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HEADER HYDROLASE 30-SEP-13 4C87
TITLE ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM WCFS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CARBOXYLESTERASE LPEST1;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 220668;
SOURCE 4 STRAIN: WCFS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PURI3-TEV-LPEST1
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ALVAREZ,M.ESTEBAN-TORRES,A.CORTES-CABRERA,F.GAGO,I.ACEBRON,
AUTHOR 2 R.BENAVENTE,K.MARDO,B.DE-LAS-RIVAS,R.MUNOZ,J.M.MANCHENO
REVDAT 1 02-APR-14 4C87 0
JRNL AUTH Y.ALVAREZ,M.ESTEBAN-TORRES,A.CORTES-CABRERA,F.GAGO,
JRNL AUTH 2 I.ACEBRON,R.BENAVENTE,K.MARDO,B.DE-LAS-RIVAS,R.MUNOZ,
JRNL AUTH 3 J.M.MANCHENO
JRNL TITL ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM: A NOVEL AND
JRNL TITL 2 ATYPICAL MEMBER OF THE ALPHA BETA HYDROLASE SUPERFAMILY OF
JRNL TITL 3 ENZYMES
JRNL REF PLOS ONE V. 9 92257 2014
JRNL REFN ISSN 1932-6203
JRNL PMID 24663330
JRNL DOI 10.1371/JOURNAL.PONE.0092257
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.650
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.234
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.97
REMARK 3 NUMBER OF REFLECTIONS : 74240
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1508
REMARK 3 R VALUE (WORKING SET) : 0.1491
REMARK 3 FREE R VALUE : 0.1825
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3736
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 53.2445 - 7.9418 0.99 2652 141 0.1937 0.1952
REMARK 3 2 7.9418 - 6.3069 1.00 2646 139 0.1630 0.1965
REMARK 3 3 6.3069 - 5.5106 1.00 2624 139 0.1556 0.1841
REMARK 3 4 5.5106 - 5.0072 1.00 2627 130 0.1318 0.1656
REMARK 3 5 5.0072 - 4.6485 1.00 2621 140 0.1173 0.1422
REMARK 3 6 4.6485 - 4.3746 1.00 2616 143 0.1138 0.1333
REMARK 3 7 4.3746 - 4.1556 1.00 2593 143 0.1122 0.1474
REMARK 3 8 4.1556 - 3.9748 1.00 2636 116 0.1176 0.1541
REMARK 3 9 3.9748 - 3.8218 1.00 2595 161 0.1249 0.1404
REMARK 3 10 3.8218 - 3.6899 1.00 2615 130 0.1228 0.1733
REMARK 3 11 3.6899 - 3.5746 1.00 2584 150 0.1263 0.1602
REMARK 3 12 3.5746 - 3.4724 1.00 2635 135 0.1331 0.1647
REMARK 3 13 3.4724 - 3.3810 1.00 2583 146 0.1474 0.1701
REMARK 3 14 3.3810 - 3.2985 1.00 2622 124 0.1592 0.1944
REMARK 3 15 3.2985 - 3.2236 1.00 2619 130 0.1568 0.1859
REMARK 3 16 3.2236 - 3.1550 1.00 2623 130 0.1598 0.2002
REMARK 3 17 3.1550 - 3.0919 1.00 2569 138 0.1591 0.2170
REMARK 3 18 3.0919 - 3.0335 1.00 2628 148 0.1738 0.1892
REMARK 3 19 3.0335 - 2.9794 1.00 2608 134 0.1702 0.2371
REMARK 3 20 2.9794 - 2.9289 1.00 2581 140 0.1780 0.2293
REMARK 3 21 2.9289 - 2.8816 1.00 2591 159 0.1726 0.2001
REMARK 3 22 2.8816 - 2.8373 1.00 2566 143 0.1763 0.2315
REMARK 3 23 2.8373 - 2.7956 1.00 2635 121 0.1791 0.2292
REMARK 3 24 2.7956 - 2.7562 1.00 2601 132 0.1766 0.2424
REMARK 3 25 2.7562 - 2.7189 1.00 2641 135 0.1819 0.2229
REMARK 3 26 2.7189 - 2.6836 1.00 2553 142 0.1840 0.2365
REMARK 3 27 2.6836 - 2.6501 1.00 2640 147 0.2040 0.2492
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) : 0.23
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.8
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 10940
REMARK 3 ANGLE : 1.049 14998
REMARK 3 CHIRALITY : 0.076 1721
REMARK 3 PLANARITY : 0.005 1982
REMARK 3 DIHEDRAL : 15.196 3922
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID -1 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5471 148.8467 -73.2783
REMARK 3 T TENSOR
REMARK 3 T11: 0.1610 T22: 0.1774
REMARK 3 T33: 0.0820 T12: 0.0040
REMARK 3 T13: -0.0803 T23: 0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 0.6956 L22: 0.6858
REMARK 3 L33: 1.2116 L12: -0.1162
REMARK 3 L13: 0.4915 L23: 0.1450
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: -0.0749 S13: -0.3038
REMARK 3 S21: 0.0290 S22: -0.0954 S23: -0.2201
REMARK 3 S31: 0.0884 S32: 0.0507 S33: -0.2584
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 59 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6786 160.6799 -69.9938
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: -0.0851
REMARK 3 T33: 0.2104 T12: 0.1243
REMARK 3 T13: -0.0645 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 0.2682 L22: 1.1374
REMARK 3 L33: 0.7229 L12: 0.0847
REMARK 3 L13: 0.3790 L23: -0.1556
REMARK 3 S TENSOR
REMARK 3 S11: 0.0532 S12: -0.2336 S13: 0.0436
REMARK 3 S21: -0.0537 S22: -0.1806 S23: 0.4506
REMARK 3 S31: 0.1374 S32: -0.4134 S33: -0.2109
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 147 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7669 165.5928 -71.2105
REMARK 3 T TENSOR
REMARK 3 T11: 0.0534 T22: 0.0872
REMARK 3 T33: 0.1091 T12: 0.0005
REMARK 3 T13: -0.0258 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.5262 L22: 1.2483
REMARK 3 L33: 0.4479 L12: -0.2223
REMARK 3 L13: 0.3139 L23: 0.1276
REMARK 3 S TENSOR
REMARK 3 S11: -0.0469 S12: -0.0937 S13: -0.0022
REMARK 3 S21: 0.0384 S22: 0.0650 S23: -0.0684
REMARK 3 S31: -0.0857 S32: 0.2122 S33: 0.0180
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 250 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9816 161.7585 -67.2024
REMARK 3 T TENSOR
REMARK 3 T11: 0.0958 T22: 0.1422
REMARK 3 T33: 0.1325 T12: 0.0094
REMARK 3 T13: -0.0703 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.6171 L22: 1.1382
REMARK 3 L33: 0.8598 L12: -0.7401
REMARK 3 L13: -0.1364 L23: -0.3668
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: -0.1043 S13: 0.0439
