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HEADER HYDROLASE 29-JUL-15 5CXX
TITLE STRUCTURE OF A CE1 FERULIC ACID ESTERASE, AMCE1/FAE1A, FROM
TITLE 2 ANAEROMYCES MUCRONATUS IN COMPLEX WITH FERULIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE, AMCE1/FAE1A;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANAEROMYCES MUCRONATUS;
SOURCE 3 ORGANISM_TAXID: 994854;
SOURCE 4 GENE: FAE1A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS FERULIC ACID, ESTERASE, ANAEROBIC FUNGI, ALPHA/BETA-HYDROLASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,D.W.ABBOTT
REVDAT 1 27-APR-16 5CXX 0
JRNL AUTH R.J.GRUNINGER,C.COTE,T.A.MCALLISTER,D.W.ABBOTT
JRNL TITL CONTRIBUTIONS OF A UNIQUE BETA-CLAMP TO SUBSTRATE
JRNL TITL 2 RECOGNITION ILLUMINATES THE MOLECULAR BASIS OF EXOLYSIS IN
JRNL TITL 3 FERULIC ACID ESTERASES.
JRNL REF BIOCHEM.J. V. 473 839 2016
JRNL REFN ESSN 1470-8728
JRNL PMID 27026397
JRNL DOI 10.1042/BJ20151153
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 169424
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8471
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 48.7139 - 4.8147 1.00 5660 299 0.1499 0.1571
REMARK 3 2 4.8147 - 3.8221 1.00 5472 288 0.1139 0.1204
REMARK 3 3 3.8221 - 3.3391 1.00 5457 287 0.1238 0.1374
REMARK 3 4 3.3391 - 3.0338 1.00 5425 285 0.1323 0.1456
REMARK 3 5 3.0338 - 2.8164 1.00 5419 285 0.1341 0.1464
REMARK 3 6 2.8164 - 2.6504 1.00 5363 283 0.1345 0.1588
REMARK 3 7 2.6504 - 2.5176 1.00 5403 284 0.1394 0.1502
REMARK 3 8 2.5176 - 2.4080 1.00 5370 283 0.1362 0.1465
REMARK 3 9 2.4080 - 2.3153 1.00 5361 282 0.1381 0.1631
REMARK 3 10 2.3153 - 2.2354 1.00 5364 282 0.1304 0.1573
REMARK 3 11 2.2354 - 2.1655 1.00 5344 282 0.1313 0.1543
REMARK 3 12 2.1655 - 2.1036 1.00 5358 282 0.1298 0.1622
REMARK 3 13 2.1036 - 2.0483 1.00 5366 282 0.1338 0.1654
REMARK 3 14 2.0483 - 1.9983 1.00 5338 281 0.1380 0.1704
REMARK 3 15 1.9983 - 1.9529 1.00 5333 281 0.1388 0.1797
REMARK 3 16 1.9529 - 1.9113 1.00 5368 282 0.1391 0.1745
REMARK 3 17 1.9113 - 1.8731 1.00 5340 281 0.1429 0.1671
REMARK 3 18 1.8731 - 1.8377 1.00 5303 279 0.1463 0.1877
REMARK 3 19 1.8377 - 1.8049 1.00 5360 282 0.1538 0.1868
REMARK 3 20 1.8049 - 1.7743 1.00 5305 280 0.1618 0.1880
REMARK 3 21 1.7743 - 1.7457 1.00 5366 282 0.1688 0.1901
REMARK 3 22 1.7457 - 1.7188 1.00 5341 280 0.1761 0.2101
REMARK 3 23 1.7188 - 1.6935 1.00 5298 279 0.1759 0.1990
REMARK 3 24 1.6935 - 1.6697 1.00 5323 280 0.1968 0.2189
REMARK 3 25 1.6697 - 1.6471 1.00 5376 283 0.2072 0.2115
REMARK 3 26 1.6471 - 1.6257 1.00 5324 280 0.2165 0.2617
REMARK 3 27 1.6257 - 1.6054 1.00 5287 279 0.2384 0.2558
REMARK 3 28 1.6054 - 1.5861 1.00 5323 280 0.2411 0.2542
REMARK 3 29 1.5861 - 1.5676 1.00 5319 280 0.2671 0.2872
REMARK 3 30 1.5676 - 1.5500 1.00 5287 278 0.2981 0.3274
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.020 6973
REMARK 3 ANGLE : 1.753 9505
REMARK 3 CHIRALITY : 0.101 1018
REMARK 3 PLANARITY : 0.010 1226
REMARK 3 DIHEDRAL : 14.308 2632
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 4:33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 111.3275 29.8806 34.5820
REMARK 3 T TENSOR
REMARK 3 T11: 0.2168 T22: 0.1440
REMARK 3 T33: 0.1815 T12: -0.0265
REMARK 3 T13: -0.0139 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 2.1864 L22: 0.8545
REMARK 3 L33: 1.0035 L12: 0.2179
