273 L12: -0.0836
REMARK 3 L13: 0.2336 L23: 1.2374
REMARK 3 S TENSOR
REMARK 3 S11: -0.1881 S12: -0.2651 S13: 0.0423
REMARK 3 S21: 0.2383 S22: 0.1418 S23: 0.0989
REMARK 3 S31: -0.2103 S32: -0.1032 S33: 0.0550
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 100 THROUGH 197 )
REMARK 3 ORIGIN FOR THE GROUP (A): 85.7376 71.3825 49.2473
REMARK 3 T TENSOR
REMARK 3 T11: 0.1487 T22: 0.1285
REMARK 3 T33: 0.1474 T12: -0.0149
REMARK 3 T13: 0.0144 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.8077 L22: 1.6607
REMARK 3 L33: 2.4988 L12: 0.2925
REMARK 3 L13: 0.7929 L23: 0.5660
REMARK 3 S TENSOR
REMARK 3 S11: -0.1159 S12: 0.0608 S13: 0.0818
REMARK 3 S21: -0.0144 S22: 0.0458 S23: -0.0863
REMARK 3 S31: -0.2064 S32: 0.1254 S33: 0.0574
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 198 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0319 51.4672 55.1791
REMARK 3 T TENSOR
REMARK 3 T11: 0.2810 T22: 0.1729
REMARK 3 T33: 0.3240 T12: 0.0081
REMARK 3 T13: 0.0958 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 1.4913 L22: 2.0632
REMARK 3 L33: 6.1393 L12: -0.4856
REMARK 3 L13: 1.4741 L23: -2.5370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0922 S12: -0.2405 S13: -0.4462
REMARK 3 S21: 0.0954 S22: 0.2638 S23: 0.3398
REMARK 3 S31: 0.4372 S32: -0.4718 S33: -0.1842
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 251 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.7738 69.5595 46.9539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1715 T22: 0.2149
REMARK 3 T33: 0.2151 T12: -0.0425
REMARK 3 T13: 0.0283 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 5.1267 L22: 2.0039
REMARK 3 L33: 2.7059 L12: 0.2364
REMARK 3 L13: 1.4026 L23: 0.1350
REMARK 3 S TENSOR
REMARK 3 S11: -0.1554 S12: 0.1450 S13: 0.2592
REMARK 3 S21: -0.1661 S22: 0.0505 S23: -0.3469
REMARK 3 S31: -0.1893 S32: 0.5658 S33: 0.1004
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 281 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): 91.9778 64.2403 65.6827
REMARK 3 T TENSOR
REMARK 3 T11: 0.2424 T22: 0.2727
REMARK 3 T33: 0.1864 T12: 0.1040
REMARK 3 T13: -0.0370 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.5079 L22: 1.9731
REMARK 3 L33: 2.3738 L12: 0.2116
REMARK 3 L13: -0.7620 L23: -0.3581
REMARK 3 S TENSOR
REMARK 3 S11: -0.2055 S12: -0.3281 S13: -0.1134
REMARK 3 S21: 0.2695 S22: 0.1250 S23: -0.2520
REMARK 3 S31: 0.0901 S32: 0.4541 S33: 0.0720
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2069 40.4446 25.5679
REMARK 3 T TENSOR
REMARK 3 T11: 0.7367 T22: 0.4085
REMARK 3 T33: 0.2470 T12: -0.4982
REMARK 3 T13: -0.1045 T23: 0.3623
REMARK 3 L TENSOR
REMARK 3 L11: 0.3365 L22: 0.3028
REMARK 3 L33: 0.3967 L12: 0.0034
REMARK 3 L13: 0.1661 L23: -0.0874
REMARK 3 S TENSOR
REMARK 3 S11: 0.2130 S12: -0.2500 S13: -0.2878
REMARK 3 S21: -0.1163 S22: 0.2093 S23: 0.3215
REMARK 3 S31: 1.0661 S32: -0.8419 S33: -0.0397
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3724 47.3321 12.9923
REMARK 3 T TENSOR
REMARK 3 T11: 0.4055 T22: 0.1594
REMARK 3 T33: 0.1716 T12: 0.0275
REMARK 3 T13: -0.0056 T23: 0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 2.4849 L22: 1.5811
REMARK 3 L33: 2.5279 L12: 0.2795
REMARK 3 L13: 0.7566 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0861 S12: 0.0374 S13: -0.3205
REMARK 3 S21: -0.3580 S22: 0.0594 S23: -0.0518
REMARK 3 S31: 0.6264 S32: 0.1421 S33: -0.1298
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 276 THROUGH 346 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0150 50.4632 34.8917
REMARK 3 T TENSOR
REMARK 3 T11: 0.2388 T22: 0.2194
REMARK 3 T33: 0.1168 T12: -0.0171
REMARK 3 T13: -0.0331 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 2.6590 L22: 3.0482
REMARK 3 L33: 3.5188 L12: -0.0206
REMARK 3 L13: -0.7398 L23: -1.1755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: -0.4180 S13: -0.0374
REMARK 3 S21: 0.2542 S22: 0.0122 S23: -0.0374
REMARK 3 S31: 0.3117 S32: 0.0448 S33: -0.0293
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 3 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8767 19.7995 38.7853
REMARK 3 T TENSOR
REMARK 3 T11: 0.7525 T22: 0.5162
REMARK 3 T33: 0.4966 T12: 0.2207
REMARK 3 T13: -0.2355 T23: -0.2354
REMARK 3 L TENSOR
REMARK 3 L11: 0.7343 L22: 1.7396
REMARK 3 L33: 0.4197 L12: -0.6837
REMARK 3 L13: -0.4772 L23: 0.1067
REMARK 3 S TENSOR
REMARK 3 S11: 0.1561 S12: 0.4335 S13: -0.3328
REMARK 3 S21: -0.4260 S22: -0.0826 S23: -0.0482
REMARK 3 S31: 0.4374 S32: 0.0288 S33: -0.0543
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 41 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.8847 22.0262 48.4842
REMARK 3 T TENSOR
REMARK 3 T11: 0.6488 T22: 0.4358
REMARK 3 T33: 0.3960 T12: 0.2548
REMARK 3 T13: -0.0921 T23: -0.1262
REMARK 3 L TENSOR
REMARK 3 L11: 2.9831 L22: 3.3341