REMARK 3 S21: 0.2414 S22: 0.0388 S23: -0.2151
REMARK 3 S31: -0.0881 S32: 0.1274 S33: 0.0144
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 0 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9088 118.1897 -59.1068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1900 T22: 0.1553
REMARK 3 T33: 0.1601 T12: 0.1029
REMARK 3 T13: -0.0160 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 0.9104 L22: 1.6073
REMARK 3 L33: 1.2303 L12: -0.0400
REMARK 3 L13: 0.3246 L23: 0.8423
REMARK 3 S TENSOR
REMARK 3 S11: 0.1128 S12: 0.1529 S13: -0.1814
REMARK 3 S21: -0.1150 S22: 0.1787 S23: -0.1578
REMARK 3 S31: 0.1892 S32: 0.3258 S33: 0.1646
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESID 43 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1037 137.2183 -70.8536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0544 T22: 0.0745
REMARK 3 T33: 0.1018 T12: 0.0305
REMARK 3 T13: -0.0195 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.9359 L22: 0.4053
REMARK 3 L33: 0.8176 L12: -0.2233
REMARK 3 L13: 0.0077 L23: 0.1170
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: 0.2807 S13: 0.4359
REMARK 3 S21: -0.1288 S22: 0.2825 S23: -0.1955
REMARK 3 S31: -0.0998 S32: -0.0255 S33: 0.2497
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 81 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6031 128.9655 -77.2520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0862 T22: 0.1415
REMARK 3 T33: 0.0771 T12: 0.0202
REMARK 3 T13: -0.0520 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.3377 L22: 0.6689
REMARK 3 L33: 0.5570 L12: -0.1976
REMARK 3 L13: -0.4463 L23: -0.1336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0209 S12: 0.2879 S13: 0.0376
REMARK 3 S21: -0.2869 S22: 0.0114 S23: 0.0699
REMARK 3 S31: -0.0152 S32: -0.1057 S33: 0.0384
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESID 147 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9590 124.2494 -63.9231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0772 T22: 0.1268
REMARK 3 T33: 0.0871 T12: 0.0467
REMARK 3 T13: -0.0270 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.9676 L22: 0.4274
REMARK 3 L33: 0.3579 L12: -0.0617
REMARK 3 L13: 0.5214 L23: -0.2858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0150 S12: -0.0959 S13: -0.1364
REMARK 3 S21: -0.0093 S22: -0.0404 S23: -0.0321
REMARK 3 S31: 0.2189 S32: -0.1391 S33: -0.0604
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6525 120.6714 -60.5197
REMARK 3 T TENSOR
REMARK 3 T11: 0.1056 T22: 0.1278
REMARK 3 T33: 0.0931 T12: -0.0207
REMARK 3 T13: -0.0174 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.5759 L22: 1.1581
REMARK 3 L33: 0.9694 L12: -0.9743
REMARK 3 L13: -0.0175 L23: -0.2775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0484 S12: -0.1883 S13: -0.1974
REMARK 3 S21: -0.0288 S22: 0.0587 S23: 0.1081
REMARK 3 S31: 0.2771 S32: -0.2289 S33: 0.0053
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN B AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2366 118.1973 -65.1044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.0886
REMARK 3 T33: 0.1322 T12: 0.0741
REMARK 3 T13: -0.0307 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.0074 L22: 0.5933
REMARK 3 L33: 0.8148 L12: 0.1736
REMARK 3 L13: 0.1899 L23: -0.0763
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: 0.0272 S13: -0.2360
REMARK 3 S21: 0.0545 S22: 0.1488 S23: -0.0527
REMARK 3 S31: 0.1358 S32: 0.0425 S33: -0.0245
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND (RESID -1 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2869 130.7338-119.5130
REMARK 3 T TENSOR
REMARK 3 T11: 0.0665 T22: 0.1588
REMARK 3 T33: 0.0698 T12: 0.0720
REMARK 3 T13: 0.0944 T23: -0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 0.5059 L22: 0.6564
REMARK 3 L33: 3.2014 L12: -0.0268
REMARK 3 L13: 0.8212 L23: 0.2237
REMARK 3 S TENSOR
REMARK 3 S11: -0.1815 S12: 0.0675 S13: 0.0483
REMARK 3 S21: 0.0512 S22: -0.0441 S23: -0.3018
REMARK 3 S31: -0.3943 S32: 0.6262 S33: -0.7593
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND (RESID 43 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7801 141.5297-106.8970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.2297
REMARK 3 T33: 0.0788 T12: 0.0406
REMARK 3 T13: 0.0320 T23: -0.0893
REMARK 3 L TENSOR
REMARK 3 L11: 0.4020 L22: 0.4370
REMARK 3 L33: 0.2916 L12: 0.1798
REMARK 3 L13: -0.3504 L23: -0.0811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.2886 S13: 0.1408
REMARK 3 S21: 0.1618 S22: -0.2226 S23: 0.1199
REMARK 3 S31: -0.2092 S32: 0.0406 S33: -0.1439
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESID 81 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8683 140.9271-117.3302
REMARK 3 T TENSOR
REMARK 3 T11: -0.0864 T22: 0.1073
REMARK 3 T33: 0.0983 T12: 0.1442
REMARK 3 T13: 0.0359 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 0.9221 L22: 0.6283
REMARK 3 L33: 0.8297 L12: 0.3290
REMARK 3 L13: -0.2265 L23: 0.4232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0976 S12: -0.0734 S13: 0.3541
REMARK 3 S21: -0.3289 S22: -0.0380 S23: 0.2576
REMARK 3 S31: -0.4783 S32: -0.2782 S33: -0.3633
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN C AND (RESID 147 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4169 128.5684-119.7114
REMARK 3 T TENSOR
REMARK 3 T11: 0.0778 T22: 0.1253
REMARK 3 T33: 0.0812 T12: 0.0566
REMARK 3 T13: 0.0115 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.2048 L22: 0.4855