REMARK 3 L13: 0.5996 L23: 0.1259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0126 S12: -0.1870 S13: 0.0823
REMARK 3 S21: 0.1254 S22: -0.0866 S23: -0.1132
REMARK 3 S31: -0.1078 S32: 0.2472 S33: 0.0013
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 34:88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.7460 27.8649 35.4446
REMARK 3 T TENSOR
REMARK 3 T11: 0.2183 T22: 0.1503
REMARK 3 T33: 0.1548 T12: -0.0200
REMARK 3 T13: 0.0165 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.6221 L22: 1.0290
REMARK 3 L33: 1.2267 L12: 0.2838
REMARK 3 L13: 0.3409 L23: -0.2172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.1329 S13: 0.0928
REMARK 3 S21: 0.1769 S22: -0.0194 S23: 0.0418
REMARK 3 S31: -0.0789 S32: 0.0653 S33: 0.0490
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 89:115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 98.5891 21.0653 28.5721
REMARK 3 T TENSOR
REMARK 3 T11: 0.1995 T22: 0.1483
REMARK 3 T33: 0.1764 T12: -0.0076
REMARK 3 T13: 0.0320 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 1.5824 L22: 1.4763
REMARK 3 L33: 1.6573 L12: 0.6707
REMARK 3 L13: 0.1114 L23: 0.3348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0850 S12: -0.0527 S13: -0.0412
REMARK 3 S21: -0.0419 S22: -0.0311 S23: 0.0494
REMARK 3 S31: 0.0932 S32: -0.0610 S33: 0.1145
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 116:168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 94.5878 26.9328 26.5061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1977 T22: 0.1729
REMARK 3 T33: 0.1986 T12: -0.0130
REMARK 3 T13: 0.0241 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 1.1521 L22: 1.1570
REMARK 3 L33: 1.5588 L12: -0.2925
REMARK 3 L13: -0.3415 L23: 0.2472
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: 0.0470 S13: 0.0667
REMARK 3 S21: 0.0528 S22: 0.0063 S23: 0.1307
REMARK 3 S31: -0.0320 S32: -0.0757 S33: 0.0364
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 169:243 )
REMARK 3 ORIGIN FOR THE GROUP (A): 101.7285 26.5396 12.4265
REMARK 3 T TENSOR
REMARK 3 T11: 0.1582 T22: 0.2013
REMARK 3 T33: 0.1394 T12: -0.0324
REMARK 3 T13: 0.0201 T23: 0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.8418 L22: 1.5185
REMARK 3 L33: 1.4850 L12: -0.4518
REMARK 3 L13: 0.0722 L23: 0.0208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0301 S12: 0.3569 S13: 0.0944
REMARK 3 S21: -0.0840 S22: -0.0390 S23: 0.0277
REMARK 3 S31: 0.0457 S32: 0.0062 S33: 0.0597
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 244:274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 112.0844 30.0103 21.9735
REMARK 3 T TENSOR
REMARK 3 T11: 0.1688 T22: 0.2015
REMARK 3 T33: 0.1679 T12: -0.0315
REMARK 3 T13: 0.0052 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 1.9655 L22: 0.7691
REMARK 3 L33: 1.8096 L12: 0.1230
REMARK 3 L13: -0.3115 L23: 0.0731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0329 S12: 0.1324 S13: 0.1886
REMARK 3 S21: 0.0295 S22: -0.0126 S23: -0.1097
REMARK 3 S31: -0.1184 S32: 0.1652 S33: -0.0304
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 1:25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.7205 33.9259 25.0482
REMARK 3 T TENSOR
REMARK 3 T11: 0.2825 T22: 0.3165
REMARK 3 T33: 0.2039 T12: 0.0075
REMARK 3 T13: 0.0616 T23: 0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 2.2622 L22: 4.1829
REMARK 3 L33: 2.9604 L12: 0.7325
REMARK 3 L13: 0.0533 L23: 1.8882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0235 S12: -0.2928 S13: -0.1193
