HEADER OXIDOREDUCTASE 30-MAR-16 5J32
TITLE ISOPROPYLMALATE DEHYDROGENASE IN COMPLEX WITH ISOPROPYLMALATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE 2, CHLOROPLASTIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: IMDH 2,BETA-IPM DEHYDROGENASE 2;
COMPND 5 EC: 1.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: IMDH2, IMDH, AT1G80560, T21F11.11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHYDROGENASE, LEUCINE BIOSYNTHESIS, GLUCOSINOLATE BIOSYNTHESIS,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.JEZ,S.G.LEE
REVDAT 6 27-SEP-23 5J32 1 REMARK LINK
REVDAT 5 27-NOV-19 5J32 1 REMARK
REVDAT 4 27-SEP-17 5J32 1 JRNL REMARK
REVDAT 3 06-JUL-16 5J32 1 JRNL
REVDAT 2 18-MAY-16 5J32 1 JRNL
REVDAT 1 11-MAY-16 5J32 0
JRNL AUTH S.G.LEE,R.NWUMEH,J.M.JEZ
JRNL TITL STRUCTURE AND MECHANISM OF ISOPROPYLMALATE DEHYDROGENASE
JRNL TITL 2 FROM ARABIDOPSIS THALIANA: INSIGHTS ON LEUCINE AND ALIPHATIC
JRNL TITL 3 GLUCOSINOLATE BIOSYNTHESIS.
JRNL REF J.BIOL.CHEM. V. 291 13421 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27137927
JRNL DOI 10.1074/JBC.M116.730358
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 104735
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5246
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 32.4792 - 5.9935 0.93 3408 163 0.1881 0.2122
REMARK 3 2 5.9935 - 4.7621 0.95 3373 176 0.1756 0.1715
REMARK 3 3 4.7621 - 4.1615 0.96 3317 191 0.1399 0.1579
REMARK 3 4 4.1615 - 3.7816 0.96 3369 175 0.1376 0.1839
REMARK 3 5 3.7816 - 3.5109 0.97 3374 184 0.1420 0.1608
REMARK 3 6 3.5109 - 3.3041 0.98 3385 174 0.1388 0.1942
REMARK 3 7 3.3041 - 3.1388 0.98 3421 163 0.1397 0.1640
REMARK 3 8 3.1388 - 3.0023 0.97 3339 195 0.1477 0.1974
REMARK 3 9 3.0023 - 2.8868 0.98 3393 164 0.1593 0.1890
REMARK 3 10 2.8868 - 2.7872 0.99 3429 166 0.1543 0.2065
REMARK 3 11 2.7872 - 2.7001 0.97 3347 189 0.1566 0.1872
REMARK 3 12 2.7001 - 2.6230 1.00 3422 160 0.1600 0.2020
REMARK 3 13 2.6230 - 2.5539 0.96 3367 170 0.1612 0.2159
REMARK 3 14 2.5539 - 2.4917 1.00 3387 179 0.1582 0.2262
REMARK 3 15 2.4917 - 2.4350 0.96 3335 176 0.1539 0.1973
REMARK 3 16 2.4350 - 2.3832 0.99 3408 166 0.1556 0.2067
REMARK 3 17 2.3832 - 2.3356 0.96 3296 162 0.1597 0.2060
REMARK 3 18 2.3356 - 2.2915 0.97 3317 200 0.1543 0.2022
REMARK 3 19 2.2915 - 2.2506 0.98 3325 183 0.1617 0.2090
REMARK 3 20 2.2506 - 2.2124 0.94 3319 157 0.1647 0.1992
REMARK 3 21 2.2124 - 2.1768 0.98 3348 181 0.1600 0.2184
REMARK 3 22 2.1768 - 2.1433 0.97 3314 173 0.1637 0.2197
REMARK 3 23 2.1433 - 2.1118 0.94 3249 163 0.1709 0.2104
REMARK 3 24 2.1118 - 2.0820 0.97 3270 175 0.1698 0.2301
REMARK 3 25 2.0820 - 2.0539 0.96 3266 203 0.1765 0.2282
REMARK 3 26 2.0539 - 2.0272 0.93 3208 174 0.1774 0.2294
REMARK 3 27 2.0272 - 2.0019 0.95 3183 161 0.1885 0.2633
REMARK 3 28 2.0019 - 1.9778 0.95 3324 179 0.1923 0.2319
REMARK 3 29 1.9778 - 1.9548 0.93 3206 167 0.1925 0.2526
REMARK 3 30 1.9548 - 1.9328 0.83 2790 177 0.2045 0.2697
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.510
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 : 0.007 11222
REMARK 3 ANGLE : 1.021 15189
REMARK 3 CHIRALITY : 0.066 1746
REMARK 3 PLANARITY : 0.005 1998
REMARK 3 DIHEDRAL : 13.326 4201
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 31:142
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8399 9.5734 35.9181
REMARK 3 T TENSOR
REMARK 3 T11: 0.1356 T22: 0.1349
REMARK 3 T33: 0.0967 T12: -0.0223
REMARK 3 T13: 0.0315 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.3596 L22: 0.8829
REMARK 3 L33: 1.7092 L12: 0.0705
REMARK 3 L13: 0.0443 L23: -0.1380
REMARK 3 S TENSOR
REMARK 3 S11: 0.0466 S12: -0.2056 S13: 0.1715
REMARK 3 S21: 0.1025 S22: 0.0434 S23: 0.0917
REMARK 3 S31: -0.1754 S32: -0.0075 S33: -0.0869
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 143:316
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3769 -3.6797 16.5068
REMARK 3 T TENSOR
REMARK 3 T11: 0.0818 T22: 0.0810
REMARK 3 T33: 0.0845 T12: -0.0052
REMARK 3 T13: 0.0184 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.9847 L22: 0.6558
REMARK 3 L33: 0.7887 L12: 0.2399
REMARK 3 L13: 0.0057 L23: -0.0960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: -0.0858 S13: -0.0715
REMARK 3 S21: 0.0380 S22: -0.0336 S23: -0.0232
REMARK 3 S31: 0.0753 S32: 0.0022 S33: 0.0176
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 317:337
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4924 8.2654 25.4838
REMARK 3 T TENSOR
REMARK 3 T11: 0.1282 T22: 0.1105
REMARK 3 T33: 0.1729 T12: -0.0156
REMARK 3 T13: 0.0283 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 1.1790 L22: 2.6256
REMARK 3 L33: 2.3037 L12: 1.2918
REMARK 3 L13: 0.3059 L23: -0.1920
REMARK 3 S TENSOR
REMARK 3 S11: -0.1341 S12: 0.2377 S13: 0.4104
REMARK 3 S21: -0.1015 S22: 0.0165 S23: 0.5299
REMARK 3 S31: -0.2509 S32: -0.1426 S33: 0.0019
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 338:367
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0691 -6.7963 34.8097
REMARK 3 T TENSOR
REMARK 3 T11: 0.1667 T22: 0.1487
REMARK 3 T33: 0.1537 T12: -0.0331
REMARK 3 T13: 0.0698 T23: 0.0509
REMARK 3 L TENSOR
REMARK 3 L11: 2.1857 L22: 0.7393
REMARK 3 L33: 1.2582 L12: 1.0605
REMARK 3 L13: 0.6865 L23: 0.2788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0988 S12: -0.2021 S13: -0.4372
REMARK 3 S21: 0.1559 S22: -0.0444 S23: -0.0308
REMARK 3 S31: 0.1602 S32: 0.0711 S33: -0.0056
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 368:399
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7243 -1.4921 29.2475
REMARK 3 T TENSOR
REMARK 3 T11: 0.1035 T22: 0.2241
REMARK 3 T33: 0.1734 T12: -0.0153
REMARK 3 T13: 0.0586 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.4459 L22: 1.9207
REMARK 3 L33: 3.2336 L12: -0.1287
REMARK 3 L13: -0.0504 L23: -0.1349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0335 S12: -0.2630 S13: 0.0200
REMARK 3 S21: 0.1709 S22: -0.1501 S23: 0.3004
REMARK 3 S31: -0.0776 S32: -0.3507 S33: 0.0480
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESID 36:142
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9227 -3.9421 -16.8130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0938 T22: 0.1134
REMARK 3 T33: 0.0865 T12: 0.0054
REMARK 3 T13: 0.0738 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.6718 L22: 1.5462