REMARK 3 L33: 0.3972 L12: 0.2121
REMARK 3 L13: -0.2126 L23: 0.4051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: 0.1677 S13: -0.0248
REMARK 3 S21: -0.0254 S22: 0.0035 S23: 0.1497
REMARK 3 S31: 0.0481 S32: -0.1092 S33: 0.0135
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN C AND (RESID 225 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6392 123.8165-103.3766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.2172
REMARK 3 T33: 0.0979 T12: 0.0843
REMARK 3 T13: -0.0259 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 3.2137 L22: 0.4084
REMARK 3 L33: 0.0925 L12: -0.4076
REMARK 3 L13: 0.1040 L23: 0.1132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: 0.0426 S13: -0.2727
REMARK 3 S21: 0.2401 S22: -0.0042 S23: -0.0083
REMARK 3 S31: 0.3130 S32: 0.0744 S33: -0.0205
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN C AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5657 121.1919-116.7485
REMARK 3 T TENSOR
REMARK 3 T11: 0.1075 T22: 0.1252
REMARK 3 T33: 0.0991 T12: 0.0338
REMARK 3 T13: 0.0114 T23: -0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 1.6342 L22: 0.5862
REMARK 3 L33: 0.7666 L12: 0.0220
REMARK 3 L13: -0.7168 L23: -0.3489
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0040 S13: -0.2343
REMARK 3 S21: -0.1184 S22: 0.0844 S23: 0.0905
REMARK 3 S31: 0.1120 S32: -0.0423 S33: 0.0281
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN C AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6259 130.0417-121.5712
REMARK 3 T TENSOR
REMARK 3 T11: 0.0672 T22: 0.1343
REMARK 3 T33: 0.0921 T12: 0.0496
REMARK 3 T13: 0.0083 T23: -0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 0.8591 L22: 0.6631
REMARK 3 L33: 0.4459 L12: 0.1399
REMARK 3 L13: 0.0595 L23: 0.0939
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: 0.0973 S13: 0.0126
REMARK 3 S21: -0.0520 S22: 0.0693 S23: -0.0185
REMARK 3 S31: -0.0244 S32: 0.0718 S33: 0.0038
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN D AND (RESID 0 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.2571 152.6791-127.9183
REMARK 3 T TENSOR
REMARK 3 T11: 0.2354 T22: 0.2323
REMARK 3 T33: 0.5123 T12: 0.0831
REMARK 3 T13: 0.2435 T23: -0.0870
REMARK 3 L TENSOR
REMARK 3 L11: 1.0100 L22: 0.1559
REMARK 3 L33: 1.0843 L12: 0.1302
REMARK 3 L13: 0.1128 L23: -0.3064
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: 0.0320 S13: -0.1780
REMARK 3 S21: -0.3539 S22: -0.0187 S23: -0.4745
REMARK 3 S31: 0.5227 S32: 0.4800 S33: 0.1640
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN D AND (RESID 43 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4305 153.6272-116.0854
REMARK 3 T TENSOR
REMARK 3 T11: 0.1530 T22: 0.1277
REMARK 3 T33: 0.0867 T12: 0.0154
REMARK 3 T13: 0.0280 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 0.8850 L22: 0.8513
REMARK 3 L33: 0.2888 L12: 0.0185
REMARK 3 L13: 0.0186 L23: 0.0501
REMARK 3 S TENSOR
REMARK 3 S11: 0.0683 S12: 0.0369 S13: -0.1637
REMARK 3 S21: -0.0411 S22: 0.0476 S23: 0.0032
REMARK 3 S31: 0.0551 S32: -0.0103 S33: -0.0053
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN D AND (RESID 81 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.1207 161.6781-109.5339
REMARK 3 T TENSOR
REMARK 3 T11: 0.1131 T22: 0.0752
REMARK 3 T33: 0.0954 T12: 0.0007
REMARK 3 T13: -0.0067 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.2459 L22: 0.9826
REMARK 3 L33: 1.0293 L12: -0.3235
REMARK 3 L13: 0.4047 L23: -0.5830
REMARK 3 S TENSOR
REMARK 3 S11: -0.0298 S12: -0.0620 S13: 0.0253
REMARK 3 S21: 0.1539 S22: 0.0241 S23: -0.0850
REMARK 3 S31: -0.0246 S32: 0.0327 S33: -0.0248
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN D AND (RESID 147 THROUGH 249 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7042 166.5174-123.0763
REMARK 3 T TENSOR
REMARK 3 T11: 0.2314 T22: 0.1041
REMARK 3 T33: 0.0465 T12: 0.0109
REMARK 3 T13: 0.1165 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.9152 L22: 1.2111
REMARK 3 L33: 0.7593 L12: -0.0233
REMARK 3 L13: -0.2576 L23: -0.3843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.1879 S13: 0.2228
REMARK 3 S21: -0.4211 S22: 0.0526 S23: -0.4372
REMARK 3 S31: 0.1614 S32: 0.1850 S33: -0.0264
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN D AND (RESID 250 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5901 172.0645-126.1639
REMARK 3 T TENSOR
REMARK 3 T11: 0.2299 T22: 0.1202
REMARK 3 T33: 0.2034 T12: -0.0584
REMARK 3 T13: 0.0835 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 2.2507 L22: 0.8486
REMARK 3 L33: 0.9743 L12: -0.5646
REMARK 3 L13: 0.0276 L23: -0.0813
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: 0.1098 S13: 0.2837
REMARK 3 S21: -0.4337 S22: 0.0038 S23: -0.3248
REMARK 3 S31: -0.3196 S32: 0.1944 S33: -0.0261
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN D AND (RESID 286 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.3174 160.8516-121.6891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.2101
REMARK 3 T33: 0.3253 T12: -0.0017
REMARK 3 T13: 0.2155 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.3851 L22: 0.4772
REMARK 3 L33: 0.5134 L12: 0.1393
REMARK 3 L13: -0.1984 L23: 0.0315
REMARK 3 S TENSOR
REMARK 3 S11: 0.0236 S12: 0.1453 S13: 0.0618
REMARK 3 S21: -0.2658 S22: 0.0340 S23: -0.6533
REMARK 3 S31: 0.0802 S32: 0.2839 S33: 0.0090
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 4C87 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-13.
