HEADER OXIDOREDUCTASE 27-AUG-14 4W9U
TITLE CRYSTAL STRUCTURE OF AN ACYL-COA DEHYDROGENASE FROM BRUCELLA
TITLE 2 MELITENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COA DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRUCELLA ABORTUS 2308;
SOURCE 3 ORGANISM_COMMON: BRUCELLA MELITENSIS BIOVAR ABORTUS 2308;
SOURCE 4 ORGANISM_TAXID: 359391;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SSGCID, NIAID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS
KEYWDS 2 CENTER FOR INFECTIOUS DISEASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 27-DEC-23 4W9U 1 REMARK
REVDAT 3 22-NOV-17 4W9U 1 SOURCE REMARK
REVDAT 2 25-FEB-15 4W9U 1 REMARK
REVDAT 1 10-SEP-14 4W9U 0
JRNL AUTH D.M.DRANOW,T.E.EDWARDS,D.LORIMER,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF AN ACYL-COA DEHYDROGENASE FROM BRUCELLA
JRNL TITL 2 MELITENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1769)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 56423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2806
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 47.2396 - 6.5094 1.00 3093 164 0.1616 0.1908
REMARK 3 2 6.5094 - 5.1688 0.99 3009 162 0.1729 0.2166
REMARK 3 3 5.1688 - 4.5160 0.99 3018 135 0.1370 0.1868
REMARK 3 4 4.5160 - 4.1033 0.97 2958 154 0.1255 0.1830
REMARK 3 5 4.1033 - 3.8094 0.95 2904 142 0.1434 0.1966
REMARK 3 6 3.8094 - 3.5849 0.94 2814 173 0.1682 0.2418
REMARK 3 7 3.5849 - 3.4054 0.96 2896 146 0.1866 0.2338
REMARK 3 8 3.4054 - 3.2572 0.95 2879 140 0.1933 0.2603
REMARK 3 9 3.2572 - 3.1318 0.93 2827 130 0.1962 0.2525
REMARK 3 10 3.1318 - 3.0238 0.89 2703 144 0.2037 0.2685
REMARK 3 11 3.0238 - 2.9292 0.87 2615 147 0.2051 0.2655
REMARK 3 12 2.9292 - 2.8455 0.86 2606 132 0.2133 0.3510
REMARK 3 13 2.8455 - 2.7706 0.83 2503 152 0.2239 0.2973
REMARK 3 14 2.7706 - 2.7030 0.82 2461 133 0.2189 0.2754
REMARK 3 15 2.7030 - 2.6416 0.82 2450 135 0.2213 0.3074
REMARK 3 16 2.6416 - 2.5854 0.81 2458 132 0.2216 0.3004
REMARK 3 17 2.5854 - 2.5337 0.80 2405 107 0.2303 0.2711
REMARK 3 18 2.5337 - 2.4858 0.79 2375 137 0.2398 0.3253
REMARK 3 19 2.4858 - 2.4414 0.77 2320 128 0.2614 0.3231
REMARK 3 20 2.4414 - 2.4001 0.77 2323 113 0.2711 0.3501
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.31
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.97
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 : 0.009 11183
REMARK 3 ANGLE : 1.173 15107
REMARK 3 CHIRALITY : 0.045 1664
REMARK 3 PLANARITY : 0.006 1980
REMARK 3 DIHEDRAL : 12.181 3972
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0493 72.0982 49.8983
REMARK 3 T TENSOR
REMARK 3 T11: 0.3207 T22: 0.2345
REMARK 3 T33: 0.3972 T12: 0.0572
REMARK 3 T13: 0.0105 T23: -0.0844
REMARK 3 L TENSOR
REMARK 3 L11: 2.2099 L22: 2.5247
REMARK 3 L33: 3.8549 L12: 1.2890
REMARK 3 L13: 0.8508 L23: 0.7782
REMARK 3 S TENSOR
REMARK 3 S11: -0.2137 S12: -0.3819 S13: 0.2184
REMARK 3 S21: 0.2584 S22: 0.1843 S23: -0.3391
REMARK 3 S31: -0.3066 S32: -0.3493 S33: -0.0723
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1257 62.6882 59.3029
REMARK 3 T TENSOR
REMARK 3 T11: 0.4832 T22: 0.3604
REMARK 3 T33: 0.5015 T12: 0.0739
REMARK 3 T13: -0.2176 T23: -0.1402
REMARK 3 L TENSOR
REMARK 3 L11: 2.6854 L22: 2.6381
REMARK 3 L33: 3.6062 L12: 0.7424
REMARK 3 L13: 0.0589 L23: -0.3474
REMARK 3 S TENSOR
REMARK 3 S11: 0.3048 S12: -0.2842 S13: -0.2497
REMARK 3 S21: 0.7425 S22: 0.0330 S23: -0.5347
REMARK 3 S31: 0.2290 S32: 0.4286 S33: -0.1904
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3027 54.2831 60.1929
REMARK 3 T TENSOR
REMARK 3 T11: 0.6125 T22: 0.4373
REMARK 3 T33: 0.4650 T12: 0.0717
REMARK 3 T13: -0.2393 T23: -0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 1.9345 L22: 0.3444
REMARK 3 L33: 1.6486 L12: -0.5561
REMARK 3 L13: 1.0875 L23: 0.0798
REMARK 3 S TENSOR
REMARK 3 S11: 0.2791 S12: -0.3337 S13: -0.5093
REMARK 3 S21: 0.6034 S22: 0.1753 S23: -0.6029
REMARK 3 S31: 0.1521 S32: 0.0167 S33: -0.2074
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0464 44.1850 68.0078
REMARK 3 T TENSOR
REMARK 3 T11: 0.9512 T22: 0.5639
REMARK 3 T33: 0.6877 T12: 0.0821
REMARK 3 T13: -0.4453 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.4195 L22: 0.6867
REMARK 3 L33: 1.8005 L12: 0.4293
REMARK 3 L13: 0.6200 L23: 0.4064
REMARK 3 S TENSOR
REMARK 3 S11: 0.2727 S12: -0.5032 S13: -0.8882
REMARK 3 S21: 0.4625 S22: -0.1303 S23: -0.8357
REMARK 3 S31: 0.3513 S32: 0.0424 S33: -0.2620
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9818 38.2526 70.4875
REMARK 3 T TENSOR
REMARK 3 T11: 1.3362 T22: 0.4650
REMARK 3 T33: 0.8512 T12: 0.1323
REMARK 3 T13: -0.6771 T23: 0.2384
REMARK 3 L TENSOR
REMARK 3 L11: 0.4317 L22: 1.0282
REMARK 3 L33: 0.7081 L12: -0.6019
REMARK 3 L13: -0.1884 L23: 0.6040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.5681 S13: -0.5313
REMARK 3 S21: 0.3662 S22: 0.2026 S23: 0.2182
REMARK 3 S31: 0.9256 S32: -0.1265 S33: -0.2176
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 199 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5043 40.9670 68.2798
