HEADER HYDROLASE 22-JAN-18 6C7G
TITLE CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A WITH N-(1-ADAMANTYL)-
TITLE 2 1-(2-CHLORO-5-ISOBUTOXY-PHENYL)-4-METHYL-[1,2,4]TRIAZOLO[4,3-
TITLE 3 A]QUINOXALINE-8-CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT 3',5'-CYCLIC PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PHOSPHODIESTERASE 2A (UNP RESIDUES 323-661);
COMPND 5 SYNONYM: CYCLIC GMP-STIMULATED PHOSPHODIESTERASE, CGSPDE;
COMPND 6 EC: 3.1.4.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDE2A;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-HT
KEYWDS PHOSPHODIESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.XU,K.AERTGEERTS
REVDAT 4 13-MAR-24 6C7G 1 REMARK LINK
REVDAT 3 26-SEP-18 6C7G 1 JRNL
REVDAT 2 29-AUG-18 6C7G 1 JRNL
REVDAT 1 15-AUG-18 6C7G 0
JRNL AUTH L.GOMEZ,R.XU,W.SINKO,B.SELFRIDGE,W.VERNIER,K.LY,R.TRUONG,
JRNL AUTH 2 M.METZ,T.MARRONE,K.SEBRING,Y.YAN,B.APPLETON,K.AERTGEERTS,
JRNL AUTH 3 M.E.MASSARI,J.G.BREITENBUCHER
JRNL TITL MATHEMATICAL AND STRUCTURAL CHARACTERIZATION OF STRONG
JRNL TITL 2 NONADDITIVE STRUCTURE-ACTIVITY RELATIONSHIP CAUSED BY
JRNL TITL 3 PROTEIN CONFORMATIONAL CHANGES.
JRNL REF J. MED. CHEM. V. 61 7754 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30070482
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00713
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 146405
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830
REMARK 3 FREE R VALUE TEST SET COUNT : 7078
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 66.1840 - 5.2193 0.97 4930 208 0.1895 0.1960
REMARK 3 2 5.2193 - 4.1429 0.93 4710 233 0.1587 0.1710
REMARK 3 3 4.1429 - 3.6193 0.97 4892 241 0.1705 0.1977
REMARK 3 4 3.6193 - 3.2884 0.94 4699 260 0.1939 0.2176
REMARK 3 5 3.2884 - 3.0527 0.92 4625 274 0.1955 0.2316
REMARK 3 6 3.0527 - 2.8727 0.94 4723 229 0.2031 0.2623
REMARK 3 7 2.8727 - 2.7288 0.97 4863 239 0.1916 0.2392
REMARK 3 8 2.7288 - 2.6100 0.97 4831 253 0.1914 0.2489
REMARK 3 9 2.6100 - 2.5096 0.96 4914 216 0.1875 0.2306
REMARK 3 10 2.5096 - 2.4230 0.92 4549 234 0.1933 0.2121
REMARK 3 11 2.4230 - 2.3472 0.91 4577 234 0.1934 0.2477
REMARK 3 12 2.3472 - 2.2801 0.92 4667 232 0.1892 0.2210
REMARK 3 13 2.2801 - 2.2201 0.92 4640 230 0.1847 0.2272
REMARK 3 14 2.2201 - 2.1659 0.95 4714 265 0.1894 0.2190
REMARK 3 15 2.1659 - 2.1167 0.94 4727 242 0.1882 0.2406
REMARK 3 16 2.1167 - 2.0716 0.93 4644 244 0.1987 0.2455
REMARK 3 17 2.0716 - 2.0302 0.92 4676 247 0.2116 0.2677
REMARK 3 18 2.0302 - 1.9919 0.93 4649 187 0.2192 0.2637
REMARK 3 19 1.9919 - 1.9563 0.93 4703 233 0.2084 0.2565
REMARK 3 20 1.9563 - 1.9231 0.90 4514 219 0.2088 0.2461
REMARK 3 21 1.9231 - 1.8921 0.87 4382 223 0.2111 0.2442
REMARK 3 22 1.8921 - 1.8630 0.88 4368 249 0.2215 0.2745
REMARK 3 23 1.8630 - 1.8356 0.88 4486 210 0.2230 0.2887
REMARK 3 24 1.8356 - 1.8097 0.88 4365 216 0.2278 0.2654
REMARK 3 25 1.8097 - 1.7853 0.91 4708 233 0.2334 0.2862
REMARK 3 26 1.7853 - 1.7621 0.92 4561 242 0.2425 0.2801
REMARK 3 27 1.7621 - 1.7401 0.91 4560 262 0.2540 0.3054
REMARK 3 28 1.7401 - 1.7191 0.91 4552 241 0.2578 0.2720
REMARK 3 29 1.7191 - 1.6991 0.90 4463 240 0.2747 0.3325
REMARK 3 30 1.6991 - 1.6800 0.90 4635 242 0.2765 0.2937
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.77
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 11409
REMARK 3 ANGLE : 1.030 15426
REMARK 3 CHIRALITY : 0.040 1633
REMARK 3 PLANARITY : 0.005 1987
REMARK 3 DIHEDRAL : 13.653 4192
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 576 THROUGH 611 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9902 -16.5760 2.2677
REMARK 3 T TENSOR
REMARK 3 T11: 0.1144 T22: 0.1941
REMARK 3 T33: 0.1641 T12: -0.0445
REMARK 3 T13: 0.0193 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.3989 L22: 2.8589
REMARK 3 L33: 1.8660 L12: 0.9039
REMARK 3 L13: 0.6778 L23: 0.8749
REMARK 3 S TENSOR
REMARK 3 S11: 0.0818 S12: -0.2705 S13: -0.1991
REMARK 3 S21: 0.1779 S22: -0.1125 S23: 0.1097
REMARK 3 S31: 0.1472 S32: -0.0846 S33: 0.0356
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 612 THROUGH 635 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0265 -12.4842 -5.5162
REMARK 3 T TENSOR
REMARK 3 T11: 0.0786 T22: 0.1449
REMARK 3 T33: 0.1236 T12: -0.0472
REMARK 3 T13: 0.0025 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 1.3092 L22: 2.1563
REMARK 3 L33: 3.2114 L12: 0.4228
REMARK 3 L13: 0.4765 L23: 0.1823
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: -0.0440 S13: -0.1880
REMARK 3 S21: 0.0144 S22: -0.0607 S23: 0.2184
REMARK 3 S31: 0.0970 S32: -0.3426 S33: 0.0029
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 636 THROUGH 657 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1603 -13.1233 -5.8372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.0738
REMARK 3 T33: 0.0718 T12: 0.0062
REMARK 3 T13: 0.0227 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 5.7466 L22: 2.4132
REMARK 3 L33: 2.6652 L12: 2.3190
REMARK 3 L13: 2.4448 L23: 1.1901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: -0.1639 S13: -0.3251
REMARK 3 S21: -0.0271 S22: 0.0005 S23: -0.1349
REMARK 3 S31: 0.1783 S32: 0.0012 S33: -0.1432
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 658 THROUGH 750 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5458 -2.8543 -8.9154
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.0817
REMARK 3 T33: 0.0452 T12: -0.0178
REMARK 3 T13: 0.0070 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 2.2335 L22: 1.1499
REMARK 3 L33: 1.1717 L12: 0.2873
REMARK 3 L13: -0.0556 L23: -0.0911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: 0.0495 S13: 0.0037