REMARK 3 S21: 0.2364 S22: -0.0265 S23: 0.1336
REMARK 3 S31: 0.2708 S32: -0.4989 S33: 0.0305
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 26:88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.8854 29.7415 7.6758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1867 T22: 0.2279
REMARK 3 T33: 0.2194 T12: -0.0114
REMARK 3 T13: 0.0382 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 0.9553 L22: 1.2892
REMARK 3 L33: 2.3746 L12: -0.2823
REMARK 3 L13: -0.0416 L23: 0.4772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0396 S12: 0.0943 S13: -0.2024
REMARK 3 S21: 0.0625 S22: -0.0706 S23: 0.0974
REMARK 3 S31: 0.2517 S32: -0.3191 S33: 0.0041
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN B AND RESID 89:187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 74.8989 40.2599 3.1781
REMARK 3 T TENSOR
REMARK 3 T11: 0.1855 T22: 0.2402
REMARK 3 T33: 0.1723 T12: 0.0561
REMARK 3 T13: 0.0340 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.9653 L22: 2.0982
REMARK 3 L33: 1.8613 L12: 0.1853
REMARK 3 L13: 0.1802 L23: 1.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0630 S12: 0.1880 S13: -0.0769
REMARK 3 S21: -0.2419 S22: -0.0385 S23: -0.0008
REMARK 3 S31: -0.1803 S32: -0.2877 S33: -0.0192
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND RESID 188:212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1983 55.1983 4.5820
REMARK 3 T TENSOR
REMARK 3 T11: 0.3719 T22: 0.2183
REMARK 3 T33: 0.1954 T12: 0.0957
REMARK 3 T13: 0.0620 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 4.3152 L22: 2.9573
REMARK 3 L33: 2.6680 L12: -0.3988
REMARK 3 L13: -0.5249 L23: -0.3423
REMARK 3 S TENSOR
REMARK 3 S11: 0.1704 S12: 0.6571 S13: 0.6080
REMARK 3 S21: -0.3060 S22: -0.0689 S23: 0.0020
REMARK 3 S31: -0.5449 S32: -0.3167 S33: -0.0720
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN B AND RESID 213:243 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.9563 53.8803 15.0551
REMARK 3 T TENSOR
REMARK 3 T11: 0.2743 T22: 0.2046
REMARK 3 T33: 0.1977 T12: 0.0939
REMARK 3 T13: 0.0587 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 2.9924 L22: 2.2094
REMARK 3 L33: 1.3908 L12: -1.2931
REMARK 3 L13: 0.4488 L23: -0.2315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0518 S12: -0.0555 S13: 0.2417
REMARK 3 S21: -0.1026 S22: 0.0025 S23: -0.0917
REMARK 3 S31: -0.4083 S32: -0.2751 S33: -0.0384
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN B AND RESID 244:274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 74.9036 42.5730 19.7144
REMARK 3 T TENSOR
REMARK 3 T11: 0.1791 T22: 0.2223
REMARK 3 T33: 0.1597 T12: 0.0537
REMARK 3 T13: 0.0468 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 1.0853 L22: 2.1167
REMARK 3 L33: 1.8342 L12: -0.0818
REMARK 3 L13: -0.4081 L23: 0.4830
REMARK 3 S TENSOR
REMARK 3 S11: -0.0562 S12: -0.0065 S13: 0.0214
REMARK 3 S21: 0.1086 S22: 0.0036 S23: 0.1230
REMARK 3 S31: -0.0850 S32: -0.3811 S33: 0.0423
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 3:33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.3712 79.5849 39.5893
REMARK 3 T TENSOR
REMARK 3 T11: 0.2277 T22: 0.3363
REMARK 3 T33: 0.4724 T12: -0.0131
REMARK 3 T13: 0.0492 T23: -0.1230
REMARK 3 L TENSOR
REMARK 3 L11: 0.8049 L22: 1.5091
REMARK 3 L33: 0.5727 L12: -0.1344
REMARK 3 L13: 0.1629 L23: 0.1095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: -0.1402 S13: 0.3568
