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HEADER HYDROLASE/HYDROLASE INHIBITOR 15-SEP-17 5YE9
TITLE THE CRYSTAL STRUCTURE OF LP-PLA2 IN COMPLEX WITH A NOVEL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 47-429;
COMPND 5 SYNONYM: LP-PLA2,PAF ACETYLHYDROLASE,1-ALKYL-2-
COMPND 6 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE,2-ACETYL-1-
COMPND 7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA PHOSPHOLIPASE A2,
COMPND 8 GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-PLA(2),PAF 2-
COMPND 9 ACYLHYDROLASE;
COMPND 10 EC: 3.1.1.47;
COMPND 11 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: PLA2G7, PAFAH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.F.LIU,Y.C.XU
REVDAT 1 25-JUL-18 5YE9 0
JRNL AUTH Q.LIU,F.HUANG,X.YUAN,K.WANG,Y.ZOU,J.SHEN,Y.XU
JRNL TITL STRUCTURE-GUIDED DISCOVERY OF NOVEL, POTENT, AND ORALLY
JRNL TITL 2 BIOAVAILABLE INHIBITORS OF LIPOPROTEIN-ASSOCIATED
JRNL TITL 3 PHOSPHOLIPASE A2.
JRNL REF J. MED. CHEM. V. 60 10231 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29193967
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01530
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 66566
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3333
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 29.7401 - 5.3998 0.99 2758 132 0.1633 0.1875
REMARK 3 2 5.3998 - 4.2901 1.00 2731 128 0.1385 0.1436
REMARK 3 3 4.2901 - 3.7490 0.95 2590 129 0.1416 0.1541
REMARK 3 4 3.7490 - 3.4068 0.91 2467 136 0.1498 0.1808
REMARK 3 5 3.4068 - 3.1629 1.00 2700 150 0.1640 0.1965
REMARK 3 6 3.1629 - 2.9766 1.00 2675 136 0.1748 0.2307
REMARK 3 7 2.9766 - 2.8276 1.00 2700 138 0.1733 0.2365
REMARK 3 8 2.8276 - 2.7046 1.00 2709 134 0.1773 0.2120
REMARK 3 9 2.7046 - 2.6006 1.00 2657 146 0.1722 0.2144
REMARK 3 10 2.6006 - 2.5109 1.00 2729 128 0.1714 0.2243
REMARK 3 11 2.5109 - 2.4324 1.00 2691 153 0.1729 0.2161
REMARK 3 12 2.4324 - 2.3629 1.00 2650 147 0.1685 0.2192
REMARK 3 13 2.3629 - 2.3007 1.00 2668 140 0.1739 0.2406
REMARK 3 14 2.3007 - 2.2446 1.00 2682 138 0.1743 0.1931
REMARK 3 15 2.2446 - 2.1936 0.85 2266 122 0.1788 0.2396
REMARK 3 16 2.1936 - 2.1469 1.00 2683 144 0.1694 0.1960
REMARK 3 17 2.1469 - 2.1040 1.00 2682 140 0.1755 0.2031
REMARK 3 18 2.1040 - 2.0643 1.00 2716 142 0.1817 0.1995
REMARK 3 19 2.0643 - 2.0275 0.80 2105 107 0.1926 0.2427
REMARK 3 20 2.0275 - 1.9931 1.00 2696 141 0.1887 0.2212
REMARK 3 21 1.9931 - 1.9610 1.00 2705 141 0.1960 0.2384
REMARK 3 22 1.9610 - 1.9308 1.00 2660 135 0.2075 0.2500
REMARK 3 23 1.9308 - 1.9024 1.00 2655 163 0.2261 0.2610
REMARK 3 24 1.9024 - 1.8756 1.00 2658 163 0.2509 0.3096
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 5938
REMARK 3 ANGLE : 1.071 8063
REMARK 3 CHIRALITY : 0.047 874
REMARK 3 PLANARITY : 0.005 1034
REMARK 3 DIHEDRAL : 12.510 2197
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.9982 -40.9097 15.6206
REMARK 3 T TENSOR
REMARK 3 T11: 0.2212 T22: 0.1307
REMARK 3 T33: 0.1905 T12: 0.0260
REMARK 3 T13: 0.0252 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 1.0797 L22: 1.0851
REMARK 3 L33: 2.9316 L12: -0.0334
REMARK 3 L13: 0.3919 L23: -0.3191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.0987 S13: -0.1113
REMARK 3 S21: -0.2269 S22: -0.0883 S23: -0.0596
REMARK 3 S31: 0.3196 S32: 0.0718 S33: 0.0702
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.8331 -38.2275 20.7059
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.1579
REMARK 3 T33: 0.1609 T12: -0.0257
REMARK 3 T13: -0.0190 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 4.1793 L22: 1.8233
REMARK 3 L33: 2.2048 L12: -0.3562