REMARK 3 L33: 0.8470 L12: 0.1019
REMARK 3 L13: 0.3412 L23: 0.2733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: 0.1137 S13: -0.1077
REMARK 3 S21: -0.0879 S22: 0.0446 S23: -0.1190
REMARK 3 S31: 0.0435 S32: 0.1588 S33: -0.0276
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND RESID 143:316
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0279 7.8485 0.4631
REMARK 3 T TENSOR
REMARK 3 T11: 0.0665 T22: 0.0639
REMARK 3 T33: 0.0795 T12: -0.0056
REMARK 3 T13: 0.0238 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.6414 L22: 0.6699
REMARK 3 L33: 0.8544 L12: 0.0375
REMARK 3 L13: 0.0349 L23: -0.1294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: -0.0013 S13: 0.0516
REMARK 3 S21: -0.0054 S22: -0.0089 S23: 0.0302
REMARK 3 S31: -0.0646 S32: -0.0059 S33: 0.0052
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND RESID 317:337
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7143 -13.0217 -10.8299
REMARK 3 T TENSOR
REMARK 3 T11: 0.0961 T22: 0.0952
REMARK 3 T33: 0.1356 T12: -0.0097
REMARK 3 T13: 0.0058 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 1.5574 L22: 2.6755
REMARK 3 L33: 2.2496 L12: -0.2374
REMARK 3 L13: 0.1630 L23: -0.6066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.1075 S13: -0.3305
REMARK 3 S21: 0.1551 S22: 0.0154 S23: -0.0862
REMARK 3 S31: 0.1853 S32: 0.0659 S33: -0.0225
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND RESID 338:367
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4281 -0.1801 -21.5297
REMARK 3 T TENSOR
REMARK 3 T11: 0.0960 T22: 0.1053
REMARK 3 T33: 0.1262 T12: 0.0198
REMARK 3 T13: -0.0016 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 2.2621 L22: 2.0322
REMARK 3 L33: 1.1647 L12: 1.7019
REMARK 3 L13: 0.1952 L23: -0.3106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.1612 S13: 0.3431
REMARK 3 S21: -0.1587 S22: 0.1059 S23: 0.4740
REMARK 3 S31: -0.0968 S32: -0.0945 S33: -0.0973
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND RESID 368:400
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6495 -15.4787 -19.2714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1080 T22: 0.0932
REMARK 3 T33: 0.1221 T12: -0.0221
REMARK 3 T13: -0.0309 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.4235 L22: 3.2403
REMARK 3 L33: 3.3686 L12: 0.2568
REMARK 3 L13: -0.1807 L23: -1.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: 0.2371 S13: -0.2497
REMARK 3 S21: -0.2804 S22: 0.1052 S23: 0.0685
REMARK 3 S31: 0.2464 S32: -0.1840 S33: -0.1167
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND RESID 41:142
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1615 6.8926 63.9835
REMARK 3 T TENSOR
REMARK 3 T11: 0.1514 T22: 0.1595
REMARK 3 T33: 0.0871 T12: 0.0077
REMARK 3 T13: 0.0541 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.7177 L22: 1.7612
REMARK 3 L33: 0.9804 L12: -0.6183
REMARK 3 L13: 0.3716 L23: 0.4261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0596 S12: 0.2203 S13: -0.0772
REMARK 3 S21: -0.1914 S22: -0.0390 S23: 0.0158
REMARK 3 S31: 0.0457 S32: 0.1075 S33: 0.0041
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND RESID 143:316
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2934 21.8088 82.9807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1481 T22: 0.0982
REMARK 3 T33: 0.0991 T12: -0.0261
REMARK 3 T13: 0.0192 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.1352 L22: 0.9223
REMARK 3 L33: 0.9061 L12: -0.1347
REMARK 3 L13: 0.0293 L23: -0.1318
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: 0.0877 S13: 0.1127
REMARK 3 S21: -0.0030 S22: -0.0473 S23: -0.0714
REMARK 3 S31: -0.1778 S32: 0.0958 S33: 0.0343
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND RESID 317:337
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8130 10.2236 65.5609
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.1235
REMARK 3 T33: 0.1320 T12: 0.0469
REMARK 3 T13: -0.0041 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 3.1489 L22: 3.8482
REMARK 3 L33: 2.9519 L12: 0.6147
REMARK 3 L13: -0.2710 L23: -0.4885
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: -0.0830 S13: -0.2428
REMARK 3 S21: -0.2695 S22: -0.1696 S23: 0.3549
REMARK 3 S31: -0.0252 S32: -0.1505 S33: 0.1409
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN C AND RESID 338:367
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2082 25.1095 60.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.2762 T22: 0.1617
REMARK 3 T33: 0.1999 T12: 0.0060
REMARK 3 T13: 0.0444 T23: 0.0727
REMARK 3 L TENSOR
REMARK 3 L11: 2.6689 L22: 0.0958
REMARK 3 L33: 1.1890 L12: 0.4931
REMARK 3 L13: 0.1854 L23: 0.0356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0951 S12: 0.0549 S13: 0.5769
REMARK 3 S21: -0.2928 S22: -0.1768 S23: -0.1564
REMARK 3 S31: -0.3356 S32: 0.0857 S33: 0.0247
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN C AND RESID 368:396
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5061 19.7789 58.1289
REMARK 3 T TENSOR
REMARK 3 T11: 0.2326 T22: 0.2826
REMARK 3 T33: 0.2007 T12: 0.0599
REMARK 3 T13: -0.1115 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.2706 L22: 2.6403
REMARK 3 L33: 2.7156 L12: 0.3984
REMARK 3 L13: -0.3887 L23: -0.7348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0906 S12: 0.4188 S13: 0.0437
REMARK 3 S21: -0.3908 S22: -0.1436 S23: 0.4057
REMARK 3 S31: -0.0381 S32: -0.2565 S33: 0.0625
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN D AND RESID 38:142
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0576 22.1909 116.3212
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1197
REMARK 3 T33: 0.0860 T12: -0.0040
REMARK 3 T13: 0.0123 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 1.1540 L22: 1.4509
REMARK 3 L33: 1.6568 L12: -0.4022
REMARK 3 L13: 0.4560 L23: 0.0539
REMARK 3 S TENSOR
REMARK 3 S11: -0.0875 S12: 0.0621 S13: 0.1261
REMARK 3 S21: 0.1473 S22: 0.0785 S23: -0.0942
REMARK 3 S31: -0.0431 S32: 0.1014 S33: -0.0151
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN D AND RESID 143:316
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7121 10.2715 95.1167
REMARK 3 T TENSOR
REMARK 3 T11: 0.1298 T22: 0.0794
REMARK 3 T33: 0.0797 T12: -0.0016
REMARK 3 T13: 0.0179 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.8867 L22: 0.4797
REMARK 3 L33: 0.7828 L12: 0.0367