REMARK 3 S21: 0.0385 S22: 0.2309 S23: -0.8245
REMARK 3 S31: -0.1190 S32: 0.3687 S33: -0.1850
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN C AND RESID 34:115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.8338 69.4021 35.8996
REMARK 3 T TENSOR
REMARK 3 T11: 0.1890 T22: 0.2861
REMARK 3 T33: 0.3027 T12: 0.0617
REMARK 3 T13: 0.0264 T23: -0.0706
REMARK 3 L TENSOR
REMARK 3 L11: 0.8788 L22: 1.9716
REMARK 3 L33: 1.2153 L12: -0.2182
REMARK 3 L13: -0.3483 L23: 0.9072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0400 S12: -0.1305 S13: 0.1527
REMARK 3 S21: -0.0226 S22: 0.1382 S23: -0.4701
REMARK 3 S31: 0.0009 S32: 0.3108 S33: -0.1231
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN C AND RESID 116:131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2262 62.2050 31.0188
REMARK 3 T TENSOR
REMARK 3 T11: 0.2221 T22: 0.1765
REMARK 3 T33: 0.2010 T12: 0.0590
REMARK 3 T13: 0.0383 T23: -0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 2.9072 L22: 3.0972
REMARK 3 L33: 6.2384 L12: -2.0594
REMARK 3 L13: 2.5056 L23: -3.2185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: 0.0628 S13: -0.0905
REMARK 3 S21: -0.2029 S22: -0.0527 S23: 0.0069
REMARK 3 S31: 0.3883 S32: 0.0801 S33: -0.0624
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN C AND RESID 132:146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.8339 59.2327 43.8755
REMARK 3 T TENSOR
REMARK 3 T11: 0.2751 T22: 0.3162
REMARK 3 T33: 0.3021 T12: 0.1383
REMARK 3 T13: -0.0502 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 2.1365 L22: 1.6352
REMARK 3 L33: 4.2388 L12: 0.6373
REMARK 3 L13: 0.2235 L23: 2.5081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: -0.2205 S13: -0.1796
REMARK 3 S21: 0.4071 S22: 0.1499 S23: -0.5638
REMARK 3 S31: 0.5627 S32: 0.3412 S33: -0.1693
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN C AND RESID 147:187 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8973 70.1541 40.8758
REMARK 3 T TENSOR
REMARK 3 T11: 0.2040 T22: 0.2072
REMARK 3 T33: 0.2064 T12: 0.0445
REMARK 3 T13: 0.0047 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 1.6057 L22: 1.3997
REMARK 3 L33: 0.5546 L12: -0.4233
REMARK 3 L13: -0.1238 L23: -0.3924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: -0.1203 S13: 0.0262
REMARK 3 S21: 0.0655 S22: 0.0095 S23: -0.1249
REMARK 3 S31: 0.0646 S32: 0.1135 S33: -0.0407
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN C AND RESID 188:212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1820 70.8344 37.3965
REMARK 3 T TENSOR
REMARK 3 T11: 0.2102 T22: 0.1735
REMARK 3 T33: 0.2168 T12: 0.0345
REMARK 3 T13: 0.0204 T23: -0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 2.0133 L22: 1.9203
REMARK 3 L33: 3.1783 L12: -0.1002
REMARK 3 L13: 0.0828 L23: -0.6308
REMARK 3 S TENSOR
REMARK 3 S11: 0.1030 S12: -0.0136 S13: -0.0259
REMARK 3 S21: 0.0130 S22: -0.0055 S23: 0.1946
REMARK 3 S31: 0.2385 S32: -0.2049 S33: -0.1128
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN C AND RESID 213:243 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.1064 80.4229 39.6082
REMARK 3 T TENSOR
REMARK 3 T11: 0.1928 T22: 0.1709
REMARK 3 T33: 0.2083 T12: 0.0366
REMARK 3 T13: 0.0430 T23: -0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 1.6387 L22: 2.3226
REMARK 3 L33: 2.6041 L12: 0.4242
REMARK 3 L13: -0.1359 L23: -0.1900
REMARK 3 S TENSOR