REMARK 3 S21: -0.0965 S22: 0.0092 S23: 0.0460
REMARK 3 S31: -0.0574 S32: 0.0320 S33: -0.0262
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 751 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4346 0.9936 -17.3285
REMARK 3 T TENSOR
REMARK 3 T11: 0.1283 T22: 0.1637
REMARK 3 T33: 0.0894 T12: 0.0081
REMARK 3 T13: 0.0089 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 4.3666 L22: 3.7478
REMARK 3 L33: 5.1645 L12: 1.0123
REMARK 3 L13: 2.3357 L23: 1.6115
REMARK 3 S TENSOR
REMARK 3 S11: -0.1227 S12: 0.4383 S13: 0.2087
REMARK 3 S21: -0.5402 S22: 0.0613 S23: 0.2800
REMARK 3 S31: -0.2634 S32: -0.0657 S33: 0.0291
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9698 16.6611 -4.7309
REMARK 3 T TENSOR
REMARK 3 T11: 0.2311 T22: 0.1106
REMARK 3 T33: 0.2706 T12: -0.0481
REMARK 3 T13: -0.0307 T23: -0.0422
REMARK 3 L TENSOR
REMARK 3 L11: 4.9363 L22: 4.5103
REMARK 3 L33: 2.8987 L12: -2.3976
REMARK 3 L13: -0.4643 L23: 0.2687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: -0.0047 S13: 1.0349
REMARK 3 S21: 0.0448 S22: 0.0001 S23: -0.2348
REMARK 3 S31: -0.6378 S32: 0.2015 S33: 0.0466
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3038 8.4750 -4.0293
REMARK 3 T TENSOR
REMARK 3 T11: 0.0719 T22: 0.0758
REMARK 3 T33: 0.1294 T12: -0.0182
REMARK 3 T13: 0.0226 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 3.3774 L22: 4.5003
REMARK 3 L33: 6.4550 L12: -1.6399
REMARK 3 L13: 2.2686 L23: -2.7470
REMARK 3 S TENSOR
REMARK 3 S11: 0.0335 S12: -0.0499 S13: 0.2313
REMARK 3 S21: -0.0952 S22: -0.0084 S23: 0.2764
REMARK 3 S31: -0.2609 S32: 0.0141 S33: -0.0298
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 816 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1385 -1.3986 8.7494
REMARK 3 T TENSOR
REMARK 3 T11: 0.0001 T22: 0.3960
REMARK 3 T33: 0.0410 T12: -0.0448
REMARK 3 T13: -0.1075 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 6.1510 L22: 1.3133
REMARK 3 L33: 1.5539 L12: -0.0608
REMARK 3 L13: -1.3582 L23: 0.4901
REMARK 3 S TENSOR
REMARK 3 S11: -0.1073 S12: -0.2315 S13: -0.0977
REMARK 3 S21: 0.5133 S22: 0.0953 S23: 0.0494
REMARK 3 S31: 0.1003 S32: 0.5112 S33: 0.0248
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 840 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7085 9.2511 7.2791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.2794
REMARK 3 T33: 0.1429 T12: -0.0621
REMARK 3 T13: -0.0006 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 1.8323 L22: 1.4283
REMARK 3 L33: 1.1649 L12: -0.3315
REMARK 3 L13: 0.7576 L23: -0.1194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.0701 S13: 0.4527
REMARK 3 S21: 0.1183 S22: -0.0697 S23: -0.1662
REMARK 3 S31: -0.2764 S32: 0.3441 S33: 0.0351
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8347 5.2479 21.2514
REMARK 3 T TENSOR
REMARK 3 T11: 0.2538 T22: 0.3621
REMARK 3 T33: 0.1662 T12: -0.0265
REMARK 3 T13: 0.0365 T23: -0.0810
REMARK 3 L TENSOR
REMARK 3 L11: 8.5611 L22: 0.6822
REMARK 3 L33: 4.8043 L12: -1.5270
REMARK 3 L13: 6.4753 L23: -0.8728
REMARK 3 S TENSOR
REMARK 3 S11: -0.1677 S12: -0.4734 S13: 0.0673
REMARK 3 S21: 0.1992 S22: 0.1369 S23: -0.0483
REMARK 3 S31: -0.2080 S32: -0.1957 S33: 0.0343
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 579 THROUGH 611 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0964 -19.7798 -42.4155
REMARK 3 T TENSOR
REMARK 3 T11: 0.2682 T22: 0.1189
REMARK 3 T33: 0.2130 T12: 0.0430
REMARK 3 T13: 0.0221 T23: -0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 1.0192 L22: 2.0078
REMARK 3 L33: 1.5732 L12: -1.2721
REMARK 3 L13: 0.9159 L23: -0.7169
REMARK 3 S TENSOR
REMARK 3 S11: 0.0498 S12: 0.0778 S13: -0.2917
REMARK 3 S21: -0.2561 S22: -0.0151 S23: -0.0116
REMARK 3 S31: 0.4515 S32: -0.0826 S33: -0.0359
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 612 THROUGH 635 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7676 -15.7012 -34.8963
REMARK 3 T TENSOR
REMARK 3 T11: 0.2072 T22: 0.1663
REMARK 3 T33: 0.2089 T12: 0.0917
REMARK 3 T13: -0.0217 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 3.0895 L22: 3.2185
REMARK 3 L33: 2.7465 L12: 0.1545
REMARK 3 L13: -1.7665 L23: -0.4363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.5426 S13: -0.2417
REMARK 3 S21: 0.1002 S22: -0.1045 S23: -0.3573
REMARK 3 S31: 0.2078 S32: 0.6336 S33: 0.0178
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 636 THROUGH 657 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8512 -14.4373 -32.5164
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.0470
REMARK 3 T33: 0.1473 T12: 0.0006
REMARK 3 T13: -0.0263 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 4.8017 L22: 3.8650
REMARK 3 L33: 3.4810 L12: -3.0391
REMARK 3 L13: 2.5697 L23: -2.8088
REMARK 3 S TENSOR
REMARK 3 S11: 0.1390 S12: -0.0639 S13: -0.4213
REMARK 3 S21: 0.0811 S22: 0.0678 S23: 0.0717
REMARK 3 S31: 0.4007 S32: -0.0633 S33: -0.2150
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 658 THROUGH 718 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7525 -3.5487 -35.5327
REMARK 3 T TENSOR
REMARK 3 T11: 0.1125 T22: 0.0280
REMARK 3 T33: 0.0530 T12: 0.0186
REMARK 3 T13: -0.0047 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 2.4273 L22: 1.7735
REMARK 3 L33: 2.0736 L12: 0.0915
REMARK 3 L13: -0.2574 L23: 0.3129
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.0808 S13: -0.0420
REMARK 3 S21: -0.0237 S22: 0.0628 S23: -0.1008
REMARK 3 S31: 0.0327 S32: 0.0398 S33: -0.0569
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 719 THROUGH 738 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5816 -0.6268 -25.5511