REMARK 100 THE PDBE ID CODE IS EBI-58525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75273
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.65
REMARK 200 RESOLUTION RANGE LOW (A) : 47.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.9
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.1
REMARK 200 R MERGE FOR SHELL (I) : 0.59
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.3
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SODIUM MALONATE, 0.5 %
REMARK 280 (V/V) JEFFAMINE ED-2001, 100 MM HEPES PH 7.0, 5 MM DTT
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 84.17000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.17000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.17000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 84.17000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 92.10000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 84.17000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 84.17000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 92.10000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.5 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 350
REMARK 350 BIOMOLECULE: 2
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -16
REMARK 465 GLY A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 GLY B -16
REMARK 465 GLY B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 GLY B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY C -16
REMARK 465 GLY C -15
REMARK 465 SER C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 GLY C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLY D -16
REMARK 465 GLY D -15
REMARK 465 SER D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 GLY D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
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 OE1 GLN A 36 O HOH A 2050 1.89
REMARK 500 OG SER A 174 O HOH A 2122 2.09
REMARK 500 ND2B ASN A 193 O HOH A 2160 2.17
REMARK 500 O THR A 270 O HOH A 2196 2.11
REMARK 500 N TRP A 323 O2 GOL A 1344 2.10
REMARK 500 OD1 ASN B 97 O HOH B 2082 2.15
REMARK 500 O THR B 99 O HOH B 2083 2.16
REMARK 500 O GLY B 112 O HOH A 2088 2.09
REMARK 500 OD2 ASP B 163 OG1 THR B 166 2.10
REMARK 500 OG SER B 174 O HOH B 2089 1.92
REMARK 500 O PRO B 214 O HOH B 2141 2.16
REMARK 500 OH TYR B 234 O HOH A 2001 1.96
REMARK 500 OD1 ASP B 236 O HOH B 2163 2.19
REMARK 500 O ASN C 5 O HOH C 2011 2.02
REMARK 500 NE2 GLN C 36 O2 GOL C 1339 2.14
REMARK 500 O ALA C 45 O HOH B 2079 2.12
REMARK 500 OE1 GLN C 321 O1 GOL C 1339 2.19
REMARK 500 OG SER D 174 O HOH D 2084 2.20
REMARK 500 OH TYR D 292 O HOH D 2143 2.14
REMARK 500 O1 GOL D 1338 O HOH D 2096 2.06
REMARK 500 O HOH A 2002 O HOH B 2047 2.13
REMARK 500 O HOH A 2005 O HOH A 2022 2.11
REMARK 500 O HOH A 2038 O HOH A 2105 1.84
REMARK 500 O HOH A 2042 O HOH A 2051 1.90
REMARK 500 O HOH A 2043 O HOH B 2051 2.01
REMARK 500 O HOH A 2107 O HOH A 2134 2.11
REMARK 500 O HOH A 2109 O HOH A 2184 2.09
REMARK 500 O HOH A 2130 O HOH A 2209 1.89
REMARK 500 O HOH A 2183 O HOH A 2184 2.01
REMARK 500 O HOH B 2002 O HOH B 2018 2.05
REMARK 500 O HOH B 2134 O HOH B 2137 2.14
REMARK 500 O HOH B 2151 O HOH B 2152 2.15
REMARK 500 O HOH C 2012 O HOH C 2050 2.07
REMARK 500 O HOH C 2072 O HOH C 2142 2.06
REMARK 500 O HOH C 2078 O HOH C 2150 1.98
REMARK 500 O HOH C 2107 O HOH C 2110 2.02
REMARK 500 O HOH C 2112 O HOH C 2195 1.83
REMARK 500 O HOH C 2128 O HOH C 2129 2.16
REMARK 500 O HOH C 2237 O HOH C 2239 2.03
REMARK 500 O HOH D 2018 O HOH D 2092 1.93
REMARK 500 O HOH D 2051 O HOH D 2066 2.15
REMARK 500 O HOH D 2067 O HOH D 2135 1.94
REMARK 500 O HOH D 2084 O HOH D 2108 2.01
REMARK 500 O HOH D 2147 O HOH D 2154 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2152 O HOH C 2238 6565 1.71
REMARK 500 O HOH C 2082 O HOH D 2099 4465 2.19
REMARK 500 O HOH D 2139 O HOH C 2173 3665 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 PHE A -2 139.52 -173.42
REMARK 500 GLN A -1 -179.02 59.32
REMARK 500 MSE A 1 111.72 -167.46
REMARK 500 HIS A 98 -55.09 74.85
REMARK 500 PHE A 109 -29.95 75.95
REMARK 500 SER A 174 -129.49 57.00
REMARK 500 TYR A 202 65.15 38.70
REMARK 500 ASN A 312 -156.67 -103.76
REMARK 500 ASN B 49 55.05 70.63
REMARK 500 ASN B 82 19.18 58.73
REMARK 500 HIS B 98 18.65 59.50
REMARK 500 PHE B 109 -22.92 73.43
REMARK 500 SER B 174 -124.68 56.32
REMARK 500 TYR B 202 62.33 37.41
REMARK 500 ASN B 312 -155.11 -105.38
REMARK 500 HIS C 98 -26.12 72.00
REMARK 500 PHE C 109 -26.54 74.08
REMARK 500 PRO C 146 31.72 -99.82
REMARK 500 SER C 174 -128.18 55.52
REMARK 500 TYR C 202 63.78 31.69
REMARK 500 ALA C 206 77.63 -150.41
REMARK 500 ASN C 312 -152.89 -106.10
REMARK 500 PHE D 109 -24.97 72.67
REMARK 500 ASN D 117 27.84 -140.14
REMARK 500 SER D 174 -125.33 53.45
REMARK 500 TYR D 202 64.97 34.56
REMARK 500 PHE D 221 79.15 -118.82
REMARK 500 ASN D 312 -153.54 -103.04
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 GOL A1338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1338
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1339
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1340
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1343
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1339
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1344
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C88 RELATED DB: PDB
