LinkDB: 5TZZ
Original site: 5TZZ
Chemical substance (3) PDB-CCD (3) Chemical reaction (1) KEGG ENZYME (1) Gene (1) KEGG GENES (1) Protein sequence (6) UniProt (1) SWISS-PROT (1) PDBSTR (4) DNA sequence (2) EMBL (2) Protein domain (7) InterPro (5) PROSITE (2) Literature (1) PubMed (1) All databases (21)
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HEADER HYDROLASE/HYDROLASE INHIBITOR 22-NOV-16 5TZZ
TITLE CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX WITH 1-[(3-
TITLE 2 BROMO-4-FLUOROPHENYL)CARBONYL]-3,3-DIFLUORO-5-{5-METHYL-[1,2,
TITLE 3 4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL}PIPERIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-DEPENDENT 3',5'-CYCLIC PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 323-663;
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: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BACULOVIRUS INSECT CELL HI5;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID
KEYWDS PHOSPHODIESTERASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.XU,K.AERTGEERTS
REVDAT 3 06-MAR-24 5TZZ 1 LINK
REVDAT 2 22-MAR-17 5TZZ 1 JRNL
REVDAT 1 22-FEB-17 5TZZ 0
JRNL AUTH L.GOMEZ,M.E.MASSARI,T.VICKERS,G.FREESTONE,W.VERNIER,K.LY,
JRNL AUTH 2 R.XU,M.MCCARRICK,T.MARRONE,M.METZ,Y.G.YAN,Z.W.YODER,R.LEMUS,
JRNL AUTH 3 N.J.BROADBENT,R.BARIDO,N.WARREN,K.SCHMELZER,D.NEUL,D.LEE,
JRNL AUTH 4 C.B.ANDERSEN,K.SEBRING,K.AERTGEERTS,X.ZHOU,A.TABATABAEI,
JRNL AUTH 5 M.PETERS,J.G.BREITENBUCHER
JRNL TITL DESIGN AND SYNTHESIS OF NOVEL AND SELECTIVE
JRNL TITL 2 PHOSPHODIESTERASE 2 (PDE2A) INHIBITORS FOR THE TREATMENT OF
JRNL TITL 3 MEMORY DISORDERS.
JRNL REF J. MED. CHEM. V. 60 2037 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28165743
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01793
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1-2155_1692: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 170005
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 8378
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 55.7560 - 4.9705 0.98 5559 295 0.1769 0.1805
REMARK 3 2 4.9705 - 3.9455 0.98 5542 321 0.1459 0.1838
REMARK 3 3 3.9455 - 3.4469 0.98 5499 324 0.1546 0.1779
REMARK 3 4 3.4469 - 3.1318 0.97 5514 301 0.1668 0.1938
REMARK 3 5 3.1318 - 2.9073 0.97 5527 250 0.1831 0.2182
REMARK 3 6 2.9073 - 2.7359 0.97 5506 301 0.1771 0.2146
REMARK 3 7 2.7359 - 2.5989 0.97 5458 318 0.1856 0.2227
REMARK 3 8 2.5989 - 2.4857 0.97 5516 292 0.1837 0.2271
REMARK 3 9 2.4857 - 2.3901 0.97 5413 311 0.1863 0.2512
REMARK 3 10 2.3901 - 2.3076 0.96 5489 276 0.1862 0.2353
REMARK 3 11 2.3076 - 2.2354 0.97 5473 265 0.1934 0.2197
REMARK 3 12 2.2354 - 2.1715 0.96 5476 289 0.1859 0.2227
REMARK 3 13 2.1715 - 2.1144 0.96 5501 263 0.1913 0.2320
REMARK 3 14 2.1144 - 2.0628 0.96 5436 271 0.2004 0.2414
REMARK 3 15 2.0628 - 2.0159 0.96 5427 312 0.2044 0.2409
REMARK 3 16 2.0159 - 1.9730 0.96 5448 276 0.2173 0.2626
REMARK 3 17 1.9730 - 1.9335 0.96 5466 246 0.2191 0.2565
REMARK 3 18 1.9335 - 1.8970 0.96 5458 258 0.2278 0.2930
REMARK 3 19 1.8970 - 1.8631 0.95 5417 269 0.2423 0.3000
REMARK 3 20 1.8631 - 1.8315 0.96 5444 292 0.2513 0.2982
REMARK 3 21 1.8315 - 1.8020 0.95 5407 276 0.2596 0.3200
REMARK 3 22 1.8020 - 1.7743 0.95 5408 274 0.2589 0.3040
REMARK 3 23 1.7743 - 1.7482 0.95 5314 286 0.2689 0.3430
REMARK 3 24 1.7482 - 1.7236 0.95 5462 293 0.2787 0.3120
REMARK 3 25 1.7236 - 1.7003 0.95 5358 260 0.2799 0.3174
REMARK 3 26 1.7003 - 1.6782 0.95 5365 257 0.2909 0.3369
REMARK 3 27 1.6782 - 1.6572 0.95 5390 250 0.2837 0.3325
REMARK 3 28 1.6572 - 1.6372 0.94 5387 276 0.2948 0.3333
REMARK 3 29 1.6372 - 1.6182 0.86 4882 260 0.3077 0.3425
REMARK 3 30 1.6182 - 1.6000 0.73 4085 216 0.3061 0.3371
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.56
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 : 0.006 11353
REMARK 3 ANGLE : 0.812 15336
REMARK 3 CHIRALITY : 0.044 1634
REMARK 3 PLANARITY : 0.005 1978
REMARK 3 DIHEDRAL : 17.531 4190
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 35
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 576 THROUGH 635 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2345 -15.5721 -1.7465
REMARK 3 T TENSOR
REMARK 3 T11: 0.1025 T22: 0.1661
REMARK 3 T33: 0.1521 T12: -0.0308
REMARK 3 T13: 0.0155 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 1.3750 L22: 1.9184
REMARK 3 L33: 1.7634 L12: 0.4062
REMARK 3 L13: 0.4009 L23: 0.4068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0837 S12: -0.1927 S13: -0.2448
REMARK 3 S21: 0.1641 S22: -0.0570 S23: 0.0408
REMARK 3 S31: 0.2093 S32: -0.1597 S33: -0.0120
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 636 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6240 -4.7467 -10.3418
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.0687
REMARK 3 T33: 0.0768 T12: -0.0030
REMARK 3 T13: 0.0121 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.7381 L22: 0.8826
REMARK 3 L33: 1.0399 L12: 0.0840
REMARK 3 L13: 0.2576 L23: 0.0106
REMARK 3 S TENSOR
REMARK 3 S11: 0.0291 S12: 0.0327 S13: -0.0368
REMARK 3 S21: -0.0615 S22: 0.0146 S23: 0.0476
REMARK 3 S31: 0.0207 S32: -0.0048 S33: -0.0442
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8145 15.7920 -5.2272