REMARK 3 T TENSOR
REMARK 3 T11: 0.1768 T22: 0.0737
REMARK 3 T33: 0.0618 T12: 0.0217
REMARK 3 T13: 0.0376 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 4.0998 L22: 1.8544
REMARK 3 L33: 3.3714 L12: 0.5877
REMARK 3 L13: 0.5506 L23: -0.3603
REMARK 3 S TENSOR
REMARK 3 S11: -0.0973 S12: -0.3130 S13: 0.2244
REMARK 3 S21: 0.5622 S22: 0.0313 S23: 0.3661
REMARK 3 S31: -0.1957 S32: -0.0676 S33: 0.0126
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 739 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9930 -4.4417 -22.9726
REMARK 3 T TENSOR
REMARK 3 T11: 0.1189 T22: 0.1454
REMARK 3 T33: 0.0840 T12: 0.0130
REMARK 3 T13: 0.0070 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 2.4825 L22: 1.8165
REMARK 3 L33: 2.3265 L12: 0.1671
REMARK 3 L13: 0.6451 L23: 0.3055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0713 S12: -0.3838 S13: -0.1457
REMARK 3 S21: 0.1618 S22: 0.0343 S23: -0.1589
REMARK 3 S31: 0.1428 S32: 0.1483 S33: -0.0912
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 769 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1648 8.5758 -39.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1884 T22: 0.0658
REMARK 3 T33: 0.1697 T12: 0.0040
REMARK 3 T13: 0.0404 T23: -0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 2.3150 L22: 2.3739
REMARK 3 L33: 1.3889 L12: 0.9169
REMARK 3 L13: 0.5777 L23: 0.4678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0413 S12: 0.0563 S13: 0.3089
REMARK 3 S21: -0.0539 S22: 0.1370 S23: -0.1786
REMARK 3 S31: -0.3273 S32: 0.1190 S33: -0.0967
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 816 THROUGH 840 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4858 -3.5074 -46.3494
REMARK 3 T TENSOR
REMARK 3 T11: 0.1361 T22: 0.2105
REMARK 3 T33: 0.1081 T12: -0.0121
REMARK 3 T13: -0.0627 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 9.2013 L22: 2.1569
REMARK 3 L33: 2.6459 L12: -1.1802
REMARK 3 L13: -4.0398 L23: -0.2688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0166 S12: 0.4036 S13: -0.1569
REMARK 3 S21: -0.1758 S22: -0.1131 S23: 0.2156
REMARK 3 S31: 0.1538 S32: -0.4385 S33: 0.0891
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 841 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2119 6.4879 -48.3971
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1807
REMARK 3 T33: 0.1657 T12: 0.0405
REMARK 3 T13: 0.0043 T23: 0.0729
REMARK 3 L TENSOR
REMARK 3 L11: 4.3021 L22: 1.0162
REMARK 3 L33: 1.3318 L12: 1.2119
REMARK 3 L13: 0.0357 L23: 0.2885
REMARK 3 S TENSOR
REMARK 3 S11: 0.0796 S12: 0.4119 S13: 0.5780
REMARK 3 S21: -0.2204 S22: -0.0276 S23: 0.1336
REMARK 3 S31: -0.2829 S32: -0.2772 S33: -0.0277
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3433 -0.3842 -60.9976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3405 T22: 0.3354
REMARK 3 T33: 0.1379 T12: 0.0223
REMARK 3 T13: 0.0052 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 8.6597 L22: 0.7181
REMARK 3 L33: 2.9748 L12: 1.3084
REMARK 3 L13: 4.9236 L23: 0.9909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0853 S12: 0.4741 S13: 0.0342
REMARK 3 S21: -0.3154 S22: 0.0610 S23: 0.0455
REMARK 3 S31: -0.0846 S32: -0.0442 S33: -0.0042
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 591 THROUGH 675 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5526 -46.1064 -37.9537
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.3202
REMARK 3 T33: 0.3662 T12: 0.3123
REMARK 3 T13: 0.0141 T23: -0.2287
REMARK 3 L TENSOR
REMARK 3 L11: 0.5816 L22: 1.5626
REMARK 3 L33: 2.3592 L12: 0.4943
REMARK 3 L13: 0.0492 L23: -0.7560
REMARK 3 S TENSOR
REMARK 3 S11: 0.2003 S12: 0.1837 S13: -0.6177
REMARK 3 S21: 0.0901 S22: -0.3318 S23: -0.6859
REMARK 3 S31: 0.4640 S32: 1.5344 S33: 0.0447
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 676 THROUGH 695 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8935 -34.2092 -32.6217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1372 T22: 0.5473
REMARK 3 T33: 0.2640 T12: -0.0516
REMARK 3 T13: -0.0129 T23: -0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 4.4478 L22: 4.3817
REMARK 3 L33: 1.7660 L12: 1.5475
REMARK 3 L13: 0.4871 L23: 0.1967
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: 0.1283 S13: 0.0826
REMARK 3 S21: -0.0275 S22: 0.0360 S23: -0.6040
REMARK 3 S31: -0.2050 S32: 1.0283 S33: -0.0347
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 696 THROUGH 724 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5421 -38.4376 -28.2992
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.0646
REMARK 3 T33: 0.1153 T12: -0.0040
REMARK 3 T13: -0.0347 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 4.2688 L22: 1.0569
REMARK 3 L33: 1.8912 L12: -0.8547
REMARK 3 L13: -1.2587 L23: -0.7482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: -0.0086 S13: -0.1416
REMARK 3 S21: 0.0755 S22: 0.0564 S23: 0.0520
REMARK 3 S31: 0.0726 S32: -0.0471 S33: -0.0977
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 725 THROUGH 750 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7736 -43.1546 -22.2907
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.1632
REMARK 3 T33: 0.1892 T12: 0.0331
REMARK 3 T13: -0.0491 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 2.8774 L22: 1.0764
REMARK 3 L33: 1.9912 L12: 0.1356
REMARK 3 L13: 0.7634 L23: -0.1916
REMARK 3 S TENSOR
REMARK 3 S11: 0.1610 S12: -0.1694 S13: -0.4490
REMARK 3 S21: 0.0706 S22: -0.0103 S23: -0.2257
REMARK 3 S31: 0.1808 S32: 0.3454 S33: -0.0998
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 751 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.6304 -33.9094 -22.6451
REMARK 3 T TENSOR