REMARK 900 ESTERASE LPEST1 FROM LACTOBACILLUS PLANTARUM: NATIVE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 4C89 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CARBOXYLESTERASE LPEST1 FROM
REMARK 900 LACTOBACILLUS PLANTARUM: HIGH RESOLUTION MODEL
DBREF 4C87 A 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C87 B 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C87 C 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
DBREF 4C87 D 1 337 UNP Q88Y25 Q88Y25_LACPN 1 337
SEQADV 4C87 GLY A -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY A -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 SER A -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS A -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY A -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLU A -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 ASN A -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 LEU A -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 TYR A -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 PHE A -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLN A -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY A 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY B -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY B -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 SER B -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS B -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY B -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLU B -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 ASN B -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 LEU B -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 TYR B -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 PHE B -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLN B -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY B 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY C -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY C -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 SER C -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS C -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY C -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLU C -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 ASN C -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 LEU C -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 TYR C -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 PHE C -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLN C -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY C 0 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY D -16 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY D -15 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 SER D -14 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -13 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -12 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -11 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -10 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -9 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 HIS D -8 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY D -7 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLU D -6 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 ASN D -5 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 LEU D -4 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 TYR D -3 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 PHE D -2 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLN D -1 UNP Q88Y25 EXPRESSION TAG
SEQADV 4C87 GLY D 0 UNP Q88Y25 EXPRESSION TAG
SEQRES 1 A 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 A 354 TYR PHE GLN GLY MSE PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 A 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 A 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 A 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 A 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 A 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 A 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 A 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 A 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 A 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 A 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 A 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 A 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 A 354 THR MSE ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 A 354 VAL ILE MSE ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 A 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 A 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 A 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 A 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 A 354 ILE MSE THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 A 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 A 354 THR MSE THR PRO PRO THR THR ILE MSE VAL GLY GLU PHE
SEQRES 24 A 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 A 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 A 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 A 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MSE ALA ALA
SEQRES 28 A 354 ALA LEU ILE