REMARK 3 T TENSOR
REMARK 3 T11: 0.2742 T22: 0.1172
REMARK 3 T33: 0.2950 T12: 0.0042
REMARK 3 T13: -0.0074 T23: -0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 3.9604 L22: 3.9670
REMARK 3 L33: 1.2062 L12: -3.6497
REMARK 3 L13: 0.2619 L23: -0.6903
REMARK 3 S TENSOR
REMARK 3 S11: -0.1556 S12: -0.2667 S13: 0.8668
REMARK 3 S21: 0.0922 S22: 0.0867 S23: -0.1886
REMARK 3 S31: -0.4714 S32: 0.0591 S33: -0.0222
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9520 7.8137 -4.9045
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.0631
REMARK 3 T33: 0.1279 T12: 0.0043
REMARK 3 T13: 0.0219 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 4.0043 L22: 4.5167
REMARK 3 L33: 4.8914 L12: -2.0287
REMARK 3 L13: 2.4912 L23: -2.6926
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: -0.0271 S13: 0.1767
REMARK 3 S21: -0.1381 S22: -0.0285 S23: 0.2200
REMARK 3 S31: -0.1422 S32: -0.0976 S33: -0.0220
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 816 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2889 -1.9623 8.0572
REMARK 3 T TENSOR
REMARK 3 T11: 0.1476 T22: 0.2128
REMARK 3 T33: 0.0950 T12: -0.0037
REMARK 3 T13: -0.0324 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 6.7323 L22: 2.1105
REMARK 3 L33: 3.3488 L12: -0.4959
REMARK 3 L13: -1.7389 L23: 0.6899
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: -0.7174 S13: -0.0148
REMARK 3 S21: 0.2030 S22: 0.0060 S23: -0.1394
REMARK 3 S31: -0.0153 S32: 0.5801 S33: 0.0308
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 840 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9074 8.7870 6.5803
REMARK 3 T TENSOR
REMARK 3 T11: 0.2133 T22: 0.1454
REMARK 3 T33: 0.1122 T12: -0.0226
REMARK 3 T13: 0.0008 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 4.7588 L22: 1.7418
REMARK 3 L33: 2.0030 L12: -1.0912
REMARK 3 L13: 1.1729 L23: -0.0139
REMARK 3 S TENSOR
REMARK 3 S11: -0.0889 S12: -0.3164 S13: 0.4116
REMARK 3 S21: 0.1228 S22: 0.0141 S23: -0.1382
REMARK 3 S31: -0.2270 S32: 0.1558 S33: 0.0708
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 879 THROUGH 917 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0416 4.4558 20.4248
REMARK 3 T TENSOR
REMARK 3 T11: 0.3124 T22: 0.3939
REMARK 3 T33: 0.1807 T12: 0.0423
REMARK 3 T13: 0.0242 T23: -0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 4.6947 L22: 0.2078
REMARK 3 L33: 3.4926 L12: -0.9021
REMARK 3 L13: 4.4366 L23: -0.7263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0061 S12: -0.3678 S13: 0.0701
REMARK 3 S21: 0.1182 S22: 0.0288 S23: -0.0647
REMARK 3 S31: -0.0410 S32: -0.1356 S33: -0.0283
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 578 THROUGH 635 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8877 -19.0409 -39.5911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1851 T22: 0.1362
REMARK 3 T33: 0.2025 T12: 0.0665
REMARK 3 T13: -0.0011 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 1.4224 L22: 2.5087
REMARK 3 L33: 3.8332 L12: -0.4669
REMARK 3 L13: 0.2206 L23: -1.2734
REMARK 3 S TENSOR
REMARK 3 S11: 0.1079 S12: 0.0139 S13: -0.2396
REMARK 3 S21: -0.2073 S22: -0.0827 S23: -0.0683
REMARK 3 S31: 0.4297 S32: 0.2927 S33: -0.0203
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 636 THROUGH 695 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6688 -9.4519 -36.9814
REMARK 3 T TENSOR
REMARK 3 T11: 0.1255 T22: 0.0760
REMARK 3 T33: 0.1120 T12: 0.0373
REMARK 3 T13: -0.0041 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.8995 L22: 1.4661
REMARK 3 L33: 1.6956 L12: -0.2035
REMARK 3 L13: 0.3104 L23: 0.0961
REMARK 3 S TENSOR
REMARK 3 S11: 0.0664 S12: 0.0374 S13: -0.1524
REMARK 3 S21: -0.0203 S22: 0.0329 S23: -0.1312
REMARK 3 S31: 0.1171 S32: 0.1820 S33: -0.0710
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 696 THROUGH 738 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4802 -1.3090 -28.5057
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.1288
REMARK 3 T33: 0.1217 T12: 0.0210
REMARK 3 T13: 0.0461 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 4.1643 L22: 2.4771
REMARK 3 L33: 2.8741 L12: -0.4570
REMARK 3 L13: 0.5350 L23: 0.2329
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: -0.2667 S13: 0.2133
REMARK 3 S21: 0.2621 S22: 0.0359 S23: 0.3575
REMARK 3 S31: -0.2607 S32: -0.2514 S33: 0.0119
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 739 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0272 -5.3073 -23.6244
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.1329
REMARK 3 T33: 0.1203 T12: 0.0162
REMARK 3 T13: 0.0123 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 1.6474 L22: 2.4376
REMARK 3 L33: 3.1936 L12: -0.1512
REMARK 3 L13: 0.8520 L23: -0.3178
REMARK 3 S TENSOR
REMARK 3 S11: 0.0464 S12: -0.1575 S13: -0.2161
REMARK 3 S21: 0.2624 S22: 0.0761 S23: -0.1332
REMARK 3 S31: -0.0074 S32: 0.2090 S33: -0.0926
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0182 12.9181 -40.4162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.0977
REMARK 3 T33: 0.1794 T12: 0.0085
REMARK 3 T13: 0.0204 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 7.3209 L22: 3.1402
REMARK 3 L33: 1.4759 L12: 3.0636