REMARK 3 T11: 0.1111 T22: 0.3596
REMARK 3 T33: 0.2563 T12: -0.0285
REMARK 3 T13: -0.0079 T23: -0.1712
REMARK 3 L TENSOR
REMARK 3 L11: 7.2230 L22: 2.6288
REMARK 3 L33: 8.4924 L12: -1.1866
REMARK 3 L13: 7.2826 L23: -1.6872
REMARK 3 S TENSOR
REMARK 3 S11: -0.0899 S12: -0.6095 S13: 0.3629
REMARK 3 S21: 0.1558 S22: 0.1908 S23: -0.3928
REMARK 3 S31: -0.3421 S32: 0.4149 S33: 0.0567
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5897 -20.6242 -36.5145
REMARK 3 T TENSOR
REMARK 3 T11: 0.4005 T22: 0.2068
REMARK 3 T33: 0.2726 T12: -0.0441
REMARK 3 T13: 0.1031 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 8.0151 L22: 8.1533
REMARK 3 L33: 1.9506 L12: 5.2598
REMARK 3 L13: 0.9628 L23: -0.3896
REMARK 3 S TENSOR
REMARK 3 S11: 0.0999 S12: 0.1706 S13: 0.8066
REMARK 3 S21: -0.1247 S22: 0.2435 S23: 0.1289
REMARK 3 S31: -0.9766 S32: 0.3086 S33: -0.2453
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1046 -27.6259 -36.7325
REMARK 3 T TENSOR
REMARK 3 T11: 0.2120 T22: 0.3585
REMARK 3 T33: 0.2569 T12: -0.1168
REMARK 3 T13: 0.0622 T23: -0.1158
REMARK 3 L TENSOR
REMARK 3 L11: 2.8154 L22: 4.4114
REMARK 3 L33: 2.9371 L12: 1.2637
REMARK 3 L13: 2.0456 L23: 1.2822
REMARK 3 S TENSOR
REMARK 3 S11: 0.1538 S12: -0.0283 S13: 0.3645
REMARK 3 S21: 0.2854 S22: -0.0090 S23: -0.3008
REMARK 3 S31: -0.4077 S32: 0.6706 S33: -0.1259
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 816 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0667 -41.8899 -46.9445
REMARK 3 T TENSOR
REMARK 3 T11: 0.1609 T22: 0.2244
REMARK 3 T33: 0.1533 T12: -0.0145
REMARK 3 T13: -0.0617 T23: -0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 6.8333 L22: 2.3792
REMARK 3 L33: 2.8280 L12: 1.4428
REMARK 3 L13: -1.6857 L23: -1.2515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: 0.4120 S13: -0.2768
REMARK 3 S21: -0.1750 S22: 0.0178 S23: 0.0344
REMARK 3 S31: 0.3714 S32: -0.4939 S33: 0.0524
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 840 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7402 -30.5792 -47.0330
REMARK 3 T TENSOR
REMARK 3 T11: 0.2093 T22: 0.2460
REMARK 3 T33: 0.1096 T12: 0.0323
REMARK 3 T13: 0.0227 T23: -0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 3.4590 L22: 2.7782
REMARK 3 L33: 2.0645 L12: 1.4608
REMARK 3 L13: -0.3984 L23: -0.4079
REMARK 3 S TENSOR
REMARK 3 S11: 0.2778 S12: 0.0093 S13: 0.2926
REMARK 3 S21: -0.0698 S22: -0.1543 S23: 0.1569
REMARK 3 S31: -0.2717 S32: -0.3740 S33: -0.1098
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8385 -36.3248 -60.6469
REMARK 3 T TENSOR
REMARK 3 T11: 0.2434 T22: 0.2831
REMARK 3 T33: 0.1456 T12: 0.0051
REMARK 3 T13: 0.0309 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 6.6221 L22: 2.0976
REMARK 3 L33: 5.8388 L12: 3.1565
REMARK 3 L13: 6.0857 L23: 3.0667
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: 0.4367 S13: -0.1919
REMARK 3 S21: -0.1491 S22: 0.1684 S23: -0.1531
REMARK 3 S31: -0.0638 S32: 0.3734 S33: -0.1861
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 582 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7896 -43.8745 2.5353
REMARK 3 T TENSOR
REMARK 3 T11: 0.2145 T22: 0.3386
REMARK 3 T33: 0.3398 T12: -0.1725
REMARK 3 T13: -0.0185 T23: 0.1418
REMARK 3 L TENSOR
REMARK 3 L11: 0.9511 L22: 1.1968
REMARK 3 L33: 1.2856 L12: -0.2014
REMARK 3 L13: 0.1227 L23: 0.4445
REMARK 3 S TENSOR
REMARK 3 S11: 0.1557 S12: -0.3345 S13: -0.5297
REMARK 3 S21: 0.1517 S22: -0.1492 S23: 0.4063
REMARK 3 S31: 0.4359 S32: -0.4780 S33: 0.0185
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 675 THROUGH 695 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7967 -31.1576 -4.4158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.2853
REMARK 3 T33: 0.1883 T12: -0.0277
REMARK 3 T13: -0.0188 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 3.4451 L22: 7.6046
REMARK 3 L33: 2.7008 L12: -1.9931
REMARK 3 L13: 1.0268 L23: 0.8442
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: -0.1622 S13: -0.2690
REMARK 3 S21: -0.1285 S22: -0.1676 S23: 0.7297
REMARK 3 S31: -0.1167 S32: -0.5361 S33: 0.0759
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 696 THROUGH 724 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1469 -36.6457 -8.4184
REMARK 3 T TENSOR
REMARK 3 T11: 0.0809 T22: 0.0898
REMARK 3 T33: 0.1070 T12: -0.0023
REMARK 3 T13: -0.0345 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 5.3627 L22: 1.6700
REMARK 3 L33: 2.3641 L12: 1.3471
REMARK 3 L13: -0.7810 L23: 0.9014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.1824 S13: -0.3503
REMARK 3 S21: -0.0528 S22: 0.0305 S23: -0.1519
REMARK 3 S31: 0.0660 S32: 0.1099 S33: -0.0598
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 725 THROUGH 750 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8281 -42.3686 -13.3651
REMARK 3 T TENSOR
REMARK 3 T11: 0.1523 T22: 0.1485
REMARK 3 T33: 0.2350 T12: -0.0287
REMARK 3 T13: -0.0863 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 3.4469 L22: 0.5463
REMARK 3 L33: 1.5312 L12: 0.7903
REMARK 3 L13: 0.8548 L23: 0.6898
REMARK 3 S TENSOR
REMARK 3 S11: 0.1912 S12: 0.1176 S13: -0.5150
REMARK 3 S21: -0.1641 S22: -0.0238 S23: 0.0923
REMARK 3 S31: 0.2729 S32: -0.2383 S33: -0.1360
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 751 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0882 -33.2625 -14.6846
REMARK 3 T TENSOR
REMARK 3 T11: 0.1112 T22: 0.3603
REMARK 3 T33: 0.1938 T12: -0.0233
REMARK 3 T13: 0.0126 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.0669 L22: 4.6178
REMARK 3 L33: 2.0738 L12: 3.9339
REMARK 3 L13: 9.2149 L23: 3.7706
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: 0.4364 S13: 0.0973