REMARK 3 L13: -0.0598 L23: 0.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0431 S12: -0.0657 S13: -0.0612
REMARK 3 S21: -0.0216 S22: 0.0188 S23: 0.0274
REMARK 3 S31: 0.0083 S32: -0.0604 S33: 0.0242
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN D AND RESID 317:337
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1448 31.2629 106.4195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1759 T22: 0.1303
REMARK 3 T33: 0.1407 T12: -0.0190
REMARK 3 T13: 0.0080 T23: 0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 2.3188 L22: 0.8367
REMARK 3 L33: 1.2262 L12: 0.0086
REMARK 3 L13: 0.2970 L23: 0.1460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1496 S12: -0.0111 S13: 0.3838
REMARK 3 S21: -0.1339 S22: -0.0206 S23: -0.2355
REMARK 3 S31: -0.1514 S32: 0.1028 S33: 0.1105
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN D AND RESID 338:367
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9144 18.2510 111.5848
REMARK 3 T TENSOR
REMARK 3 T11: 0.1356 T22: 0.1711
REMARK 3 T33: 0.1867 T12: -0.0272
REMARK 3 T13: -0.0123 T23: 0.0642
REMARK 3 L TENSOR
REMARK 3 L11: 1.2241 L22: 1.7031
REMARK 3 L33: 1.6556 L12: -0.9785
REMARK 3 L13: 0.1341 L23: -1.3385
REMARK 3 S TENSOR
REMARK 3 S11: 0.1937 S12: -0.2049 S13: -0.3783
REMARK 3 S21: -0.2211 S22: 0.0882 S23: 0.4601
REMARK 3 S31: 0.3079 S32: -0.3139 S33: -0.2516
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN D AND RESID 368:397
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0970 34.3630 106.1833
REMARK 3 T TENSOR
REMARK 3 T11: 0.1580 T22: 0.1488
REMARK 3 T33: 0.1815 T12: 0.0330
REMARK 3 T13: 0.0482 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 2.6004 L22: 2.7593
REMARK 3 L33: 3.7530 L12: 0.1658
REMARK 3 L13: 0.3145 L23: -1.0187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0419 S12: -0.1398 S13: 0.2662
REMARK 3 S21: 0.3026 S22: 0.0823 S23: 0.1993
REMARK 3 S31: -0.2411 S32: -0.3803 S33: -0.0275
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 5J32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104824
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 32.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.150
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.62400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3R8W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM PHOSPHATE, 0.1 M
REMARK 280 IMIDAZOLE, PH 8.0, AND 5 MM ISOPROPYLMALATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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 24.81100
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 SER A 13
REMARK 465 SER A 14
REMARK 465 GLY A 15
REMARK 465 LEU A 16
REMARK 465 VAL A 17
REMARK 465 PRO A 18
REMARK 465 ARG A 19
REMARK 465 GLY A 20
REMARK 465 SER A 21
REMARK 465 HIS A 22
REMARK 465 MET A 23
REMARK 465 ALA A 24
REMARK 465 SER A 25
REMARK 465 MET A 26
REMARK 465 THR A 27
REMARK 465 GLY A 28
REMARK 465 GLY A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 400
REMARK 465 VAL A 401
REMARK 465 PRO A 402
REMARK 465 ALA A 403
REMARK 465 SER A 404
REMARK 465 VAL A 405
REMARK 465 MET B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 SER B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 LEU B 16
REMARK 465 VAL B 17
REMARK 465 PRO B 18
REMARK 465 ARG B 19
REMARK 465 GLY B 20
REMARK 465 SER B 21
REMARK 465 HIS B 22
REMARK 465 MET B 23
REMARK 465 ALA B 24
REMARK 465 SER B 25
REMARK 465 MET B 26
REMARK 465 THR B 27
REMARK 465 GLY B 28
REMARK 465 GLY B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 MET B 32
REMARK 465 GLY B 33
REMARK 465 ARG B 34
REMARK 465 GLY B 35
REMARK 465 VAL B 401
REMARK 465 PRO B 402
REMARK 465 ALA B 403
REMARK 465 SER B 404
REMARK 465 VAL B 405
REMARK 465 MET C 3
REMARK 465 GLY C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 SER C 13
REMARK 465 SER C 14
REMARK 465 GLY C 15
REMARK 465 LEU C 16
REMARK 465 VAL C 17
REMARK 465 PRO C 18
REMARK 465 ARG C 19
REMARK 465 GLY C 20
REMARK 465 SER C 21
REMARK 465 HIS C 22
REMARK 465 MET C 23
REMARK 465 ALA C 24
REMARK 465 SER C 25
REMARK 465 MET C 26
REMARK 465 THR C 27
REMARK 465 GLY C 28
REMARK 465 GLY C 29
REMARK 465 GLN C 30
REMARK 465 GLN C 31
REMARK 465 MET C 32
REMARK 465 GLY C 33
REMARK 465 ARG C 34
REMARK 465 GLY C 35
REMARK 465 SER C 36
REMARK 465 GLU C 37
REMARK 465 PHE C 38
REMARK 465 GLY C 39
REMARK 465 LYS C 40
REMARK 465 VAL C 397
REMARK 465 ASP C 398
REMARK 465 SER C 399
REMARK 465 GLN C 400
REMARK 465 VAL C 401
REMARK 465 PRO C 402
REMARK 465 ALA C 403
REMARK 465 SER C 404
REMARK 465 VAL C 405
REMARK 465 MET D 3
REMARK 465 GLY D 4
REMARK 465 SER D 5
REMARK 465 SER D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 HIS D 12
REMARK 465 SER D 13
REMARK 465 SER D 14
REMARK 465 GLY D 15
REMARK 465 LEU D 16
REMARK 465 VAL D 17
REMARK 465 PRO D 18
REMARK 465 ARG D 19
REMARK 465 GLY D 20
REMARK 465 SER D 21
REMARK 465 HIS D 22
REMARK 465 MET D 23
REMARK 465 ALA D 24
REMARK 465 SER D 25
REMARK 465 MET D 26
REMARK 465 THR D 27
REMARK 465 GLY D 28
REMARK 465 GLY D 29
REMARK 465 GLN D 30
REMARK 465 GLN D 31
REMARK 465 MET D 32
REMARK 465 GLY D 33
REMARK 465 ARG D 34
REMARK 465 GLY D 35
REMARK 465 SER D 36
REMARK 465 GLU D 37
REMARK 465 ASP D 398
REMARK 465 SER D 399
REMARK 465 GLN D 400
REMARK 465 VAL D 401
REMARK 465 PRO D 402
REMARK 465 ALA D 403
REMARK 465 SER D 404
REMARK 465 VAL D 405
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 129 CG
REMARK 480 GLU C 129 CG
REMARK 480 GLU C 318 CD
REMARK 480 GLU D 129 CD
REMARK 480 GLU D 318 CD
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 B 843 O HOH B 955 1.79
REMARK 500 O HOH C 731 O HOH C 795 1.82
REMARK 500 O HOH D 835 O HOH D 904 1.84
REMARK 500 OE2 GLU D 252 O HOH D 601 1.86
REMARK 500 O HOH C 850 O HOH C 880 1.86
REMARK 500 O HOH B 688 O HOH B 901 1.87
REMARK 500 OE1 GLU D 56 O HOH D 602 1.88
REMARK 500 O HOH B 970 O HOH B 977 1.91
REMARK 500 O HOH A 934 O HOH A 950 1.92
REMARK 500 O HOH B 677 O HOH B 864 1.93
REMARK 500 O HOH A 867 O HOH A 881 1.93
REMARK 500 OE1 GLN A 67 O HOH A 601 1.93
REMARK 500 O HOH D 917 O HOH D 935 1.94
REMARK 500 O HOH C 869 O HOH C 914 1.94
REMARK 500 O HOH C 723 O HOH C 871 1.95
REMARK 500 O HOH B 801 O HOH B 977 1.95
REMARK 500 O HOH D 795 O HOH D 855 1.96
REMARK 500 O HOH D 869 O HOH D 877 1.96
REMARK 500 O HOH A 939 O HOH B 853 1.97