REMARK 3 L13: -0.8515 L23: -0.9593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0383 S12: 0.2612 S13: 0.7684
REMARK 3 S21: -0.1874 S22: 0.2296 S23: 0.1647
REMARK 3 S31: -0.4336 S32: -0.1374 S33: -0.1667
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0086 4.2220 -40.1284
REMARK 3 T TENSOR
REMARK 3 T11: 0.1299 T22: 0.0600
REMARK 3 T33: 0.1185 T12: 0.0164
REMARK 3 T13: 0.0322 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 6.6330 L22: 4.6869
REMARK 3 L33: 3.3054 L12: 3.4755
REMARK 3 L13: 3.0918 L23: 2.3849
REMARK 3 S TENSOR
REMARK 3 S11: 0.0529 S12: -0.0228 S13: 0.1081
REMARK 3 S21: -0.1329 S22: -0.0116 S23: -0.2363
REMARK 3 S31: -0.2549 S32: 0.0041 S33: -0.0234
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 816 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5742 1.6104 -48.2966
REMARK 3 T TENSOR
REMARK 3 T11: 0.1940 T22: 0.2536
REMARK 3 T33: 0.1265 T12: 0.0559
REMARK 3 T13: -0.0136 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 2.7972 L22: 0.8584
REMARK 3 L33: 0.5797 L12: 0.4193
REMARK 3 L13: 0.0737 L23: 0.5055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: 0.4681 S13: 0.2297
REMARK 3 S21: -0.1748 S22: -0.0319 S23: 0.1253
REMARK 3 S31: -0.1199 S32: -0.2045 S33: -0.0398
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1799 -1.3254 -61.5487
REMARK 3 T TENSOR
REMARK 3 T11: 0.3079 T22: 0.4585
REMARK 3 T33: 0.1151 T12: 0.0407
REMARK 3 T13: 0.0354 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 7.1822 L22: 0.6704
REMARK 3 L33: 2.5012 L12: 1.4390
REMARK 3 L13: 4.6131 L23: 0.9739
REMARK 3 S TENSOR
REMARK 3 S11: -0.2763 S12: 0.1665 S13: 0.1712
REMARK 3 S21: -0.2942 S22: 0.0903 S23: 0.1209
REMARK 3 S31: -0.1550 S32: 0.1421 S33: 0.1236
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 590 THROUGH 675 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7625 -46.4875 -38.8032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.2428
REMARK 3 T33: 0.3144 T12: 0.0633
REMARK 3 T13: 0.0491 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.4545 L22: 1.0907
REMARK 3 L33: 1.6904 L12: -0.0594
REMARK 3 L13: -0.1987 L23: -0.7500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0901 S13: -0.2927
REMARK 3 S21: -0.1990 S22: -0.1853 S23: -0.4622
REMARK 3 S31: 0.2653 S32: 0.5028 S33: 0.0740
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 676 THROUGH 695 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8792 -34.5981 -33.3100
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.3541
REMARK 3 T33: 0.2657 T12: -0.0878
REMARK 3 T13: 0.0258 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 3.9037 L22: 4.0185
REMARK 3 L33: 0.8429 L12: 1.3695
REMARK 3 L13: 0.2741 L23: -0.3577
REMARK 3 S TENSOR
REMARK 3 S11: 0.1302 S12: -0.0283 S13: 0.0253
REMARK 3 S21: -0.0392 S22: -0.0740 S23: -0.6217
REMARK 3 S31: -0.1006 S32: 0.7966 S33: 0.0147
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 696 THROUGH 724 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8123 -39.0485 -28.9872
REMARK 3 T TENSOR
REMARK 3 T11: 0.1086 T22: 0.0938
REMARK 3 T33: 0.1165 T12: -0.0131
REMARK 3 T13: -0.0071 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 5.7177 L22: 1.9418
REMARK 3 L33: 3.1425 L12: -1.6977
REMARK 3 L13: -1.2397 L23: -0.4589
REMARK 3 S TENSOR
REMARK 3 S11: -0.0390 S12: -0.0048 S13: -0.0631
REMARK 3 S21: 0.1194 S22: 0.0824 S23: 0.1278
REMARK 3 S31: -0.0797 S32: -0.1666 S33: -0.0424
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 725 THROUGH 750 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0007 -43.7777 -23.0584
REMARK 3 T TENSOR
REMARK 3 T11: 0.1035 T22: 0.1590
REMARK 3 T33: 0.1876 T12: -0.0145
REMARK 3 T13: -0.0146 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 3.8403 L22: 1.0411
REMARK 3 L33: 2.1797 L12: -0.2162
REMARK 3 L13: 0.8556 L23: 0.2180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.4278 S13: -0.2836
REMARK 3 S21: 0.1613 S22: 0.0463 S23: -0.2108
REMARK 3 S31: 0.1219 S32: 0.1243 S33: -0.0301
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 751 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5494 -34.4433 -23.4944
REMARK 3 T TENSOR
REMARK 3 T11: 0.1105 T22: 0.2575
REMARK 3 T33: 0.1828 T12: -0.0323
REMARK 3 T13: 0.0349 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 7.4541 L22: 2.9592
REMARK 3 L33: 6.5023 L12: -1.8652
REMARK 3 L13: 5.6461 L23: -1.0805
REMARK 3 S TENSOR
REMARK 3 S11: -0.2161 S12: -0.6900 S13: 0.3244
REMARK 3 S21: 0.1502 S22: 0.1208 S23: -0.3936
REMARK 3 S31: -0.2845 S32: 0.1282 S33: 0.1039
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 769 THROUGH 792 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6805 -20.7050 -36.0657
REMARK 3 T TENSOR
REMARK 3 T11: 0.4465 T22: 0.1884
REMARK 3 T33: 0.3275 T12: -0.0105
REMARK 3 T13: 0.1577 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 3.5742 L22: 3.0722
REMARK 3 L33: 1.7419 L12: 0.8904
REMARK 3 L13: 0.4935 L23: -0.3089
REMARK 3 S TENSOR
REMARK 3 S11: 0.2461 S12: 0.0083 S13: 0.7591
REMARK 3 S21: 0.0329 S22: -0.1051 S23: -0.4382
REMARK 3 S31: -0.7772 S32: 0.1837 S33: -0.1545
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 793 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0216 -30.0834 -38.6231
REMARK 3 T TENSOR