REMARK 3 S11: 0.1097 S12: -0.0750 S13: 0.1439
REMARK 3 S21: -0.0392 S22: -0.0659 S23: 0.0690
REMARK 3 S31: -0.1154 S32: -0.0855 S33: -0.0948
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ( CHAIN C AND RESID 244:274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.2904 82.6390 40.6511
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.2216
REMARK 3 T33: 0.2822 T12: 0.0020
REMARK 3 T13: 0.0541 T23: -0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 1.6789 L22: 2.8549
REMARK 3 L33: 0.7745 L12: -0.6452
REMARK 3 L13: 0.0839 L23: 0.5229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0425 S12: -0.0751 S13: 0.2277
REMARK 3 S21: -0.0128 S22: 0.1458 S23: -0.3493
REMARK 3 S31: -0.1406 S32: 0.1906 S33: -0.1782
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 5CXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 169434
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 48.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07037
REMARK 200 R SYM (I) : 0.07560
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.930
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5CXU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM SULFATE, 16% PEG 3350,
REMARK 280 16% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 49.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.32500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 77.06000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.89500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.32500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.06000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.89500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.32500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.06000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.89500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.32500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.06000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: BIOLOGICAL UNIT WAS SUPPORTED BY GEL FILTRATION METHOD
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 410 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 574 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 471 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 SER A 2
REMARK 465 ASN A 275
REMARK 465 ASN B 275
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASN C 275
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 627 O HOH B 640 2.04
REMARK 500 OE2 GLU B 39 O HOH B 401 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 VAL A 132 -55.88 -123.12
REMARK 500 SER A 156 -117.97 58.59
REMARK 500 SER A 156 -119.37 60.85
REMARK 500 ASP A 252 -157.00 -110.77
REMARK 500 VAL B 132 -54.52 -123.65
REMARK 500 SER B 156 -113.27 60.42
REMARK 500 SER B 193 18.92 -146.60
REMARK 500 ASP B 252 -155.67 -103.06
REMARK 500 VAL C 132 -56.08 -122.11
REMARK 500 SER C 156 -111.98 53.95
REMARK 500 ASP C 252 -152.51 -104.70
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 C 672 DISTANCE = 7.42 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FER A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FER B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FER C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CXU RELATED DB: PDB
DBREF 5CXX A 1 275 UNP F2YCB6 F2YCB6_9FUNG 1 275
DBREF 5CXX B 1 275 UNP F2YCB6 F2YCB6_9FUNG 1 275
DBREF 5CXX C 1 275 UNP F2YCB6 F2YCB6_9FUNG 1 275
