HEADER HYDROLASE/HYDROLASE INHIBITOR 24-NOV-10 3PPM
TITLE CRYSTAL STRUCTURE OF A NONCOVALENTLY BOUND ALPHA-KETOHETEROCYCLE
TITLE 2 INHIBITOR (PHENHEXYL/OXADIAZOLE/PYRIDINE) TO A HUMANIZED VARIANT OF
TITLE 3 FATTY ACID AMIDE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY-ACID AMIDE HYDROLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DELTATM-FAAH, UNP RESIDUES 30-579;
COMPND 5 SYNONYM: ANANDAMIDE AMIDOHYDROLASE 1, OLEAMIDE HYDROLASE 1;
COMPND 6 EC: 3.5.1.99;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: FAAH, FAAH-1, FAAH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 AI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PROTEIN-INHIBITOR COMPLEX, FAAH, OXAZOLE, OXADIAZOLE, ENDOCANNABINOID
KEYWDS 2 DEGRADATION, MEMBRANE PROTEIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MILENI,G.W.HAN,D.L.BOGER,R.C.STEVENS
REVDAT 2 06-SEP-23 3PPM 1 REMARK SEQADV
REVDAT 1 09-NOV-11 3PPM 0
JRNL AUTH M.MILENI,J.GARFUNKLE,C.EZZILI,B.F.CRAVATT,R.C.STEVENS,
JRNL AUTH 2 D.L.BOGER
JRNL TITL FLUORIDE-MEDIATED CAPTURE OF A NONCOVALENT BOUND STATE OF A
JRNL TITL 2 REVERSIBLE COVALENT ENZYME INHIBITOR: X-RAY CRYSTALLOGRAPHIC
JRNL TITL 3 ANALYSIS OF AN EXCEPTIONALLY POTENT ALPHA-KETOHETEROCYCLE
JRNL TITL 4 INHIBITOR OF FATTY ACID AMIDE HYDROLASE.
JRNL REF J.AM.CHEM.SOC. V. 133 4092 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 21355555
JRNL DOI 10.1021/JA110877Y
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 151735
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 7621
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 33.9473 - 5.5232 0.95 4940 256 0.1727 0.1840
REMARK 3 2 5.5232 - 4.3869 0.98 4859 267 0.1335 0.1483
REMARK 3 3 4.3869 - 3.8332 0.99 4859 254 0.1370 0.1735
REMARK 3 4 3.8332 - 3.4831 0.99 4872 247 0.1374 0.1562
REMARK 3 5 3.4831 - 3.2337 1.00 4838 258 0.1469 0.1495
REMARK 3 6 3.2337 - 3.0432 1.00 4814 273 0.1501 0.1702
REMARK 3 7 3.0432 - 2.8909 1.00 4865 239 0.1566 0.1756
REMARK 3 8 2.8909 - 2.7651 1.00 4861 248 0.1516 0.1724
REMARK 3 9 2.7651 - 2.6587 1.00 4807 258 0.1513 0.1973
REMARK 3 10 2.6587 - 2.5670 1.00 4798 269 0.1468 0.1739
REMARK 3 11 2.5670 - 2.4867 1.00 4851 243 0.1424 0.1712
REMARK 3 12 2.4867 - 2.4157 1.00 4752 269 0.1350 0.1624
REMARK 3 13 2.4157 - 2.3521 1.00 4784 269 0.1411 0.1901
REMARK 3 14 2.3521 - 2.2947 1.00 4786 265 0.1427 0.1801
REMARK 3 15 2.2947 - 2.2426 1.00 4836 236 0.1423 0.1850
REMARK 3 16 2.2426 - 2.1948 1.00 4755 276 0.1395 0.1451
REMARK 3 17 2.1948 - 2.1509 1.00 4800 255 0.1363 0.1754
REMARK 3 18 2.1509 - 2.1104 1.00 4769 252 0.1411 0.1636
REMARK 3 19 2.1104 - 2.0727 1.00 4808 247 0.1430 0.1836
REMARK 3 20 2.0727 - 2.0375 1.00 4759 251 0.1449 0.1813
REMARK 3 21 2.0375 - 2.0047 1.00 4815 251 0.1502 0.1805
REMARK 3 22 2.0047 - 1.9738 1.00 4778 253 0.1536 0.2067
REMARK 3 23 1.9738 - 1.9448 1.00 4799 244 0.1619 0.1857
REMARK 3 24 1.9448 - 1.9174 1.00 4785 226 0.1632 0.1967
REMARK 3 25 1.9174 - 1.8915 1.00 4780 242 0.1722 0.1981
REMARK 3 26 1.8915 - 1.8669 1.00 4764 252 0.1898 0.2344
REMARK 3 27 1.8669 - 1.8436 1.00 4761 267 0.2112 0.2363
REMARK 3 28 1.8436 - 1.8214 1.00 4737 261 0.2227 0.2595
REMARK 3 29 1.8214 - 1.8002 1.00 4805 249 0.2522 0.2896
REMARK 3 30 1.8002 - 1.7800 0.99 4677 244 0.2756 0.2932
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 47.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.62490
REMARK 3 B22 (A**2) : 1.62490
REMARK 3 B33 (A**2) : -3.24970
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 8866
REMARK 3 ANGLE : 1.081 12047
REMARK 3 CHIRALITY : 0.073 1343
REMARK 3 PLANARITY : 0.005 1559
REMARK 3 DIHEDRAL : 12.542 3400
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 33:70)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2008 -33.8612 -14.4200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2877 T22: 0.3525