REMARK 3 T11: 0.1495 T22: 0.0975
REMARK 3 T33: 0.1592 T12: -0.0195
REMARK 3 T13: 0.0558 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 3.9557 L22: 4.3830
REMARK 3 L33: 3.3122 L12: 0.7442
REMARK 3 L13: 1.0100 L23: 1.3142
REMARK 3 S TENSOR
REMARK 3 S11: 0.1403 S12: -0.1260 S13: 0.2757
REMARK 3 S21: 0.0876 S22: -0.0749 S23: -0.2342
REMARK 3 S31: -0.4530 S32: 0.0055 S33: -0.0446
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 816 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0666 -42.1058 -47.6805
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.2422
REMARK 3 T33: 0.1559 T12: -0.0019
REMARK 3 T13: -0.0422 T23: -0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 6.6689 L22: 2.2730
REMARK 3 L33: 2.4103 L12: 0.9355
REMARK 3 L13: -1.7415 L23: -1.1697
REMARK 3 S TENSOR
REMARK 3 S11: 0.0748 S12: 0.5953 S13: -0.3925
REMARK 3 S21: -0.1497 S22: -0.0639 S23: 0.0751
REMARK 3 S31: 0.1815 S32: -0.6000 S33: 0.0503
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 840 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7052 -30.7767 -47.6694
REMARK 3 T TENSOR
REMARK 3 T11: 0.2481 T22: 0.2045
REMARK 3 T33: 0.1085 T12: 0.0686
REMARK 3 T13: 0.0409 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 3.4598 L22: 2.4236
REMARK 3 L33: 2.1074 L12: 1.0231
REMARK 3 L13: 0.0385 L23: -0.4130
REMARK 3 S TENSOR
REMARK 3 S11: 0.1306 S12: 0.1961 S13: 0.2578
REMARK 3 S21: -0.1834 S22: -0.0308 S23: 0.1241
REMARK 3 S31: -0.1807 S32: -0.4262 S33: -0.1102
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 879 THROUGH 916 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5042 -36.3008 -61.1033
REMARK 3 T TENSOR
REMARK 3 T11: 0.2956 T22: 0.3197
REMARK 3 T33: 0.1303 T12: 0.0452
REMARK 3 T13: 0.0349 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 7.1093 L22: 1.9972
REMARK 3 L33: 4.4206 L12: 3.6214
REMARK 3 L13: 5.5169 L23: 2.4989
REMARK 3 S TENSOR
REMARK 3 S11: -0.1301 S12: 0.2186 S13: 0.0954
REMARK 3 S21: -0.2761 S22: 0.0956 S23: 0.0371
REMARK 3 S31: -0.1770 S32: 0.0060 S33: 0.0094
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 582 THROUGH 611 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7845 -44.9232 8.6656
REMARK 3 T TENSOR
REMARK 3 T11: 0.2669 T22: 0.3755
REMARK 3 T33: 0.3715 T12: -0.0709
REMARK 3 T13: 0.1194 T23: 0.1065
REMARK 3 L TENSOR
REMARK 3 L11: 2.2064 L22: 1.3194
REMARK 3 L33: 2.1899 L12: -1.0538
REMARK 3 L13: -1.1228 L23: 0.8749
REMARK 3 S TENSOR
REMARK 3 S11: -0.1859 S12: -0.1992 S13: -0.5453
REMARK 3 S21: 0.4604 S22: -0.0448 S23: 0.6183
REMARK 3 S31: 0.5279 S32: -0.3414 S33: 0.2467
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 612 THROUGH 674 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4082 -43.6592 -0.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1624
REMARK 3 T33: 0.2942 T12: -0.0383
REMARK 3 T13: 0.0292 T23: 0.0571
REMARK 3 L TENSOR
REMARK 3 L11: 0.8461 L22: 1.5595
REMARK 3 L33: 1.4074 L12: 0.2816
REMARK 3 L13: 0.0213 L23: 0.8255
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.2725 S13: -0.4049
REMARK 3 S21: 0.1057 S22: -0.0809 S23: 0.3941
REMARK 3 S31: 0.2114 S32: -0.2919 S33: 0.0449
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 675 THROUGH 695 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2216 -31.8667 -5.2215
REMARK 3 T TENSOR
REMARK 3 T11: 0.0822 T22: 0.1952
REMARK 3 T33: 0.2080 T12: 0.0068
REMARK 3 T13: 0.0020 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 3.1062 L22: 5.0226
REMARK 3 L33: 2.6493 L12: -1.2553
REMARK 3 L13: -0.0707 L23: 0.6421
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: -0.2615 S13: -0.2314
REMARK 3 S21: -0.1281 S22: 0.0641 S23: 0.6966
REMARK 3 S31: -0.1978 S32: -0.3735 S33: 0.0347
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 696 THROUGH 724 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3354 -37.3270 -9.1658
REMARK 3 T TENSOR
REMARK 3 T11: 0.0829 T22: 0.0810
REMARK 3 T33: 0.1384 T12: -0.0000
REMARK 3 T13: 0.0043 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 5.4716 L22: 1.3941
REMARK 3 L33: 3.2370 L12: 0.3660
REMARK 3 L13: -1.5140 L23: 0.8979
REMARK 3 S TENSOR
REMARK 3 S11: -0.0760 S12: 0.0647 S13: -0.2135
REMARK 3 S21: -0.0572 S22: 0.0549 S23: -0.1683
REMARK 3 S31: -0.0004 S32: 0.1780 S33: 0.0146
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 725 THROUGH 750 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0754 -43.1336 -14.1031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1015 T22: 0.0963
REMARK 3 T33: 0.1843 T12: 0.0102
REMARK 3 T13: -0.0129 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 3.8270 L22: 1.0147
REMARK 3 L33: 2.3950 L12: -0.0353
REMARK 3 L13: 0.5351 L23: 0.3669
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: 0.2868 S13: -0.4303
REMARK 3 S21: -0.0814 S22: -0.0180 S23: 0.1109
REMARK 3 S31: 0.0942 S32: -0.0868 S33: -0.0047
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 751 THROUGH 768 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5594 -34.0223 -15.4210
REMARK 3 T TENSOR
REMARK 3 T11: 0.1044 T22: 0.2006
REMARK 3 T33: 0.1915 T12: -0.0019
REMARK 3 T13: 0.0164 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 7.7886 L22: 3.9208