REMARK 500 O HOH C 715 O HOH C 877 1.99
REMARK 500 O HOH D 646 O HOH D 850 2.00
REMARK 500 O HOH A 742 O HOH A 857 2.00
REMARK 500 O HOH B 622 O HOH B 953 2.01
REMARK 500 O HOH A 671 O HOH A 814 2.01
REMARK 500 O HOH D 629 O HOH D 853 2.02
REMARK 500 O HOH C 783 O HOH C 907 2.02
REMARK 500 O HOH D 885 O HOH D 915 2.04
REMARK 500 O HOH A 605 O HOH A 817 2.05
REMARK 500 OE2 GLU D 98 O HOH D 603 2.05
REMARK 500 O HOH B 834 O HOH B 868 2.05
REMARK 500 O HOH D 621 O HOH D 857 2.05
REMARK 500 O HOH B 830 O HOH B 939 2.05
REMARK 500 O HOH A 958 O HOH A 965 2.06
REMARK 500 O HOH D 748 O HOH D 863 2.06
REMARK 500 O HOH A 881 O HOH A 945 2.07
REMARK 500 O HOH B 890 O HOH B 918 2.07
REMARK 500 NH1 ARG D 214 OE1 GLU D 252 2.07
REMARK 500 O HOH C 794 O HOH C 885 2.08
REMARK 500 O HOH B 771 O HOH B 861 2.09
REMARK 500 O HOH B 616 O HOH B 950 2.09
REMARK 500 SD MET C 261 O HOH C 858 2.09
REMARK 500 NZ LYS B 189 O HOH B 601 2.10
REMARK 500 OE2 GLU B 252 O HOH B 602 2.10
REMARK 500 OE2 GLU D 56 O HOH D 604 2.10
REMARK 500 O HOH D 620 O HOH D 820 2.11
REMARK 500 O HOH A 735 O HOH A 940 2.11
REMARK 500 O HOH C 667 O HOH C 888 2.11
REMARK 500 N SER B 36 O HOH B 603 2.12
REMARK 500 O HOH D 750 O HOH D 844 2.13
REMARK 500 NZ LYS D 124 O HOH D 605 2.13
REMARK 500
REMARK 500 THIS ENTRY HAS 79 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 870 O HOH B 901 2555 1.94
REMARK 500 O HOH B 770 O HOH D 821 1554 1.94
REMARK 500 O HOH A 797 O HOH A 852 1565 1.99
REMARK 500 O HOH B 908 O HOH B 935 1565 2.00
REMARK 500 O HOH B 874 O HOH D 795 1554 2.05
REMARK 500 O HOH A 671 O HOH D 603 2646 2.11
REMARK 500 O HOH B 905 O HOH D 821 1554 2.13
REMARK 500 O HOH A 804 O HOH B 980 2555 2.17
REMARK 500 O HOH A 851 O HOH B 982 1545 2.18
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 ASP A 169 91.53 -160.72
REMARK 500 ARG A 223 -107.63 -116.14
REMARK 500 VAL A 235 -42.51 -132.68
REMARK 500 ASP A 273 69.12 -153.20
REMARK 500 ASP A 278 -77.40 -104.70
REMARK 500 SER A 312 -18.64 73.82
REMARK 500 ALA A 324 59.43 35.17
REMARK 500 ASP B 169 90.33 -160.35
REMARK 500 ARG B 223 -109.12 -104.90
REMARK 500 VAL B 235 -43.78 -134.25
REMARK 500 ASP B 273 69.02 -158.99
REMARK 500 ASP B 278 -74.08 -104.00
REMARK 500 ARG C 223 -106.42 -117.90
REMARK 500 VAL C 235 -41.39 -133.23
REMARK 500 ASP C 273 69.64 -152.58
REMARK 500 ASP C 278 -76.25 -109.38
REMARK 500 ALA C 324 65.98 32.54
REMARK 500 ASP D 169 94.76 -160.03
REMARK 500 ARG D 223 -104.42 -111.66
REMARK 500 VAL D 235 -43.67 -132.07
REMARK 500 ASP D 273 72.37 -158.01
REMARK 500 ASP D 278 -76.24 -102.68
REMARK 500 ASN D 283 -169.47 -77.34
REMARK 500 ALA D 324 58.25 38.22
REMARK 500 GLU D 352 71.96 -103.78
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 A 966 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 967 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 968 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 15.36 ANGSTROMS
REMARK 525 HOH C 926 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 927 DISTANCE = 6.05 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 264 OD2
REMARK 620 2 IPM A 504 O2 148.3
REMARK 620 3 IPM A 504 O1 88.2 63.3
REMARK 620 4 ASP B 288 OD1 84.6 81.1 88.1
REMARK 620 5 ASP B 292 OD2 84.3 127.3 157.7 112.0
REMARK 620 6 HOH B 654 O 135.3 68.8 131.7 78.5 64.9
REMARK 620 7 HOH B 655 O 92.6 101.8 92.7 177.1 66.7 102.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 288 OD1
REMARK 620 2 ASP A 292 OD2 108.3
REMARK 620 3 IPM A 502 O1 93.7 150.0
REMARK 620 4 IPM A 502 O3 82.7 133.6 67.8
REMARK 620 5 HOH A 623 O 69.7 71.7 136.8 70.6
REMARK 620 6 HOH A 657 O 177.3 71.5 85.5 99.3 112.6
REMARK 620 7 ASP B 264 OD2 83.2 82.2 80.4 144.1 133.1 94.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 264 OD2
REMARK 620 2 IPM C 504 O1 80.1
REMARK 620 3 IPM C 504 O3 142.0 65.4
REMARK 620 4 HOH C 625 O 138.5 135.9 70.9
REMARK 620 5 ASP D 288 OD1 86.0 92.0 80.1 74.9
REMARK 620 6 ASP D 292 OD2 81.6 148.4 136.4 72.6 112.2
REMARK 620 7 HOH D 799 O 85.8 80.8 103.0 115.1 170.0 72.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 288 OD1
REMARK 620 2 ASP C 292 OD2 113.5
REMARK 620 3 IPM C 502 O1 89.0 149.2
REMARK 620 4 IPM C 502 O2 84.0 130.1 70.3
REMARK 620 5 HOH C 622 O 67.6 77.4 132.5 66.6
REMARK 620 6 HOH C 803 O 171.6 72.6 83.3 96.5 120.3
REMARK 620 7 ASP D 264 OD2 82.6 84.7 77.3 145.1 134.8 92.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPM A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPM A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPM C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPM C 504
DBREF 5J32 A 39 405 UNP P93832 LEU32_ARATH 39 405
DBREF 5J32 B 39 405 UNP P93832 LEU32_ARATH 39 405
DBREF 5J32 C 39 405 UNP P93832 LEU32_ARATH 39 405
DBREF 5J32 D 39 405 UNP P93832 LEU32_ARATH 39 405
SEQADV 5J32 MET A 3 UNP P93832 INITIATING METHIONINE
SEQADV 5J32 GLY A 4 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 5 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 6 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 7 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 8 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 9 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 10 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 11 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 12 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 13 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 14 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 15 UNP P93832 EXPRESSION TAG
SEQADV 5J32 LEU A 16 UNP P93832 EXPRESSION TAG
SEQADV 5J32 VAL A 17 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PRO A 18 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG A 19 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 20 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 21 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS A 22 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET A 23 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ALA A 24 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 25 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET A 26 UNP P93832 EXPRESSION TAG