REMARK 3 L13: -1.2677 L23: -0.3911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: 0.1905 S13: -0.1603
REMARK 3 S21: -0.1112 S22: -0.0606 S23: 0.4366
REMARK 3 S31: 0.2931 S32: -0.3591 S33: 0.1541
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3943 -37.5244 20.2646
REMARK 3 T TENSOR
REMARK 3 T11: 0.1502 T22: 0.1412
REMARK 3 T33: 0.1791 T12: -0.0085
REMARK 3 T13: -0.0119 T23: -0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.2490 L22: 1.9755
REMARK 3 L33: 1.6192 L12: 0.1742
REMARK 3 L13: 0.0225 L23: -0.3674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.0146 S13: -0.0808
REMARK 3 S21: -0.0597 S22: -0.0167 S23: 0.1059
REMARK 3 S31: 0.1804 S32: -0.1719 S33: 0.0300
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6823 -28.2066 26.8597
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.1766
REMARK 3 T33: 0.1533 T12: -0.0079
REMARK 3 T13: 0.0065 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 3.5697 L22: 7.7870
REMARK 3 L33: 3.2503 L12: -3.5161
REMARK 3 L13: -1.4401 L23: 2.8955
REMARK 3 S TENSOR
REMARK 3 S11: -0.1302 S12: -0.1364 S13: 0.0008
REMARK 3 S21: 0.2234 S22: 0.1102 S23: -0.2171
REMARK 3 S31: 0.0663 S32: 0.0637 S33: 0.0347
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5061 -28.0284 16.7582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1476 T22: 0.1445
REMARK 3 T33: 0.1617 T12: 0.0362
REMARK 3 T13: 0.0247 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.3023 L22: 1.9656
REMARK 3 L33: 1.1224 L12: 0.0999
REMARK 3 L13: -0.1330 L23: -0.1579
REMARK 3 S TENSOR
REMARK 3 S11: -0.0529 S12: -0.0254 S13: -0.1271
REMARK 3 S21: -0.0521 S22: -0.0478 S23: -0.2985
REMARK 3 S31: 0.1618 S32: 0.1440 S33: 0.0584
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 376 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0784 -18.4384 10.8022
REMARK 3 T TENSOR
REMARK 3 T11: 0.1707 T22: 0.1777
REMARK 3 T33: 0.1842 T12: 0.0648
REMARK 3 T13: -0.0145 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 1.1883 L22: 2.8954
REMARK 3 L33: 1.9700 L12: 0.3292
REMARK 3 L13: -0.1753 L23: -0.2548
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: 0.0782 S13: 0.0965
REMARK 3 S21: -0.1482 S22: -0.0194 S23: 0.1587
REMARK 3 S31: -0.0579 S32: -0.1651 S33: 0.0275
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 377 THROUGH 425 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0153 -21.4597 1.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2750 T22: 0.2732
REMARK 3 T33: 0.1845 T12: 0.0529
REMARK 3 T13: 0.0400 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.7318 L22: 2.4815
REMARK 3 L33: 1.2137 L12: -0.8747
REMARK 3 L13: 0.0279 L23: 0.0456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: 0.3311 S13: 0.0467
REMARK 3 S21: -0.5393 S22: -0.1531 S23: -0.0953
REMARK 3 S31: 0.0124 S32: -0.0370 S33: 0.0458
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6688 -26.9597 32.8792
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.1506
REMARK 3 T33: 0.1236 T12: 0.0003
REMARK 3 T13: -0.0145 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 1.1743 L22: 1.3667
REMARK 3 L33: 1.6740 L12: 0.0480
REMARK 3 L13: -0.0959 L23: -0.2522
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.1301 S13: 0.0733
REMARK 3 S21: 0.1003 S22: 0.0209 S23: -0.0715
REMARK 3 S31: -0.0124 S32: 0.1577 S33: 0.0085
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 211 THROUGH 312 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4600 -33.4569 23.1920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.1452
REMARK 3 T33: 0.1231 T12: -0.0049
REMARK 3 T13: -0.0011 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.8876 L22: 1.9491
REMARK 3 L33: 1.5937 L12: -0.3711