REMARK 3 L33: 3.6928 L12: 3.3453
REMARK 3 L13: 5.1075 L23: 2.4973
REMARK 3 S TENSOR
REMARK 3 S11: -0.2287 S12: 0.6177 S13: 0.0604
REMARK 3 S21: -0.1774 S22: 0.2152 S23: 0.2627
REMARK 3 S31: -0.2043 S32: 0.1836 S33: 0.0021
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 769 THROUGH 786 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6060 -18.2280 -4.4763
REMARK 3 T TENSOR
REMARK 3 T11: 0.0873 T22: 0.1295
REMARK 3 T33: 0.1370 T12: 0.0005
REMARK 3 T13: 0.0192 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 8.1741 L22: 4.7606
REMARK 3 L33: 1.0376 L12: -4.4053
REMARK 3 L13: 0.2478 L23: -0.2626
REMARK 3 S TENSOR
REMARK 3 S11: -0.0745 S12: 0.1377 S13: 0.5632
REMARK 3 S21: 0.0730 S22: -0.0272 S23: -0.3845
REMARK 3 S31: -0.1032 S32: 0.0483 S33: 0.0792
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 787 THROUGH 815 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1225 -24.7692 -2.7709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0508 T22: 0.1216
REMARK 3 T33: 0.1317 T12: -0.0039
REMARK 3 T13: 0.0287 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 3.0023 L22: 4.2390
REMARK 3 L33: 4.3779 L12: -2.5944
REMARK 3 L13: 2.8850 L23: -3.2103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0265 S12: -0.0197 S13: -0.0057
REMARK 3 S21: -0.0488 S22: -0.0030 S23: 0.0902
REMARK 3 S31: 0.0385 S32: -0.0253 S33: -0.0100
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 816 THROUGH 878 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3008 -30.0212 8.4341
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.2212
REMARK 3 T33: 0.1109 T12: 0.0036
REMARK 3 T13: -0.0001 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 2.5020 L22: 1.7217
REMARK 3 L33: 0.8610 L12: -1.3086
REMARK 3 L13: 0.4525 L23: 0.1104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: -0.2972 S13: -0.0169
REMARK 3 S21: 0.1188 S22: 0.0701 S23: -0.1140
REMARK 3 S31: -0.0166 S32: 0.1407 S33: -0.0927
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 879 THROUGH 917 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1787 -29.1331 21.5831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2302 T22: 0.3941
REMARK 3 T33: 0.1511 T12: 0.0592
REMARK 3 T13: 0.0115 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 3.3206 L22: 0.7897
REMARK 3 L33: 3.0868 L12: -1.3401
REMARK 3 L13: 3.3865 L23: -0.9279
REMARK 3 S TENSOR
REMARK 3 S11: -0.1103 S12: -0.2648 S13: 0.0338
REMARK 3 S21: 0.1980 S22: 0.1072 S23: -0.0237
REMARK 3 S31: -0.0054 S32: 0.0114 S33: 0.0070
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 5TZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000225089.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-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 : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741
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 : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 55.722
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
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 2.6.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17-19% PEG3350, 0.2M MGCL2, 0.1M TRIS,
REMARK 280 PH 8.4, VAPOR DIFFUSION, HANGING DROP, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLU A 918
REMARK 465 GLU A 919
REMARK 465 SER B 576
REMARK 465 ALA B 577
REMARK 465 ASP B 917
REMARK 465 GLU B 918
REMARK 465 GLU B 919
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 ASP C 917
REMARK 465 GLU C 918
REMARK 465 GLU C 919
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 LEU D 586
REMARK 465 HIS D 587
REMARK 465 ASP D 588
REMARK 465 GLY D 589
REMARK 465 GLU D 918
REMARK 465 GLU D 919
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1338 O HOH A 1387 2.17
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 TYR B 719 67.99 -102.87
REMARK 500 SER B 721 -61.52 -93.62
REMARK 500 LYS B 814 -152.87 -97.25
REMARK 500 PRO B 908 170.73 -58.98
REMARK 500 ILE C 866 -55.51 -120.41
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 B1403 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH D1418 DISTANCE = 5.87 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 ZN A1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 660 NE2
REMARK 620 2 HIS A 696 NE2 101.7
REMARK 620 3 ASP A 697 OD2 91.8 89.1
REMARK 620 4 ASP A 808 OD1 89.0 86.4 175.5
REMARK 620 5 HOH A1174 O 154.3 103.9 86.1 95.2
REMARK 620 N 1 2 3 4
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 A1164 O 85.2
REMARK 620 3 HOH A1174 O 99.5 97.9
REMARK 620 4 HOH A1216 O 86.6 89.0 171.1
REMARK 620 5 HOH A1220 O 102.6 166.4 91.8 80.6
REMARK 620 6 HOH A1222 O 164.3 82.2 91.5 83.8 88.0
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 102.0
REMARK 620 3 ASP B 697 OD2 89.1 90.5
REMARK 620 4 ASP B 808 OD1 88.4 89.0 177.3
REMARK 620 5 HOH B1147 O 152.0 106.0 91.9 90.8
REMARK 620 N 1 2 3 4
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 B1144 O 84.9
REMARK 620 3 HOH B1147 O 96.8 96.6
REMARK 620 4 HOH B1178 O 86.0 92.3 170.9
REMARK 620 5 HOH B1209 O 169.2 84.9 87.9 90.9
REMARK 620 6 HOH B1286 O 103.2 171.1 86.1 84.8 86.8
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 98.3
REMARK 620 3 ASP C 697 OD2 90.5 87.9