REMARK 3 T33: 0.2005 T12: -0.0270
REMARK 3 T13: -0.0949 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.8273 L22: 0.9411
REMARK 3 L33: 0.4350 L12: 0.0721
REMARK 3 L13: 0.3850 L23: 0.3527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0480 S12: 0.4349 S13: -0.0302
REMARK 3 S21: -0.3739 S22: -0.0432 S23: 0.2082
REMARK 3 S31: -0.0576 S32: -0.0704 S33: 0.0645
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 71:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9180 -19.2981 -5.1822
REMARK 3 T TENSOR
REMARK 3 T11: 0.1882 T22: 0.1958
REMARK 3 T33: 0.1733 T12: 0.0243
REMARK 3 T13: -0.0640 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 1.0338 L22: 1.6312
REMARK 3 L33: 0.7429 L12: -0.3517
REMARK 3 L13: 0.2695 L23: -0.4897
REMARK 3 S TENSOR
REMARK 3 S11: -0.0961 S12: 0.1938 S13: 0.0945
REMARK 3 S21: -0.2367 S22: 0.0267 S23: 0.2746
REMARK 3 S31: -0.2312 S32: -0.1918 S33: 0.0357
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 135:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2645 -37.2489 0.4736
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.2445
REMARK 3 T33: 0.1904 T12: -0.0128
REMARK 3 T13: -0.0206 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.1482 L22: 1.9378
REMARK 3 L33: 0.5699 L12: -0.2547
REMARK 3 L13: -0.2063 L23: 0.6086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0256 S12: 0.1208 S13: -0.0464
REMARK 3 S21: -0.0357 S22: -0.1238 S23: 0.2632
REMARK 3 S31: 0.0359 S32: -0.2947 S33: 0.0993
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 166:276)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1010 -33.5383 2.5970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1426 T22: 0.1758
REMARK 3 T33: 0.1267 T12: -0.0129
REMARK 3 T13: -0.0029 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.2122 L22: 0.4714
REMARK 3 L33: 0.4161 L12: -0.0671
REMARK 3 L13: 0.1099 L23: 0.1597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0993 S13: -0.0147
REMARK 3 S21: -0.0759 S22: 0.0062 S23: 0.0286
REMARK 3 S31: -0.0180 S32: -0.0084 S33: -0.0010
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 277:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1939 -24.3490 14.2577
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.1661
REMARK 3 T33: 0.1610 T12: 0.0099
REMARK 3 T13: 0.0057 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.2034 L22: 0.0720
REMARK 3 L33: 0.7582 L12: 0.1330
REMARK 3 L13: 0.2039 L23: 0.1323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.0013 S13: 0.0220
REMARK 3 S21: 0.0052 S22: -0.0137 S23: 0.0406
REMARK 3 S31: -0.1087 S32: -0.0525 S33: 0.0266
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 316:410)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5264 -34.8416 10.9307
REMARK 3 T TENSOR
REMARK 3 T11: 0.0837 T22: 0.1446
REMARK 3 T33: 0.1147 T12: -0.0168
REMARK 3 T13: 0.0093 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.2445 L22: 0.7656
REMARK 3 L33: 0.6196 L12: 0.0898
REMARK 3 L13: -0.0552 L23: 0.1208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: 0.0271 S13: -0.0333
REMARK 3 S21: -0.0131 S22: 0.0134 S23: -0.0937
REMARK 3 S31: 0.0043 S32: 0.1321 S33: -0.0006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 411:451)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4145 -54.7916 16.4170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1614 T22: 0.1589
REMARK 3 T33: 0.1811 T12: 0.0462
REMARK 3 T13: 0.0285 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 1.6524 L22: 0.3893
REMARK 3 L33: 1.5111 L12: -0.4314
REMARK 3 L13: -1.1985 L23: 0.2544
REMARK 3 S TENSOR
REMARK 3 S11: -0.0614 S12: -0.0972 S13: -0.1753
REMARK 3 S21: -0.0119 S22: -0.0979 S23: -0.1231
REMARK 3 S31: 0.2776 S32: 0.2012 S33: 0.1333
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 452:578)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2792 -30.0279 8.8301