REMARK 3 T TENSOR
REMARK 3 T11: 0.9728 T22: 0.5556
REMARK 3 T33: 0.8281 T12: 0.2075
REMARK 3 T13: -0.5521 T23: 0.1200
REMARK 3 L TENSOR
REMARK 3 L11: 2.8799 L22: 0.2145
REMARK 3 L33: 1.8253 L12: 0.7682
REMARK 3 L13: -0.1321 L23: -0.2095
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.2752 S13: -1.0301
REMARK 3 S21: 0.3658 S22: 0.2123 S23: -0.7423
REMARK 3 S31: 0.9366 S32: -0.0001 S33: -0.2236
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 242 THROUGH 277 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8986 58.2290 46.1936
REMARK 3 T TENSOR
REMARK 3 T11: 0.3904 T22: 0.2693
REMARK 3 T33: 0.4049 T12: 0.0264
REMARK 3 T13: -0.0758 T23: -0.1200
REMARK 3 L TENSOR
REMARK 3 L11: 1.3469 L22: 1.4405
REMARK 3 L33: 3.1409 L12: 0.0225
REMARK 3 L13: 0.3594 L23: -1.0442
REMARK 3 S TENSOR
REMARK 3 S11: 0.1557 S12: -0.2011 S13: -0.0798
REMARK 3 S21: 0.2387 S22: -0.0204 S23: -0.3279
REMARK 3 S31: 0.1432 S32: 0.5888 S33: -0.1305
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5082 59.0005 39.6192
REMARK 3 T TENSOR
REMARK 3 T11: 0.2959 T22: 0.2788
REMARK 3 T33: 0.3234 T12: 0.0095
REMARK 3 T13: -0.0656 T23: -0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 0.6295 L22: 1.3311
REMARK 3 L33: 2.5253 L12: 0.0493
REMARK 3 L13: -0.6698 L23: -0.0555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.0062 S13: -0.0342
REMARK 3 S21: 0.0346 S22: 0.0856 S23: -0.2333
REMARK 3 S31: 0.1298 S32: 0.0530 S33: -0.1132
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 348 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7651 54.7053 39.3853
REMARK 3 T TENSOR
REMARK 3 T11: 0.4183 T22: 0.6444
REMARK 3 T33: 0.5117 T12: 0.1989
REMARK 3 T13: -0.1224 T23: -0.2968
REMARK 3 L TENSOR
REMARK 3 L11: 3.8140 L22: 2.0975
REMARK 3 L33: 7.3513 L12: 0.0037
REMARK 3 L13: -0.2927 L23: -2.9437
REMARK 3 S TENSOR
REMARK 3 S11: 0.4924 S12: 0.3949 S13: 0.0695
REMARK 3 S21: -0.3733 S22: 0.3605 S23: -0.3854
REMARK 3 S31: 1.2742 S32: 0.2002 S33: -0.2951
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 372 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9931 38.8252 47.6213
REMARK 3 T TENSOR
REMARK 3 T11: 0.4544 T22: 0.2417
REMARK 3 T33: 0.3165 T12: 0.0108
REMARK 3 T13: -0.0777 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 2.2720 L22: 7.8094
REMARK 3 L33: 6.1574 L12: 1.2002
REMARK 3 L13: -2.4606 L23: -0.6916
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: -0.1981 S13: -0.4130
REMARK 3 S21: -0.1327 S22: -0.0823 S23: -0.7296
REMARK 3 S31: -0.3681 S32: 0.1223 S33: 0.0033
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1184 64.9080 40.6220
REMARK 3 T TENSOR
REMARK 3 T11: 0.2657 T22: 0.3592
REMARK 3 T33: 0.2919 T12: 0.0233
REMARK 3 T13: 0.0845 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.7348 L22: 1.5112
REMARK 3 L33: 1.3976 L12: -0.6569
REMARK 3 L13: 0.6956 L23: -0.7349
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.2405 S13: -0.0530
REMARK 3 S21: 0.2718 S22: 0.1085 S23: 0.2321
REMARK 3 S31: -0.1505 S32: -0.2507 S33: -0.0871
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 130 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4811 79.0499 20.5288
REMARK 3 T TENSOR
REMARK 3 T11: 0.2749 T22: 0.3135
REMARK 3 T33: 0.2908 T12: 0.0267
REMARK 3 T13: 0.0540 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 3.7793 L22: 5.4314
REMARK 3 L33: 3.4910 L12: 0.9999
REMARK 3 L13: 0.1904 L23: -0.0593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0873 S12: 0.3042 S13: 0.2515
REMARK 3 S21: -0.1581 S22: 0.1184 S23: -0.1161
REMARK 3 S31: -0.3772 S32: -0.1425 S33: -0.0157
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 242 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5724 53.8345 36.5533
REMARK 3 T TENSOR
REMARK 3 T11: 0.2116 T22: 0.2946
REMARK 3 T33: 0.2418 T12: -0.0027
REMARK 3 T13: 0.0176 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.1547 L22: 1.4062
REMARK 3 L33: 0.3456 L12: -0.3478
REMARK 3 L13: -0.0836 L23: -0.3121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: -0.0023 S13: -0.1047
REMARK 3 S21: -0.0520 S22: 0.0431 S23: 0.1043
REMARK 3 S31: 0.0280 S32: -0.1116 S33: -0.0977
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2467 69.4220 25.2105
REMARK 3 T TENSOR
REMARK 3 T11: 0.4362 T22: 0.2189
REMARK 3 T33: 0.3705 T12: 0.0300
REMARK 3 T13: 0.0242 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 3.1338 L22: 3.1800
REMARK 3 L33: 2.4342 L12: -0.1508
REMARK 3 L13: 0.2063 L23: 0.8604
REMARK 3 S TENSOR
REMARK 3 S11: -0.1169 S12: 0.0537 S13: -0.0586
REMARK 3 S21: -0.3783 S22: 0.1067 S23: 0.2065
REMARK 3 S31: -0.1015 S32: 0.0387 S33: -0.1372
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8151 33.6382 0.6855
REMARK 3 T TENSOR
REMARK 3 T11: 0.4497 T22: 0.2738
REMARK 3 T33: 0.3028 T12: 0.0090
REMARK 3 T13: -0.1463 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 2.8629 L22: 3.2064
REMARK 3 L33: 0.9151 L12: 2.1931
REMARK 3 L13: 1.2846 L23: -0.0373
REMARK 3 S TENSOR
REMARK 3 S11: 0.1896 S12: 0.1530 S13: -0.0518