REMARK 3 L33: 0.0261 L12: -1.3713
REMARK 3 L13: -0.2144 L23: 0.2437
REMARK 3 S TENSOR
REMARK 3 S11: 0.1640 S12: 0.0409 S13: -0.2836
REMARK 3 S21: -0.2734 S22: 0.0114 S23: -0.4089
REMARK 3 S31: 0.4080 S32: 0.4354 S33: -0.1428
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 81 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.6779 24.2104 49.8492
REMARK 3 T TENSOR
REMARK 3 T11: 0.5245 T22: 0.2459
REMARK 3 T33: 0.3552 T12: 0.0957
REMARK 3 T13: -0.1639 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 0.7566 L22: 1.3869
REMARK 3 L33: 0.4921 L12: 0.0449
REMARK 3 L13: -0.5357 L23: 0.3610
REMARK 3 S TENSOR
REMARK 3 S11: 0.3192 S12: 0.2327 S13: -0.3740
REMARK 3 S21: -0.1822 S22: -0.1210 S23: 0.1702
REMARK 3 S31: 0.3777 S32: -0.0292 S33: -0.1514
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 181 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.8450 39.9260 31.2560
REMARK 3 T TENSOR
REMARK 3 T11: 0.9323 T22: 0.7384
REMARK 3 T33: 0.3968 T12: 0.4898
REMARK 3 T13: 0.0276 T23: 0.1204
REMARK 3 L TENSOR
REMARK 3 L11: 2.5862 L22: 3.5776
REMARK 3 L33: 1.3765 L12: -1.5176
REMARK 3 L13: 1.4936 L23: -2.0519
REMARK 3 S TENSOR
REMARK 3 S11: 0.1822 S12: 0.2168 S13: -0.0306
REMARK 3 S21: -0.2646 S22: -0.0248 S23: 0.1326
REMARK 3 S31: 0.0938 S32: -0.0256 S33: -0.1076
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 201 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.8213 49.1582 42.8461
REMARK 3 T TENSOR
REMARK 3 T11: 0.6403 T22: 0.3519
REMARK 3 T33: 0.4263 T12: 0.1283
REMARK 3 T13: 0.2483 T23: 0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 4.9236 L22: 2.0989
REMARK 3 L33: 3.8693 L12: 1.2575
REMARK 3 L13: 2.6315 L23: 1.5881
REMARK 3 S TENSOR
REMARK 3 S11: 0.2131 S12: 0.7292 S13: 0.5887
REMARK 3 S21: -0.7483 S22: -0.0755 S23: -0.3268
REMARK 3 S31: -0.5503 S32: 0.4670 S33: -0.1322
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 241 THROUGH 260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.0699 36.4375 38.4735
REMARK 3 T TENSOR
REMARK 3 T11: 0.5312 T22: 0.3698
REMARK 3 T33: 0.2617 T12: 0.2351
REMARK 3 T13: 0.0204 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.0260 L22: 3.2208
REMARK 3 L33: 2.5068 L12: 1.5672
REMARK 3 L13: 0.9660 L23: 0.3788
REMARK 3 S TENSOR
REMARK 3 S11: 0.3320 S12: 0.7161 S13: -0.0260
REMARK 3 S21: -0.6955 S22: 0.0116 S23: -0.1970
REMARK 3 S31: 0.0044 S32: 0.1182 S33: -0.3225
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 261 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.9122 27.4022 61.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.4007 T22: 0.2045
REMARK 3 T33: 0.3347 T12: -0.0466
REMARK 3 T13: -0.0908 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 3.3903 L22: 1.9812
REMARK 3 L33: 5.3064 L12: 1.0239
REMARK 3 L13: -0.6509 L23: -0.5027
REMARK 3 S TENSOR
REMARK 3 S11: 0.1189 S12: -0.1414 S13: -0.4769
REMARK 3 S21: -0.4301 S22: 0.0180 S23: 0.1079
REMARK 3 S31: 0.6954 S32: -0.4169 S33: -0.1168
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 281 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 99.1603 33.9405 60.1891
REMARK 3 T TENSOR
REMARK 3 T11: 0.2704 T22: 0.2488
REMARK 3 T33: 0.2205 T12: 0.0513
REMARK 3 T13: -0.0588 T23: -0.1035
REMARK 3 L TENSOR
REMARK 3 L11: 3.6094 L22: 2.8778
REMARK 3 L33: 3.1141 L12: -0.3734
REMARK 3 L13: -0.8352 L23: -0.7642
REMARK 3 S TENSOR
REMARK 3 S11: 0.2522 S12: -0.2212 S13: 0.0466
REMARK 3 S21: -0.0993 S22: 0.0356 S23: -0.2436
REMARK 3 S31: 0.2595 S32: 0.4880 S33: -0.2687
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 3 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.4697 73.1884 5.2854
REMARK 3 T TENSOR
REMARK 3 T11: 0.0985 T22: 0.2398
REMARK 3 T33: 0.1474 T12: -0.0185
REMARK 3 T13: 0.0195 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.4517 L22: 1.2076
REMARK 3 L33: 0.9079 L12: 0.6834
REMARK 3 L13: 0.1265 L23: -0.0847
REMARK 3 S TENSOR
REMARK 3 S11: -0.0188 S12: 0.1927 S13: 0.0640
REMARK 3 S21: -0.1031 S22: -0.0059 S23: -0.0749
REMARK 3 S31: -0.0615 S32: 0.2747 S33: 0.0199
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 181 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0665 65.3986 7.3815
REMARK 3 T TENSOR
REMARK 3 T11: 0.0964 T22: 0.0960
REMARK 3 T33: 0.1797 T12: -0.0319
REMARK 3 T13: -0.0101 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.6740 L22: 1.4745
REMARK 3 L33: 6.5303 L12: -0.3834
REMARK 3 L13: -1.2680 L23: 2.3768
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: 0.2056 S13: -0.0101
REMARK 3 S21: -0.0479 S22: -0.1206 S23: 0.2583
REMARK 3 S31: 0.0868 S32: -0.3597 S33: 0.1300
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 241 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.2044 62.6581 6.8755
REMARK 3 T TENSOR
REMARK 3 T11: 0.1186 T22: 0.1874