REMARK 3 S21: -0.3343 S22: 0.1533 S23: 0.3068
REMARK 3 S31: -0.2347 S32: -0.1592 S33: -0.0030
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3888 -17.5755 -3.8271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1393 T22: 0.2784
REMARK 3 T33: 0.2638 T12: -0.0138
REMARK 3 T13: 0.0052 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 7.9601 L22: 2.0889
REMARK 3 L33: 0.0461 L12: -8.4397
REMARK 3 L13: -0.6018 L23: 0.6456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0885 S12: 0.3020 S13: 0.4575
REMARK 3 S21: -0.0691 S22: -0.0705 S23: -0.3025
REMARK 3 S31: 0.0126 S32: 0.0798 S33: -0.0228
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6777 -24.2078 -2.0607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0723 T22: 0.1652
REMARK 3 T33: 0.1010 T12: -0.0021
REMARK 3 T13: 0.0134 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 2.8291 L22: 5.5454
REMARK 3 L33: 5.0074 L12: -2.5531
REMARK 3 L13: 2.0175 L23: -4.0056
REMARK 3 S TENSOR
REMARK 3 S11: 0.1881 S12: -0.0483 S13: -0.0501
REMARK 3 S21: -0.1700 S22: -0.1023 S23: 0.1681
REMARK 3 S31: 0.0705 S32: 0.0315 S33: -0.0836
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 816 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7607 -36.4600 10.5356
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.2701
REMARK 3 T33: 0.1258 T12: -0.0096
REMARK 3 T13: -0.0561 T23: 0.0920
REMARK 3 L TENSOR
REMARK 3 L11: 5.2507 L22: 2.2504
REMARK 3 L33: 4.1784 L12: -1.1695
REMARK 3 L13: -3.2462 L23: 0.9911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0356 S12: -0.5186 S13: -0.2610
REMARK 3 S21: 0.2394 S22: 0.0437 S23: -0.0462
REMARK 3 S31: 0.2908 S32: 0.0882 S33: -0.0014
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 840 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9142 -25.4378 8.4954
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.2965
REMARK 3 T33: 0.1226 T12: -0.0379
REMARK 3 T13: -0.0211 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 1.4535 L22: 1.7492
REMARK 3 L33: 1.6486 L12: -1.0159
REMARK 3 L13: 0.6672 L23: 0.3077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: -0.2710 S13: 0.1019
REMARK 3 S21: 0.0650 S22: 0.0903 S23: -0.1687
REMARK 3 S31: -0.0731 S32: 0.1146 S33: -0.0684
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0145 -28.4025 22.5318
REMARK 3 T TENSOR
REMARK 3 T11: 0.2330 T22: 0.3843
REMARK 3 T33: 0.1414 T12: 0.0055
REMARK 3 T13: 0.0283 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 9.2962 L22: 1.7291
REMARK 3 L33: 4.7976 L12: -3.2005
REMARK 3 L13: 6.5172 L23: -2.0835
REMARK 3 S TENSOR
REMARK 3 S11: -0.1454 S12: -0.5204 S13: -0.0480
REMARK 3 S21: 0.2676 S22: 0.1956 S23: 0.0687
REMARK 3 S31: 0.0187 S32: -0.3701 S33: -0.0410
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6C7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000232179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
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) : 1.00000
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200 BENT, SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146602
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 66.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.60400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-19% PEG3350, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 0.1 M TRIS, PH 8.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASP A 917
REMARK 465 SER B 576
REMARK 465 ALA B 577
REMARK 465 MET B 578
REMARK 465 ASP B 917
REMARK 465 SER C 576
REMARK 465 ALA C 577
REMARK 465 MET C 578
REMARK 465 ASP C 579
REMARK 465 ASP C 580
REMARK 465 GLU C 581
REMARK 465 TYR C 582
REMARK 465 THR C 583
REMARK 465 LYS C 584
REMARK 465 LEU C 585
REMARK 465 LEU C 586
REMARK 465 HIS C 587
REMARK 465 ASP C 588
REMARK 465 GLY C 589
REMARK 465 ILE C 590
REMARK 465 ASP C 917
REMARK 465 SER D 576
REMARK 465 ALA D 577
REMARK 465 MET D 578
REMARK 465 ASP D 579
REMARK 465 ASP D 580
REMARK 465 GLU D 581
REMARK 465 ASP D 917
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 CD2 LEU C 770 C39 EOY C 1001 1.95
REMARK 500 NH1 ARG D 843 OD2 ASP D 849 2.06
REMARK 500 O ASN C 627 ND2 ASN C 631 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP D 808 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
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 652 51.13 -119.73
REMARK 500 LYS A 814 -162.64 -106.26
REMARK 500 GLU B 722 -132.99 42.00
REMARK 500 LYS B 814 -151.09 -99.52
REMARK 500 ILE B 866 -60.32 -128.04
REMARK 500 ASP C 597 136.70 -170.86
REMARK 500 ASN C 627 18.82 53.39
REMARK 500 LYS C 814 -158.11 -101.02
REMARK 500 LYS D 814 -149.46 -97.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 721 GLU B 722 145.52
REMARK 500 GLU B 722 GLY B 723 -141.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 EOY A 1001
REMARK 615 EOY B 1001
REMARK 615 EOY C 1001
REMARK 615 EOY D 1001
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 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 660 NE2
REMARK 620 2 HIS A 696 NE2 100.0
REMARK 620 3 ASP A 697 OD2 91.4 84.3
REMARK 620 4 ASP A 808 OD1 96.7 91.5 171.5
REMARK 620 5 HOH A1121 O 163.5 96.0 86.1 86.9
REMARK 620 6 HOH A1197 O 91.9 167.9 97.9 84.6 72.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 697 OD1
REMARK 620 2 HOH A1121 O 96.5
REMARK 620 3 HOH A1128 O 82.5 97.3
REMARK 620 4 HOH A1129 O 169.3 91.0 89.0
REMARK 620 5 HOH A1138 O 87.8 168.5 93.8 86.3
REMARK 620 6 HOH A1161 O 94.0 84.3 176.3 94.3 84.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 660 NE2
REMARK 620 2 HIS B 696 NE2 106.8