REMARK 3 T TENSOR
REMARK 3 T11: 0.1145 T22: 0.1615
REMARK 3 T33: 0.1263 T12: -0.0188
REMARK 3 T13: 0.0179 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.4207 L22: 0.4514
REMARK 3 L33: 0.7156 L12: -0.0053
REMARK 3 L13: -0.0247 L23: -0.1555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: 0.0283 S13: 0.0242
REMARK 3 S21: -0.0453 S22: 0.0146 S23: -0.0674
REMARK 3 S31: -0.0437 S32: 0.1257 S33: -0.0076
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 33:70)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8430 -38.4508 64.3126
REMARK 3 T TENSOR
REMARK 3 T11: 0.1606 T22: 0.2599
REMARK 3 T33: 0.1723 T12: -0.0044
REMARK 3 T13: -0.0270 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1796 L22: 0.3026
REMARK 3 L33: 0.7784 L12: 0.1339
REMARK 3 L13: 0.2375 L23: -0.1496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0605 S12: -0.1151 S13: -0.0475
REMARK 3 S21: 0.0413 S22: -0.2304 S23: -0.0347
REMARK 3 S31: -0.0622 S32: -0.1118 S33: 0.1323
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 71:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8897 -24.4606 57.7939
REMARK 3 T TENSOR
REMARK 3 T11: 0.1667 T22: 0.1808
REMARK 3 T33: 0.1600 T12: -0.0175
REMARK 3 T13: -0.0063 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.7146 L22: 0.8862
REMARK 3 L33: 0.7297 L12: 0.4592
REMARK 3 L13: 0.0731 L23: 0.1986
REMARK 3 S TENSOR
REMARK 3 S11: -0.0385 S12: -0.1336 S13: 0.0831
REMARK 3 S21: 0.1630 S22: 0.0299 S23: -0.0800
REMARK 3 S31: -0.2022 S32: 0.0557 S33: 0.0144
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 135:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8873 -39.5421 48.7588
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.1634
REMARK 3 T33: 0.1498 T12: -0.0031
REMARK 3 T13: -0.0069 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 1.4403
REMARK 3 L33: 0.2295 L12: -0.0517
REMARK 3 L13: -0.0445 L23: -0.1975
REMARK 3 S TENSOR
REMARK 3 S11: 0.0390 S12: -0.0235 S13: 0.0121
REMARK 3 S21: 0.0379 S22: -0.0895 S23: -0.2253
REMARK 3 S31: -0.0183 S32: 0.1358 S33: 0.0458
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 166:276)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3095 -39.3100 47.0620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1094 T22: 0.1528
REMARK 3 T33: 0.1399 T12: -0.0033
REMARK 3 T13: 0.0059 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.1143 L22: 0.2338
REMARK 3 L33: 0.3470 L12: -0.0477
REMARK 3 L13: 0.0527 L23: -0.1012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.0347 S13: -0.0417
REMARK 3 S21: -0.0008 S22: -0.0005 S23: -0.0135
REMARK 3 S31: 0.0166 S32: -0.0059 S33: 0.0047
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 277:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8664 -26.5377 37.8408
REMARK 3 T TENSOR
REMARK 3 T11: 0.1433 T22: 0.1601
REMARK 3 T33: 0.1491 T12: -0.0078
REMARK 3 T13: 0.0064 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.1585 L22: 0.1726
REMARK 3 L33: 0.6648 L12: -0.0333
REMARK 3 L13: 0.2053 L23: -0.1807
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: -0.0046 S13: 0.0514
REMARK 3 S21: -0.0022 S22: 0.0108 S23: 0.0380
REMARK 3 S31: -0.0582 S32: 0.0101 S33: 0.0050
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 316:410)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2915 -44.3381 38.1685
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: 0.1339
REMARK 3 T33: 0.1078 T12: -0.0135
REMARK 3 T13: 0.0118 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3619 L22: 0.4113
REMARK 3 L33: 0.4272 L12: 0.0669
REMARK 3 L13: -0.0494 L23: -0.0182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: 0.0346 S13: -0.0158
REMARK 3 S21: -0.0035 S22: 0.0263 S23: 0.0743
REMARK 3 S31: 0.0325 S32: -0.1153 S33: -0.0087