REMARK 3 L13: -0.2566 L23: 0.4226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.0192 S13: -0.0613
REMARK 3 S21: 0.0551 S22: -0.0575 S23: 0.1866
REMARK 3 S31: 0.0193 S32: -0.0973 S33: 0.0459
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 313 THROUGH 376 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1594 -37.4250 14.6264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.1811
REMARK 3 T33: 0.1492 T12: 0.0190
REMARK 3 T13: 0.0053 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.6962 L22: 1.4764
REMARK 3 L33: 1.1697 L12: -0.0934
REMARK 3 L13: -0.2081 L23: 0.3714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: -0.0171 S13: -0.0502
REMARK 3 S21: 0.0287 S22: 0.0484 S23: -0.0989
REMARK 3 S31: 0.0184 S32: 0.1305 S33: -0.0461
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 377 THROUGH 424 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4477 -26.7921 7.9583
REMARK 3 T TENSOR
REMARK 3 T11: 0.1908 T22: 0.1567
REMARK 3 T33: 0.1472 T12: -0.0285
REMARK 3 T13: 0.0139 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 3.5770 L22: 2.1662
REMARK 3 L33: 2.3278 L12: -1.5577
REMARK 3 L13: 0.0427 L23: -0.6694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.2362 S13: 0.1699
REMARK 3 S21: -0.2290 S22: -0.0143 S23: -0.0284
REMARK 3 S31: -0.1770 S32: 0.0919 S33: 0.0631
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 5YE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300005134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66597
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.876
REMARK 200 RESOLUTION RANGE LOW (A) : 87.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 1.10500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: NULL
REMARK 200 STARTING MODEL: 5I8P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.6, 0.4M LI2SO4, 27%
REMARK 280 (W/V) (NH4)2SO4, 1M NA-AC, 1.4% 1,4-BUTANEDIOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.54550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.80600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.54550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.80600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 GLY A 42
REMARK 465 PRO A 43
REMARK 465 LEU A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 ALA A 47
REMARK 465 ALA A 48
REMARK 465 ALA A 49
REMARK 465 SER A 50
REMARK 465 PHE A 51
REMARK 465 GLY A 52
REMARK 465 GLN A 53
REMARK 465 THR A 54
REMARK 465 ASP A 89
REMARK 465 ASN A 90
REMARK 465 ASP A 91
REMARK 465 ARG A 92
REMARK 465 HIS A 428
REMARK 465 ILE A 429
REMARK 465 GLY B 42
REMARK 465 PRO B 43
REMARK 465 LEU B 44
REMARK 465 GLY B 45
REMARK 465 SER B 46
REMARK 465 ALA B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 SER B 50
REMARK 465 PHE B 51
REMARK 465 GLY B 52
REMARK 465 GLN B 53
REMARK 465 THR B 425
REMARK 465 ASN B 426
REMARK 465 GLN B 427
REMARK 465 HIS B 428
REMARK 465 ILE B 429
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ARG A 58 CD NE CZ NH1 NH2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 LEU A 93 CG CD1 CD2
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 HIS A 114 CG ND1 CD2 CE1 NE2
REMARK 470 TRP A 115 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 115 CZ3 CH2
REMARK 470 LEU A 116 CG CD1 CD2
REMARK 470 LEU A 123 CG CD1 CD2
REMARK 470 ASN A 133 OD1 ND2
REMARK 470 GLU A 142 CG CD OE1 OE2
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 GLN A 193 CD OE1 NE2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLN A 211 CG CD OE1 NE2
REMARK 470 GLU A 212 CG CD OE1 OE2
REMARK 470 LYS A 227 CD CE NZ
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 ASP A 304 CG OD1 OD2
REMARK 470 GLU A 340 CG CD OE1 OE2