SEQRES 1 B 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 B 354 TYR PHE GLN GLY MSE PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 B 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 B 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 B 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 B 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 B 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 B 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 B 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 B 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 B 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 B 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 B 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 B 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 B 354 THR MSE ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 B 354 VAL ILE MSE ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 B 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 B 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 B 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 B 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 B 354 ILE MSE THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 B 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 B 354 THR MSE THR PRO PRO THR THR ILE MSE VAL GLY GLU PHE
SEQRES 24 B 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 B 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 B 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 B 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MSE ALA ALA
SEQRES 28 B 354 ALA LEU ILE
SEQRES 1 C 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 C 354 TYR PHE GLN GLY MSE PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 C 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 C 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 C 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 C 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 C 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 C 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 C 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 C 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 C 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 C 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 C 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 C 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 C 354 THR MSE ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 C 354 VAL ILE MSE ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 C 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 C 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 C 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 C 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 C 354 ILE MSE THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 C 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 C 354 THR MSE THR PRO PRO THR THR ILE MSE VAL GLY GLU PHE
SEQRES 24 C 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 C 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 C 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 C 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MSE ALA ALA
SEQRES 28 C 354 ALA LEU ILE
SEQRES 1 D 354 GLY GLY SER HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU
SEQRES 2 D 354 TYR PHE GLN GLY MSE PRO THR ILE ASN SER ILE GLN THR
SEQRES 3 D 354 THR VAL ASN GLY VAL VAL LYS ILE VAL LYS PRO PHE ASN
SEQRES 4 D 354 ASN ASP ILE ALA GLY GLU GLN PHE ASP PRO HIS VAL LEU
SEQRES 5 D 354 GLN THR LEU THR ALA PHE LYS GLN PRO ALA ILE LEU GLU
SEQRES 6 D 354 ASN ASP LEU ALA ALA LEU ARG SER GLY SER LEU THR PRO
SEQRES 7 D 354 ALA ILE ALA ASP PRO VAL GLY ASP ALA VAL THR VAL GLN
SEQRES 8 D 354 SER ARG ASN ILE THR ALA LEU ASN ARG THR VAL SER VAL
SEQRES 9 D 354 GLU TRP LEU THR PRO GLN ASN VAL ILE ASN HIS THR VAL
SEQRES 10 D 354 LEU VAL TYR PHE HIS GLY GLY ALA PHE TYR GLY GLY VAL
SEQRES 11 D 354 PRO GLY ASN ASN THR VAL LEU LEU LYS LEU VAL ALA ALA
SEQRES 12 D 354 LYS SER HIS CYS GLU ILE LEU ASN VAL ASP TYR SER LEU
SEQRES 13 D 354 ALA PRO GLU ALA PRO ALA PRO ALA GLY ILE LEU ASP GLY
SEQRES 14 D 354 LEU ALA ILE PHE GLN TYR LEU GLU GLN ARG ASP ALA GLU
SEQRES 15 D 354 THR MSE ILE THR VAL ALA GLY ASP SER ALA GLY ALA ASN
SEQRES 16 D 354 VAL ILE MSE ALA ALA THR ASN LEU ASN GLN GLN LEU GLY
SEQRES 17 D 354 SER ASN ARG ILE ASN GLN GLN LEU LEU LEU TYR PRO VAL
SEQRES 18 D 354 THR ALA PRO ASN ALA ASP HIS ALA GLY PRO LEU TRP ASP
SEQRES 19 D 354 LEU ALA ALA PHE PRO ILE ILE ASP SER GLN ARG ALA ILE
SEQRES 20 D 354 LEU THR ASN TYR HIS ASP LEU PHE ARG GLN LEU ASP SER
SEQRES 21 D 354 ILE MSE THR ASP TYR TYR VAL PRO GLU ASN PHE ASP SER
SEQRES 22 D 354 HIS SER PRO LEU ILE SER PRO LEU HIS GLN GLU ASN PHE
SEQRES 23 D 354 THR MSE THR PRO PRO THR THR ILE MSE VAL GLY GLU PHE
SEQRES 24 D 354 ASP PRO PHE ARG PRO GLN ALA TRP ALA TYR ALA GLN ARG
SEQRES 25 D 354 LEU ALA ALA ALA ASP THR ALA THR THR PHE ILE GLN TYR
SEQRES 26 D 354 GLN GLY LEU ASN HIS ALA PHE ALA PRO LEU VAL ASP GLN
SEQRES 27 D 354 TYR TRP GLN SER GLN ASP VAL ALA GLN VAL MSE ALA ALA
SEQRES 28 D 354 ALA LEU ILE
MODRES 4C87 MSE A 1 MET SELENOMETHIONINE
MODRES 4C87 MSE A 167 MET SELENOMETHIONINE
MODRES 4C87 MSE A 181 MET SELENOMETHIONINE
MODRES 4C87 MSE A 245 MET SELENOMETHIONINE
MODRES 4C87 MSE A 271 MET SELENOMETHIONINE
MODRES 4C87 MSE A 278 MET SELENOMETHIONINE
MODRES 4C87 MSE A 332 MET SELENOMETHIONINE
MODRES 4C87 MSE B 1 MET SELENOMETHIONINE