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 411:451)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2353 -61.0169 28.7098
REMARK 3 T TENSOR
REMARK 3 T11: 0.1806 T22: 0.1154
REMARK 3 T33: 0.1974 T12: -0.0574
REMARK 3 T13: 0.0627 T23: -0.0694
REMARK 3 L TENSOR
REMARK 3 L11: 1.6743 L22: 0.1403
REMARK 3 L33: 0.7583 L12: 0.3447
REMARK 3 L13: -0.8718 L23: -0.3352
REMARK 3 S TENSOR
REMARK 3 S11: -0.1751 S12: 0.2517 S13: -0.3421
REMARK 3 S21: -0.0425 S22: -0.0203 S23: -0.0066
REMARK 3 S31: 0.2618 S32: -0.1922 S33: 0.1967
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 452:577)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7315 -40.9369 41.0943
REMARK 3 T TENSOR
REMARK 3 T11: 0.0402 T22: 0.1105
REMARK 3 T33: 0.0784 T12: -0.0032
REMARK 3 T13: 0.0087 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.5223 L22: 0.3483
REMARK 3 L33: 0.3406 L12: 0.0960
REMARK 3 L13: -0.1111 L23: -0.0985
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.0109 S13: 0.0070
REMARK 3 S21: 0.0045 S22: 0.0150 S23: 0.0434
REMARK 3 S31: -0.0099 S32: -0.0859 S33: -0.0176
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 3PPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-ROOT I
REMARK 200 -BEAM SINGLE CRYSTAL; ASYMMETRIC
REMARK 200 CUT 4.965 DEGS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 33.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WJ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 100 MM MES PH 5.5, 100 MM
REMARK 280 KCL, 200 MM NACL, 100 MM NAF, AND 8% POLYPROPYLENE GLYCOL-P400,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 169.80333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.90167
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.90167
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 169.80333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 SER A 17
REMARK 465 SER A 18
REMARK 465 GLY A 19
REMARK 465 LEU A 20
REMARK 465 VAL A 21
REMARK 465 PRO A 22
REMARK 465 ARG A 23
REMARK 465 GLY A 24
REMARK 465 SER A 25
REMARK 465 HIS A 26
REMARK 465 MET A 27
REMARK 465 ALA A 28
REMARK 465 SER A 29
REMARK 465 ARG A 30
REMARK 465 TRP A 31
REMARK 465 THR A 32
REMARK 465 SER A 579
REMARK 465 MET B 7
REMARK 465 GLY B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 SER B 17
REMARK 465 SER B 18
REMARK 465 GLY B 19
REMARK 465 LEU B 20
REMARK 465 VAL B 21
REMARK 465 PRO B 22
REMARK 465 ARG B 23
REMARK 465 GLY B 24
REMARK 465 SER B 25
REMARK 465 HIS B 26
REMARK 465 MET B 27
REMARK 465 ALA B 28
REMARK 465 SER B 29
REMARK 465 ARG B 30
REMARK 465 TRP B 31
REMARK 465 THR B 32
REMARK 465 PRO B 578
REMARK 465 SER B 579
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 SER A 190 -12.61 82.09
REMARK 500 MET A 191 -4.86 70.63
REMARK 500 SER A 193 147.65 -177.44
REMARK 500 ASP A 195 -161.71 -106.38
REMARK 500 CYS A 196 59.84 -155.31
REMARK 500 LYS A 209 117.80 -165.89
REMARK 500 SER A 218 48.23 -80.60
REMARK 500 TYR A 335 -59.05 -126.46
REMARK 500 GLN A 557 51.54 -107.06
REMARK 500 GLN A 557 45.66 -102.80
REMARK 500 SER B 190 -9.00 81.28
REMARK 500 MET B 191 -3.83 68.51
REMARK 500 SER B 193 148.52 -175.80
REMARK 500 ASP B 195 -163.90 -102.62
REMARK 500 CYS B 196 56.42 -154.41
REMARK 500 LYS B 209 116.47 -167.60
REMARK 500 SER B 218 48.76 -84.83
REMARK 500 ASP B 237 118.72 -160.57
REMARK 500 ASN B 334 19.66 57.72
REMARK 500 TYR B 335 -56.57 -122.45
REMARK 500 GLN B 557 50.85 -107.80
REMARK 500 GLN B 557 45.08 -103.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JG1 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JG1 B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1DO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WJ1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER ALPHA-KETOOXAZOLE INHIBITOR
REMARK 900 RELATED ID: 2WJ2 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER ALPHA-KETOOXAZOLE INHIBITOR