SEQRES 1 A 275 MET SER LYS LEU GLN ILE SER ASN THR CYS PRO ASP LYS
SEQRES 2 A 275 TYR ARG THR LYS GLN GLU GLY VAL GLU TYR PRO THR ALA
SEQRES 3 A 275 LYS LYS ILE THR TYR TYR SER LYS VAL THR GLU THR GLU
SEQRES 4 A 275 ARG LYS MET ASN VAL ILE LEU PRO VAL GLY TYR ASP GLU
SEQRES 5 A 275 ASN LYS LYS TYR PRO VAL VAL TYR TYR LEU HIS GLY LEU
SEQRES 6 A 275 MET SER TYR GLU ASP SER MET LEU GLU ASP ASP SER THR
SEQRES 7 A 275 LEU ALA ILE PRO THR ASN LEU LEU LYS GLU GLY ARG ALA
SEQRES 8 A 275 LYS GLU MET ILE ILE VAL LEU PRO ASP VAL TYR ALA PRO
SEQRES 9 A 275 LYS PRO GLY THR ALA VAL THR PRO ASP PHE ASN PRO GLU
SEQRES 10 A 275 TYR TYR LYS GLY TYR ASP ASN PHE ILE ASN GLU LEU ILE
SEQRES 11 A 275 GLU VAL ILE MET PRO TYR MET GLU GLU HIS TYR SER ILE
SEQRES 12 A 275 LEU THR GLY ARG GLU ASN THR ALA LEU CYS GLY PHE SER
SEQRES 13 A 275 MET GLY ALA ARG THR SER LEU TYR ILE GLY TYR MET ARG
SEQRES 14 A 275 SER ASP LEU ILE GLY TYR VAL GLY ALA PHE ALA PRO ALA
SEQRES 15 A 275 PRO GLY ILE THR PRO GLY GLU ASP SER PHE SER GLY LYS
SEQRES 16 A 275 HIS GLU GLY LEU ILE SER GLU ASP GLU PHE ARG ALA GLU
SEQRES 17 A 275 ILE GLN PRO ILE VAL SER LEU ILE ASP CYS GLY THR ASN
SEQRES 18 A 275 ASP SER VAL VAL GLY GLN PHE PRO LYS SER TYR HIS GLU
SEQRES 19 A 275 ILE LEU THR ARG ASN ASN GLN GLU HIS ILE TRP PHE GLU
SEQRES 20 A 275 VAL PRO GLY ALA ASP HIS ASP TRP ASN ALA ILE SER ALA
SEQRES 21 A 275 GLY PHE TYR ASN PHE ILE GLN THR THR PHE GLY ALA LEU
SEQRES 22 A 275 ASN ASN
SEQRES 1 B 275 MET SER LYS LEU GLN ILE SER ASN THR CYS PRO ASP LYS
SEQRES 2 B 275 TYR ARG THR LYS GLN GLU GLY VAL GLU TYR PRO THR ALA
SEQRES 3 B 275 LYS LYS ILE THR TYR TYR SER LYS VAL THR GLU THR GLU
SEQRES 4 B 275 ARG LYS MET ASN VAL ILE LEU PRO VAL GLY TYR ASP GLU
SEQRES 5 B 275 ASN LYS LYS TYR PRO VAL VAL TYR TYR LEU HIS GLY LEU
SEQRES 6 B 275 MET SER TYR GLU ASP SER MET LEU GLU ASP ASP SER THR
SEQRES 7 B 275 LEU ALA ILE PRO THR ASN LEU LEU LYS GLU GLY ARG ALA
SEQRES 8 B 275 LYS GLU MET ILE ILE VAL LEU PRO ASP VAL TYR ALA PRO
SEQRES 9 B 275 LYS PRO GLY THR ALA VAL THR PRO ASP PHE ASN PRO GLU
SEQRES 10 B 275 TYR TYR LYS GLY TYR ASP ASN PHE ILE ASN GLU LEU ILE
SEQRES 11 B 275 GLU VAL ILE MET PRO TYR MET GLU GLU HIS TYR SER ILE
SEQRES 12 B 275 LEU THR GLY ARG GLU ASN THR ALA LEU CYS GLY PHE SER
SEQRES 13 B 275 MET GLY ALA ARG THR SER LEU TYR ILE GLY TYR MET ARG
SEQRES 14 B 275 SER ASP LEU ILE GLY TYR VAL GLY ALA PHE ALA PRO ALA
SEQRES 15 B 275 PRO GLY ILE THR PRO GLY GLU ASP SER PHE SER GLY LYS
SEQRES 16 B 275 HIS GLU GLY LEU ILE SER GLU ASP GLU PHE ARG ALA GLU
SEQRES 17 B 275 ILE GLN PRO ILE VAL SER LEU ILE ASP CYS GLY THR ASN
SEQRES 18 B 275 ASP SER VAL VAL GLY GLN PHE PRO LYS SER TYR HIS GLU
SEQRES 19 B 275 ILE LEU THR ARG ASN ASN GLN GLU HIS ILE TRP PHE GLU
SEQRES 20 B 275 VAL PRO GLY ALA ASP HIS ASP TRP ASN ALA ILE SER ALA
SEQRES 21 B 275 GLY PHE TYR ASN PHE ILE GLN THR THR PHE GLY ALA LEU
SEQRES 22 B 275 ASN ASN
SEQRES 1 C 275 MET SER LYS LEU GLN ILE SER ASN THR CYS PRO ASP LYS
SEQRES 2 C 275 TYR ARG THR LYS GLN GLU GLY VAL GLU TYR PRO THR ALA
SEQRES 3 C 275 LYS LYS ILE THR TYR TYR SER LYS VAL THR GLU THR GLU
SEQRES 4 C 275 ARG LYS MET ASN VAL ILE LEU PRO VAL GLY TYR ASP GLU
SEQRES 5 C 275 ASN LYS LYS TYR PRO VAL VAL TYR TYR LEU HIS GLY LEU
SEQRES 6 C 275 MET SER TYR GLU ASP SER MET LEU GLU ASP ASP SER THR
SEQRES 7 C 275 LEU ALA ILE PRO THR ASN LEU LEU LYS GLU GLY ARG ALA