REMARK 620 3 ASP B 697 OD2 92.6 88.0
REMARK 620 4 ASP B 808 OD1 92.8 87.7 173.9
REMARK 620 5 HOH B1118 O 159.6 93.6 88.1 87.8
REMARK 620 6 HOH B1199 O 92.5 159.5 98.5 84.0 67.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 697 OD1
REMARK 620 2 HOH B1118 O 93.9
REMARK 620 3 HOH B1140 O 86.2 98.8
REMARK 620 4 HOH B1151 O 172.5 92.2 88.5
REMARK 620 5 HOH B1156 O 91.9 169.0 91.0 82.9
REMARK 620 6 HOH B1225 O 97.3 84.1 175.3 87.6 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 660 NE2
REMARK 620 2 HIS C 696 NE2 105.0
REMARK 620 3 ASP C 697 OD2 94.6 85.7
REMARK 620 4 ASP C 808 OD1 90.7 91.1 174.4
REMARK 620 5 HOH C1137 O 158.0 97.0 86.3 89.6
REMARK 620 6 HOH C1161 O 87.6 167.1 96.5 85.6 70.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 697 OD1
REMARK 620 2 HOH C1116 O 86.7
REMARK 620 3 HOH C1137 O 96.2 98.4
REMARK 620 4 HOH C1160 O 90.3 91.3 168.6
REMARK 620 5 HOH C1182 O 170.0 85.0 90.5 84.3
REMARK 620 6 HOH C1197 O 98.2 175.2 80.9 89.0 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 660 NE2
REMARK 620 2 HIS D 696 NE2 99.9
REMARK 620 3 ASP D 697 OD2 92.2 83.6
REMARK 620 4 ASP D 808 OD1 93.9 94.7 173.9
REMARK 620 5 HOH D1107 O 163.5 96.3 86.5 87.8
REMARK 620 6 HOH D1193 O 92.5 167.4 93.8 86.5 71.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 697 OD1
REMARK 620 2 HOH D1107 O 97.1
REMARK 620 3 HOH D1130 O 88.3 170.4
REMARK 620 4 HOH D1132 O 84.9 96.5 91.9
REMARK 620 5 HOH D1190 O 169.3 90.3 85.5 86.6
REMARK 620 6 HOH D1216 O 100.8 83.4 87.8 174.3 87.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOY A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOY B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOY C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOY D 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1003
DBREF 6C7G A 579 917 UNP O00408 PDE2A_HUMAN 323 661
DBREF 6C7G B 579 917 UNP O00408 PDE2A_HUMAN 323 661
DBREF 6C7G C 579 917 UNP O00408 PDE2A_HUMAN 323 661
DBREF 6C7G D 579 917 UNP O00408 PDE2A_HUMAN 323 661
SEQADV 6C7G SER A 576 UNP O00408 EXPRESSION TAG
SEQADV 6C7G ALA A 577 UNP O00408 EXPRESSION TAG
SEQADV 6C7G MET A 578 UNP O00408 EXPRESSION TAG
SEQADV 6C7G SER B 576 UNP O00408 EXPRESSION TAG
SEQADV 6C7G ALA B 577 UNP O00408 EXPRESSION TAG
SEQADV 6C7G MET B 578 UNP O00408 EXPRESSION TAG
SEQADV 6C7G SER C 576 UNP O00408 EXPRESSION TAG
SEQADV 6C7G ALA C 577 UNP O00408 EXPRESSION TAG
SEQADV 6C7G MET C 578 UNP O00408 EXPRESSION TAG
SEQADV 6C7G SER D 576 UNP O00408 EXPRESSION TAG
SEQADV 6C7G ALA D 577 UNP O00408 EXPRESSION TAG
SEQADV 6C7G MET D 578 UNP O00408 EXPRESSION TAG
SEQRES 1 A 342 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 A 342 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 A 342 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 A 342 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 A 342 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 A 342 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 A 342 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 A 342 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 A 342 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 A 342 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 A 342 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 A 342 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 A 342 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 A 342 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 A 342 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 A 342 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 A 342 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 A 342 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 A 342 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 A 342 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 A 342 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 A 342 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 A 342 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 A 342 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 A 342 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 A 342 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 A 342 ASP PHE LEU ASP
SEQRES 1 B 342 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 B 342 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 B 342 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 B 342 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 B 342 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 B 342 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 B 342 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 B 342 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 B 342 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 B 342 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 B 342 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 B 342 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 B 342 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 B 342 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 B 342 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 B 342 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 B 342 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 B 342 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 B 342 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 B 342 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 B 342 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 B 342 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 B 342 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 B 342 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 B 342 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 B 342 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 B 342 ASP PHE LEU ASP