MODRES 4C87 MSE B 167 MET SELENOMETHIONINE
MODRES 4C87 MSE B 181 MET SELENOMETHIONINE
MODRES 4C87 MSE B 245 MET SELENOMETHIONINE
MODRES 4C87 MSE B 271 MET SELENOMETHIONINE
MODRES 4C87 MSE B 278 MET SELENOMETHIONINE
MODRES 4C87 MSE B 332 MET SELENOMETHIONINE
MODRES 4C87 MSE C 1 MET SELENOMETHIONINE
MODRES 4C87 MSE C 167 MET SELENOMETHIONINE
MODRES 4C87 MSE C 181 MET SELENOMETHIONINE
MODRES 4C87 MSE C 245 MET SELENOMETHIONINE
MODRES 4C87 MSE C 271 MET SELENOMETHIONINE
MODRES 4C87 MSE C 278 MET SELENOMETHIONINE
MODRES 4C87 MSE C 332 MET SELENOMETHIONINE
MODRES 4C87 MSE D 1 MET SELENOMETHIONINE
MODRES 4C87 MSE D 167 MET SELENOMETHIONINE
MODRES 4C87 MSE D 181 MET SELENOMETHIONINE
MODRES 4C87 MSE D 245 MET SELENOMETHIONINE
MODRES 4C87 MSE D 271 MET SELENOMETHIONINE
MODRES 4C87 MSE D 278 MET SELENOMETHIONINE
MODRES 4C87 MSE D 332 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 167 8
HET MSE A 181 8
HET MSE A 245 8
HET MSE A 271 8
HET MSE A 278 8
HET MSE A 332 8
HET MSE B 1 8
HET MSE B 167 8
HET MSE B 181 8
HET MSE B 245 8
HET MSE B 271 8
HET MSE B 278 8
HET MSE B 332 8
HET MSE C 1 8
HET MSE C 167 8
HET MSE C 181 8
HET MSE C 245 8
HET MSE C 271 8
HET MSE C 278 8
HET MSE C 332 8
HET MSE D 1 8
HET MSE D 167 8
HET MSE D 181 8
HET MSE D 245 8
HET MSE D 271 8
HET MSE D 278 8
HET MSE D 332 8
HET GOL A1338 6
HET GOL D1338 6
HET GOL A1339 6
HET GOL D1339 6
HET GOL A1340 6
HET GOL A1341 6
HET GOL D1340 6
HET GOL A1342 6
HET GOL B1338 6
HET GOL D1341 6
HET GOL B1339 6
HET GOL B1340 6
HET GOL C1338 6
HET GOL A1343 6
HET GOL B1341 6
HET GOL C1339 6
HET GOL A1344 6
HETNAM GOL GLYCEROL
HETNAM MSE SELENOMETHIONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 17(C3 H8 O3)
FORMUL 6 MSE 28(C5 H11 N O2 SE)
FORMUL 7 HOH *823(H2 O)
HELIX 1 1 ASP A 31 GLN A 36 1 6
HELIX 2 2 THR A 37 GLN A 43 5 7
HELIX 3 3 ASP A 50 GLY A 57 1 8
HELIX 4 4 VAL A 67 ASP A 69 5 3
HELIX 5 5 VAL A 113 ASN A 116 5 4
HELIX 6 6 ASN A 117 HIS A 129 1 13
HELIX 7 7 PRO A 146 ASP A 163 1 18
HELIX 8 8 SER A 174 LEU A 190 1 17
HELIX 9 9 GLY A 213 ASP A 217 5 5
HELIX 10 10 ASP A 217 PHE A 221 5 5
HELIX 11 11 ILE A 224 SER A 226 5 3
HELIX 12 12 GLN A 227 VAL A 250 1 24
HELIX 13 13 SER A 262 GLN A 266 5 5
HELIX 14 14 PHE A 285 ALA A 299 1 15
HELIX 15 15 TYR A 322 ALA A 335 1 14
HELIX 16 16 ASP B 31 GLN B 36 1 6
HELIX 17 17 THR B 37 GLN B 43 5 7
HELIX 18 18 ASP B 50 GLY B 57 1 8
HELIX 19 19 VAL B 67 ASP B 69 5 3
HELIX 20 20 VAL B 113 ASN B 116 5 4
HELIX 21 21 ASN B 117 HIS B 129 1 13
HELIX 22 22 PRO B 146 ASP B 163 1 18
HELIX 23 23 SER B 174 LEU B 190 1 17
HELIX 24 24 GLY B 213 ASP B 217 5 5
HELIX 25 25 ASP B 217 PHE B 221 5 5
HELIX 26 26 ILE B 224 SER B 226 5 3
HELIX 27 27 GLN B 227 VAL B 250 1 24
HELIX 28 28 SER B 262 GLN B 266 5 5
HELIX 29 29 PHE B 285 ALA B 299 1 15
HELIX 30 30 TYR B 322 ILE B 337 1 16
HELIX 31 31 ASP C 31 GLN C 36 1 6
HELIX 32 32 THR C 37 GLN C 43 5 7
HELIX 33 33 ASP C 50 SER C 58 1 9
HELIX 34 34 VAL C 67 ASP C 69 5 3
HELIX 35 35 VAL C 113 ASN C 116 5 4
HELIX 36 36 ASN C 117 HIS C 129 1 13
HELIX 37 37 PRO C 146 ASP C 163 1 18
HELIX 38 38 SER C 174 LEU C 190 1 17
HELIX 39 39 GLY C 213 ASP C 217 5 5
HELIX 40 40 ASP C 217 PHE C 221 5 5
HELIX 41 41 ILE C 224 SER C 226 5 3
HELIX 42 42 GLN C 227 VAL C 250 1 24
HELIX 43 43 SER C 262 GLN C 266 5 5
HELIX 44 44 PHE C 285 ALA C 299 1 15
HELIX 45 45 TYR C 322 ILE C 337 1 16
HELIX 46 46 ASP D 31 GLN D 36 1 6
HELIX 47 47 THR D 37 LYS D 42 5 6
HELIX 48 48 ASP D 50 SER D 56 1 7
HELIX 49 49 VAL D 67 ASP D 69 5 3
HELIX 50 50 VAL D 113 ASN D 116 5 4
HELIX 51 51 ASN D 117 HIS D 129 1 13
HELIX 52 52 PRO D 146 ASP D 163 1 18
HELIX 53 53 SER D 174 LEU D 190 1 17
HELIX 54 54 GLY D 213 ASP D 217 5 5
HELIX 55 55 ASP D 217 PHE D 221 5 5
HELIX 56 56 ILE D 224 VAL D 250 1 27
HELIX 57 57 SER D 262 GLN D 266 5 5
HELIX 58 58 PHE D 285 ALA D 298 1 14
HELIX 59 59 TYR D 322 ILE D 337 1 16
SHEET 1 AA10 ILE A 7 VAL A 11 0
SHEET 2 AA10 VAL A 14 LYS A 19 -1 O VAL A 14 N VAL A 11
SHEET 3 AA10 THR A 303 TYR A 308 1 O THR A 303 N VAL A 15
SHEET 4 AA10 THR A 275 GLY A 280 1 O THR A 275 N THR A 304
SHEET 5 AA10 ILE A 195 LEU A 201 1 O GLN A 198 N THR A 276
SHEET 6 AA10 MSE A 167 ASP A 173 1 O ILE A 168 N ASN A 196
SHEET 7 AA10 THR A 99 PHE A 104 1 O VAL A 100 N THR A 169
SHEET 8 AA10 GLU A 131 ASP A 136 1 O GLU A 131 N LEU A 101
SHEET 9 AA10 ARG A 83 PRO A 92 -1 O SER A 86 N ASP A 136
SHEET 10 AA10 VAL A 71 ALA A 80 -1 O THR A 72 N THR A 91
SHEET 1 BA10 ILE B 7 VAL B 11 0
SHEET 2 BA10 VAL B 14 LYS B 19 -1 O VAL B 14 N VAL B 11
SHEET 3 BA10 THR B 303 TYR B 308 1 O THR B 303 N VAL B 15
SHEET 4 BA10 THR B 275 GLY B 280 1 O THR B 275 N THR B 304
SHEET 5 BA10 ILE B 195 LEU B 201 1 O GLN B 198 N THR B 276
SHEET 6 BA10 MSE B 167 ASP B 173 1 O ILE B 168 N ASN B 196
SHEET 7 BA10 THR B 99 PHE B 104 1 O VAL B 100 N THR B 169
SHEET 8 BA10 GLU B 131 VAL B 135 1 O GLU B 131 N LEU B 101
SHEET 9 BA10 ARG B 83 PRO B 92 -1 O GLU B 88 N ASN B 134
SHEET 10 BA10 VAL B 71 ALA B 80 -1 O THR B 72 N THR B 91
SHEET 1 CA10 ILE C 7 VAL C 11 0
SHEET 2 CA10 VAL C 14 LYS C 19 -1 O VAL C 14 N VAL C 11
SHEET 3 CA10 THR C 303 TYR C 308 1 O THR C 303 N VAL C 15
SHEET 4 CA10 THR C 275 GLY C 280 1 O THR C 275 N THR C 304
SHEET 5 CA10 ILE C 195 LEU C 201 1 O GLN C 198 N THR C 276
SHEET 6 CA10 MSE C 167 ASP C 173 1 O ILE C 168 N ASN C 196
SHEET 7 CA10 THR C 99 PHE C 104 1 O VAL C 100 N THR C 169