REMARK 3 S21: -0.4013 S22: -0.0271 S23: 0.2807
REMARK 3 S31: 0.2298 S32: -0.0610 S33: -0.0398
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3446 18.7040 12.4992
REMARK 3 T TENSOR
REMARK 3 T11: 0.5176 T22: 0.4506
REMARK 3 T33: 0.5921 T12: -0.1784
REMARK 3 T13: -0.1780 T23: 0.0749
REMARK 3 L TENSOR
REMARK 3 L11: 1.8217 L22: 1.6732
REMARK 3 L33: 0.9164 L12: 0.5728
REMARK 3 L13: 0.6336 L23: 0.3074
REMARK 3 S TENSOR
REMARK 3 S11: 0.2681 S12: -0.3453 S13: -0.4729
REMARK 3 S21: -0.0742 S22: 0.0441 S23: 0.3006
REMARK 3 S31: 0.5876 S32: -0.4658 S33: -0.1265
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 178 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0281 13.8598 18.0505
REMARK 3 T TENSOR
REMARK 3 T11: 0.5853 T22: 0.5471
REMARK 3 T33: 0.8197 T12: -0.2638
REMARK 3 T13: -0.1768 T23: 0.3152
REMARK 3 L TENSOR
REMARK 3 L11: 0.0409 L22: 3.3343
REMARK 3 L33: 0.8844 L12: -0.3464
REMARK 3 L13: 0.0234 L23: -0.4157
REMARK 3 S TENSOR
REMARK 3 S11: 0.1713 S12: -0.6511 S13: -0.7531
REMARK 3 S21: 0.5933 S22: 0.0135 S23: 0.6357
REMARK 3 S31: 0.4059 S32: -0.8281 S33: -0.3206
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 219 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2104 11.9486 18.0567
REMARK 3 T TENSOR
REMARK 3 T11: 0.7191 T22: 0.6139
REMARK 3 T33: 0.8148 T12: -0.2669
REMARK 3 T13: -0.1418 T23: 0.2280
REMARK 3 L TENSOR
REMARK 3 L11: 1.2753 L22: 3.1802
REMARK 3 L33: 2.0562 L12: 0.3262
REMARK 3 L13: 0.3228 L23: 0.2849
REMARK 3 S TENSOR
REMARK 3 S11: 0.1955 S12: -0.5465 S13: -0.7088
REMARK 3 S21: 0.6240 S22: -0.0759 S23: 0.4375
REMARK 3 S31: 0.9532 S32: -0.7308 S33: -0.2858
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 243 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7855 42.0168 13.8030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2411 T22: 0.2528
REMARK 3 T33: 0.2420 T12: 0.0036
REMARK 3 T13: -0.0294 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.7128 L22: 2.6487
REMARK 3 L33: 0.7449 L12: 0.3735
REMARK 3 L13: 0.1060 L23: 0.2321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0934 S12: 0.0434 S13: 0.0367
REMARK 3 S21: -0.1188 S22: -0.0641 S23: 0.2169
REMARK 3 S31: -0.0035 S32: -0.1488 S33: -0.0201
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 348 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2563 45.3612 17.0965
REMARK 3 T TENSOR
REMARK 3 T11: 0.3100 T22: 0.6196
REMARK 3 T33: 0.4766 T12: -0.0846
REMARK 3 T13: 0.0203 T23: -0.1640
REMARK 3 L TENSOR
REMARK 3 L11: 4.7735 L22: 7.5774
REMARK 3 L33: 5.0525 L12: -0.2189
REMARK 3 L13: -0.1264 L23: -2.4578
REMARK 3 S TENSOR
REMARK 3 S11: 0.1686 S12: -0.1480 S13: 0.1421
REMARK 3 S21: 0.0458 S22: -0.3824 S23: 1.1294
REMARK 3 S31: 0.4555 S32: -0.8375 S33: 0.4452
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 372 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8676 27.7747 30.3937
REMARK 3 T TENSOR
REMARK 3 T11: 0.2989 T22: 0.2090
REMARK 3 T33: 0.3863 T12: -0.0440
REMARK 3 T13: -0.0412 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 6.6294 L22: 4.5674
REMARK 3 L33: 3.2975 L12: -0.1669
REMARK 3 L13: -1.8446 L23: 1.2558
REMARK 3 S TENSOR
REMARK 3 S11: 0.2066 S12: 0.0926 S13: 0.2232
REMARK 3 S21: -0.0202 S22: -0.1222 S23: 0.2607
REMARK 3 S31: 0.0325 S32: -0.1954 S33: -0.0875
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4491 37.4386 13.1802
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.2643
REMARK 3 T33: 0.3702 T12: 0.0782
REMARK 3 T13: -0.0125 T23: -0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 2.2808 L22: 1.4489
REMARK 3 L33: 1.3783 L12: 0.9319
REMARK 3 L13: -0.7806 L23: -0.6242
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: 0.0605 S13: -0.4226
REMARK 3 S21: -0.2477 S22: -0.0073 S23: -0.3215
REMARK 3 S31: 0.2632 S32: 0.1764 S33: -0.0063
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 130 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0952 63.4573 7.6022
REMARK 3 T TENSOR
REMARK 3 T11: 0.2810 T22: 0.2811
REMARK 3 T33: 0.2829 T12: 0.0637
REMARK 3 T13: 0.0260 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 2.7144 L22: 4.4769
REMARK 3 L33: 3.6900 L12: 1.2123
REMARK 3 L13: -1.2570 L23: -3.3509
REMARK 3 S TENSOR
REMARK 3 S11: 0.1548 S12: 0.0462 S13: 0.4983
REMARK 3 S21: -0.0251 S22: 0.0815 S23: 0.3223
REMARK 3 S31: -0.2443 S32: -0.0287 S33: -0.2169
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 168 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.5125 60.1044 7.4946
REMARK 3 T TENSOR
REMARK 3 T11: 0.2418 T22: 0.3233
REMARK 3 T33: 0.2781 T12: 0.0653
REMARK 3 T13: 0.0492 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 4.1641 L22: 3.2563
REMARK 3 L33: 5.9811 L12: -0.1910
REMARK 3 L13: 1.8958 L23: -1.9331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0951 S12: 0.1724 S13: 0.2158
REMARK 3 S21: -0.0546 S22: 0.0894 S23: 0.1048
REMARK 3 S31: -0.1395 S32: -0.2034 S33: 0.1606
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 199 THROUGH 242 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7192 59.1186 11.6907