SEQADV 5J32 THR A 27 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 28 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 29 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN A 30 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN A 31 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET A 32 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 33 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG A 34 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY A 35 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER A 36 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLU A 37 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PHE A 38 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET B 3 UNP P93832 INITIATING METHIONINE
SEQADV 5J32 GLY B 4 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 5 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 6 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 7 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 8 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 9 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 10 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 11 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 12 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 13 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 14 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 15 UNP P93832 EXPRESSION TAG
SEQADV 5J32 LEU B 16 UNP P93832 EXPRESSION TAG
SEQADV 5J32 VAL B 17 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PRO B 18 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG B 19 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 20 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 21 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS B 22 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET B 23 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ALA B 24 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 25 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET B 26 UNP P93832 EXPRESSION TAG
SEQADV 5J32 THR B 27 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 28 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 29 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN B 30 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN B 31 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET B 32 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 33 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG B 34 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY B 35 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER B 36 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLU B 37 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PHE B 38 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET C 3 UNP P93832 INITIATING METHIONINE
SEQADV 5J32 GLY C 4 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 5 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 6 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 7 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 8 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 9 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 10 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 11 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 12 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 13 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 14 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 15 UNP P93832 EXPRESSION TAG
SEQADV 5J32 LEU C 16 UNP P93832 EXPRESSION TAG
SEQADV 5J32 VAL C 17 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PRO C 18 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG C 19 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 20 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 21 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS C 22 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET C 23 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ALA C 24 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 25 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET C 26 UNP P93832 EXPRESSION TAG
SEQADV 5J32 THR C 27 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 28 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 29 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN C 30 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN C 31 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET C 32 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 33 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG C 34 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY C 35 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER C 36 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLU C 37 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PHE C 38 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET D 3 UNP P93832 INITIATING METHIONINE
SEQADV 5J32 GLY D 4 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 5 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 6 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 7 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 8 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 9 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 10 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 11 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 12 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 13 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 14 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 15 UNP P93832 EXPRESSION TAG
SEQADV 5J32 LEU D 16 UNP P93832 EXPRESSION TAG
SEQADV 5J32 VAL D 17 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PRO D 18 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG D 19 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 20 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 21 UNP P93832 EXPRESSION TAG
SEQADV 5J32 HIS D 22 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET D 23 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ALA D 24 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 25 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET D 26 UNP P93832 EXPRESSION TAG
SEQADV 5J32 THR D 27 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 28 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 29 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN D 30 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLN D 31 UNP P93832 EXPRESSION TAG