REMARK 620 4 ASP C 808 OD1 86.6 89.3 175.7
REMARK 620 5 HOH C1132 O 155.6 106.1 89.8 94.1
REMARK 620 6 HOH C1221 O 86.3 167.8 103.3 79.7 69.9
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 C1132 O 95.2
REMARK 620 3 HOH C1136 O 82.7 97.0
REMARK 620 4 HOH C1175 O 167.0 92.6 86.0
REMARK 620 5 HOH C1235 O 103.1 88.6 171.5 87.5
REMARK 620 6 HOH C1251 O 87.8 171.0 91.8 86.1 82.4
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 103.5
REMARK 620 3 ASP D 697 OD2 89.9 89.4
REMARK 620 4 ASP D 808 OD1 86.0 86.3 173.3
REMARK 620 5 HOH D1130 O 153.5 103.0 92.5 93.5
REMARK 620 6 HOH D1173 O 88.7 163.0 102.6 82.6 64.9
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 D1130 O 97.5
REMARK 620 3 HOH D1150 O 87.2 97.6
REMARK 620 4 HOH D1199 O 165.4 92.1 80.5
REMARK 620 5 HOH D1228 O 90.5 168.6 90.8 81.7
REMARK 620 6 HOH D1261 O 101.9 87.9 168.7 89.4 82.6
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 7OJ 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 7OJ 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 7OJ 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 7OJ 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
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TZ3 RELATED DB: PDB
REMARK 900 RELATED ID: 5TZA RELATED DB: PDB
REMARK 900 RELATED ID: 5TZC RELATED DB: PDB
REMARK 900 RELATED ID: 5TZH RELATED DB: PDB
REMARK 900 RELATED ID: 5TZW RELATED DB: PDB
REMARK 900 RELATED ID: 5TZX RELATED DB: PDB
REMARK 900 RELATED ID: 5U00 RELATED DB: PDB
DBREF 5TZZ A 579 919 UNP O00408 PDE2A_HUMAN 323 663
DBREF 5TZZ B 579 919 UNP O00408 PDE2A_HUMAN 323 663
DBREF 5TZZ C 579 919 UNP O00408 PDE2A_HUMAN 323 663
DBREF 5TZZ D 579 919 UNP O00408 PDE2A_HUMAN 323 663
SEQADV 5TZZ SER A 576 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ ALA A 577 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ MET A 578 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ SER B 576 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ ALA B 577 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ MET B 578 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ SER C 576 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ ALA C 577 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ MET C 578 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ SER D 576 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ ALA D 577 UNP O00408 EXPRESSION TAG
SEQADV 5TZZ MET D 578 UNP O00408 EXPRESSION TAG
SEQRES 1 A 344 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 A 344 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 A 344 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 A 344 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 A 344 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 A 344 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 A 344 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 A 344 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 A 344 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 A 344 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 A 344 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 A 344 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 A 344 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 A 344 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 A 344 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 A 344 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 A 344 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 A 344 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 A 344 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 A 344 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 A 344 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 A 344 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 A 344 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 A 344 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 A 344 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 A 344 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 A 344 ASP PHE LEU ASP GLU GLU
SEQRES 1 B 344 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 B 344 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 B 344 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 B 344 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 B 344 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 B 344 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 B 344 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 B 344 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 B 344 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 B 344 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 B 344 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 B 344 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 B 344 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 B 344 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 B 344 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 B 344 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 B 344 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 B 344 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 B 344 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 B 344 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 B 344 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 B 344 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 B 344 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 B 344 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 B 344 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 B 344 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 B 344 ASP PHE LEU ASP GLU GLU