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.2660
REMARK 3 T33: 0.3034 T12: 0.0547
REMARK 3 T13: 0.0652 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 3.4759 L22: 3.9731
REMARK 3 L33: 3.9980 L12: 1.1883
REMARK 3 L13: 0.5403 L23: -0.4074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.1351 S13: -0.0515
REMARK 3 S21: 0.1023 S22: -0.2044 S23: 0.0949
REMARK 3 S31: -0.3256 S32: 0.0860 S33: 0.2054
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 243 THROUGH 347 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5704 39.5154 22.2499
REMARK 3 T TENSOR
REMARK 3 T11: 0.2382 T22: 0.2198
REMARK 3 T33: 0.3067 T12: 0.0115
REMARK 3 T13: -0.0326 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.8180 L22: 1.0391
REMARK 3 L33: 1.8598 L12: 0.1451
REMARK 3 L13: -0.2260 L23: -0.7597
REMARK 3 S TENSOR
REMARK 3 S11: 0.0925 S12: -0.0262 S13: -0.0549
REMARK 3 S21: -0.0077 S22: 0.0213 S23: 0.0018
REMARK 3 S31: 0.1091 S32: 0.1845 S33: -0.0388
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 348 THROUGH 371 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4408 45.0376 31.4055
REMARK 3 T TENSOR
REMARK 3 T11: 0.2709 T22: 0.3851
REMARK 3 T33: 0.4532 T12: 0.0031
REMARK 3 T13: -0.0368 T23: -0.1186
REMARK 3 L TENSOR
REMARK 3 L11: 9.5538 L22: 3.9535
REMARK 3 L33: 9.5368 L12: 1.5713
REMARK 3 L13: -4.3203 L23: 0.0633
REMARK 3 S TENSOR
REMARK 3 S11: 0.3129 S12: -0.9945 S13: 0.4220
REMARK 3 S21: 0.3469 S22: 0.3406 S23: -0.6428
REMARK 3 S31: -0.1806 S32: 0.6655 S33: -0.5771
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 372 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9472 58.6274 12.3568
REMARK 3 T TENSOR
REMARK 3 T11: 0.3390 T22: 0.2926
REMARK 3 T33: 0.3858 T12: 0.0140
REMARK 3 T13: 0.0753 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 9.2503 L22: 6.3233
REMARK 3 L33: 2.7005 L12: -0.9153
REMARK 3 L13: 4.0014 L23: -0.5582
REMARK 3 S TENSOR
REMARK 3 S11: 0.2916 S12: 0.2545 S13: 0.1710
REMARK 3 S21: -0.5497 S22: 0.0102 S23: -0.6021
REMARK 3 S31: 0.0200 S32: 0.7754 S33: -0.1660
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 6561
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 6561
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 6561
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4W9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63306
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.510
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG(D2): 30% PEG-400, 100MM HEPES
REMARK 280 FREE ACID/ NAOH, 200MM MGCL2, PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
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 53.33000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 43
REMARK 465 ALA A 44
REMARK 465 TYR A 45
REMARK 465 LEU A 46
REMARK 465 GLU A 47
REMARK 465 GLU A 48
REMARK 465 THR A 49
REMARK 465 THR A 50
REMARK 465 ASP A 142
REMARK 465 ALA A 143
REMARK 465 GLY A 144
REMARK 465 SER A 145
REMARK 465 ASP A 146
REMARK 465 PRO A 147
REMARK 465 ALA A 148
REMARK 465 GLY A 149
REMARK 465 GLY A 210
REMARK 465 GLY A 211
REMARK 465 LYS A 212
REMARK 465 LEU A 213
REMARK 465 SER A 214
REMARK 465 LEU A 215
REMARK 465 ARG A 216
REMARK 465 GLY A 350
REMARK 465 ASN A 351
REMARK 465 GLY A 352
REMARK 465 ILE A 353
REMARK 465 GLN A 354
REMARK 465 ILE A 355
REMARK 465 GLU A 356
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 44
REMARK 465 TYR B 45
REMARK 465 LEU B 46
REMARK 465 ALA B 143
REMARK 465 GLY B 144
REMARK 465 SER B 145
REMARK 465 ASP B 146
REMARK 465 LYS B 212
REMARK 465 LEU B 213
REMARK 465 SER B 214
REMARK 465 GLY B 350
REMARK 465 ASN B 351
REMARK 465 GLY B 352
REMARK 465 ILE B 353
REMARK 465 GLN B 354
REMARK 465 ILE B 355
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ARG C 3
REMARK 465 ALA C 44
REMARK 465 TYR C 45
REMARK 465 LEU C 46
REMARK 465 GLU C 47
REMARK 465 GLU C 48
REMARK 465 THR C 49
REMARK 465 ASP C 142
REMARK 465 ALA C 143
REMARK 465 GLY C 144
REMARK 465 SER C 145
REMARK 465 ASP C 146
REMARK 465 PRO C 147
REMARK 465 ALA C 148
REMARK 465 GLY C 149
REMARK 465 GLY C 210
REMARK 465 GLY C 211
REMARK 465 LYS C 212
REMARK 465 LEU C 213
REMARK 465 SER C 214
REMARK 465 ASN C 351
REMARK 465 GLY C 352
REMARK 465 ILE C 353
REMARK 465 GLN C 354
REMARK 465 ILE C 355
REMARK 465 GLU C 356
REMARK 465 TYR C 357
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ARG D 3
REMARK 465 LYS D 43
REMARK 465 ALA D 44
REMARK 465 TYR D 45
REMARK 465 LEU D 46
REMARK 465 GLU D 47
REMARK 465 GLU D 48
REMARK 465 THR D 49
REMARK 465 ASP D 146
REMARK 465 PRO D 147
REMARK 465 LEU D 213
REMARK 465 GLY D 350
REMARK 465 ASN D 351
REMARK 465 GLY D 352
REMARK 465 ILE D 353
REMARK 465 GLN D 354
REMARK 465 ILE D 355
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 41 CG1 CG2
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 ASP A 51 CG OD1 OD2
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 ASP A 71 CG OD1 OD2
REMARK 470 ALA A 74 CB
REMARK 470 SER A 116 OG
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 SER A 129 OG