SEQRES 1 C 342 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 C 342 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 C 342 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 C 342 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 C 342 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 C 342 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 C 342 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 C 342 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 C 342 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 C 342 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 C 342 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 C 342 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 C 342 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 C 342 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 C 342 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 C 342 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 C 342 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 C 342 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 C 342 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 C 342 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 C 342 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 C 342 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 C 342 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 C 342 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 C 342 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 C 342 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 C 342 ASP PHE LEU ASP
SEQRES 1 D 342 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 D 342 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 D 342 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 D 342 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 D 342 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 D 342 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 D 342 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 D 342 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 D 342 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 D 342 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 D 342 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 D 342 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 D 342 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 D 342 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 D 342 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 D 342 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 D 342 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 D 342 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 D 342 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 D 342 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 D 342 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 D 342 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 D 342 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 D 342 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 D 342 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 D 342 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 D 342 ASP PHE LEU ASP
HET EOY A1001 39
HET ZN A1002 1
HET MG A1003 1
HET EOY B1001 39
HET ZN B1002 1
HET MG B1003 1
HET EOY C1001 39
HET ZN C1002 1
HET MG C1003 1
HET EOY D1001 39
HET ZN D1002 1
HET MG D1003 1
HETNAM EOY 1-[2-CHLORO-5-(2-METHYLPROPOXY)PHENYL]-4-METHYL-N-[(3S,
HETNAM 2 EOY 5S,7S)-TRICYCLO[3.3.1.1~3,7~]DECAN-1-YL][1,2,
HETNAM 3 EOY 4]TRIAZOLO[4,3-A]QUINOXALINE-8-CARBOXAMIDE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 5 EOY 4(C31 H34 CL N5 O2)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 7 MG 4(MG 2+)
FORMUL 17 HOH *676(H2 O)
HELIX 1 AA1 SER A 576 ASP A 588 1 13
HELIX 2 AA2 PRO A 592 ILE A 596 5 5
HELIX 3 AA3 THR A 606 LEU A 610 5 5
HELIX 4 AA4 PRO A 611 ASP A 613 5 3
HELIX 5 AA5 ASP A 614 MET A 626 1 13
HELIX 6 AA6 ASN A 627 TYR A 632 1 6
HELIX 7 AA7 ASP A 635 GLY A 649 1 15
HELIX 8 AA8 ASN A 657 GLU A 676 1 20
HELIX 9 AA9 LEU A 677 TYR A 680 5 4
HELIX 10 AB1 GLU A 682 HIS A 696 1 15
HELIX 11 AB2 ASN A 704 SER A 711 1 8
HELIX 12 AB3 SER A 713 SER A 720 1 8
HELIX 13 AB4 SER A 724 ASN A 739 1 16
HELIX 14 AB5 SER A 750 ALA A 767 1 18
HELIX 15 AB6 ASP A 769 GLY A 787 1 19
HELIX 16 AB7 ASN A 792 LEU A 809 1 18
HELIX 17 AB8 SER A 810 LYS A 814 5 5
HELIX 18 AB9 GLY A 815 MET A 840 1 26
HELIX 19 AC1 MET A 845 ASP A 849 5 5
HELIX 20 AC2 TYR A 854 ILE A 866 1 13
HELIX 21 AC3 ILE A 866 PHE A 878 1 13
HELIX 22 AC4 ALA A 881 SER A 899 1 19
HELIX 23 AC5 HIS A 900 THR A 903 5 4
HELIX 24 AC6 ASP B 580 ASP B 588 1 9
HELIX 25 AC7 PRO B 592 ASP B 597 1 6
HELIX 26 AC8 THR B 606 LEU B 610 5 5
HELIX 27 AC9 PRO B 611 ASP B 613 5 3
HELIX 28 AD1 ASP B 614 MET B 626 1 13
HELIX 29 AD2 ASN B 627 TYR B 632 1 6
HELIX 30 AD3 ASP B 635 GLY B 649 1 15
HELIX 31 AD4 ASN B 657 GLU B 676 1 20
HELIX 32 AD5 LEU B 677 TYR B 680 5 4
HELIX 33 AD6 GLU B 682 HIS B 696 1 15
HELIX 34 AD7 ASN B 704 SER B 711 1 8
HELIX 35 AD8 SER B 713 TYR B 719 1 7
HELIX 36 AD9 SER B 724 ASN B 739 1 16
HELIX 37 AE1 SER B 750 ALA B 767 1 18
HELIX 38 AE2 ASP B 769 GLY B 787 1 19
HELIX 39 AE3 ASN B 792 LEU B 809 1 18
HELIX 40 AE4 SER B 810 LYS B 814 5 5
HELIX 41 AE5 GLY B 815 GLY B 841 1 27
HELIX 42 AE6 MET B 845 ASP B 849 5 5
HELIX 43 AE7 TYR B 854 ILE B 866 1 13