SEQRES 1 C 344 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 C 344 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 C 344 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 C 344 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 C 344 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 C 344 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 C 344 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 C 344 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 C 344 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 C 344 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 C 344 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 C 344 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 C 344 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 C 344 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 C 344 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 C 344 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 C 344 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 C 344 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 C 344 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 C 344 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 C 344 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 C 344 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 C 344 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 C 344 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 C 344 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 C 344 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 C 344 ASP PHE LEU ASP GLU GLU
SEQRES 1 D 344 SER ALA MET ASP ASP GLU TYR THR LYS LEU LEU HIS ASP
SEQRES 2 D 344 GLY ILE GLN PRO VAL ALA ALA ILE ASP SER ASN PHE ALA
SEQRES 3 D 344 SER PHE THR TYR THR PRO ARG SER LEU PRO GLU ASP ASP
SEQRES 4 D 344 THR SER MET ALA ILE LEU SER MET LEU GLN ASP MET ASN
SEQRES 5 D 344 PHE ILE ASN ASN TYR LYS ILE ASP CYS PRO THR LEU ALA
SEQRES 6 D 344 ARG PHE CYS LEU MET VAL LYS LYS GLY TYR ARG ASP PRO
SEQRES 7 D 344 PRO TYR HIS ASN TRP MET HIS ALA PHE SER VAL SER HIS
SEQRES 8 D 344 PHE CYS TYR LEU LEU TYR LYS ASN LEU GLU LEU THR ASN
SEQRES 9 D 344 TYR LEU GLU ASP ILE GLU ILE PHE ALA LEU PHE ILE SER
SEQRES 10 D 344 CYS MET CYS HIS ASP LEU ASP HIS ARG GLY THR ASN ASN
SEQRES 11 D 344 SER PHE GLN VAL ALA SER LYS SER VAL LEU ALA ALA LEU
SEQRES 12 D 344 TYR SER SER GLU GLY SER VAL MET GLU ARG HIS HIS PHE
SEQRES 13 D 344 ALA GLN ALA ILE ALA ILE LEU ASN THR HIS GLY CYS ASN
SEQRES 14 D 344 ILE PHE ASP HIS PHE SER ARG LYS ASP TYR GLN ARG MET
SEQRES 15 D 344 LEU ASP LEU MET ARG ASP ILE ILE LEU ALA THR ASP LEU
SEQRES 16 D 344 ALA HIS HIS LEU ARG ILE PHE LYS ASP LEU GLN LYS MET
SEQRES 17 D 344 ALA GLU VAL GLY TYR ASP ARG ASN ASN LYS GLN HIS HIS
SEQRES 18 D 344 ARG LEU LEU LEU CYS LEU LEU MET THR SER CYS ASP LEU
SEQRES 19 D 344 SER ASP GLN THR LYS GLY TRP LYS THR THR ARG LYS ILE
SEQRES 20 D 344 ALA GLU LEU ILE TYR LYS GLU PHE PHE SER GLN GLY ASP
SEQRES 21 D 344 LEU GLU LYS ALA MET GLY ASN ARG PRO MET GLU MET MET
SEQRES 22 D 344 ASP ARG GLU LYS ALA TYR ILE PRO GLU LEU GLN ILE SER
SEQRES 23 D 344 PHE MET GLU HIS ILE ALA MET PRO ILE TYR LYS LEU LEU
SEQRES 24 D 344 GLN ASP LEU PHE PRO LYS ALA ALA GLU LEU TYR GLU ARG
SEQRES 25 D 344 VAL ALA SER ASN ARG GLU HIS TRP THR LYS VAL SER HIS
SEQRES 26 D 344 LYS PHE THR ILE ARG GLY LEU PRO SER ASN ASN SER LEU
SEQRES 27 D 344 ASP PHE LEU ASP GLU GLU
HET 7OJ A1001 28
HET ZN A1002 1
HET MG A1003 1
HET 7OJ B1001 28
HET ZN B1002 1
HET MG B1003 1
HET 7OJ C1001 28
HET ZN C1002 1
HET MG C1003 1
HET 7OJ D1001 28
HET ZN D1002 1
HET MG D1003 1
HETNAM 7OJ (3-BROMO-4-FLUOROPHENYL)[(5S)-3,3-DIFLUORO-5-(5-
HETNAM 2 7OJ METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL)PIPERIDIN-
HETNAM 3 7OJ 1-YL]METHANONE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 5 7OJ 4(C18 H15 BR F3 N5 O)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 7 MG 4(MG 2+)
FORMUL 17 HOH *1262(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 LEU A 675 1 19
HELIX 9 AA9 GLU A 676 TYR A 680 5 5
HELIX 10 AB1 GLU A 682 HIS A 696 1 15
HELIX 11 AB2 ASN A 704 LYS A 712 1 9
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 LEU A 913 ASP A 917 5 5
HELIX 25 AC7 ASP B 579 ASP B 588 1 10
HELIX 26 AC8 PRO B 592 ASP B 597 1 6
HELIX 27 AC9 THR B 606 LEU B 610 5 5
HELIX 28 AD1 PRO B 611 ASP B 613 5 3
HELIX 29 AD2 ASP B 614 MET B 626 1 13
HELIX 30 AD3 ASN B 627 TYR B 632 1 6
HELIX 31 AD4 ASP B 635 GLY B 649 1 15
HELIX 32 AD5 ASN B 657 GLU B 676 1 20
HELIX 33 AD6 LEU B 677 TYR B 680 5 4
HELIX 34 AD7 GLU B 682 HIS B 696 1 15
HELIX 35 AD8 ASN B 704 SER B 711 1 8
HELIX 36 AD9 SER B 713 TYR B 719 1 7