REMARK 3 T33: 0.1219 T12: 0.0054
REMARK 3 T13: 0.0317 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 2.0603 L22: 1.0561
REMARK 3 L33: 2.1507 L12: 0.4887
REMARK 3 L13: 1.0778 L23: -0.2906
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: 0.1852 S13: -0.2087
REMARK 3 S21: -0.1086 S22: 0.0326 S23: 0.0122
REMARK 3 S31: 0.1484 S32: 0.3226 S33: -0.0525
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 281 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.9112 70.6093 23.4919
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.2123
REMARK 3 T33: 0.1103 T12: -0.0421
REMARK 3 T13: 0.0203 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 2.8446 L22: 1.8982
REMARK 3 L33: 0.9329 L12: 0.4619
REMARK 3 L13: 0.1131 L23: -0.1557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: -0.1733 S13: 0.0270
REMARK 3 S21: 0.1296 S22: -0.0602 S23: -0.0324
REMARK 3 S31: -0.0409 S32: 0.2314 S33: 0.0240
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 5EFZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 201791
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 46.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.89300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.5 0.8 M
REMARK 280 SODIUM DIHYDROGEN PHOSPHATE 1.2 M DI-POTASSIUM HYDROGEN
REMARK 280 PHOSPHATE DROP: 0.1 MICROLITER ETHYLENE GLYCOL 0.8 MICROLITER
REMARK 280 PROTEIN SOLUTION 0.8 MICROLITER RESERVOIR SOLUTION, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 55.17100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -11
REMARK 465 THR A -10
REMARK 465 MET A -9
REMARK 465 ILE A -8
REMARK 465 THR A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 MET B -11
REMARK 465 THR B -10
REMARK 465 MET B -9
REMARK 465 ILE B -8
REMARK 465 THR B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 348
REMARK 465 TYR B 349
REMARK 465 MET C -11
REMARK 465 THR C -10
REMARK 465 MET C -9
REMARK 465 ILE C -8
REMARK 465 THR C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 SER C 3
REMARK 465 TYR C 4
REMARK 465 TYR C 5
REMARK 465 THR C 6
REMARK 465 GLU C 7
REMARK 465 GLU C 8
REMARK 465 ASN C 9
REMARK 465 TYR C 349
REMARK 465 MET D -11
REMARK 465 THR D -10
REMARK 465 MET D -9
REMARK 465 ILE D -8
REMARK 465 THR D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 PRO D 347
REMARK 465 ALA D 348
REMARK 465 TYR D 349
REMARK 465 MET E -11
REMARK 465 THR E -10
REMARK 465 MET E -9
REMARK 465 ILE E -8
REMARK 465 THR E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 GLY E 0
REMARK 465 SER E 1
REMARK 465 ASN E 2
REMARK 465 ALA E 348
REMARK 465 TYR E 349
REMARK 465 MET F -11
REMARK 465 THR F -10
REMARK 465 MET F -9
REMARK 465 ILE F -8
REMARK 465 THR F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 GLY F 0
REMARK 465 SER F 1
REMARK 465 ASN F 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 643 O HOH A 705 2.05
REMARK 500 O HOH D 517 O HOH D 595 2.06
REMARK 500 O HOH F 538 O HOH F 550 2.07
REMARK 500 O HOH A 503 O HOH A 660 2.08
REMARK 500 O1 EDO D 401 O HOH D 501 2.11
REMARK 500 O HOH A 661 O HOH A 668 2.12
REMARK 500 O HOH C 622 O HOH C 667 2.13
REMARK 500 O HOH C 582 O HOH C 673 2.14
REMARK 500 NH1 ARG D 195 O HOH D 502 2.15
REMARK 500 O HOH F 669 O HOH F 709 2.15
REMARK 500 O HOH F 698 O HOH F 718 2.16
REMARK 500 O HOH B 534 O HOH B 611 2.18
REMARK 500 O HOH F 689 O HOH F 727 2.18
REMARK 500 O HOH B 636 O HOH B 672 2.18
REMARK 500 O HOH A 667 O HOH A 699 2.19
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 ASN A 97 13.94 -141.43
REMARK 500 SER A 139 -114.01 54.01
REMARK 500 TRP A 216 -122.71 -116.02
REMARK 500 PHE A 241 -60.35 -107.65
REMARK 500 ASP A 265 96.44 -164.71
REMARK 500 ASN A 310 -12.26 81.56
REMARK 500 SER B 139 -112.83 55.79
REMARK 500 TRP B 216 -120.18 -116.56
REMARK 500 ASP B 265 96.74 -167.57
REMARK 500 SER C 139 -115.56 59.79
REMARK 500 TRP C 216 -121.82 -114.45
REMARK 500 ASP C 265 96.09 -167.30
REMARK 500 ASN D 97 11.09 -143.65
REMARK 500 SER D 139 -117.32 59.46
REMARK 500 VAL D 200 31.25 -98.64
REMARK 500 TRP D 216 -119.62 -114.29
REMARK 500 ASP D 265 94.86 -169.85
REMARK 500 SER E 139 -113.05 58.73
REMARK 500 VAL E 200 31.25 -94.48
REMARK 500 TRP E 216 -115.99 -117.27
REMARK 500 PHE E 241 -61.88 -109.52
REMARK 500 ASP E 265 97.31 -166.09
REMARK 500 ASN E 310 17.17 56.05
REMARK 500 SER F 57 -0.66 70.27
REMARK 500 SER F 139 -114.39 56.74
REMARK 500 TRP F 216 -120.63 -115.21
REMARK 500 ASP F 265 96.66 -167.76
REMARK 500 ASN F 310 -0.85 74.79
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 D 624 DISTANCE = 6.42 ANGSTROMS
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT F 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E4Y RELATED DB: PDB
REMARK 900 5E4Y CONTAINS THE SAME PROTEIN IN OTHER CRYSTAL FORM.