SEQRES 8 C 275 LYS GLU MET ILE ILE VAL LEU PRO ASP VAL TYR ALA PRO
SEQRES 9 C 275 LYS PRO GLY THR ALA VAL THR PRO ASP PHE ASN PRO GLU
SEQRES 10 C 275 TYR TYR LYS GLY TYR ASP ASN PHE ILE ASN GLU LEU ILE
SEQRES 11 C 275 GLU VAL ILE MET PRO TYR MET GLU GLU HIS TYR SER ILE
SEQRES 12 C 275 LEU THR GLY ARG GLU ASN THR ALA LEU CYS GLY PHE SER
SEQRES 13 C 275 MET GLY ALA ARG THR SER LEU TYR ILE GLY TYR MET ARG
SEQRES 14 C 275 SER ASP LEU ILE GLY TYR VAL GLY ALA PHE ALA PRO ALA
SEQRES 15 C 275 PRO GLY ILE THR PRO GLY GLU ASP SER PHE SER GLY LYS
SEQRES 16 C 275 HIS GLU GLY LEU ILE SER GLU ASP GLU PHE ARG ALA GLU
SEQRES 17 C 275 ILE GLN PRO ILE VAL SER LEU ILE ASP CYS GLY THR ASN
SEQRES 18 C 275 ASP SER VAL VAL GLY GLN PHE PRO LYS SER TYR HIS GLU
SEQRES 19 C 275 ILE LEU THR ARG ASN ASN GLN GLU HIS ILE TRP PHE GLU
SEQRES 20 C 275 VAL PRO GLY ALA ASP HIS ASP TRP ASN ALA ILE SER ALA
SEQRES 21 C 275 GLY PHE TYR ASN PHE ILE GLN THR THR PHE GLY ALA LEU
SEQRES 22 C 275 ASN ASN
HET FER A 301 14
HET SO4 A 302 5
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET FER B 301 14
HET SO4 B 302 5
HET GOL B 303 6
HET GOL B 304 6
HET GOL B 305 6
HET FER C 301 14
HET SO4 C 302 5
HET GOL C 303 6
HET GOL C 304 6
HET GOL C 305 6
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN FER FERULIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 FER 3(C10 H10 O4)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 6 GOL 11(C3 H8 O3)
FORMUL 21 HOH *856(H2 O)
HELIX 1 AA1 PRO A 11 THR A 16 1 6
HELIX 2 AA2 ASP A 70 GLU A 74 5 5
HELIX 3 AA3 ASP A 76 GLU A 88 1 13
HELIX 4 AA4 ASN A 115 ASN A 124 1 10
HELIX 5 AA5 ASN A 124 VAL A 132 1 9
HELIX 6 AA6 VAL A 132 TYR A 141 1 10
HELIX 7 AA7 GLY A 146 GLU A 148 5 3
HELIX 8 AA8 SER A 156 ARG A 169 1 14
HELIX 9 AA9 SER A 201 PHE A 205 5 5
HELIX 10 AB1 GLN A 227 ASN A 239 1 13
HELIX 11 AB2 ASP A 254 GLN A 267 1 14
HELIX 12 AB3 THR A 268 ALA A 272 5 5
HELIX 13 AB4 PRO B 11 THR B 16 1 6
HELIX 14 AB5 ASP B 70 GLU B 74 5 5
HELIX 15 AB6 ASP B 76 GLU B 88 1 13
HELIX 16 AB7 ASN B 115 ASN B 124 1 10
HELIX 17 AB8 ASN B 124 VAL B 132 1 9
HELIX 18 AB9 VAL B 132 TYR B 141 1 10
HELIX 19 AC1 GLY B 146 GLU B 148 5 3
HELIX 20 AC2 SER B 156 ARG B 169 1 14
HELIX 21 AC3 SER B 201 PHE B 205 5 5
HELIX 22 AC4 GLN B 227 ASN B 239 1 13
HELIX 23 AC5 ASP B 254 GLN B 267 1 14
HELIX 24 AC6 THR B 268 ALA B 272 5 5
HELIX 25 AC7 PRO C 11 THR C 16 1 6
HELIX 26 AC8 ASP C 70 GLU C 74 5 5
HELIX 27 AC9 ASP C 76 GLU C 88 1 13
HELIX 28 AD1 ASN C 115 ASN C 124 1 10
HELIX 29 AD2 ASN C 124 VAL C 132 1 9
HELIX 30 AD3 VAL C 132 TYR C 141 1 10
HELIX 31 AD4 GLY C 146 GLU C 148 5 3
HELIX 32 AD5 SER C 156 ARG C 169 1 14
HELIX 33 AD6 SER C 201 PHE C 205 5 5
HELIX 34 AD7 GLN C 227 ASN C 239 1 13
HELIX 35 AD8 ASP C 254 GLN C 267 1 14
HELIX 36 AD9 THR C 268 ALA C 272 5 5
SHEET 1 AA1 8 ALA A 26 SER A 33 0
SHEET 2 AA1 8 THR A 38 ILE A 45 -1 O MET A 42 N ILE A 29
SHEET 3 AA1 8 ILE A 95 PRO A 99 -1 O ILE A 96 N ILE A 45
SHEET 4 AA1 8 VAL A 58 LEU A 62 1 N VAL A 59 O VAL A 97
SHEET 5 AA1 8 THR A 150 PHE A 155 1 O CYS A 153 N LEU A 62
SHEET 6 AA1 8 TYR A 175 PHE A 179 1 O PHE A 179 N GLY A 154
SHEET 7 AA1 8 VAL A 213 GLY A 219 1 O LEU A 215 N ALA A 178
SHEET 8 AA1 8 ILE A 244 VAL A 248 1 O ILE A 244 N ILE A 216
SHEET 1 AA2 2 GLY A 188 ASP A 190 0
SHEET 2 AA2 2 GLY A 194 HIS A 196 -1 O HIS A 196 N GLY A 188
SHEET 1 AA3 8 ALA B 26 SER B 33 0