REMARK 900 RELATED ID: 3K7F RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER ALPHA-KETOOXAZOLE INHIBITOR
REMARK 900 RELATED ID: 3K83 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER ALPHA-KETOOXAZOLE INHIBITOR
REMARK 900 RELATED ID: 3K84 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER ALPHA-KETOOXAZOLE INHIBITOR
REMARK 900 RELATED ID: 3PR0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COVALENTLY BOUND TO THE SAME INHIBITOR
DBREF 3PPM A 30 579 UNP P97612 FAAH1_RAT 30 579
DBREF 3PPM B 30 579 UNP P97612 FAAH1_RAT 30 579
SEQADV 3PPM MET A 7 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY A 8 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 9 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 10 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 11 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 12 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 13 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 14 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 15 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 16 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 17 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 18 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY A 19 UNP P97612 EXPRESSION TAG
SEQADV 3PPM LEU A 20 UNP P97612 EXPRESSION TAG
SEQADV 3PPM VAL A 21 UNP P97612 EXPRESSION TAG
SEQADV 3PPM PRO A 22 UNP P97612 EXPRESSION TAG
SEQADV 3PPM ARG A 23 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY A 24 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 25 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS A 26 UNP P97612 EXPRESSION TAG
SEQADV 3PPM MET A 27 UNP P97612 EXPRESSION TAG
SEQADV 3PPM ALA A 28 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER A 29 UNP P97612 EXPRESSION TAG
SEQADV 3PPM PHE A 192 UNP P97612 LEU 192 ENGINEERED MUTATION
SEQADV 3PPM TYR A 194 UNP P97612 PHE 194 ENGINEERED MUTATION
SEQADV 3PPM THR A 377 UNP P97612 ALA 377 ENGINEERED MUTATION
SEQADV 3PPM ASN A 435 UNP P97612 SER 435 ENGINEERED MUTATION
SEQADV 3PPM VAL A 491 UNP P97612 ILE 491 ENGINEERED MUTATION
SEQADV 3PPM MET A 495 UNP P97612 VAL 495 ENGINEERED MUTATION
SEQADV 3PPM MET B 7 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY B 8 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 9 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 10 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 11 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 12 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 13 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 14 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 15 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 16 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 17 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 18 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY B 19 UNP P97612 EXPRESSION TAG
SEQADV 3PPM LEU B 20 UNP P97612 EXPRESSION TAG
SEQADV 3PPM VAL B 21 UNP P97612 EXPRESSION TAG
SEQADV 3PPM PRO B 22 UNP P97612 EXPRESSION TAG
SEQADV 3PPM ARG B 23 UNP P97612 EXPRESSION TAG
SEQADV 3PPM GLY B 24 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 25 UNP P97612 EXPRESSION TAG
SEQADV 3PPM HIS B 26 UNP P97612 EXPRESSION TAG
SEQADV 3PPM MET B 27 UNP P97612 EXPRESSION TAG
SEQADV 3PPM ALA B 28 UNP P97612 EXPRESSION TAG
SEQADV 3PPM SER B 29 UNP P97612 EXPRESSION TAG
SEQADV 3PPM PHE B 192 UNP P97612 LEU 192 ENGINEERED MUTATION
SEQADV 3PPM TYR B 194 UNP P97612 PHE 194 ENGINEERED MUTATION
SEQADV 3PPM THR B 377 UNP P97612 ALA 377 ENGINEERED MUTATION
SEQADV 3PPM ASN B 435 UNP P97612 SER 435 ENGINEERED MUTATION
SEQADV 3PPM VAL B 491 UNP P97612 ILE 491 ENGINEERED MUTATION
SEQADV 3PPM MET B 495 UNP P97612 VAL 495 ENGINEERED MUTATION