DBREF 5EFZ A 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5EFZ B 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5EFZ C 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5EFZ D 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5EFZ E 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
DBREF 5EFZ F 2 349 UNP Q0MRG5 Q0MRG5_9PSED 2 349
SEQADV 5EFZ MET A -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR A -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET A -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE A -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR A -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS A -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY A 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER A 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET B -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR B -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET B -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE B -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR B -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS B -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY B 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER B 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET C -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR C -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET C -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE C -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR C -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS C -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY C 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER C 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET D -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR D -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET D -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE D -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR D -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS D -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY D 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER D 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET E -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR E -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET E -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE E -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR E -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS E -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY E 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER E 1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET F -11 UNP Q0MRG5 INITIATING METHIONINE
SEQADV 5EFZ THR F -10 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ MET F -9 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ ILE F -8 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ THR F -7 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -6 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -5 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -4 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -3 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -2 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ HIS F -1 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ GLY F 0 UNP Q0MRG5 EXPRESSION TAG
SEQADV 5EFZ SER F 1 UNP Q0MRG5 EXPRESSION TAG
SEQRES 1 A 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 A 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 A 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 A 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 A 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 A 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 A 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 A 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 A 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 A 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 A 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 A 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 A 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 A 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 A 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 A 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 A 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 A 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 A 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 A 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 A 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 A 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 A 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 A 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 A 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 A 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 A 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 