SEQADV 5J32 MET D 32 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 33 UNP P93832 EXPRESSION TAG
SEQADV 5J32 ARG D 34 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLY D 35 UNP P93832 EXPRESSION TAG
SEQADV 5J32 SER D 36 UNP P93832 EXPRESSION TAG
SEQADV 5J32 GLU D 37 UNP P93832 EXPRESSION TAG
SEQADV 5J32 PHE D 38 UNP P93832 EXPRESSION TAG
SEQRES 1 A 403 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 403 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 403 GLY GLN GLN MET GLY ARG GLY SER GLU PHE GLY LYS LYS
SEQRES 4 A 403 ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY ILE GLY
SEQRES 5 A 403 PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU GLN GLN
SEQRES 6 A 403 ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE ARG GLU
SEQRES 7 A 403 MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL GLY VAL
SEQRES 8 A 403 PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS GLU SER
SEQRES 9 A 403 ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR LYS TRP
SEQRES 10 A 403 ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS GLY LEU
SEQRES 11 A 403 LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA ASN LEU
SEQRES 12 A 403 ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP ALA SER
SEQRES 13 A 403 THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP LEU MET
SEQRES 14 A 403 VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU
SEQRES 15 A 403 PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU GLU VAL
SEQRES 16 A 403 GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU ILE ASP
SEQRES 17 A 403 ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG LYS ARG
SEQRES 18 A 403 ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN VAL LEU
SEQRES 19 A 403 GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR ALA LEU
SEQRES 20 A 403 ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS MET TYR
SEQRES 21 A 403 VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP PRO LYS
SEQRES 22 A 403 GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE GLY ASP
SEQRES 23 A 403 ILE LEU SER ASP GLU ALA SER MET ILE THR GLY SER ILE
SEQRES 24 A 403 GLY MET LEU PRO SER ALA SER LEU SER ASP SER GLY PRO
SEQRES 25 A 403 GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO ASP ILE
SEQRES 26 A 403 ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU
SEQRES 27 A 403 SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY GLU GLU
SEQRES 28 A 403 LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU VAL ALA
SEQRES 29 A 403 LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR SER ALA
SEQRES 30 A 403 GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY GLU GLU
SEQRES 31 A 403 VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA SER VAL
SEQRES 1 B 403 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 403 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 403 GLY GLN GLN MET GLY ARG GLY SER GLU PHE GLY LYS LYS
SEQRES 4 B 403 ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY ILE GLY
SEQRES 5 B 403 PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU GLN GLN
SEQRES 6 B 403 ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE ARG GLU
SEQRES 7 B 403 MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL GLY VAL
SEQRES 8 B 403 PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS GLU SER
SEQRES 9 B 403 ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR LYS TRP
SEQRES 10 B 403 ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS GLY LEU
SEQRES 11 B 403 LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA ASN LEU
SEQRES 12 B 403 ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP ALA SER
SEQRES 13 B 403 THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP LEU MET
SEQRES 14 B 403 VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU
SEQRES 15 B 403 PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU GLU VAL
SEQRES 16 B 403 GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU ILE ASP
SEQRES 17 B 403 ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG LYS ARG
SEQRES 18 B 403 ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN VAL LEU
SEQRES 19 B 403 GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR ALA LEU
SEQRES 20 B 403 ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS MET TYR
SEQRES 21 B 403 VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP PRO LYS
SEQRES 22 B 403 GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE GLY ASP
SEQRES 23 B 403 ILE LEU SER ASP GLU ALA SER MET ILE THR GLY SER ILE
SEQRES 24 B 403 GLY MET LEU PRO SER ALA SER LEU SER ASP SER GLY PRO
SEQRES 25 B 403 GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO ASP ILE
SEQRES 26 B 403 ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU
SEQRES 27 B 403 SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY GLU GLU
SEQRES 28 B 403 LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU VAL ALA
SEQRES 29 B 403 LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR SER ALA
SEQRES 30 B 403 GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY GLU GLU
SEQRES 31 B 403 VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA SER VAL
SEQRES 1 C 403 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 403 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 403 GLY GLN GLN MET GLY ARG GLY SER GLU PHE GLY LYS LYS
SEQRES 4 C 403 ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY ILE GLY
SEQRES 5 C 403 PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU GLN GLN
SEQRES 6 C 403 ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE ARG GLU
SEQRES 7 C 403 MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL GLY VAL
SEQRES 8 C 403 PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS GLU SER
SEQRES 9 C 403 ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR LYS TRP
SEQRES 10 C 403 ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS GLY LEU
SEQRES 11 C 403 LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA ASN LEU
SEQRES 12 C 403 ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP ALA SER
SEQRES 13 C 403 THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP LEU MET
SEQRES 14 C 403 VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU
SEQRES 15 C 403 PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU GLU VAL
SEQRES 16 C 403 GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU ILE ASP
SEQRES 17 C 403 ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG LYS ARG
SEQRES 18 C 403 ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN VAL LEU
SEQRES 19 C 403 GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR ALA LEU
SEQRES 20 C 403 ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS MET TYR
SEQRES 21 C 403 VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP PRO LYS
SEQRES 22 C 403 GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE GLY ASP
SEQRES 23 C 403 ILE LEU SER ASP GLU ALA SER MET ILE THR GLY SER ILE
SEQRES 24 C 403 GLY MET LEU PRO SER ALA SER LEU SER ASP SER GLY PRO
SEQRES 25 C 403 GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO ASP ILE
SEQRES 26 C 403 ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU
SEQRES 27 C 403 SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY GLU GLU
SEQRES 28 C 403 LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU VAL ALA
SEQRES 29 C 403 LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR SER ALA
SEQRES 30 C 403 GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY GLU GLU
SEQRES 31 C 403 VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA SER VAL
SEQRES 1 D 403 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 403 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 D 403 GLY GLN GLN MET GLY ARG GLY SER GLU PHE GLY LYS LYS
SEQRES 4 D 403 ARG TYR THR ILE THR LEU LEU PRO GLY ASP GLY ILE GLY
SEQRES 5 D 403 PRO GLU VAL VAL SER ILE ALA LYS ASN VAL LEU GLN GLN
SEQRES 6 D 403 ALA GLY SER LEU GLU GLY VAL GLU PHE ASN PHE ARG GLU
SEQRES 7 D 403 MET PRO ILE GLY GLY ALA ALA LEU ASP LEU VAL GLY VAL
SEQRES 8 D 403 PRO LEU PRO GLU GLU THR ILE SER ALA ALA LYS GLU SER
SEQRES 9 D 403 ASP ALA VAL LEU LEU GLY ALA ILE GLY GLY TYR LYS TRP
SEQRES 10 D 403 ASP ASN ASN GLU LYS HIS LEU ARG PRO GLU LYS GLY LEU
SEQRES 11 D 403 LEU GLN ILE ARG ALA ALA LEU LYS VAL PHE ALA ASN LEU
SEQRES 12 D 403 ARG PRO ALA THR VAL LEU PRO GLN LEU VAL ASP ALA SER
SEQRES 13 D 403 THR LEU LYS ARG GLU VAL ALA GLU GLY VAL ASP LEU MET
SEQRES 14 D 403 VAL VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU
SEQRES 15 D 403 PRO ARG GLY ILE LYS THR ASN GLU ASN GLY GLU GLU VAL
SEQRES 16 D 403 GLY PHE ASN THR GLU VAL TYR ALA ALA HIS GLU ILE ASP
SEQRES 17 D 403 ARG ILE ALA ARG VAL ALA PHE GLU THR ALA ARG LYS ARG
SEQRES 18 D 403 ARG GLY LYS LEU CYS SER VAL ASP LYS ALA ASN VAL LEU
SEQRES 19 D 403 GLU ALA SER ILE LEU TRP ARG LYS ARG VAL THR ALA LEU
SEQRES 20 D 403 ALA SER GLU TYR PRO ASP VAL GLU LEU SER HIS MET TYR
SEQRES 21 D 403 VAL ASP ASN ALA ALA MET GLN LEU VAL ARG ASP PRO LYS
SEQRES 22 D 403 GLN PHE ASP THR ILE VAL THR ASN ASN ILE PHE GLY ASP
SEQRES 23 D 403 ILE LEU SER ASP GLU ALA SER MET ILE THR GLY SER ILE
SEQRES 24 D 403 GLY MET LEU PRO SER ALA SER LEU SER ASP SER GLY PRO
SEQRES 25 D 403 GLY LEU PHE GLU PRO ILE HIS GLY SER ALA PRO ASP ILE
SEQRES 26 D 403 ALA GLY GLN ASP LYS ALA ASN PRO LEU ALA THR ILE LEU
SEQRES 27 D 403 SER ALA ALA MET LEU LEU LYS TYR GLY LEU GLY GLU GLU
SEQRES 28 D 403 LYS ALA ALA LYS ARG ILE GLU ASP ALA VAL LEU VAL ALA
SEQRES 29 D 403 LEU ASN ASN GLY PHE ARG THR GLY ASP ILE TYR SER ALA
SEQRES 30 D 403 GLY THR LYS LEU VAL GLY CYS LYS GLU MET GLY GLU GLU
SEQRES 31 D 403 VAL LEU LYS SER VAL ASP SER GLN VAL PRO ALA SER VAL
HET MG A 501 1
HET IPM A 502 12
HET MG A 503 1
HET IPM A 504 12
HET MG C 501 1
HET IPM C 502 12
HET MG C 503 1
HET IPM C 504 12
HETNAM MG MAGNESIUM ION
HETNAM IPM 3-ISOPROPYLMALIC ACID
FORMUL 5 MG 4(MG 2+)
FORMUL 6 IPM 4(C7 H12 O5)
FORMUL 13 HOH *1434(H2 O)
HELIX 1 AA1 ILE A 53 LEU A 71 1 19
HELIX 2 AA2 GLY A 84 GLY A 92 1 9
HELIX 3 AA3 PRO A 96 GLU A 105 1 10
HELIX 4 AA4 GLY A 116 ASP A 120 5 5
HELIX 5 AA5 GLU A 123 LEU A 126 5 4
HELIX 6 AA6 ARG A 127 LYS A 140 1 14
HELIX 7 AA7 LEU A 151 SER A 158 5 8
HELIX 8 AA8 LYS A 161 GLU A 166 1 6
HELIX 9 AA9 GLY A 178 PHE A 182 5 5
HELIX 10 AB1 ALA A 206 LYS A 222 1 17
HELIX 11 AB2 LEU A 236 ALA A 250 1 15
HELIX 12 AB3 SER A 251 TYR A 253 5 3
HELIX 13 AB4 VAL A 263 ASP A 273 1 11
HELIX 14 AB5 PRO A 274 PHE A 277 5 4
HELIX 15 AB6 ASN A 283 GLY A 299 1 17
HELIX 16 AB7 SER A 300 LEU A 304 5 5
HELIX 17 AB8 ALA A 324 ALA A 328 5 5
HELIX 18 AB9 PRO A 335 GLY A 351 1 17
HELIX 19 AC1 GLU A 352 ASN A 369 1 18
HELIX 20 AC2 THR A 373 TYR A 377 5 5
HELIX 21 AC3 GLY A 385 ASP A 398 1 14
HELIX 22 AC4 ILE B 53 LEU B 71 1 19
HELIX 23 AC5 GLY B 84 GLY B 92 1 9
HELIX 24 AC6 PRO B 96 SER B 106 1 11
HELIX 25 AC7 GLY B 116 ASP B 120 5 5
HELIX 26 AC8 GLU B 123 LEU B 126 5 4
HELIX 27 AC9 ARG B 127 LYS B 140 1 14
HELIX 28 AD1 LEU B 151 SER B 158 5 8
HELIX 29 AD2 LYS B 161 GLU B 166 1 6
HELIX 30 AD3 GLY B 178 PHE B 182 5 5
HELIX 31 AD4 ALA B 206 ARG B 223 1 18
HELIX 32 AD5 LEU B 236 ALA B 250 1 15
HELIX 33 AD6 SER B 251 TYR B 253 5 3
HELIX 34 AD7 VAL B 263 ASP B 273 1 11
HELIX 35 AD8 PRO B 274 PHE B 277 5 4
HELIX 36 AD9 ASN B 283 GLY B 299 1 17
HELIX 37 AE1 SER B 300 LEU B 304 5 5
HELIX 38 AE2 ALA B 324 ALA B 328 5 5
HELIX 39 AE3 PRO B 335 GLY B 349 1 15
HELIX 40 AE4 GLU B 352 ASN B 369 1 18
HELIX 41 AE5 THR B 373 TYR B 377 5 5
HELIX 42 AE6 GLY B 385 GLN B 400 1 16
HELIX 43 AE7 ILE C 53 LEU C 71 1 19
HELIX 44 AE8 GLY C 84 GLY C 92 1 9
HELIX 45 AE9 PRO C 96 GLU C 105 1 10
HELIX 46 AF1 GLY C 116 ASP C 120 5 5
HELIX 47 AF2 GLU C 123 LEU C 126 5 4
HELIX 48 AF3 ARG C 127 LYS C 140 1 14
HELIX 49 AF4 LEU C 151 SER C 158 5 8
HELIX 50 AF5 LYS C 161 GLU C 166 1 6
HELIX 51 AF6 GLY C 178 PHE C 182 5 5
HELIX 52 AF7 ALA C 206 LYS C 222 1 17
HELIX 53 AF8 LEU C 236 ALA C 250 1 15
HELIX 54 AF9 SER C 251 TYR C 253 5 3
HELIX 55 AG1 VAL C 263 ASP C 273 1 11
HELIX 56 AG2 PRO C 274 PHE C 277 5 4
HELIX 57 AG3 ASN C 283 GLY C 299 1 17
HELIX 58 AG4 SER C 300 LEU C 304 5 5
HELIX 59 AG5 ALA C 324 ALA C 328 5 5
HELIX 60 AG6 PRO C 335 GLY C 351 1 17
HELIX 61 AG7 GLU C 352 ASN C 369 1 18
HELIX 62 AG8 THR C 373 TYR C 377 5 5
HELIX 63 AG9 GLY C 385 SER C 396 1 12
HELIX 64 AH1 ILE D 53 LEU D 71 1 19
HELIX 65 AH2 ILE D 83 GLY D 92 1 10
HELIX 66 AH3 PRO D 96 GLU D 105 1 10
HELIX 67 AH4 GLY D 116 ASP D 120 5 5
HELIX 68 AH5 GLU D 123 LEU D 126 5 4
HELIX 69 AH6 ARG D 127 LYS D 140 1 14