SEQRES 1 A 573 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 573 LEU VAL PRO ARG GLY SER HIS MET ALA SER ARG TRP THR
SEQRES 3 A 573 GLY ARG GLN LYS ALA ARG GLY ALA ALA THR ARG ALA ARG
SEQRES 4 A 573 GLN LYS GLN ARG ALA SER LEU GLU THR MET ASP LYS ALA
SEQRES 5 A 573 VAL GLN ARG PHE ARG LEU GLN ASN PRO ASP LEU ASP SER
SEQRES 6 A 573 GLU ALA LEU LEU THR LEU PRO LEU LEU GLN LEU VAL GLN
SEQRES 7 A 573 LYS LEU GLN SER GLY GLU LEU SER PRO GLU ALA VAL PHE
SEQRES 8 A 573 PHE THR TYR LEU GLY LYS ALA TRP GLU VAL ASN LYS GLY
SEQRES 9 A 573 THR ASN CYS VAL THR SER TYR LEU THR ASP CYS GLU THR
SEQRES 10 A 573 GLN LEU SER GLN ALA PRO ARG GLN GLY LEU LEU TYR GLY
SEQRES 11 A 573 VAL PRO VAL SER LEU LYS GLU CYS PHE SER TYR LYS GLY
SEQRES 12 A 573 HIS ASP SER THR LEU GLY LEU SER LEU ASN GLU GLY MET
SEQRES 13 A 573 PRO SER GLU SER ASP CYS VAL VAL VAL GLN VAL LEU LYS
SEQRES 14 A 573 LEU GLN GLY ALA VAL PRO PHE VAL HIS THR ASN VAL PRO
SEQRES 15 A 573 GLN SER MET PHE SER TYR ASP CYS SER ASN PRO LEU PHE
SEQRES 16 A 573 GLY GLN THR MET ASN PRO TRP LYS SER SER LYS SER PRO
SEQRES 17 A 573 GLY GLY SER SER GLY GLY GLU GLY ALA LEU ILE GLY SER
SEQRES 18 A 573 GLY GLY SER PRO LEU GLY LEU GLY THR ASP ILE GLY GLY
SEQRES 19 A 573 SER ILE ARG PHE PRO SER ALA PHE CYS GLY ILE CYS GLY
SEQRES 20 A 573 LEU LYS PRO THR GLY ASN ARG LEU SER LYS SER GLY LEU
SEQRES 21 A 573 LYS GLY CYS VAL TYR GLY GLN THR ALA VAL GLN LEU SER
SEQRES 22 A 573 LEU GLY PRO MET ALA ARG ASP VAL GLU SER LEU ALA LEU
SEQRES 23 A 573 CYS LEU LYS ALA LEU LEU CYS GLU HIS LEU PHE THR LEU
SEQRES 24 A 573 ASP PRO THR VAL PRO PRO LEU PRO PHE ARG GLU GLU VAL
SEQRES 25 A 573 TYR ARG SER SER ARG PRO LEU ARG VAL GLY TYR TYR GLU
SEQRES 26 A 573 THR ASP ASN TYR THR MET PRO SER PRO ALA MET ARG ARG
SEQRES 27 A 573 ALA LEU ILE GLU THR LYS GLN ARG LEU GLU ALA ALA GLY
SEQRES 28 A 573 HIS THR LEU ILE PRO PHE LEU PRO ASN ASN ILE PRO TYR
SEQRES 29 A 573 ALA LEU GLU VAL LEU SER THR GLY GLY LEU PHE SER ASP
SEQRES 30 A 573 GLY GLY ARG SER PHE LEU GLN ASN PHE LYS GLY ASP PHE
SEQRES 31 A 573 VAL ASP PRO CYS LEU GLY ASP LEU ILE LEU ILE LEU ARG
SEQRES 32 A 573 LEU PRO SER TRP PHE LYS ARG LEU LEU SER LEU LEU LEU
SEQRES 33 A 573 LYS PRO LEU PHE PRO ARG LEU ALA ALA PHE LEU ASN ASN
SEQRES 34 A 573 MET ARG PRO ARG SER ALA GLU LYS LEU TRP LYS LEU GLN
SEQRES 35 A 573 HIS GLU ILE GLU MET TYR ARG GLN SER VAL ILE ALA GLN
SEQRES 36 A 573 TRP LYS ALA MET ASN LEU ASP VAL LEU LEU THR PRO MET
SEQRES 37 A 573 LEU GLY PRO ALA LEU ASP LEU ASN THR PRO GLY ARG ALA
SEQRES 38 A 573 THR GLY ALA VAL SER TYR THR MET LEU TYR ASN CYS LEU
SEQRES 39 A 573 ASP PHE PRO ALA GLY VAL VAL PRO VAL THR THR VAL THR
SEQRES 40 A 573 ALA GLU ASP ASP ALA GLN MET GLU LEU TYR LYS GLY TYR
SEQRES 41 A 573 PHE GLY ASP ILE TRP ASP ILE ILE LEU LYS LYS ALA MET
SEQRES 42 A 573 LYS ASN SER VAL GLY LEU PRO VAL ALA VAL GLN CYS VAL
SEQRES 43 A 573 ALA LEU PRO TRP GLN GLU GLU LEU CYS LEU ARG PHE MET
SEQRES 44 A 573 ARG GLU VAL GLU GLN LEU MET THR PRO GLN LYS GLN PRO
SEQRES 45 A 573 SER
SEQRES 1 B 573 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 573 LEU VAL PRO ARG GLY SER HIS MET ALA SER ARG TRP THR
SEQRES 3 B 573 GLY ARG GLN LYS ALA ARG GLY ALA ALA THR ARG ALA ARG
SEQRES 4 B 573 GLN LYS GLN ARG ALA SER LEU GLU THR MET ASP LYS ALA
SEQRES 5 B 573 VAL GLN ARG PHE ARG LEU GLN ASN PRO ASP LEU ASP SER
SEQRES 6 B 573 GLU ALA LEU LEU THR LEU PRO LEU LEU GLN LEU VAL GLN
SEQRES 7 B 573 LYS LEU GLN SER GLY GLU LEU SER PRO GLU ALA VAL PHE
SEQRES 8 B 573 PHE THR TYR LEU GLY LYS ALA TRP GLU VAL ASN LYS GLY
SEQRES 9 B 573 THR ASN CYS VAL THR SER TYR LEU THR ASP CYS GLU THR
SEQRES 10 B 573 GLN LEU SER GLN ALA PRO ARG GLN GLY LEU LEU TYR GLY
SEQRES 11 B 573 VAL PRO VAL SER LEU LYS GLU CYS PHE SER TYR LYS GLY