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 LEU A 138 CG CD1 CD2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 155 CG CD OE1 OE2
REMARK 470 LYS A 156 CG CD CE NZ
REMARK 470 ILE A 157 CG1 CG2 CD1
REMARK 470 ASP A 158 CG OD1 OD2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 163 CG CD1 CD2
REMARK 470 MET A 168 CG SD CE
REMARK 470 TRP A 169 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 169 CZ3 CH2
REMARK 470 ILE A 170 CG1 CG2 CD1
REMARK 470 SER A 171 OG
REMARK 470 LYS A 184 CG CD CE NZ
REMARK 470 ASP A 189 CG OD1 OD2
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 470 LEU A 204 CG CD1 CD2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 SER A 218 OG
REMARK 470 THR A 220 OG1 CG2
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 ILE A 223 CG1 CG2 CD1
REMARK 470 VAL A 224 CG1 CG2
REMARK 470 VAL A 228 CG1 CG2
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 GLU A 232 CG CD OE1 OE2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 470 ARG A 278 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 ASN A 282 CG OD1 ND2
REMARK 470 LYS A 283 CG CD CE NZ
REMARK 470 TYR A 357 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 360 CG SD CE
REMARK 470 GLN A 364 CG CD OE1 NE2
REMARK 470 TYR A 372 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 9 OE1 OE2
REMARK 470 GLU B 20 CG CD OE1 OE2
REMARK 470 MET B 24 CG SD CE
REMARK 470 ASP B 35 CG OD1 OD2
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 GLU B 47 CG CD OE1 OE2
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 ALA B 74 CB
REMARK 470 GLU B 118 CG CD OE1 OE2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 ASP B 142 CG OD1 OD2
REMARK 470 LYS B 151 CG CD CE NZ
REMARK 470 ILE B 157 CG1 CG2 CD1
REMARK 470 ASP B 158 CG OD1 OD2
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 ASN B 190 CG OD1 ND2
REMARK 470 LYS B 202 CG CD CE NZ
REMARK 470 GLU B 232 CG CD OE1 OE2
REMARK 470 LYS B 243 CG CD CE NZ
REMARK 470 ARG B 278 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 282 CG OD1 ND2
REMARK 470 LYS B 283 CG CD CE NZ
REMARK 470 GLU B 356 CG CD OE1 OE2
REMARK 470 TYR B 357 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 372 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 42 CG CD OE1 OE2
REMARK 470 LYS C 43 CG CD CE NZ
REMARK 470 GLU C 53 CG CD OE1 OE2
REMARK 470 GLN C 60 CG CD OE1 NE2
REMARK 470 ALA C 74 CB
REMARK 470 ASP C 117 CG OD1 OD2
REMARK 470 GLU C 118 CG CD OE1 OE2
REMARK 470 GLU C 131 CG CD OE1 OE2
REMARK 470 LEU C 132 CG CD1 CD2
REMARK 470 LYS C 151 CG CD CE NZ
REMARK 470 ARG C 153 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 156 CG CD CE NZ
REMARK 470 ILE C 157 CG1 CG2 CD1
REMARK 470 ASP C 158 CG OD1 OD2
REMARK 470 ARG C 162 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 163 CG CD1 CD2
REMARK 470 SER C 164 OG
REMARK 470 SER C 166 OG
REMARK 470 LYS C 167 CG CD CE NZ
REMARK 470 MET C 168 CG SD CE
REMARK 470 TRP C 169 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 169 CZ3 CH2
REMARK 470 ILE C 170 CG1 CG2 CD1
REMARK 470 SER C 171 OG
REMARK 470 VAL C 181 CG1 CG2
REMARK 470 LYS C 184 CG CD CE NZ
REMARK 470 ASP C 189 CG OD1 OD2
REMARK 470 ASN C 190 CG OD1 ND2
REMARK 470 ILE C 192 CG1 CG2 CD1
REMARK 470 LYS C 199 CG CD CE NZ
REMARK 470 LYS C 202 CG CD CE NZ
REMARK 470 LEU C 204 CG CD1 CD2
REMARK 470 LYS C 208 CG CD CE NZ
REMARK 470 ILE C 209 CG1 CG2 CD1
REMARK 470 LEU C 215 CG CD1 CD2
REMARK 470 ARG C 216 CG CD NE CZ NH1 NH2
REMARK 470 SER C 218 OG
REMARK 470 VAL C 228 CG1 CG2
REMARK 470 GLU C 229 CG CD OE1 OE2
REMARK 470 GLU C 232 CG CD OE1 OE2
REMARK 470 ASP C 233 CG OD1 OD2
REMARK 470 ILE C 235 CG1 CG2 CD1
REMARK 470 LYS C 279 CG CD CE NZ
REMARK 470 ASN C 282 CG OD1 ND2
REMARK 470 MET C 360 CG SD CE
REMARK 470 GLU C 373 CG CD OE1 OE2
REMARK 470 ASP D 21 CG OD1 OD2
REMARK 470 MET D 24 CG SD CE
REMARK 470 GLU D 42 CG CD OE1 OE2
REMARK 470 GLU D 53 CG CD OE1 OE2
REMARK 470 ALA D 74 CB
REMARK 470 GLU D 118 CG CD OE1 OE2
REMARK 470 LYS D 121 NZ
REMARK 470 ASP D 142 CG OD1 OD2
REMARK 470 LYS D 151 CG CD CE NZ
REMARK 470 LYS D 212 CG CD CE NZ
REMARK 470 SER D 214 CB OG
REMARK 470 ASN D 282 CB CG OD1 ND2
REMARK 470 LYS D 283 CG CD CE NZ
REMARK 470 GLU D 356 CG CD OE1 OE2
REMARK 470 TYR D 357 CG CD1 CD2 CE1 CE2 CZ OH
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 OH TYR C 79 O1 EDO C 401 1.27
REMARK 500 OG SER C 105 O2 EDO C 401 1.27
REMARK 500 CZ TYR C 79 O1 EDO C 401 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 LEU A 138 -54.59 -127.68
REMARK 500 ASP A 158 107.07 -54.51
REMARK 500 ALA A 187 -2.44 86.89
REMARK 500 ASN A 190 17.39 58.56
REMARK 500 ASP A 226 78.42 -100.79
REMARK 500 ASN A 238 34.64 -95.35
REMARK 500 HIS A 348 45.69 -90.14
REMARK 500 LEU B 138 -53.64 -126.07
REMARK 500 ASP B 189 65.77 29.37
REMARK 500 ASN B 190 14.14 49.28
REMARK 500 ASP B 226 78.79 -100.76
REMARK 500 ASN B 238 34.48 -95.54
REMARK 500 LEU C 138 -55.90 -126.80
REMARK 500 ASP C 158 108.38 -53.71
REMARK 500 ASP C 189 71.14 -69.87
REMARK 500 ASN C 190 16.07 53.02