REMARK 470 LYS A 363 CG CD CE NZ
REMARK 470 MET A 368 CG SD CE
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 ASP A 374 CG OD1 OD2
REMARK 470 ASP A 401 CG OD1 OD2
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 ASN A 426 CG OD1 ND2
REMARK 470 GLN A 427 CG CD OE1 NE2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 GLN B 88 CG CD OE1 NE2
REMARK 470 ASP B 89 CG OD1 OD2
REMARK 470 ASP B 91 CG OD1 OD2
REMARK 470 ARG B 92 CZ NH1 NH2
REMARK 470 LYS B 101 CD CE NZ
REMARK 470 THR B 113 OG1 CG2
REMARK 470 HIS B 114 CG ND1 CD2 CE1 NE2
REMARK 470 TRP B 115 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 115 CZ3 CH2
REMARK 470 LEU B 116 CG CD1 CD2
REMARK 470 LEU B 123 CG CD1 CD2
REMARK 470 GLN B 193 CD OE1 NE2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLN B 211 CG CD OE1 NE2
REMARK 470 GLU B 212 CG CD OE1 OE2
REMARK 470 LYS B 227 CD CE NZ
REMARK 470 LYS B 246 CD CE NZ
REMARK 470 ASP B 250 CG OD1 OD2
REMARK 470 LYS B 252 CG CD CE NZ
REMARK 470 GLU B 256 CG CD OE1 OE2
REMARK 470 GLU B 265 CG CD OE1 OE2
REMARK 470 GLU B 285 CG CD OE1 OE2
REMARK 470 ASP B 304 CG OD1 OD2
REMARK 470 LYS B 363 CG CD CE NZ
REMARK 470 MET B 368 CG SD CE
REMARK 470 LYS B 370 CG CD CE NZ
REMARK 470 ASP B 412 CG OD1 OD2
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 ASN B 423 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 73 -167.02 -72.64
REMARK 500 HIS A 114 -157.73 -95.77
REMARK 500 ASP A 250 71.08 -104.35
REMARK 500 LYS A 252 46.05 -82.45
REMARK 500 SER A 273 -117.98 67.59
REMARK 500 HIS A 399 63.94 -104.66
REMARK 500 ASP B 73 -168.94 -75.91
REMARK 500 LYS B 252 36.37 -81.70
REMARK 500 LYS B 266 76.97 -117.01
REMARK 500 SER B 273 -114.57 65.65
REMARK 500 HIS B 399 64.13 -102.12
REMARK 500 LYS B 400 -167.33 -120.81
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 8U6 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8U6 B 501
DBREF 5YE9 A 47 429 UNP Q13093 PAFA_HUMAN 47 429
DBREF 5YE9 B 47 429 UNP Q13093 PAFA_HUMAN 47 429
SEQADV 5YE9 GLY A 42 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 PRO A 43 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 LEU A 44 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 GLY A 45 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 SER A 46 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 GLY B 42 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 PRO B 43 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 LEU B 44 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 GLY B 45 UNP Q13093 EXPRESSION TAG
SEQADV 5YE9 SER B 46 UNP Q13093 EXPRESSION TAG
SEQRES 1 A 388 GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR
SEQRES 2 A 388 LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS
SEQRES 3 A 388 THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE
SEQRES 4 A 388 LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU
SEQRES 5 A 388 ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY
SEQRES 6 A 388 LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN
SEQRES 7 A 388 ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA
SEQRES 8 A 388 ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO
SEQRES 9 A 388 LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR
SEQRES 10 A 388 LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY
SEQRES 11 A 388 PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA
SEQRES 12 A 388 SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU
SEQRES 13 A 388 ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS
SEQRES 14 A 388 GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG
SEQRES 15 A 388 GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE
SEQRES 16 A 388 LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU
SEQRES 17 A 388 ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE
SEQRES 18 A 388 ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY
SEQRES 19 A 388 GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG
SEQRES 20 A 388 PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO
SEQRES 21 A 388 LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU
SEQRES 22 A 388 PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN
SEQRES 23 A 388 ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU
SEQRES 24 A 388 ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN
SEQRES 25 A 388 PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY
SEQRES 26 A 388 HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL
SEQRES 27 A 388 ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU
SEQRES 28 A 388 GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP
SEQRES 29 A 388 ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO
SEQRES 30 A 388 GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE
SEQRES 1 B 388 GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR
SEQRES 2 B 388 LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS
SEQRES 3 B 388 THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE
SEQRES 4 B 388 LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU
SEQRES 5 B 388 ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY
SEQRES 6 B 388 LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN
SEQRES 7 B 388 ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA
SEQRES 8 B 388 ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO
SEQRES 9 B 388 LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR
SEQRES 10 B 388 LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY
SEQRES 11 B 388 PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA
SEQRES 12 B 388 SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU
SEQRES 13 B 388 ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS
SEQRES 14 B 388 GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG
SEQRES 15 B 388 GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE
SEQRES 16 B 388 LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU
SEQRES 17 B 388 ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE
SEQRES 18 B 388 ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY
SEQRES 19 B 388 GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG
SEQRES 20 B 388 PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO
SEQRES 21 B 388 LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU
SEQRES 22 B 388 PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN
SEQRES 23 B 388 ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU
SEQRES 24 B 388 ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN
SEQRES 25 B 388 PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY
SEQRES 26 B 388 HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL
SEQRES 27 B 388 ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU
SEQRES 28 B 388 GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP
SEQRES 29 B 388 ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO
SEQRES 30 B 388 GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE
HET 8U6 A 501 33
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET 8U6 B 501 33
HETNAM 8U6 N-[4-[(3-CYANO-4-NAPHTHALEN-2-YLOXY-PHENYL)
HETNAM 2 8U6 SULFAMOYL]PHENYL]ETHANAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 8U6 2(C25 H19 N3 O4 S)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 8 HOH *223(H2 O)
HELIX 1 AA1 ASN A 100 GLY A 112 1 13