SEQRES 12 B 573 HIS ASP SER THR LEU GLY LEU SER LEU ASN GLU GLY MET
SEQRES 13 B 573 PRO SER GLU SER ASP CYS VAL VAL VAL GLN VAL LEU LYS
SEQRES 14 B 573 LEU GLN GLY ALA VAL PRO PHE VAL HIS THR ASN VAL PRO
SEQRES 15 B 573 GLN SER MET PHE SER TYR ASP CYS SER ASN PRO LEU PHE
SEQRES 16 B 573 GLY GLN THR MET ASN PRO TRP LYS SER SER LYS SER PRO
SEQRES 17 B 573 GLY GLY SER SER GLY GLY GLU GLY ALA LEU ILE GLY SER
SEQRES 18 B 573 GLY GLY SER PRO LEU GLY LEU GLY THR ASP ILE GLY GLY
SEQRES 19 B 573 SER ILE ARG PHE PRO SER ALA PHE CYS GLY ILE CYS GLY
SEQRES 20 B 573 LEU LYS PRO THR GLY ASN ARG LEU SER LYS SER GLY LEU
SEQRES 21 B 573 LYS GLY CYS VAL TYR GLY GLN THR ALA VAL GLN LEU SER
SEQRES 22 B 573 LEU GLY PRO MET ALA ARG ASP VAL GLU SER LEU ALA LEU
SEQRES 23 B 573 CYS LEU LYS ALA LEU LEU CYS GLU HIS LEU PHE THR LEU
SEQRES 24 B 573 ASP PRO THR VAL PRO PRO LEU PRO PHE ARG GLU GLU VAL
SEQRES 25 B 573 TYR ARG SER SER ARG PRO LEU ARG VAL GLY TYR TYR GLU
SEQRES 26 B 573 THR ASP ASN TYR THR MET PRO SER PRO ALA MET ARG ARG
SEQRES 27 B 573 ALA LEU ILE GLU THR LYS GLN ARG LEU GLU ALA ALA GLY
SEQRES 28 B 573 HIS THR LEU ILE PRO PHE LEU PRO ASN ASN ILE PRO TYR
SEQRES 29 B 573 ALA LEU GLU VAL LEU SER THR GLY GLY LEU PHE SER ASP
SEQRES 30 B 573 GLY GLY ARG SER PHE LEU GLN ASN PHE LYS GLY ASP PHE
SEQRES 31 B 573 VAL ASP PRO CYS LEU GLY ASP LEU ILE LEU ILE LEU ARG
SEQRES 32 B 573 LEU PRO SER TRP PHE LYS ARG LEU LEU SER LEU LEU LEU
SEQRES 33 B 573 LYS PRO LEU PHE PRO ARG LEU ALA ALA PHE LEU ASN ASN
SEQRES 34 B 573 MET ARG PRO ARG SER ALA GLU LYS LEU TRP LYS LEU GLN
SEQRES 35 B 573 HIS GLU ILE GLU MET TYR ARG GLN SER VAL ILE ALA GLN
SEQRES 36 B 573 TRP LYS ALA MET ASN LEU ASP VAL LEU LEU THR PRO MET
SEQRES 37 B 573 LEU GLY PRO ALA LEU ASP LEU ASN THR PRO GLY ARG ALA
SEQRES 38 B 573 THR GLY ALA VAL SER TYR THR MET LEU TYR ASN CYS LEU
SEQRES 39 B 573 ASP PHE PRO ALA GLY VAL VAL PRO VAL THR THR VAL THR
SEQRES 40 B 573 ALA GLU ASP ASP ALA GLN MET GLU LEU TYR LYS GLY TYR
SEQRES 41 B 573 PHE GLY ASP ILE TRP ASP ILE ILE LEU LYS LYS ALA MET
SEQRES 42 B 573 LYS ASN SER VAL GLY LEU PRO VAL ALA VAL GLN CYS VAL
SEQRES 43 B 573 ALA LEU PRO TRP GLN GLU GLU LEU CYS LEU ARG PHE MET
SEQRES 44 B 573 ARG GLU VAL GLU GLN LEU MET THR PRO GLN LYS GLN PRO
SEQRES 45 B 573 SER
HET JG1 A 600 25
HET CL A 601 1
HET CL A 602 1
HET F A 603 1
HET PEG A 604 7
HET PEG A 605 7
HET JG1 B 600 25
HET CL B 601 1
HET F B 602 1
HET 1DO B 603 13
HET PEG B 604 7
HET PEG B 605 7
HETNAM JG1 7-PHENYL-1-[5-(PYRIDIN-2-YL)-1,3,4-OXADIAZOL-2-
HETNAM 2 JG1 YL]HEPTAN-1-ONE
HETNAM CL CHLORIDE ION
HETNAM F FLUORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1DO 1-DODECANOL
FORMUL 3 JG1 2(C20 H21 N3 O2)
FORMUL 4 CL 3(CL 1-)
FORMUL 6 F 2(F 1-)
FORMUL 7 PEG 4(C4 H10 O3)
FORMUL 12 1DO C12 H26 O
FORMUL 15 HOH *1054(H2 O)
HELIX 1 1 ARG A 34 ASN A 66 1 33
HELIX 2 2 ASP A 70 LEU A 77 1 8
HELIX 3 3 PRO A 78 SER A 88 1 11
HELIX 4 4 SER A 92 ASN A 112 1 21
HELIX 5 5 ASP A 120 ALA A 128 1 9
HELIX 6 6 LEU A 156 GLU A 160 5 5
HELIX 7 7 CYS A 168 GLN A 177 1 10
HELIX 8 8 SER A 218 SER A 227 1 10
HELIX 9 9 ILE A 242 GLY A 250 1 9
HELIX 10 10 THR A 257 LEU A 261 5 5
HELIX 11 11 ASP A 286 LEU A 298 1 13
HELIX 12 12 CYS A 299 ASP A 306 1 8
HELIX 13 13 ARG A 315 ARG A 320 1 6
HELIX 14 14 SER A 339 ALA A 356 1 18
HELIX 15 15 ASN A 367 VAL A 374 1 8
HELIX 16 16 VAL A 374 PHE A 381 1 8
HELIX 17 17 GLY A 385 GLN A 390 1 6
HELIX 18 18 ASN A 391 LYS A 393 5 3
HELIX 19 19 ASP A 398 GLY A 402 5 5
HELIX 20 20 ASP A 403 ARG A 409 1 7
HELIX 21 21 PRO A 411 LYS A 423 1 13
HELIX 22 22 PHE A 426 MET A 436 1 11
HELIX 23 23 SER A 440 MET A 465 1 26
HELIX 24 24 THR A 483 ALA A 490 5 8
HELIX 25 25 VAL A 491 LEU A 500 1 10
HELIX 26 26 THR A 513 GLU A 521 1 9
HELIX 27 27 ASP A 529 MET A 539 1 11
HELIX 28 28 GLN A 557 THR A 573 1 17
HELIX 29 29 ARG B 34 ASN B 66 1 33