HELIX 44 AE8 ILE B 866 PHE B 878 1 13
HELIX 45 AE9 ALA B 881 SER B 899 1 19
HELIX 46 AF1 HIS B 900 THR B 903 5 4
HELIX 47 AF2 PRO C 592 ILE C 596 5 5
HELIX 48 AF3 THR C 606 LEU C 610 5 5
HELIX 49 AF4 PRO C 611 ASP C 613 5 3
HELIX 50 AF5 ASP C 614 MET C 626 1 13
HELIX 51 AF6 ASN C 627 TYR C 632 1 6
HELIX 52 AF7 ASP C 635 GLY C 649 1 15
HELIX 53 AF8 ASN C 657 LEU C 675 1 19
HELIX 54 AF9 GLU C 676 TYR C 680 5 5
HELIX 55 AG1 GLU C 682 HIS C 696 1 15
HELIX 56 AG2 ASN C 704 SER C 711 1 8
HELIX 57 AG3 SER C 713 SER C 720 1 8
HELIX 58 AG4 SER C 724 ASN C 739 1 16
HELIX 59 AG5 SER C 750 ALA C 767 1 18
HELIX 60 AG6 ASP C 769 GLY C 787 1 19
HELIX 61 AG7 ASN C 792 LEU C 809 1 18
HELIX 62 AG8 SER C 810 LYS C 814 5 5
HELIX 63 AG9 GLY C 815 MET C 840 1 26
HELIX 64 AH1 MET C 845 ASP C 849 5 5
HELIX 65 AH2 TYR C 854 ILE C 866 1 13
HELIX 66 AH3 ILE C 866 PHE C 878 1 13
HELIX 67 AH4 ALA C 881 SER C 899 1 19
HELIX 68 AH5 HIS C 900 THR C 903 5 4
HELIX 69 AH6 THR D 583 GLY D 589 1 7
HELIX 70 AH7 PRO D 592 ASP D 597 1 6
HELIX 71 AH8 THR D 606 LEU D 610 5 5
HELIX 72 AH9 PRO D 611 ASP D 613 5 3
HELIX 73 AI1 ASP D 614 MET D 626 1 13
HELIX 74 AI2 ASN D 627 TYR D 632 1 6
HELIX 75 AI3 ASP D 635 GLY D 649 1 15
HELIX 76 AI4 ASN D 657 LEU D 675 1 19
HELIX 77 AI5 GLU D 676 TYR D 680 5 5
HELIX 78 AI6 GLU D 682 HIS D 696 1 15
HELIX 79 AI7 ASN D 704 SER D 711 1 8
HELIX 80 AI8 SER D 713 SER D 720 1 8
HELIX 81 AI9 SER D 724 ASN D 739 1 16
HELIX 82 AJ1 SER D 750 ALA D 767 1 18
HELIX 83 AJ2 ASP D 769 GLY D 787 1 19
HELIX 84 AJ3 ASN D 792 LEU D 809 1 18
HELIX 85 AJ4 SER D 810 LYS D 814 5 5
HELIX 86 AJ5 GLY D 815 MET D 840 1 26
HELIX 87 AJ6 MET D 845 ASP D 849 5 5
HELIX 88 AJ7 TYR D 854 ILE D 866 1 13
HELIX 89 AJ8 ILE D 866 PHE D 878 1 13
HELIX 90 AJ9 ALA D 881 SER D 899 1 19
HELIX 91 AK1 HIS D 900 THR D 903 5 4
LINK NE2 HIS A 660 ZN ZN A1002 1555 1555 2.06
LINK NE2 HIS A 696 ZN ZN A1002 1555 1555 2.09
LINK OD2 ASP A 697 ZN ZN A1002 1555 1555 2.09
LINK OD1 ASP A 697 MG MG A1003 1555 1555 2.02
LINK OD1 ASP A 808 ZN ZN A1002 1555 1555 2.13
LINK ZN ZN A1002 O HOH A1121 1555 1555 2.43
LINK ZN ZN A1002 O HOH A1197 1555 1555 2.16
LINK MG MG A1003 O HOH A1121 1555 1555 2.15
LINK MG MG A1003 O HOH A1128 1555 1555 1.99
LINK MG MG A1003 O HOH A1129 1555 1555 2.11
LINK MG MG A1003 O HOH A1138 1555 1555 2.18
LINK MG MG A1003 O HOH A1161 1555 1555 2.22
LINK NE2 HIS B 660 ZN ZN B1002 1555 1555 2.17
LINK NE2 HIS B 696 ZN ZN B1002 1555 1555 2.05
LINK OD2 ASP B 697 ZN ZN B1002 1555 1555 2.10
LINK OD1 ASP B 697 MG MG B1003 1555 1555 2.02
LINK OD1 ASP B 808 ZN ZN B1002 1555 1555 2.19
LINK ZN ZN B1002 O HOH B1118 1555 1555 2.26
LINK ZN ZN B1002 O HOH B1199 1555 1555 2.48
LINK MG MG B1003 O HOH B1118 1555 1555 2.26
LINK MG MG B1003 O HOH B1140 1555 1555 1.93
LINK MG MG B1003 O HOH B1151 1555 1555 2.18
LINK MG MG B1003 O HOH B1156 1555 1555 2.16
LINK MG MG B1003 O HOH B1225 1555 1555 2.01
LINK NE2 HIS C 660 ZN ZN C1002 1555 1555 2.04
LINK NE2 HIS C 696 ZN ZN C1002 1555 1555 2.06
LINK OD2 ASP C 697 ZN ZN C1002 1555 1555 2.09
LINK OD1 ASP C 697 MG MG C1003 1555 1555 2.00
LINK OD1 ASP C 808 ZN ZN C1002 1555 1555 2.13
LINK ZN ZN C1002 O HOH C1137 1555 1555 2.42
LINK ZN ZN C1002 O HOH C1161 1555 1555 2.17
LINK MG MG C1003 O HOH C1116 1555 1555 2.02
LINK MG MG C1003 O HOH C1137 1555 1555 2.14
LINK MG MG C1003 O HOH C1160 1555 1555 2.02
LINK MG MG C1003 O HOH C1182 1555 1555 2.08
LINK MG MG C1003 O HOH C1197 1555 1555 2.07
LINK NE2 HIS D 660 ZN ZN D1002 1555 1555 2.02
LINK NE2 HIS D 696 ZN ZN D1002 1555 1555 2.10
LINK OD2 ASP D 697 ZN ZN D1002 1555 1555 1.99
LINK OD1 ASP D 697 MG MG D1003 1555 1555 1.97
LINK OD1 ASP D 808 ZN ZN D1002 1555 1555 1.97
LINK ZN ZN D1002 O HOH D1107 1555 1555 2.36
LINK ZN ZN D1002 O HOH D1193 1555 1555 2.20
LINK MG MG D1003 O HOH D1107 1555 1555 2.24
LINK MG MG D1003 O HOH D1130 1555 1555 2.21
LINK MG MG D1003 O HOH D1132 1555 1555 1.98
LINK MG MG D1003 O HOH D1190 1555 1555 2.06
LINK MG MG D1003 O HOH D1216 1555 1555 2.10
SITE 1 AC1 12 THR A 768 ASP A 808 LEU A 809 GLN A 812
SITE 2 AC1 12 ILE A 826 PHE A 830 MET A 847 GLN A 859
SITE 3 AC1 12 PHE A 862 HOH A1107 HOH A1158 HOH A1206
SITE 1 AC2 6 HIS A 660 HIS A 696 ASP A 697 ASP A 808
SITE 2 AC2 6 HOH A1121 HOH A1197
SITE 1 AC3 6 ASP A 697 HOH A1121 HOH A1128 HOH A1129
SITE 2 AC3 6 HOH A1138 HOH A1161
SITE 1 AC4 11 THR B 768 ASP B 808 LEU B 809 GLN B 812
SITE 2 AC4 11 ILE B 826 PHE B 830 PHE B 862 HOH B1107
SITE 3 AC4 11 HOH B1155 HOH B1171 HOH B1196
SITE 1 AC5 6 HIS B 660 HIS B 696 ASP B 697 ASP B 808
SITE 2 AC5 6 HOH B1118 HOH B1199
SITE 1 AC6 6 ASP B 697 HOH B1118 HOH B1140 HOH B1151
SITE 2 AC6 6 HOH B1156 HOH B1225
SITE 1 AC7 12 THR C 768 LEU C 770 THR C 805 LEU C 809
SITE 2 AC7 12 GLN C 812 ILE C 826 PHE C 830 PHE C 862
SITE 3 AC7 12 HOH C1104 HOH C1107 HOH C1148 HOH C1154
SITE 1 AC8 6 HIS C 660 HIS C 696 ASP C 697 ASP C 808
SITE 2 AC8 6 HOH C1137 HOH C1161
SITE 1 AC9 6 ASP C 697 HOH C1116 HOH C1137 HOH C1160
SITE 2 AC9 6 HOH C1182 HOH C1197
SITE 1 AD1 11 THR D 768 LEU D 770 ASP D 808 GLN D 812
SITE 2 AD1 11 ILE D 826 PHE D 830 MET D 847 PHE D 862
SITE 3 AD1 11 HOH D1120 HOH D1161 HOH D1165
SITE 1 AD2 6 HIS D 660 HIS D 696 ASP D 697 ASP D 808
SITE 2 AD2 6 HOH D1107 HOH D1193
SITE 1 AD3 6 ASP D 697 HOH D1107 HOH D1130 HOH D1132
SITE 2 AD3 6 HOH D1190 HOH D1216
CRYST1 56.141 73.992 91.743 109.48 91.49 91.04 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017812 0.000324 0.000605 0.00000
SCALE2 0.000000 0.013517 0.004791 0.00000
SCALE3 0.000000 0.000000 0.011568 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