A 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 B 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 B 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 B 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 B 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 B 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 B 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 B 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 B 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 B 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 B 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 B 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 B 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 B 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 B 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 B 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 B 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 B 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 B 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 B 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 B 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 B 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 B 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 B 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 B 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 B 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 B 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 B 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 B 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 C 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 C 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 C 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 C 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 C 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 C 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 C 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 C 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 C 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 C 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 C 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 C 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 C 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 C 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 C 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 C 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 C 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 C 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 C 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 C 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 C 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 C 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 C 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 C 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 C 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 C 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 C 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 C 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 D 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 D 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 D 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 D 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 D 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 D 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 D 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 D 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 D 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 D 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 D 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 D 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 D 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 D 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 D 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 D 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 D 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 D 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 D 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 D 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 D 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 D 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 D 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 D 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 D 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 D 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 D 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 D 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 E 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 E 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 E 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 E 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 E 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 E 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 E 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 E 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 E 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 E 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 E 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 E 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 E 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 E 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 E 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 E 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 E 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 E 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 E 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 E 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 E 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 E 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 E 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 E 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 E 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 E 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 E 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 E 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
SEQRES 1 F 361 MET THR MET ILE THR HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 F 361 ASN SER TYR TYR THR GLU GLU ASN HIS GLY PRO PHE GLU
SEQRES 3 F 361 LEU ILE ASN ILE GLY PRO LEU PRO LEU GLU GLU GLY ARG
SEQRES 4 F 361 CYS MET PRO GLU CYS LEU LEU ALA VAL ALA VAL HIS GLY
SEQRES 5 F 361 ALA LEU ASN ALA ASP LYS SER ASN ALA ILE LEU VAL PRO
SEQRES 6 F 361 THR TRP TYR SER GLY THR SER LYS ALA MET GLU GLN ILE
SEQRES 7 F 361 TYR ILE GLY GLU GLY ARG ALA LEU ASP PRO SER LYS TYR
SEQRES 8 F 361 CYS ILE ILE VAL VAL ASN GLN ILE GLY ASN GLY LEU SER
SEQRES 9 F 361 SER SER ALA SER ASN THR GLY GLY SER LEU ALA GLY PRO
SEQRES 10 F 361 GLY PHE ALA ASN VAL ARG ILE GLY ASP ASP VAL SER ALA
SEQRES 11 F 361 GLN HIS THR LEU LEU THR GLU TYR PHE GLY ILE GLU SER
SEQRES 12 F 361 LEU ALA LEU VAL VAL GLY GLY SER MET GLY ALA GLN GLN
SEQRES 13 F 361 THR TYR GLU TRP ALA VAL ARG TYR PRO ASP PHE VAL LYS
SEQRES 14 F 361 ARG ALA ALA ALA ILE ALA GLY THR ALA ARG ASN SER GLU
SEQRES 15 F 361 HIS ASP PHE LEU PHE THR GLU ILE LEU ILE GLU ALA ILE
SEQRES 16 F 361 THR THR ASP PRO ALA PHE GLN ALA GLY LEU TYR ARG SER
SEQRES 17 F 361 SER SER ALA VAL ALA ALA GLY LEU GLU ARG HIS ALA LYS
SEQRES 18 F 361 LEU TRP THR LEU MET GLY TRP SER PRO GLU PHE PHE ARG
SEQRES 19 F 361 THR GLY ARG HIS LYS ALA LEU GLY PHE GLU SER MET GLN
SEQRES 20 F 361 MET PHE VAL ASP GLY PHE MET LYS ARG TYR PHE ALA PRO
SEQRES 21 F 361 MET ASP PRO ASN ASN LEU LEU THR MET ALA TRP LYS TRP
SEQRES 22 F 361 GLN ARG GLY ASP VAL SER ARG HIS THR GLY GLY ASP LEU
SEQRES 23 F 361 ALA LYS ALA LEU GLY ARG ILE LYS ALA LYS THR TYR VAL
SEQRES 24 F 361 MET PRO ILE SER HIS ASP GLN PHE PHE THR VAL ASP ASP
SEQRES 25 F 361 CYS LEU SER GLU GLN LYS MET ILE PRO ASN SER GLU PHE
SEQRES 26 F 361 ARG PRO LEU ARG SER ILE ASP GLY HIS LEU GLY LEU PHE
SEQRES 27 F 361 GLY THR ASP ALA GLN MET LEU ASP GLN LEU ASP ALA HIS
SEQRES 28 F 361 LEU ALA GLU LEU LEU SER SER PRO ALA TYR
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET GOL A 408 6
HET ACT A 409 4
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET ACT B 406 4
HET EDO C 401 4
HET EDO C 402 4
HET EDO C 403 4
HET EDO C 404 4
HET EDO C 405 4
HET EDO C 406 4
HET GOL C 407 6
HET GOL C 408 6
HET ACT C 409 4
HET EDO D 401 4
HET EDO D 402 4
HET EDO D 403 4
HET GOL D 404 6
HET GOL D 405 6
HET ACT D 406 4
HET EDO E 401 4
HET EDO E 402 4
HET ACT E 403 4
HET ACT E 404 4
HET EDO F 401 4
HET EDO F 402 4
HET GOL F 403 6
HET GOL F 404 6
HET GOL F 405 6
HET ACT F 406 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 EDO 25(C2 H6 O2)
FORMUL 14 GOL 8(C3 H8 O3)
FORMUL 15 ACT 7(C2 H3 O2 1-)
FORMUL 47 HOH *1085(H2 O)
HELIX 1 AA1 THR A 6 GLY A 11 1 6
HELIX 2 AA2 THR A 59 ILE A 68 1 10
HELIX 3 AA3 GLY A 99 PHE A 107 5 9
HELIX 4 AA4 ARG A 111 TYR A 126 1 16
HELIX 5 AA5 SER A 139 TYR A 152 1 14
HELIX 6 AA6 SER A 169 THR A 185 1 17
HELIX 7 AA7 ASP A 186 LEU A 193 5 8
HELIX 8 AA8 SER A 196 ALA A 199 5 4
HELIX 9 AA9 VAL A 200 TRP A 216 1 17
HELIX 10 AB1 SER A 217 THR A 223 1 7
HELIX 11 AB2 GLY A 224 LEU A 229 1 6
HELIX 12 AB3 SER A 233 PHE A 241 1 9
HELIX 13 AB4 PHE A 241 ALA A 247 1 7
HELIX 14 AB5 ASP A 250 ARG A 263 1 14
HELIX 15 AB6 GLY A 264 GLY A 271 5 8
HELIX 16 AB7 ASP A 273 GLY A 279 1 7
HELIX 17 AB8 THR A 297 LYS A 306 1 10
HELIX 18 AB9 ASP A 320 GLY A 327 5 8
HELIX 19 AC1 ASP A 329 SER A 345 1 17
HELIX 20 AC2 THR B 6 GLY B 11 1 6
HELIX 21 AC3 THR B 59 ILE B 68 1 10
HELIX 22 AC4 GLY B 99 PHE B 107 5 9
HELIX 23 AC5 ARG B 111 TYR B 126 1 16
HELIX 24 AC6 SER B 139 TYR B 152 1 14
HELIX 25 AC7 PRO B 153 VAL B 156 5 4