SHEET 8 CA10 GLU C 131 ASP C 136 1 O GLU C 131 N LEU C 101
SHEET 9 CA10 ARG C 83 PRO C 92 -1 O SER C 86 N ASP C 136
SHEET 10 CA10 VAL C 71 ALA C 80 -1 O THR C 72 N THR C 91
SHEET 1 DA10 ILE D 7 VAL D 11 0
SHEET 2 DA10 VAL D 14 LYS D 19 -1 O VAL D 14 N VAL D 11
SHEET 3 DA10 THR D 303 TYR D 308 1 O THR D 303 N VAL D 15
SHEET 4 DA10 THR D 275 GLY D 280 1 O THR D 275 N THR D 304
SHEET 5 DA10 ILE D 195 LEU D 201 1 O GLN D 198 N THR D 276
SHEET 6 DA10 ILE D 168 ASP D 173 1 O ILE D 168 N ASN D 196
SHEET 7 DA10 VAL D 100 PHE D 104 1 O VAL D 100 N THR D 169
SHEET 8 DA10 GLU D 131 VAL D 135 1 O GLU D 131 N LEU D 101
SHEET 9 DA10 ARG D 83 PRO D 92 -1 O GLU D 88 N ASN D 134
SHEET 10 DA10 VAL D 71 ALA D 80 -1 O THR D 72 N THR D 91
LINK C GLY A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N PRO A 2 1555 1555 1.35
LINK C THR A 166 N MSE A 167 1555 1555 1.33
LINK C MSE A 167 N ILE A 168 1555 1555 1.33
LINK C ILE A 180 N MSE A 181 1555 1555 1.33
LINK C MSE A 181 N ALA A 182 1555 1555 1.33
LINK C ILE A 244 N MSE A 245 1555 1555 1.33
LINK C MSE A 245 N THR A 246 1555 1555 1.33
LINK C THR A 270 N MSE A 271 1555 1555 1.33
LINK C MSE A 271 N THR A 272 1555 1555 1.33
LINK C ILE A 277 N MSE A 278 1555 1555 1.33
LINK C MSE A 278 N VAL A 279 1555 1555 1.33
LINK C VAL A 331 N MSE A 332 1555 1555 1.33
LINK C MSE A 332 N ALA A 333 1555 1555 1.33
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N PRO B 2 1555 1555 1.34
LINK C THR B 166 N MSE B 167 1555 1555 1.33
LINK C MSE B 167 N ILE B 168 1555 1555 1.33
LINK C ILE B 180 N MSE B 181 1555 1555 1.33
LINK C MSE B 181 N ALA B 182 1555 1555 1.33
LINK C ILE B 244 N MSE B 245 1555 1555 1.33
LINK C MSE B 245 N THR B 246 1555 1555 1.33
LINK C THR B 270 N MSE B 271 1555 1555 1.33
LINK C MSE B 271 N THR B 272 1555 1555 1.33
LINK C ILE B 277 N MSE B 278 1555 1555 1.33
LINK C MSE B 278 N VAL B 279 1555 1555 1.33
LINK C VAL B 331 N MSE B 332 1555 1555 1.33
LINK C MSE B 332 N ALA B 333 1555 1555 1.33
LINK C GLY C 0 N MSE C 1 1555 1555 1.33
LINK C MSE C 1 N PRO C 2 1555 1555 1.35
LINK C THR C 166 N MSE C 167 1555 1555 1.33
LINK C MSE C 167 N ILE C 168 1555 1555 1.33
LINK C ILE C 180 N MSE C 181 1555 1555 1.34
LINK C MSE C 181 N ALA C 182 1555 1555 1.33
LINK C ILE C 244 N MSE C 245 1555 1555 1.33
LINK C MSE C 245 N THR C 246 1555 1555 1.33
LINK C THR C 270 N MSE C 271 1555 1555 1.33
LINK C MSE C 271 N THR C 272 1555 1555 1.33
LINK C ILE C 277 N MSE C 278 1555 1555 1.34
LINK C MSE C 278 N VAL C 279 1555 1555 1.33
LINK C VAL C 331 N MSE C 332 1555 1555 1.33
LINK C MSE C 332 N ALA C 333 1555 1555 1.33
LINK C GLY D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N PRO D 2 1555 1555 1.35
LINK C THR D 166 N MSE D 167 1555 1555 1.33
LINK C MSE D 167 N ILE D 168 1555 1555 1.33
LINK C ILE D 180 N MSE D 181 1555 1555 1.33
LINK C MSE D 181 N ALA D 182 1555 1555 1.33
LINK C ILE D 244 N MSE D 245 1555 1555 1.33
LINK C MSE D 245 N THR D 246 1555 1555 1.33
LINK C THR D 270 N MSE D 271 1555 1555 1.33
LINK C MSE D 271 N THR D 272 1555 1555 1.33
LINK C ILE D 277 N MSE D 278 1555 1555 1.33
LINK C MSE D 278 N VAL D 279 1555 1555 1.33
LINK C VAL D 331 N MSE D 332 1555 1555 1.33
LINK C MSE D 332 N ALA D 333 1555 1555 1.33
CISPEP 1 ALA A 140 PRO A 141 0 1.71
CISPEP 2 ALA A 145 PRO A 146 0 7.43
CISPEP 3 ALA B 140 PRO B 141 0 -2.00
CISPEP 4 ALA B 145 PRO B 146 0 5.54
CISPEP 5 ALA C 140 PRO C 141 0 -2.73
CISPEP 6 ALA C 145 PRO C 146 0 4.83
CISPEP 7 ALA D 140 PRO D 141 0 0.72
CISPEP 8 ALA D 145 PRO D 146 0 7.84
SITE 1 AC1 6 GLN A 197 THR A 275 THR A 276 THR A 304
SITE 2 AC1 6 GOL A1340 GOL A1342
SITE 1 AC2 5 ASP D 136 SER D 138 LEU D 139 HOH D2096
SITE 2 AC2 5 HOH D2098
SITE 1 AC3 10 ASP A 136 TYR A 137 SER A 138 LEU A 139
SITE 2 AC3 10 HOH A2107 HOH A2134 HOH A2137 HOH A2210
SITE 3 AC3 10 HOH A2211 HOH A2212
SITE 1 AC4 7 GLN D 197 ALA D 335 LEU D 336 ILE D 337
SITE 2 AC4 7 HOH D2118 HOH D2162 HOH D2163
SITE 1 AC5 7 THR A 276 VAL A 331 ALA A 334 ALA A 335
SITE 2 AC5 7 GOL A1338 GOL A1342 HOH A2213
SITE 1 AC6 5 LYS A 16 ARG A 286 TRP A 290 GLN A 307
SITE 2 AC6 5 HOH A2023
SITE 1 AC7 6 ASN C 253 GLU D 160 GLY D 191 SER D 192
SITE 2 AC7 6 ASN D 193 ARG D 194
SITE 1 AC8 7 GLN A 197 ALA A 334 ALA A 335 ILE A 337
SITE 2 AC8 7 GOL A1338 GOL A1340 HOH A2214
SITE 1 AC9 8 GLY A 191 SER A 192 ASN A 193 GLU B 252
SITE 2 AC9 8 ASN B 253 PHE B 254 ASP B 255 HOH B2198
SITE 1 BC1 4 THR D 232 HIS D 235 ASP D 236 ARG D 239
SITE 1 BC2 5 ARG B 286 PRO B 287 TRP B 290 HOH B2016
SITE 2 BC2 5 HOH B2183
SITE 1 BC3 5 ASP B 136 TYR B 137 SER B 138 LEU B 139
SITE 2 BC3 5 HOH B2100
SITE 1 BC4 7 LYS C 16 ARG C 286 TRP C 290 PHE C 305
SITE 2 BC4 7 GLN C 307 HOH C2241 HOH C2242
SITE 1 BC5 8 GLU A 252 ASN A 253 PHE A 254 ASP A 255
SITE 2 BC5 8 HOH A2188 HOH A2190 GLY B 191 HOH B2125
SITE 1 BC6 7 ASN B 196 ALA B 335 LEU B 336 ILE B 337
SITE 2 BC6 7 HOH B2114 HOH B2197 HOH B2199
SITE 1 BC7 7 HIS C 33 GLN C 36 THR C 37 GLN C 321
SITE 2 BC7 7 TYR C 322 HOH C2062 ALA D 62
SITE 1 BC8 7 ASP A 31 HIS A 33 TYR A 322 TRP A 323
SITE 2 BC8 7 GLN A 324 HOH A2045 HOH A2216
CRYST1 168.340 168.340 184.200 90.00 90.00 90.00 I 4 32
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 0.005940 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005429 0.00000
TER 2662 ILE A 337
TER 5295 ILE B 337
TER 7937 ILE C 337
TER 10581 ILE D 337
MASTER 854 0 45 59 40 0 34 611502 4 382 112
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