HELIX 37 AE1 SER B 724 ASN B 739 1 16
HELIX 38 AE2 SER B 750 ALA B 767 1 18
HELIX 39 AE3 ASP B 769 GLY B 787 1 19
HELIX 40 AE4 ASN B 792 LEU B 809 1 18
HELIX 41 AE5 SER B 810 LYS B 814 5 5
HELIX 42 AE6 GLY B 815 GLY B 841 1 27
HELIX 43 AE7 MET B 845 ASP B 849 5 5
HELIX 44 AE8 TYR B 854 ILE B 866 1 13
HELIX 45 AE9 ILE B 866 PHE B 878 1 13
HELIX 46 AF1 ALA B 881 VAL B 898 1 18
HELIX 47 AF2 SER B 899 THR B 903 5 5
HELIX 48 AF3 PRO C 592 ILE C 596 5 5
HELIX 49 AF4 THR C 606 LEU C 610 5 5
HELIX 50 AF5 PRO C 611 ASP C 613 5 3
HELIX 51 AF6 ASP C 614 MET C 626 1 13
HELIX 52 AF7 ASN C 627 TYR C 632 1 6
HELIX 53 AF8 ASP C 635 GLY C 649 1 15
HELIX 54 AF9 ASN C 657 GLU C 676 1 20
HELIX 55 AG1 LEU C 677 TYR C 680 5 4
HELIX 56 AG2 GLU C 682 HIS C 696 1 15
HELIX 57 AG3 ASN C 704 SER C 711 1 8
HELIX 58 AG4 SER C 713 SER C 720 1 8
HELIX 59 AG5 SER C 724 ASN C 739 1 16
HELIX 60 AG6 SER C 750 ALA C 767 1 18
HELIX 61 AG7 ASP C 769 GLY C 787 1 19
HELIX 62 AG8 ASN C 792 LEU C 809 1 18
HELIX 63 AG9 SER C 810 LYS C 814 5 5
HELIX 64 AH1 GLY C 815 MET C 840 1 26
HELIX 65 AH2 MET C 845 ASP C 849 5 5
HELIX 66 AH3 TYR C 854 ILE C 866 1 13
HELIX 67 AH4 ILE C 866 PHE C 878 1 13
HELIX 68 AH5 ALA C 881 SER C 899 1 19
HELIX 69 AH6 HIS C 900 THR C 903 5 4
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 LEU D 681 1 6
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
HELIX 92 AK2 LEU D 913 ASP D 917 5 5
LINK NE2 HIS A 660 ZN ZN A1002 1555 1555 2.13
LINK NE2 HIS A 696 ZN ZN A1002 1555 1555 2.19
LINK OD2 ASP A 697 ZN ZN A1002 1555 1555 2.13
LINK OD1 ASP A 697 MG MG A1003 1555 1555 1.98
LINK OD1 ASP A 808 ZN ZN A1002 1555 1555 2.17
LINK ZN ZN A1002 O HOH A1174 1555 1555 2.15
LINK MG MG A1003 O HOH A1164 1555 1555 2.01
LINK MG MG A1003 O HOH A1174 1555 1555 1.95
LINK MG MG A1003 O HOH A1216 1555 1555 2.18
LINK MG MG A1003 O HOH A1220 1555 1555 2.18
LINK MG MG A1003 O HOH A1222 1555 1555 2.21
LINK NE2 HIS B 660 ZN ZN B1002 1555 1555 2.12
LINK NE2 HIS B 696 ZN ZN B1002 1555 1555 2.10
LINK OD2 ASP B 697 ZN ZN B1002 1555 1555 2.09
LINK OD1 ASP B 697 MG MG B1003 1555 1555 2.07
LINK OD1 ASP B 808 ZN ZN B1002 1555 1555 2.22
LINK ZN ZN B1002 O HOH B1147 1555 1555 2.11
LINK MG MG B1003 O HOH B1144 1555 1555 2.04
LINK MG MG B1003 O HOH B1147 1555 1555 2.09
LINK MG MG B1003 O HOH B1178 1555 1555 2.15
LINK MG MG B1003 O HOH B1209 1555 1555 2.13
LINK MG MG B1003 O HOH B1286 1555 1555 2.08
LINK NE2 HIS C 660 ZN ZN C1002 1555 1555 2.13
LINK NE2 HIS C 696 ZN ZN C1002 1555 1555 2.10
LINK OD2 ASP C 697 ZN ZN C1002 1555 1555 2.06
LINK OD1 ASP C 697 MG MG C1003 1555 1555 2.07
LINK OD1 ASP C 808 ZN ZN C1002 1555 1555 2.14
LINK ZN ZN C1002 O HOH C1132 1555 1555 2.03
LINK ZN ZN C1002 O HOH C1221 1555 1555 2.58
LINK MG MG C1003 O HOH C1132 1555 1555 2.10
LINK MG MG C1003 O HOH C1136 1555 1555 2.08
LINK MG MG C1003 O HOH C1175 1555 1555 2.08
LINK MG MG C1003 O HOH C1235 1555 1555 2.10
LINK MG MG C1003 O HOH C1251 1555 1555 2.12
LINK NE2 HIS D 660 ZN ZN D1002 1555 1555 2.15
LINK NE2 HIS D 696 ZN ZN D1002 1555 1555 2.11
LINK OD2 ASP D 697 ZN ZN D1002 1555 1555 2.13
LINK OD1 ASP D 697 MG MG D1003 1555 1555 1.97
LINK OD1 ASP D 808 ZN ZN D1002 1555 1555 2.17
LINK ZN ZN D1002 O HOH D1130 1555 1555 2.08
LINK ZN ZN D1002 O HOH D1173 1555 1555 2.67
LINK MG MG D1003 O HOH D1130 1555 1555 2.08
LINK MG MG D1003 O HOH D1150 1555 1555 2.03
LINK MG MG D1003 O HOH D1199 1555 1555 2.14
LINK MG MG D1003 O HOH D1228 1555 1555 2.22
LINK MG MG D1003 O HOH D1261 1555 1555 2.07
SITE 1 AC1 11 TYR A 655 HIS A 656 LEU A 770 GLN A 812
SITE 2 AC1 11 TYR A 827 PHE A 830 MET A 847 GLN A 859
SITE 3 AC1 11 PHE A 862 HOH A1206 HOH A1399
SITE 1 AC2 7 HIS A 660 HIS A 696 ASP A 697 ASP A 808
SITE 2 AC2 7 MG A1003 HOH A1174 HOH A1226
SITE 1 AC3 7 ASP A 697 ZN A1002 HOH A1164 HOH A1174
SITE 2 AC3 7 HOH A1216 HOH A1220 HOH A1222
SITE 1 AC4 14 TYR B 655 HIS B 656 LEU B 770 LEU B 809
SITE 2 AC4 14 GLN B 812 ILE B 826 TYR B 827 PHE B 830
SITE 3 AC4 14 MET B 847 GLN B 859 PHE B 862 HOH B1267
SITE 4 AC4 14 HOH B1295 HOH B1346
SITE 1 AC5 6 HIS B 660 HIS B 696 ASP B 697 ASP B 808
SITE 2 AC5 6 HOH B1120 HOH B1147
SITE 1 AC6 6 ASP B 697 HOH B1144 HOH B1147 HOH B1178
SITE 2 AC6 6 HOH B1209 HOH B1286
SITE 1 AC7 13 TYR C 655 HIS C 656 LEU C 770 LEU C 809
SITE 2 AC7 13 GLN C 812 ILE C 826 TYR C 827 PHE C 830
SITE 3 AC7 13 MET C 847 GLN C 859 PHE C 862 HOH C1247
SITE 4 AC7 13 HOH C1248
SITE 1 AC8 6 HIS C 660 HIS C 696 ASP C 697 ASP C 808
SITE 2 AC8 6 HOH C1132 HOH C1221
SITE 1 AC9 6 ASP C 697 HOH C1132 HOH C1136 HOH C1175
SITE 2 AC9 6 HOH C1235 HOH C1251
SITE 1 AD1 12 TYR D 655 HIS D 656 LEU D 770 LEU D 809
SITE 2 AD1 12 GLN D 812 ILE D 826 TYR D 827 PHE D 830
SITE 3 AD1 12 MET D 847 GLN D 859 PHE D 862 HOH D1316
SITE 1 AD2 7 HIS D 660 HIS D 696 ASP D 697 ASP D 808
SITE 2 AD2 7 MG D1003 HOH D1130 HOH D1173
SITE 1 AD3 7 ASP D 697 ZN D1002 HOH D1130 HOH D1150
SITE 2 AD3 7 HOH D1199 HOH D1228 HOH D1261
CRYST1 55.749 73.119 91.043 109.30 90.91 91.15 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 0.017937 0.000360 0.000428 0.00000
SCALE2 0.000000 0.013679 0.004798 0.00000
SCALE3 0.000000 0.000000 0.011641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END