REMARK 500 LYS C 202 -75.45 -63.54
REMARK 500 ASN C 238 34.19 -95.63
REMARK 500 HIS C 348 48.62 -91.03
REMARK 500 GLU C 373 73.22 21.83
REMARK 500 VAL D 107 -54.00 -120.09
REMARK 500 LEU D 138 -55.51 -124.76
REMARK 500 ALA D 143 -121.54 -173.44
REMARK 500 ASP D 158 105.58 -50.40
REMARK 500 ALA D 187 -12.62 92.17
REMARK 500 ASN D 190 18.17 56.44
REMARK 500 ASP D 226 79.07 -101.81
REMARK 500 ASN D 238 32.56 -95.49
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 C 565 DISTANCE = 5.97 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 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-BRABA.00027.A RELATED DB: TARGETTRACK
DBREF 4W9U A 0 394 PDB 4W9U 4W9U 0 394
DBREF 4W9U B 0 394 PDB 4W9U 4W9U 0 394
DBREF 4W9U C 0 394 PDB 4W9U 4W9U 0 394
DBREF 4W9U D 0 394 PDB 4W9U 4W9U 0 394
SEQRES 1 A 395 SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE
SEQRES 2 A 395 LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE
SEQRES 3 A 395 ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU
SEQRES 4 A 395 PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP
SEQRES 5 A 395 PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU
SEQRES 6 A 395 GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA
SEQRES 7 A 395 SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU
SEQRES 8 A 395 ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN
SEQRES 9 A 395 SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER
SEQRES 10 A 395 ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER
SEQRES 11 A 395 GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP
SEQRES 12 A 395 ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU
SEQRES 13 A 395 LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET
SEQRES 14 A 395 TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL
SEQRES 15 A 395 TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY
SEQRES 16 A 395 PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO
SEQRES 17 A 395 LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR
SEQRES 18 A 395 GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP
SEQRES 19 A 395 ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE
SEQRES 20 A 395 GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY
SEQRES 21 A 395 VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG
SEQRES 22 A 395 GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU
SEQRES 23 A 395 ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET
SEQRES 24 A 395 GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG
SEQRES 25 A 395 VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU
SEQRES 26 A 395 MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA
SEQRES 27 A 395 LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY
SEQRES 28 A 395 ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA
SEQRES 29 A 395 GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS
SEQRES 30 A 395 ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY
SEQRES 31 A 395 ILE GLN ALA PHE PHE
SEQRES 1 B 395 SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE
SEQRES 2 B 395 LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE
SEQRES 3 B 395 ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU
SEQRES 4 B 395 PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP
SEQRES 5 B 395 PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU
SEQRES 6 B 395 GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA
SEQRES 7 B 395 SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU
SEQRES 8 B 395 ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN
SEQRES 9 B 395 SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER
SEQRES 10 B 395 ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER
SEQRES 11 B 395 GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP
SEQRES 12 B 395 ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU
SEQRES 13 B 395 LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET
SEQRES 14 B 395 TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL
SEQRES 15 B 395 TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY
SEQRES 16 B 395 PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO
SEQRES 17 B 395 LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR
SEQRES 18 B 395 GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP
SEQRES 19 B 395 ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE
SEQRES 20 B 395 GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY
SEQRES 21 B 395 VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG
SEQRES 22 B 395 GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU
SEQRES 23 B 395 ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET
SEQRES 24 B 395 GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG
SEQRES 25 B 395 VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU
SEQRES 26 B 395 MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA
SEQRES 27 B 395 LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY
SEQRES 28 B 395 ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA
SEQRES 29 B 395 GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS
SEQRES 30 B 395 ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY
SEQRES 31 B 395 ILE GLN ALA PHE PHE
SEQRES 1 C 395 SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE
SEQRES 2 C 395 LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE
SEQRES 3 C 395 ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU
SEQRES 4 C 395 PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP
SEQRES 5 C 395 PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU
SEQRES 6 C 395 GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA
SEQRES 7 C 395 SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU
SEQRES 8 C 395 ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN
SEQRES 9 C 395 SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER
SEQRES 10 C 395 ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER
SEQRES 11 C 395 GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP
SEQRES 12 C 395 ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU
SEQRES 13 C 395 LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET
SEQRES 14 C 395 TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL
SEQRES 15 C 395 TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY
SEQRES 16 C 395 PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO
SEQRES 17 C 395 LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR
SEQRES 18 C 395 GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP
SEQRES 19 C 395 ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE
SEQRES 20 C 395 GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY
SEQRES 21 C 395 VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG
SEQRES 22 C 395 GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU
SEQRES 23 C 395 ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET
SEQRES 24 C 395 GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG
SEQRES 25 C 395 VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU
SEQRES 26 C 395 MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA
SEQRES 27 C 395 LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY
SEQRES 28 C 395 ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA
SEQRES 29 C 395 GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS
SEQRES 30 C 395 ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY
SEQRES 31 C 395 ILE GLN ALA PHE PHE
SEQRES 1 D 395 SER MET SER ARG ALA ALA PHE ALA TRP GLU ASP PRO PHE
SEQRES 2 D 395 LEU LEU GLU GLU GLN LEU THR GLU ASP GLU ARG MET ILE
SEQRES 3 D 395 ARG ASP SER ALA LYS ALA PHE ALA SER ASP VAL LEU LEU
SEQRES 4 D 395 PRO ARG VAL GLU LYS ALA TYR LEU GLU GLU THR THR ASP
SEQRES 5 D 395 PRO GLU LEU PHE HIS LEU MET GLY GLN ALA GLY LEU LEU
SEQRES 6 D 395 GLY VAL THR LEU PRO GLU ASP TYR GLY ALA ALA ASN ALA
SEQRES 7 D 395 SER TYR VAL ALA TYR GLY LEU VAL ALA ARG GLU VAL GLU
SEQRES 8 D 395 ARG ILE ASP SER GLY TYR ARG SER MET MET SER VAL GLN
SEQRES 9 D 395 SER SER LEU VAL MET TYR PRO ILE TYR ALA TYR GLY SER
SEQRES 10 D 395 ASP GLU GLN ARG LYS LYS TYR LEU PRO GLY LEU VAL SER
SEQRES 11 D 395 GLY GLU LEU ILE GLY CYS PHE GLY LEU THR GLU PRO ASP
SEQRES 12 D 395 ALA GLY SER ASP PRO ALA GLY MET LYS THR ARG ALA GLU
SEQRES 13 D 395 LYS ILE ASP GLY GLY TYR ARG LEU SER GLY SER LYS MET
SEQRES 14 D 395 TRP ILE SER ASN SER PRO ILE ALA ASP VAL PHE VAL VAL
SEQRES 15 D 395 TRP ALA LYS SER ALA ALA HIS ASP ASN ALA ILE ARG GLY
SEQRES 16 D 395 PHE ILE LEU GLU LYS GLY MET LYS GLY LEU SER ALA PRO
SEQRES 17 D 395 LYS ILE GLY GLY LYS LEU SER LEU ARG ALA SER ILE THR
SEQRES 18 D 395 GLY GLU ILE VAL MET ASP GLY VAL GLU VAL SER GLU ASP
SEQRES 19 D 395 ALA ILE LEU PRO ASN VAL SER GLY LEU LYS GLY PRO PHE
SEQRES 20 D 395 GLY CYS LEU ASN ARG ALA ARG TYR GLY ILE SER TRP GLY
SEQRES 21 D 395 VAL LEU GLY ALA ALA GLU ASP CYS TRP PHE ARG ALA ARG
SEQRES 22 D 395 GLN TYR GLY LEU ASP ARG LYS GLN PHE ASN LYS PRO LEU
SEQRES 23 D 395 ALA GLY THR GLN LEU TYR GLN LYS LYS LEU ALA ASP MET
SEQRES 24 D 395 GLN THR GLU ILE ALA LEU GLY ILE GLN ALA SER LEU ARG
SEQRES 25 D 395 VAL GLY ARG LEU PHE ASP GLU GLY LYS MET ALA PRO GLU
SEQRES 26 D 395 MET ILE SER ILE VAL LYS ARG ASN ASN CYS GLY LYS ALA
SEQRES 27 D 395 LEU ASP ILE ALA ARG GLN ALA ARG ASP MET HIS GLY GLY
SEQRES 28 D 395 ASN GLY ILE GLN ILE GLU TYR HIS VAL MET ARG HIS ALA
SEQRES 29 D 395 GLN ASN LEU GLU THR VAL ASN THR TYR GLU GLY THR HIS
SEQRES 30 D 395 ASP VAL HIS ALA LEU ILE LEU GLY ARG ALA GLN THR GLY
SEQRES 31 D 395 ILE GLN ALA PHE PHE
HET EDO A 401 4
HET EDO A 402 4
HET EDO C 401 4
HET EDO D 401 4
HET EDO D 402 4
HET EDO D 403 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 11 HOH *330(H2 O)
HELIX 1 AA1 LEU A 13 LEU A 18 5 6
HELIX 2 AA2 THR A 19 VAL A 36 1 18
HELIX 3 AA3 VAL A 36 GLU A 42 1 7
HELIX 4 AA4 PRO A 52 ALA A 61 1 10
HELIX 5 AA5 PRO A 69 GLY A 73 5 5
HELIX 6 AA6 SER A 78 ARG A 91 1 14
HELIX 7 AA7 ASP A 93 LEU A 106 1 14
HELIX 8 AA8 VAL A 107 GLY A 115 1 9
HELIX 9 AA9 SER A 116 GLY A 130 1 15
HELIX 10 AB1 SER A 173 ALA A 176 5 4