HELIX 30 30 ASP B 70 LEU B 77 1 8
HELIX 31 31 PRO B 78 SER B 88 1 11
HELIX 32 32 SER B 92 ASN B 112 1 21
HELIX 33 33 ASP B 120 ALA B 128 1 9
HELIX 34 34 LEU B 156 GLU B 160 5 5
HELIX 35 35 CYS B 168 GLN B 177 1 10
HELIX 36 36 SER B 218 SER B 227 1 10
HELIX 37 37 ILE B 242 GLY B 250 1 9
HELIX 38 38 ASP B 286 LEU B 298 1 13
HELIX 39 39 CYS B 299 ASP B 306 1 8
HELIX 40 40 ARG B 315 SER B 321 1 7
HELIX 41 41 SER B 339 ALA B 356 1 18
HELIX 42 42 ASN B 367 VAL B 374 1 8
HELIX 43 43 VAL B 374 PHE B 381 1 8
HELIX 44 44 GLY B 385 ASN B 391 1 7
HELIX 45 45 ASP B 398 GLY B 402 5 5
HELIX 46 46 ASP B 403 LEU B 410 1 8
HELIX 47 47 PRO B 411 LYS B 423 1 13
HELIX 48 48 PHE B 426 MET B 436 1 11
HELIX 49 49 SER B 440 MET B 465 1 26
HELIX 50 50 THR B 483 ALA B 490 5 8
HELIX 51 51 VAL B 491 LEU B 500 1 10
HELIX 52 52 THR B 513 GLN B 519 1 7
HELIX 53 53 MET B 520 TYR B 523 5 4
HELIX 54 54 ASP B 529 MET B 539 1 11
HELIX 55 55 GLN B 557 THR B 573 1 17
HELIX 56 56 PRO B 574 GLN B 577 5 4
SHEET 1 A11 VAL A 114 TYR A 117 0
SHEET 2 A11 VAL A 180 THR A 185 -1 O HIS A 184 N SER A 116
SHEET 3 A11 PRO A 138 LYS A 142 1 N LEU A 141 O VAL A 183
SHEET 4 A11 LEU A 232 ASP A 237 1 O LEU A 232 N SER A 140
SHEET 5 A11 SER A 279 ALA A 284 -1 O GLY A 281 N GLY A 235
SHEET 6 A11 CYS A 252 LYS A 255 -1 N CYS A 252 O ALA A 284
SHEET 7 A11 ALA A 504 THR A 511 -1 O ALA A 504 N LYS A 255
SHEET 8 A11 PRO A 546 VAL A 552 -1 O CYS A 551 N GLY A 505
SHEET 9 A11 VAL A 469 PRO A 473 -1 N THR A 472 O GLN A 550
SHEET 10 A11 ARG A 326 TYR A 329 1 N GLY A 328 O LEU A 471
SHEET 11 A11 THR A 359 PRO A 362 1 O THR A 359 N VAL A 327
SHEET 1 B 2 SER A 197 ASN A 198 0
SHEET 2 B 2 GLY A 202 GLN A 203 -1 O GLY A 202 N ASN A 198
SHEET 1 C11 VAL B 114 TYR B 117 0
SHEET 2 C11 VAL B 180 THR B 185 -1 O HIS B 184 N THR B 115
SHEET 3 C11 PRO B 138 LYS B 142 1 N LEU B 141 O VAL B 183
SHEET 4 C11 LEU B 232 ASP B 237 1 O LEU B 232 N SER B 140
SHEET 5 C11 SER B 279 ALA B 284 -1 O GLY B 281 N GLY B 235
SHEET 6 C11 CYS B 252 LYS B 255 -1 N CYS B 252 O ALA B 284
SHEET 7 C11 ALA B 504 THR B 511 -1 O ALA B 504 N LYS B 255
SHEET 8 C11 PRO B 546 VAL B 552 -1 O CYS B 551 N GLY B 505
SHEET 9 C11 VAL B 469 PRO B 473 -1 N THR B 472 O GLN B 550
SHEET 10 C11 ARG B 326 TYR B 329 1 N GLY B 328 O LEU B 471
SHEET 11 C11 THR B 359 PRO B 362 1 O THR B 359 N VAL B 327
SHEET 1 D 2 SER B 197 ASN B 198 0
SHEET 2 D 2 GLY B 202 GLN B 203 -1 O GLY B 202 N ASN B 198
CISPEP 1 GLY A 216 SER A 217 0 4.79
CISPEP 2 GLY A 476 PRO A 477 0 -0.62
CISPEP 3 GLY B 216 SER B 217 0 6.43
CISPEP 4 GLY B 476 PRO B 477 0 -1.25
SITE 1 AC1 13 LYS A 142 MET A 191 PHE A 192 SER A 193
SITE 2 AC1 13 SER A 217 THR A 236 ILE A 238 SER A 241
SITE 3 AC1 13 LYS A 267 GLY A 268 LEU A 278 THR A 488
SITE 4 AC1 13 F A 603
SITE 1 AC2 3 ASN A 259 HOH A 866 ASN B 259
SITE 1 AC3 3 LYS A 47 HIS A 150 ASP A 151
SITE 1 AC4 6 ASP A 237 ILE A 238 GLY A 239 GLY A 240
SITE 2 AC4 6 SER A 241 JG1 A 600
SITE 1 AC5 4 ASN A 434 PRO A 438 LYS A 443 HOH A 665
SITE 1 AC6 2 ASN A 334 TYR A 526
SITE 1 AC7 15 LYS B 142 MET B 191 PHE B 192 SER B 193
SITE 2 AC7 15 SER B 217 THR B 236 ILE B 238 SER B 241
SITE 3 AC7 15 LYS B 267 GLY B 268 LEU B 278 PHE B 381
SITE 4 AC7 15 THR B 488 MET B 495 F B 602
SITE 1 AC8 3 TRP B 531 HOH B 743 HOH B 947
SITE 1 AC9 6 ASP B 237 ILE B 238 GLY B 239 GLY B 240
SITE 2 AC9 6 SER B 241 JG1 B 600
SITE 1 BC1 6 SER B 146 PRO B 163 SER B 164 GLU B 165
SITE 2 BC1 6 TYR B 271 ARG B 343
SITE 1 BC2 6 ASN B 434 ARG B 437 PRO B 438 ARG B 439
SITE 2 BC2 6 HOH B 907 HOH B1094
SITE 1 BC3 2 ASN B 334 HOH B 879
CRYST1 103.692 103.692 254.705 90.00 90.00 120.00 P 32 2 1 12
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 0.009644 0.005568 0.000000 0.00000
SCALE2 0.000000 0.011136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