HELIX 2 AA2 HIS A 114 GLY A 126 1 13
HELIX 3 AA3 TYR A 160 HIS A 170 1 11
HELIX 4 AA4 ASP A 192 ILE A 198 1 7
HELIX 5 AA5 LYS A 210 GLU A 212 5 3
HELIX 6 AA6 GLU A 213 HIS A 241 1 29
HELIX 7 AA7 ASP A 254 LYS A 259 5 6
HELIX 8 AA8 SER A 273 ASP A 286 1 14
HELIX 9 AA9 GLY A 303 TYR A 307 5 5
HELIX 10 AB1 TYR A 324 CYS A 334 1 11
HELIX 11 AB2 VAL A 350 ALA A 360 5 11
HELIX 12 AB3 GLY A 362 LEU A 369 1 8
HELIX 13 AB4 ASP A 376 GLY A 397 1 22
HELIX 14 AB5 ASP A 401 GLN A 404 5 4
HELIX 15 AB6 TRP A 405 GLU A 410 1 6
HELIX 16 AB7 ASN B 100 GLY B 112 1 13
HELIX 17 AB8 TRP B 115 GLY B 126 1 12
HELIX 18 AB9 TYR B 160 HIS B 170 1 11
HELIX 19 AC1 ASP B 192 GLY B 199 1 8
HELIX 20 AC2 LYS B 210 GLU B 212 5 3
HELIX 21 AC3 GLU B 213 HIS B 241 1 29
HELIX 22 AC4 ASP B 254 LYS B 259 5 6
HELIX 23 AC5 SER B 273 ASP B 286 1 14
HELIX 24 AC6 GLY B 303 ARG B 309 5 7
HELIX 25 AC7 TYR B 324 LYS B 333 1 10
HELIX 26 AC8 VAL B 350 ALA B 360 5 11
HELIX 27 AC9 GLY B 362 LEU B 369 1 8
HELIX 28 AD1 ASP B 376 GLY B 397 1 22
HELIX 29 AD2 ASP B 401 GLN B 404 5 4
HELIX 30 AD3 TRP B 405 GLU B 410 1 6
SHEET 1 AA110 ASN A 133 TRP A 134 0
SHEET 2 AA110 VAL A 65 PHE A 72 1 N VAL A 65 O ASN A 133
SHEET 3 AA110 THR A 79 PRO A 86 -1 O TYR A 85 N GLY A 66
SHEET 4 AA110 ILE A 173 VAL A 177 -1 O VAL A 174 N TYR A 84
SHEET 5 AA110 TYR A 144 SER A 150 1 N VAL A 147 O ALA A 175
SHEET 6 AA110 ILE A 262 HIS A 272 1 O ASP A 263 N TYR A 144
SHEET 7 AA110 CYS A 291 LEU A 295 1 O LEU A 295 N GLY A 271
SHEET 8 AA110 LEU A 314 SER A 319 1 O PHE A 315 N ALA A 294
SHEET 9 AA110 ARG A 341 ILE A 346 1 O ILE A 344 N ASN A 318
SHEET 10 AA110 LEU A 416 PRO A 418 -1 O ILE A 417 N THR A 345
SHEET 1 AA2 2 THR A 95 LEU A 96 0
SHEET 2 AA2 2 THR A 129 THR A 130 -1 O THR A 130 N THR A 95
SHEET 1 AA3 2 ALA A 186 TYR A 189 0
SHEET 2 AA3 2 SER A 202 TYR A 205 -1 O LEU A 204 N THR A 187
SHEET 1 AA410 ASN B 133 TRP B 134 0
SHEET 2 AA410 VAL B 65 PHE B 72 1 N VAL B 65 O ASN B 133
SHEET 3 AA410 THR B 79 PRO B 86 -1 O TYR B 85 N GLY B 66
SHEET 4 AA410 ILE B 173 VAL B 177 -1 O ALA B 176 N ARG B 82
SHEET 5 AA410 TYR B 144 SER B 150 1 N VAL B 147 O ALA B 175
SHEET 6 AA410 ILE B 262 HIS B 272 1 O ASP B 263 N TYR B 144
SHEET 7 AA410 CYS B 291 LEU B 295 1 O LEU B 295 N GLY B 271
SHEET 8 AA410 LEU B 314 SER B 319 1 O PHE B 315 N ALA B 294
SHEET 9 AA410 ARG B 341 ILE B 346 1 O LYS B 342 N PHE B 316
SHEET 10 AA410 LEU B 416 PRO B 418 -1 O ILE B 417 N THR B 345
SHEET 1 AA5 2 THR B 95 LEU B 96 0
SHEET 2 AA5 2 THR B 129 THR B 130 -1 O THR B 130 N THR B 95
SHEET 1 AA6 2 ALA B 186 TYR B 189 0
SHEET 2 AA6 2 SER B 202 TYR B 205 -1 O LEU B 204 N THR B 187
CISPEP 1 PHE A 72 ASP A 73 0 -8.79
CISPEP 2 PHE B 72 ASP B 73 0 -5.73
SITE 1 AC1 11 LEU A 107 PHE A 110 GLY A 152 LEU A 153
SITE 2 AC1 11 GLY A 154 ALA A 155 HIS A 272 SER A 273
SITE 3 AC1 11 GLN A 352 ALA A 355 PHE A 357
SITE 1 AC2 5 TYR A 321 PHE A 322 VAL A 350 HIS A 351
SITE 2 AC2 5 HOH A 610
SITE 1 AC3 6 ASN A 100 LYS A 101 ARG A 122 ASP B 89
SITE 2 AC3 6 ASN B 90 HOH B 676
SITE 1 AC4 8 SER A 308 ILE A 310 PRO A 311 LYS A 339
SITE 2 AC4 8 LYS B 143 HIS B 241 ARG B 264 HOH B 607
SITE 1 AC5 13 LEU B 107 PHE B 110 GLY B 152 LEU B 153
SITE 2 AC5 13 GLY B 154 ALA B 155 HIS B 272 SER B 273
SITE 3 AC5 13 GLN B 352 ALA B 355 ASP B 356 PHE B 357
SITE 4 AC5 13 LEU B 371
CRYST1 115.091 83.612 96.601 90.00 114.90 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008689 0.000000 0.004034 0.00000
SCALE2 0.000000 0.011960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011413 0.00000
TER 2842 GLN A 427
TER 5715 THR B 424
MASTER 554 0 5 30 28 0 13 6 6017 2 81 60
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