SHEET 2 AA3 8 THR B 38 ILE B 45 -1 O MET B 42 N ILE B 29
SHEET 3 AA3 8 ILE B 95 PRO B 99 -1 O ILE B 96 N ILE B 45
SHEET 4 AA3 8 VAL B 58 LEU B 62 1 N VAL B 59 O VAL B 97
SHEET 5 AA3 8 THR B 150 PHE B 155 1 O CYS B 153 N LEU B 62
SHEET 6 AA3 8 TYR B 175 PHE B 179 1 O PHE B 179 N GLY B 154
SHEET 7 AA3 8 VAL B 213 GLY B 219 1 O LEU B 215 N ALA B 178
SHEET 8 AA3 8 ILE B 244 VAL B 248 1 O ILE B 244 N SER B 214
SHEET 1 AA4 2 GLY B 188 ASP B 190 0
SHEET 2 AA4 2 GLY B 194 HIS B 196 -1 O HIS B 196 N GLY B 188
SHEET 1 AA5 8 ALA C 26 SER C 33 0
SHEET 2 AA5 8 THR C 38 ILE C 45 -1 O ARG C 40 N TYR C 31
SHEET 3 AA5 8 ILE C 95 PRO C 99 -1 O ILE C 96 N ILE C 45
SHEET 4 AA5 8 VAL C 58 LEU C 62 1 N TYR C 61 O VAL C 97
SHEET 5 AA5 8 THR C 150 PHE C 155 1 O CYS C 153 N LEU C 62
SHEET 6 AA5 8 TYR C 175 PHE C 179 1 O PHE C 179 N GLY C 154
SHEET 7 AA5 8 VAL C 213 GLY C 219 1 O LEU C 215 N ALA C 178
SHEET 8 AA5 8 ILE C 244 VAL C 248 1 O ILE C 244 N SER C 214
SHEET 1 AA6 2 GLY C 188 ASP C 190 0
SHEET 2 AA6 2 GLY C 194 HIS C 196 -1 O HIS C 196 N GLY C 188
SITE 1 AC1 15 GLY A 64 LEU A 65 PHE A 114 TYR A 119
SITE 2 AC1 15 SER A 156 MET A 157 ARG A 160 ALA A 182
SITE 3 AC1 15 PRO A 183 ASP A 190 SER A 193 HIS A 196
SITE 4 AC1 15 HIS A 253 HOH A 507 GLU C 208
SITE 1 AC2 7 TYR A 31 TYR A 32 HOH A 403 HOH A 425
SITE 2 AC2 7 HOH A 462 HOH A 469 HOH A 486
SITE 1 AC3 7 ASN A 127 GLU A 131 ARG A 169 HOH A 411
SITE 2 AC3 7 GLU B 74 HOH B 515 HOH B 588
SITE 1 AC4 10 ASP A 171 GLU A 208 HOH A 421 HOH A 482
SITE 2 AC4 10 HOH A 508 HOH A 588 PHE B 155 HIS B 253
SITE 3 AC4 10 ASP B 254 ILE B 258
SITE 1 AC5 4 GLU A 202 GLU A 234 ARG A 238 HOH A 483
SITE 1 AC6 8 LEU A 73 GLU A 74 ASP A 75 ASP A 76
SITE 2 AC6 8 HOH A 404 HOH A 477 ASN C 127 GLU C 131
SITE 1 AC7 7 PHE A 155 HIS A 253 TRP A 255 ILE A 258
SITE 2 AC7 7 HOH A 459 HOH A 505 HOH A 564
SITE 1 AC8 14 GLU A 208 GLY B 64 LEU B 65 PHE B 114
SITE 2 AC8 14 TYR B 119 SER B 156 MET B 157 ARG B 160
SITE 3 AC8 14 ALA B 182 PRO B 183 ASP B 190 SER B 193
SITE 4 AC8 14 HIS B 196 HIS B 253
SITE 1 AC9 7 TYR B 31 TYR B 32 TYR B 136 HOH B 401
SITE 2 AC9 7 HOH B 443 HOH B 464 HOH B 531
SITE 1 AD1 5 ASP B 190 SER B 191 VAL B 224 HOH B 479
SITE 2 AD1 5 HOH B 499
SITE 1 AD2 7 HIS A 233 THR B 38 ALA B 109 HOH B 458
SITE 2 AD2 7 HOH B 493 HOH B 506 HOH B 510
SITE 1 AD3 9 ASP A 203 GLU A 204 ARG A 206 HOH A 417
SITE 2 AD3 9 HOH A 506 MET B 66 SER B 67 TYR B 68
SITE 3 AD3 9 HOH B 402
SITE 1 AD4 14 GLY C 64 LEU C 65 PHE C 114 TYR C 119
SITE 2 AD4 14 SER C 156 MET C 157 ARG C 160 ALA C 182
SITE 3 AD4 14 PRO C 183 ASP C 190 SER C 193 HIS C 196
SITE 4 AD4 14 HIS C 253 HOH C 477
SITE 1 AD5 8 TYR C 31 TYR C 32 HOH C 426 HOH C 451
SITE 2 AD5 8 HOH C 467 HOH C 489 HOH C 525 HOH C 585
SITE 1 AD6 6 PHE C 155 HIS C 253 TRP C 255 ILE C 258
SITE 2 AD6 6 HOH C 422 HOH C 485
SITE 1 AD7 11 PRO C 116 TYR C 119 ARG C 160 GLY C 184
SITE 2 AD7 11 HIS C 196 GLU C 197 GLY C 198 HOH C 403
SITE 3 AD7 11 HOH C 494 HOH C 512 HOH C 517
SITE 1 AD8 8 ASP C 190 SER C 191 SER C 223 GLY C 226
SITE 2 AD8 8 HOH C 424 HOH C 462 HOH C 504 HOH C 516
CRYST1 99.790 152.650 154.120 90.00 90.00 90.00 I 2 2 2 24
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 0.010021 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006488 0.00000
TER 2226 ASN A 274
TER 4455 ASN B 274
TER 6652 ASN C 274
MASTER 701 0 17 36 30 0 42 6 7485 3 123 66
END |