HELIX 26 AC8 SER B 169 THR B 185 1 17
HELIX 27 AC9 ASP B 186 LEU B 193 5 8
HELIX 28 AD1 SER B 196 ALA B 199 5 4
HELIX 29 AD2 VAL B 200 TRP B 216 1 17
HELIX 30 AD3 SER B 217 THR B 223 1 7
HELIX 31 AD4 GLY B 224 LEU B 229 1 6
HELIX 32 AD5 SER B 233 PHE B 241 1 9
HELIX 33 AD6 PHE B 241 ALA B 247 1 7
HELIX 34 AD7 ASP B 250 ARG B 263 1 14
HELIX 35 AD8 GLY B 264 THR B 270 5 7
HELIX 36 AD9 ASP B 273 GLY B 279 1 7
HELIX 37 AE1 THR B 297 LYS B 306 1 10
HELIX 38 AE2 ASP B 320 GLY B 327 5 8
HELIX 39 AE3 ASP B 329 SER B 346 1 18
HELIX 40 AE4 THR C 59 ILE C 68 1 10
HELIX 41 AE5 GLY C 99 PHE C 107 5 9
HELIX 42 AE6 ARG C 111 TYR C 126 1 16
HELIX 43 AE7 SER C 139 TYR C 152 1 14
HELIX 44 AE8 SER C 169 THR C 185 1 17
HELIX 45 AE9 ASP C 186 LEU C 193 5 8
HELIX 46 AF1 SER C 197 ALA C 199 5 3
HELIX 47 AF2 VAL C 200 TRP C 216 1 17
HELIX 48 AF3 SER C 217 THR C 223 1 7
HELIX 49 AF4 GLY C 224 LEU C 229 1 6
HELIX 50 AF5 SER C 233 PHE C 241 1 9
HELIX 51 AF6 PHE C 241 ALA C 247 1 7
HELIX 52 AF7 ASP C 250 ARG C 263 1 14
HELIX 53 AF8 GLY C 264 GLY C 271 5 8
HELIX 54 AF9 ASP C 273 ARG C 280 1 8
HELIX 55 AG1 THR C 297 LYS C 306 1 10
HELIX 56 AG2 ASP C 320 GLY C 327 5 8
HELIX 57 AG3 ASP C 329 SER C 346 1 18
HELIX 58 AG4 THR D 6 GLY D 11 1 6
HELIX 59 AG5 THR D 59 ILE D 68 1 10
HELIX 60 AG6 GLY D 99 PHE D 107 5 9
HELIX 61 AG7 ARG D 111 TYR D 126 1 16
HELIX 62 AG8 SER D 139 TYR D 152 1 14
HELIX 63 AG9 SER D 169 THR D 185 1 17
HELIX 64 AH1 ASP D 186 LEU D 193 5 8
HELIX 65 AH2 SER D 196 ALA D 199 5 4
HELIX 66 AH3 VAL D 200 TRP D 216 1 17
HELIX 67 AH4 SER D 217 THR D 223 1 7
HELIX 68 AH5 GLY D 224 LEU D 229 1 6
HELIX 69 AH6 SER D 233 PHE D 241 1 9
HELIX 70 AH7 PHE D 241 ALA D 247 1 7
HELIX 71 AH8 ASP D 250 ARG D 263 1 14
HELIX 72 AH9 GLY D 264 GLY D 271 5 8
HELIX 73 AI1 ASP D 273 GLY D 279 1 7
HELIX 74 AI2 THR D 297 LYS D 306 1 10
HELIX 75 AI3 ASP D 320 GLY D 327 5 8
HELIX 76 AI4 ASP D 329 SER D 345 1 17
HELIX 77 AI5 THR E 6 GLY E 11 1 6
HELIX 78 AI6 THR E 59 ILE E 68 1 10
HELIX 79 AI7 GLY E 99 PHE E 107 5 9
HELIX 80 AI8 ARG E 111 TYR E 126 1 16
HELIX 81 AI9 SER E 139 TYR E 152 1 14
HELIX 82 AJ1 SER E 169 THR E 185 1 17
HELIX 83 AJ2 PHE E 189 LEU E 193 5 5
HELIX 84 AJ3 SER E 196 ALA E 199 5 4
HELIX 85 AJ4 VAL E 200 TRP E 216 1 17
HELIX 86 AJ5 SER E 217 THR E 223 1 7
HELIX 87 AJ6 GLY E 224 LEU E 229 1 6
HELIX 88 AJ7 SER E 233 PHE E 241 1 9
HELIX 89 AJ8 PHE E 241 ALA E 247 1 7
HELIX 90 AJ9 ASP E 250 GLY E 264 1 15
HELIX 91 AK1 ASP E 265 GLY E 271 5 7
HELIX 92 AK2 ASP E 273 ARG E 280 1 8
HELIX 93 AK3 THR E 297 LYS E 306 1 10
HELIX 94 AK4 ASP E 320 GLY E 327 5 8
HELIX 95 AK5 ASP E 329 SER E 345 1 17
HELIX 96 AK6 THR F 6 GLY F 11 1 6
HELIX 97 AK7 THR F 59 ILE F 68 1 10
HELIX 98 AK8 GLY F 99 PHE F 107 5 9
HELIX 99 AK9 ARG F 111 TYR F 126 1 16
HELIX 100 AL1 SER F 139 TYR F 152 1 14
HELIX 101 AL2 SER F 169 THR F 185 1 17
HELIX 102 AL3 ASP F 186 LEU F 193 5 8
HELIX 103 AL4 SER F 196 ALA F 199 5 4
HELIX 104 AL5 VAL F 200 TRP F 216 1 17
HELIX 105 AL6 SER F 217 THR F 223 1 7
HELIX 106 AL7 GLY F 224 LEU F 229 1 6
HELIX 107 AL8 SER F 233 PHE F 241 1 9
HELIX 108 AL9 PHE F 241 ALA F 247 1 7
HELIX 109 AM1 ASP F 250 ARG F 263 1 14
HELIX 110 AM2 GLY F 264 GLY F 271 5 8
HELIX 111 AM3 ASP F 273 GLY F 279 1 7
HELIX 112 AM4 THR F 297 LYS F 306 1 10
HELIX 113 AM5 ASP F 320 GLY F 327 5 8
HELIX 114 AM6 ASP F 329 SER F 345 1 17
SHEET 1 AA1 8 GLU A 14 ASN A 17 0
SHEET 2 AA1 8 LEU A 33 HIS A 39 -1 O LEU A 34 N ILE A 16
SHEET 3 AA1 8 CYS A 80 VAL A 84 -1 O ILE A 81 N HIS A 39
SHEET 4 AA1 8 ALA A 49 PRO A 53 1 N ILE A 50 O ILE A 82
SHEET 5 AA1 8 LEU A 134 GLY A 138 1 O LEU A 134 N LEU A 51
SHEET 6 AA1 8 ARG A 158 ILE A 162 1 O ALA A 160 N VAL A 135
SHEET 7 AA1 8 LYS A 284 MET A 288 1 O MET A 288 N ALA A 161
SHEET 8 AA1 8 GLU A 312 PHE A 313 1 O GLU A 312 N VAL A 287
SHEET 1 AA2 2 LEU A 21 PRO A 22 0
SHEET 2 AA2 2 CYS A 28 MET A 29 -1 O MET A 29 N LEU A 21
SHEET 1 AA3 8 GLU B 14 ASN B 17 0
SHEET 2 AA3 8 LEU B 33 HIS B 39 -1 O VAL B 36 N GLU B 14
SHEET 3 AA3 8 CYS B 80 VAL B 84 -1 O ILE B 81 N HIS B 39
SHEET 4 AA3 8 ALA B 49 PRO B 53 1 N ILE B 50 O ILE B 82
SHEET 5 AA3 8 LEU B 134 GLY B 138 1 O LEU B 134 N LEU B 51
SHEET 6 AA3 8 ARG B 158 ILE B 162 1 O ALA B 160 N VAL B 135
SHEET 7 AA3 8 LYS B 284 MET B 288 1 O MET B 288 N ALA B 161
SHEET 8 AA3 8 GLU B 312 PHE B 313 1 O GLU B 312 N VAL B 287
SHEET 1 AA4 2 LEU B 21 PRO B 22 0
SHEET 2 AA4 2 CYS B 28 MET B 29 -1 O MET B 29 N LEU B 21
SHEET 1 AA5 8 GLU C 14 ASN C 17 0
SHEET 2 AA5 8 LEU C 33 HIS C 39 -1 O VAL C 36 N GLU C 14
SHEET 3 AA5 8 CYS C 80 VAL C 84 -1 O ILE C 81 N HIS C 39
SHEET 4 AA5 8 ALA C 49 PRO C 53 1 N ILE C 50 O ILE C 82
SHEET 5 AA5 8 LEU C 134 GLY C 138 1 O LEU C 134 N LEU C 51
SHEET 6 AA5 8 ARG C 158 ILE C 162 1 O ILE C 162 N GLY C 137
SHEET 7 AA5 8 LYS C 284 MET C 288 1 O MET C 288 N ALA C 161
SHEET 8 AA5 8 GLU C 312 PHE C 313 1 O GLU C 312 N VAL C 287
SHEET 1 AA6 2 LEU C 21 PRO C 22 0
SHEET 2 AA6 2 CYS C 28 MET C 29 -1 O MET C 29 N LEU C 21
SHEET 1 AA7 8 GLU D 14 ASN D 17 0