HELIX 11 AB2 LEU A 242 ARG A 278 1 37
HELIX 12 AB3 THR A 288 GLU A 318 1 31
HELIX 13 AB4 ALA A 322 MET A 347 1 26
HELIX 14 AB5 HIS A 358 TYR A 372 1 15
HELIX 15 AB6 THR A 375 GLY A 389 1 15
HELIX 16 AB7 LEU B 13 GLN B 17 5 5
HELIX 17 AB8 THR B 19 VAL B 36 1 18
HELIX 18 AB9 VAL B 36 GLU B 42 1 7
HELIX 19 AC1 PRO B 52 GLY B 62 1 11
HELIX 20 AC2 PRO B 69 GLY B 73 5 5
HELIX 21 AC3 SER B 78 ARG B 91 1 14
HELIX 22 AC4 ASP B 93 LEU B 106 1 14
HELIX 23 AC5 VAL B 107 GLY B 115 1 9
HELIX 24 AC6 SER B 116 SER B 129 1 14
HELIX 25 AC7 SER B 173 ALA B 176 5 4
HELIX 26 AC8 ALA B 187 ASP B 189 5 3
HELIX 27 AC9 ASP B 233 ILE B 235 5 3
HELIX 28 AD1 LEU B 242 ARG B 278 1 37
HELIX 29 AD2 THR B 288 GLU B 318 1 31
HELIX 30 AD3 ALA B 322 HIS B 348 1 27
HELIX 31 AD4 TYR B 357 TYR B 372 1 16
HELIX 32 AD5 THR B 375 GLY B 389 1 15
HELIX 33 AD6 LEU C 13 LEU C 18 5 6
HELIX 34 AD7 THR C 19 VAL C 36 1 18
HELIX 35 AD8 VAL C 36 GLU C 42 1 7
HELIX 36 AD9 ASP C 51 ALA C 61 1 11
HELIX 37 AE1 PRO C 69 GLY C 73 5 5
HELIX 38 AE2 SER C 78 ARG C 91 1 14
HELIX 39 AE3 ASP C 93 LEU C 106 1 14
HELIX 40 AE4 VAL C 107 GLY C 115 1 9
HELIX 41 AE5 SER C 116 SER C 129 1 14
HELIX 42 AE6 SER C 173 ALA C 176 5 4
HELIX 43 AE7 LEU C 242 ARG C 278 1 37
HELIX 44 AE8 THR C 288 GLU C 318 1 31
HELIX 45 AE9 ALA C 322 HIS C 348 1 27
HELIX 46 AF1 VAL C 359 TYR C 372 1 14
HELIX 47 AF2 THR C 375 GLY C 389 1 15
HELIX 48 AF3 LEU D 13 LEU D 18 5 6
HELIX 49 AF4 THR D 19 VAL D 36 1 18
HELIX 50 AF5 VAL D 36 GLU D 42 1 7
HELIX 51 AF6 ASP D 51 ALA D 61 1 11
HELIX 52 AF7 PRO D 69 GLY D 73 5 5
HELIX 53 AF8 SER D 78 ARG D 91 1 14
HELIX 54 AF9 ASP D 93 LEU D 106 1 14
HELIX 55 AG1 VAL D 107 GLY D 115 1 9
HELIX 56 AG2 SER D 116 SER D 129 1 14
HELIX 57 AG3 SER D 173 ALA D 176 5 4
HELIX 58 AG4 ASP D 233 ILE D 235 5 3
HELIX 59 AG5 LEU D 242 ARG D 278 1 37
HELIX 60 AG6 THR D 288 GLU D 318 1 31
HELIX 61 AG7 ALA D 322 HIS D 348 1 27
HELIX 62 AG8 TYR D 357 TYR D 372 1 16
HELIX 63 AG9 THR D 375 GLY D 389 1 15
SHEET 1 AA1 6 GLY A 134 GLY A 137 0
SHEET 2 AA1 6 VAL A 178 SER A 185 1 O VAL A 180 N GLY A 137
SHEET 3 AA1 6 ARG A 153 ILE A 157 1 N ALA A 154 O LYS A 184
SHEET 4 AA1 6 GLY A 160 SER A 171 -1 O GLY A 160 N ILE A 157
SHEET 5 AA1 6 THR A 220 SER A 231 -1 O VAL A 230 N TYR A 161
SHEET 6 AA1 6 LEU A 204 SER A 205 -1 N SER A 205 O VAL A 224
SHEET 1 AA2 4 GLY A 134 GLY A 137 0
SHEET 2 AA2 4 VAL A 178 SER A 185 1 O VAL A 180 N GLY A 137
SHEET 3 AA2 4 ILE A 192 GLU A 198 -1 O LEU A 197 N PHE A 179
SHEET 4 AA2 4 ILE A 235 LEU A 236 -1 O LEU A 236 N GLY A 194
SHEET 1 AA3 2 LYS A 279 GLN A 280 0
SHEET 2 AA3 2 LYS A 283 PRO A 284 -1 O LYS A 283 N GLN A 280
SHEET 1 AA4 3 GLY B 134 GLY B 137 0
SHEET 2 AA4 3 VAL B 178 SER B 185 1 O VAL B 180 N GLY B 137
SHEET 3 AA4 3 ILE B 192 GLU B 198 -1 O LEU B 197 N PHE B 179
SHEET 1 AA5 6 GLY B 134 GLY B 137 0
SHEET 2 AA5 6 VAL B 178 SER B 185 1 O VAL B 180 N GLY B 137
SHEET 3 AA5 6 ARG B 153 ILE B 157 1 N ALA B 154 O LYS B 184
SHEET 4 AA5 6 GLY B 160 SER B 171 -1 O GLY B 160 N ILE B 157
SHEET 5 AA5 6 THR B 220 SER B 231 -1 O GLY B 221 N ILE B 170
SHEET 6 AA5 6 LEU B 204 SER B 205 -1 N SER B 205 O VAL B 224
SHEET 1 AA6 2 LYS B 279 GLN B 280 0
SHEET 2 AA6 2 LYS B 283 PRO B 284 -1 O LYS B 283 N GLN B 280
SHEET 1 AA7 3 GLY C 134 GLY C 137 0
SHEET 2 AA7 3 VAL C 178 SER C 185 1 O VAL C 180 N GLY C 137
SHEET 3 AA7 3 ILE C 192 GLU C 198 -1 O LEU C 197 N PHE C 179
SHEET 1 AA8 6 GLY C 134 GLY C 137 0
SHEET 2 AA8 6 VAL C 178 SER C 185 1 O VAL C 180 N GLY C 137
SHEET 3 AA8 6 ARG C 153 ILE C 157 1 N ALA C 154 O LYS C 184
SHEET 4 AA8 6 GLY C 160 SER C 171 -1 O GLY C 160 N ILE C 157
SHEET 5 AA8 6 THR C 220 SER C 231 -1 O VAL C 228 N LEU C 163
SHEET 6 AA8 6 LEU C 204 SER C 205 -1 N SER C 205 O VAL C 224
SHEET 1 AA9 2 LYS C 279 GLN C 280 0
SHEET 2 AA9 2 LYS C 283 PRO C 284 -1 O LYS C 283 N GLN C 280
SHEET 1 AB1 3 GLY D 134 GLY D 137 0
SHEET 2 AB1 3 VAL D 178 SER D 185 1 O VAL D 180 N GLY D 137
SHEET 3 AB1 3 ILE D 192 GLU D 198 -1 O LEU D 197 N PHE D 179
SHEET 1 AB2 6 GLY D 134 GLY D 137 0
SHEET 2 AB2 6 VAL D 178 SER D 185 1 O VAL D 180 N GLY D 137
SHEET 3 AB2 6 ARG D 153 ILE D 157 1 N ALA D 154 O LYS D 184
SHEET 4 AB2 6 GLY D 160 SER D 171 -1 O GLY D 160 N ILE D 157
SHEET 5 AB2 6 THR D 220 SER D 231 -1 O GLY D 221 N ILE D 170
SHEET 6 AB2 6 LEU D 204 SER D 205 -1 N SER D 205 O VAL D 224
SHEET 1 AB3 2 LYS D 279 GLN D 280 0
SHEET 2 AB3 2 LYS D 283 PRO D 284 -1 O LYS D 283 N GLN D 280
CISPEP 1 HIS A 188 ASP A 189 0 -19.45
CISPEP 2 GLU C 373 GLY C 374 0 -15.10
SITE 1 AC1 2 GLN A 387 ARG B 272
SITE 1 AC2 1 HOH A 545
SITE 1 AC3 7 THR C 67 TYR C 79 TYR C 82 SER C 104
SITE 2 AC3 7 SER C 105 TYR C 109 ARG C 251
SITE 1 AC4 2 ASP D 27 SER D 28
SITE 1 AC5 3 ASP D 266 PHE D 269 ARG D 270
SITE 1 AC6 2 ARG C 272 HOH D 559
CRYST1 82.020 106.660 99.390 90.00 108.12 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012192 0.000000 0.003990 0.00000
SCALE2 0.000000 0.009376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010586 0.00000
(ATOM LINES ARE NOT SHOWN.)
END