HELIX 70 AH7 LEU D 151 SER D 158 5 8
HELIX 71 AH8 LYS D 161 GLU D 166 1 6
HELIX 72 AH9 GLY D 178 PHE D 182 5 5
HELIX 73 AI1 ALA D 206 LYS D 222 1 17
HELIX 74 AI2 LEU D 236 SER D 251 1 16
HELIX 75 AI3 VAL D 263 ASP D 273 1 11
HELIX 76 AI4 PRO D 274 PHE D 277 5 4
HELIX 77 AI5 ASN D 283 GLY D 299 1 17
HELIX 78 AI6 SER D 300 MET D 303 5 4
HELIX 79 AI7 ALA D 324 ALA D 328 5 5
HELIX 80 AI8 PRO D 335 GLY D 349 1 15
HELIX 81 AI9 GLU D 352 ASN D 369 1 18
HELIX 82 AJ1 THR D 373 TYR D 377 5 5
HELIX 83 AJ2 GLY D 385 SER D 396 1 12
SHEET 1 AA110 VAL A 74 GLU A 80 0
SHEET 2 AA110 LYS A 41 GLY A 50 1 N LYS A 41 O GLU A 75
SHEET 3 AA110 ALA A 108 ALA A 113 1 O GLY A 112 N LEU A 48
SHEET 4 AA110 GLY A 315 PHE A 317 1 O PHE A 317 N LEU A 111
SHEET 5 AA110 ALA A 307 LEU A 309 -1 N SER A 308 O LEU A 316
SHEET 6 AA110 ALA A 143 THR A 149 -1 N LEU A 145 O ALA A 307
SHEET 7 AA110 ASP A 169 GLU A 175 -1 O ARG A 174 N ASN A 144
SHEET 8 AA110 THR A 279 THR A 282 1 O ILE A 280 N VAL A 173
SHEET 9 AA110 LYS A 226 ASP A 231 1 N VAL A 230 O VAL A 281
SHEET 10 AA110 GLU A 257 TYR A 262 1 O SER A 259 N SER A 229
SHEET 1 AA2 4 GLY A 187 THR A 190 0
SHEET 2 AA2 4 GLU A 196 ALA A 205 -1 O VAL A 197 N LYS A 189
SHEET 3 AA2 4 GLU B 196 ALA B 205 -1 O TYR B 204 N GLY A 198
SHEET 4 AA2 4 GLY B 187 THR B 190 -1 N LYS B 189 O VAL B 197
SHEET 1 AA3 2 PHE A 371 ARG A 372 0
SHEET 2 AA3 2 LYS A 382 LEU A 383 1 O LYS A 382 N ARG A 372
SHEET 1 AA410 VAL B 74 GLU B 80 0
SHEET 2 AA410 LYS B 41 GLY B 50 1 N LEU B 47 O ARG B 79
SHEET 3 AA410 ALA B 108 ALA B 113 1 O LEU B 110 N LEU B 48
SHEET 4 AA410 GLY B 315 PHE B 317 1 O PHE B 317 N LEU B 111
SHEET 5 AA410 ALA B 307 LEU B 309 -1 N SER B 308 O LEU B 316
SHEET 6 AA410 ALA B 143 THR B 149 -1 N LEU B 145 O ALA B 307
SHEET 7 AA410 ASP B 169 GLU B 175 -1 O LEU B 170 N ALA B 148
SHEET 8 AA410 THR B 279 THR B 282 1 O ILE B 280 N VAL B 173
SHEET 9 AA410 LYS B 226 ASP B 231 1 N VAL B 230 O VAL B 281
SHEET 10 AA410 GLU B 257 TYR B 262 1 O GLU B 257 N LEU B 227
SHEET 1 AA5 2 PHE B 371 ARG B 372 0
SHEET 2 AA5 2 LYS B 382 LEU B 383 1 O LYS B 382 N ARG B 372
SHEET 1 AA610 GLU C 75 GLU C 80 0
SHEET 2 AA610 ARG C 42 GLY C 50 1 N LEU C 47 O ARG C 79
SHEET 3 AA610 ALA C 108 ALA C 113 1 O LEU C 110 N LEU C 48
SHEET 4 AA610 GLY C 315 PHE C 317 1 O PHE C 317 N LEU C 111
SHEET 5 AA610 ALA C 307 LEU C 309 -1 N SER C 308 O LEU C 316
SHEET 6 AA610 ALA C 143 THR C 149 -1 N LEU C 145 O ALA C 307
SHEET 7 AA610 ASP C 169 GLU C 175 -1 O ARG C 174 N ASN C 144
SHEET 8 AA610 THR C 279 THR C 282 1 O ILE C 280 N VAL C 173
SHEET 9 AA610 LYS C 226 ASP C 231 1 N VAL C 230 O VAL C 281
SHEET 10 AA610 GLU C 257 TYR C 262 1 O SER C 259 N SER C 229
SHEET 1 AA7 4 GLY C 187 THR C 190 0
SHEET 2 AA7 4 GLU C 196 ALA C 205 -1 O PHE C 199 N GLY C 187
SHEET 3 AA7 4 GLU D 196 ALA D 205 -1 O GLY D 198 N TYR C 204
SHEET 4 AA7 4 GLY D 187 THR D 190 -1 N LYS D 189 O VAL D 197
SHEET 1 AA8 2 PHE C 371 ARG C 372 0
SHEET 2 AA8 2 LYS C 382 LEU C 383 1 O LYS C 382 N ARG C 372
SHEET 1 AA910 PHE D 76 GLU D 80 0
SHEET 2 AA910 TYR D 43 GLY D 50 1 N LEU D 47 O ARG D 79
SHEET 3 AA910 ALA D 108 ALA D 113 1 O LEU D 110 N LEU D 48
SHEET 4 AA910 GLY D 315 PRO D 319 1 O PHE D 317 N LEU D 111
SHEET 5 AA910 PRO D 305 LEU D 309 -1 N SER D 308 O LEU D 316
SHEET 6 AA910 ALA D 143 THR D 149 -1 N LEU D 145 O ALA D 307
SHEET 7 AA910 ASP D 169 GLU D 175 -1 O LEU D 170 N ALA D 148
SHEET 8 AA910 THR D 279 THR D 282 1 O ILE D 280 N VAL D 173
SHEET 9 AA910 LYS D 226 ASP D 231 1 N VAL D 230 O VAL D 281
SHEET 10 AA910 GLU D 257 TYR D 262 1 O SER D 259 N SER D 229
SHEET 1 AB1 2 PHE D 371 ARG D 372 0
SHEET 2 AB1 2 LYS D 382 LEU D 383 1 O LYS D 382 N ARG D 372
LINK OD2 ASP A 264 MG MG A 503 1555 1555 2.00
LINK OD1 ASP A 288 MG MG A 501 1555 1555 2.18
LINK OD2 ASP A 292 MG MG A 501 1555 1555 2.41
LINK MG MG A 501 O1 IPM A 502 1555 1555 2.31
LINK MG MG A 501 O3 IPM A 502 1555 1555 2.34
LINK MG MG A 501 O HOH A 623 1555 1555 2.52
LINK MG MG A 501 O HOH A 657 1555 1555 2.12
LINK MG MG A 501 OD2 ASP B 264 1555 1555 2.08
LINK MG MG A 503 O2 IPM A 504 1555 1555 2.60
LINK MG MG A 503 O1 IPM A 504 1555 1555 2.21
LINK MG MG A 503 OD1 ASP B 288 1555 1555 2.20
LINK MG MG A 503 OD2 ASP B 292 1555 1555 2.53
LINK MG MG A 503 O HOH B 654 1555 1555 2.68
LINK MG MG A 503 O HOH B 655 1555 1555 2.27
LINK OD2 ASP C 264 MG MG C 503 1555 1555 2.09
LINK OD1 ASP C 288 MG MG C 501 1555 1555 2.40
LINK OD2 ASP C 292 MG MG C 501 1555 1555 2.54
LINK MG MG C 501 O1 IPM C 502 1555 1555 2.30
LINK MG MG C 501 O2 IPM C 502 1555 1555 2.26
LINK MG MG C 501 O HOH C 622 1555 1555 2.38
LINK MG MG C 501 O HOH C 803 1555 1555 2.63
LINK MG MG C 501 OD2 ASP D 264 1555 1555 2.09
LINK MG MG C 503 O1 IPM C 504 1555 1555 2.44
LINK MG MG C 503 O3 IPM C 504 1555 1555 2.36
LINK MG MG C 503 O HOH C 625 1555 1555 2.11
LINK MG MG C 503 OD1 ASP D 288 1555 1555 2.20
LINK MG MG C 503 OD2 ASP D 292 1555 1555 2.60
LINK MG MG C 503 O HOH D 799 1555 1555 2.44
CISPEP 1 GLU A 184 PRO A 185 0 0.76
CISPEP 2 GLU B 184 PRO B 185 0 6.61
CISPEP 3 GLU C 184 PRO C 185 0 1.47
CISPEP 4 GLU D 184 PRO D 185 0 0.80
SITE 1 AC1 6 ASP A 288 ASP A 292 IPM A 502 HOH A 623
SITE 2 AC1 6 HOH A 657 ASP B 264
SITE 1 AC2 11 ARG A 136 ARG A 146 ARG A 174 TYR A 181
SITE 2 AC2 11 ASP A 288 MG A 501 HOH A 623 HOH A 657
SITE 3 AC2 11 HOH A 785 LYS B 232 ASP B 264
SITE 1 AC3 6 ASP A 264 IPM A 504 ASP B 288 ASP B 292
SITE 2 AC3 6 HOH B 654 HOH B 655
SITE 1 AC4 12 LYS A 232 ASN A 234 VAL A 235 ASP A 264
SITE 2 AC4 12 MG A 503 HOH A 793 ARG B 136 ARG B 146
SITE 3 AC4 12 ARG B 174 TYR B 181 ASP B 288 HOH B 654
SITE 1 AC5 6 ASP C 288 ASP C 292 IPM C 502 HOH C 622
SITE 2 AC5 6 HOH C 803 ASP D 264
SITE 1 AC6 10 ARG C 136 ARG C 146 ARG C 174 TYR C 181
SITE 2 AC6 10 ASP C 288 MG C 501 HOH C 622 HOH C 773
SITE 3 AC6 10 LYS D 232 ASP D 264
SITE 1 AC7 6 ASP C 264 IPM C 504 HOH C 625 ASP D 288
SITE 2 AC7 6 ASP D 292 HOH D 799
SITE 1 AC8 9 LYS C 232 ASP C 264 MG C 503 HOH C 625
SITE 2 AC8 9 ARG D 136 ARG D 146 ARG D 174 TYR D 181
SITE 3 AC8 9 ASP D 288
CRYST1 96.059 49.622 158.969 90.00 105.44 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 0.010410 0.000000 0.002876 0.00000
SCALE2 0.000000 0.020152 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006526 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