SHEET 2 AA7 8 LEU D 33 HIS D 39 -1 O VAL D 36 N GLU D 14
SHEET 3 AA7 8 CYS D 80 VAL D 84 -1 O ILE D 81 N HIS D 39
SHEET 4 AA7 8 ALA D 49 PRO D 53 1 N ILE D 50 O ILE D 82
SHEET 5 AA7 8 LEU D 134 GLY D 138 1 O LEU D 134 N LEU D 51
SHEET 6 AA7 8 ARG D 158 ILE D 162 1 O ALA D 160 N VAL D 135
SHEET 7 AA7 8 LYS D 284 MET D 288 1 O MET D 288 N ALA D 161
SHEET 8 AA7 8 GLU D 312 PHE D 313 1 O GLU D 312 N VAL D 287
SHEET 1 AA8 2 LEU D 21 PRO D 22 0
SHEET 2 AA8 2 CYS D 28 MET D 29 -1 O MET D 29 N LEU D 21
SHEET 1 AA9 8 GLU E 14 ASN E 17 0
SHEET 2 AA9 8 LEU E 33 HIS E 39 -1 O VAL E 36 N GLU E 14
SHEET 3 AA9 8 CYS E 80 VAL E 84 -1 O VAL E 83 N ALA E 37
SHEET 4 AA9 8 ALA E 49 PRO E 53 1 N ILE E 50 O ILE E 82
SHEET 5 AA9 8 LEU E 134 GLY E 138 1 O VAL E 136 N LEU E 51
SHEET 6 AA9 8 ARG E 158 ILE E 162 1 O ILE E 162 N GLY E 137
SHEET 7 AA9 8 LYS E 284 MET E 288 1 O LYS E 284 N ALA E 159
SHEET 8 AA9 8 GLU E 312 PHE E 313 1 O GLU E 312 N VAL E 287
SHEET 1 AB1 2 LEU E 21 PRO E 22 0
SHEET 2 AB1 2 CYS E 28 MET E 29 -1 O MET E 29 N LEU E 21
SHEET 1 AB2 8 GLU F 14 ASN F 17 0
SHEET 2 AB2 8 LEU F 33 HIS F 39 -1 O LEU F 34 N ILE F 16
SHEET 3 AB2 8 CYS F 80 VAL F 84 -1 O ILE F 81 N HIS F 39
SHEET 4 AB2 8 ALA F 49 PRO F 53 1 N ILE F 50 O ILE F 82
SHEET 5 AB2 8 LEU F 134 GLY F 138 1 O LEU F 134 N LEU F 51
SHEET 6 AB2 8 ARG F 158 ILE F 162 1 O ALA F 160 N VAL F 135
SHEET 7 AB2 8 LYS F 284 MET F 288 1 O MET F 288 N ALA F 161
SHEET 8 AB2 8 GLU F 312 PHE F 313 1 O GLU F 312 N VAL F 287
SHEET 1 AB3 2 LEU F 21 PRO F 22 0
SHEET 2 AB3 2 CYS F 28 MET F 29 -1 O MET F 29 N LEU F 21
CISPEP 1 GLY A 11 PRO A 12 0 2.07
CISPEP 2 GLY B 11 PRO B 12 0 2.24
CISPEP 3 GLY C 11 PRO C 12 0 5.07
CISPEP 4 GLY D 11 PRO D 12 0 -0.23
CISPEP 5 GLY E 11 PRO E 12 0 6.04
CISPEP 6 GLY F 11 PRO F 12 0 -0.60
SITE 1 AC1 4 TYR A 5 GLY A 90 LEU A 91 ASN A 97
SITE 1 AC2 3 ASP A 299 LYS A 306 HOH A 563
SITE 1 AC3 5 SER A 47 ARG A 158 ALA A 348 HOH A 532
SITE 2 AC3 5 ASP F 45
SITE 1 AC4 7 THR A 184 THR A 185 ASP A 186 PRO A 187
SITE 2 AC4 7 GLN A 190 ALA A 191 HOH A 565
SITE 1 AC5 3 ARG A 167 ASN A 168 GLN A 262
SITE 1 AC6 7 GLY A 104 PRO A 105 PHE A 107 ASN A 252
SITE 2 AC6 7 THR A 256 HOH A 528 HOH A 549
SITE 1 AC7 5 ARG A 167 SER A 169 LEU A 274 GLU A 304
SITE 2 AC7 5 HOH A 531
SITE 1 AC8 2 ALA A 188 ARG A 195
SITE 1 AC9 5 TRP A 55 TYR A 56 SER A 139 MET A 140
SITE 2 AC9 5 HIS A 322
SITE 1 AD1 2 ARG B 72 ASP B 334
SITE 1 AD2 3 ARG B 27 SER B 101 SER E 101
SITE 1 AD3 3 LYS B 46 HOH B 505 HOH B 596
SITE 1 AD4 1 SER B 291
SITE 1 AD5 1 ARG B 263
SITE 1 AD6 5 TRP B 55 TYR B 56 SER B 139 MET B 140
SITE 2 AD6 5 HIS B 322
SITE 1 AD7 6 ARG C 195 EDO C 406 GOL C 407 GLN D 294
SITE 2 AD7 6 HOH D 561 GLN F 294
SITE 1 AD8 7 ARG C 167 SER C 169 LEU C 274 ASP C 300
SITE 2 AD8 7 GLU C 304 HOH C 510 HOH C 547
SITE 1 AD9 8 GLY C 104 PRO C 105 PHE C 107 ASN C 252
SITE 2 AD9 8 LEU C 255 THR C 256 HOH C 537 HOH C 546
SITE 1 AE1 8 GLU C 25 ARG C 27 PHE C 107 ASN C 109
SITE 2 AE1 8 HOH C 512 HOH C 525 HOH C 531 GLU F 312
SITE 1 AE2 4 ASP C 299 LYS C 306 HOH C 506 ARG E 222
SITE 1 AE3 6 GLN C 190 EDO C 401 SER F 291 ASP F 293
SITE 2 AE3 6 HOH F 510 HOH F 572
SITE 1 AE4 5 GLN C 190 ARG C 195 EDO C 401 HOH C 515
SITE 2 AE4 5 SER D 291
SITE 1 AE5 5 ARG C 195 SER C 196 ALA C 199 VAL D 298
SITE 2 AE5 5 PRO D 315
SITE 1 AE6 5 TRP C 55 TYR C 56 SER C 139 MET C 140
SITE 2 AE6 5 HIS C 322
SITE 1 AE7 8 SER D 169 HIS D 171 PHE D 295 ASP D 300
SITE 2 AE7 8 HOH D 501 HOH D 566 PRO F 218 ARG F 222
SITE 1 AE8 4 SER D 303 LYS D 306 HOH D 519 ARG F 222
SITE 1 AE9 3 ARG D 222 HOH D 601 ASP F 299
SITE 1 AF1 7 ARG D 27 PRO D 105 PHE D 107 ALA D 108
SITE 2 AF1 7 ASN D 109 HOH D 518 HOH D 555
SITE 1 AF2 7 ILE D 178 ALA D 182 LEU D 210 HOH D 523
SITE 2 AF2 7 HOH D 537 ILE F 178 ALA F 182
SITE 1 AF3 5 TRP D 55 TYR D 56 SER D 139 MET D 140
SITE 2 AF3 5 HIS D 322
SITE 1 AF4 3 ARG E 167 LEU E 274 GLU E 304
SITE 1 AF5 3 GLU E 312 HOH E 509 HOH E 514
SITE 1 AF6 5 TRP E 55 TYR E 56 SER E 139 MET E 140
SITE 2 AF6 5 HIS E 322
SITE 1 AF7 3 ILE C 178 ALA C 182 LEU E 210
SITE 1 AF8 5 ARG F 167 GLY F 272 ASP F 273 LEU F 274
SITE 2 AF8 5 ALA F 275
SITE 1 AF9 2 GLU F 177 HOH F 525
SITE 1 AG1 8 ARG F 167 SER F 169 LEU F 274 ASP F 300
SITE 2 AG1 8 SER F 303 GLU F 304 HOH F 504 HOH F 520
SITE 1 AG2 6 SER A 47 HOH A 522 ASN F 43 ASP F 45
SITE 2 AG2 6 SER F 47 HOH F 506
SITE 1 AG3 5 ASN A 43 ALA A 44 ASP A 45 SER A 47
SITE 2 AG3 5 HOH F 506
SITE 1 AG4 5 TRP F 55 TYR F 56 SER F 139 MET F 140
SITE 2 AG4 5 HIS F 322
CRYST1 88.848 110.342 122.817 90.00 106.89 90.00 P 1 21 1 4
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 0.011255 0.000000 0.003416 0.00000
SCALE2 0.000000 0.009063 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008509 0.00000
TER 2694 TYR A 349
TER 5373 PRO B 347
TER 7976 ALA C 348
TER 10638 SER D 346
TER 13299 PRO E 347
TER 15978 TYR F 349
MASTER 1084 0 40 114 60 0 64 617200 6 176 168
END
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