| content |
HEADER HYDROLASE 12-MAR-24 8YNW
TITLE S102A MUTANT OF POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE PHAZ FROM
TITLE 2 BACILLUS THURINGIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALPHA/BETA HYDROLASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THURINGIENSIS;
SOURCE 3 ORGANISM_TAXID: 1428;
SOURCE 4 GENE: BK719_31655;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MUTANT, DEPOLYMERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.L.WANG,L.C.YE,S.C.CHEN,C.H.HSU
REVDAT 1 11-DEC-24 8YNW 0
JRNL AUTH Y.L.WANG,L.C.YE,S.C.CHANG,S.C.CHEN,C.H.HSU
JRNL TITL STRUCTURAL INSIGHT INTO THE POLY(3-HYDROXYBUTYRATE)
JRNL TITL 2 HYDROLYSIS BY INTRACELLULAR PHB DEPOLYMERASE FROM BACILLUS
JRNL TITL 3 THURINGIENSIS.
JRNL REF INT.J.BIOL.MACROMOL. V. 284 37999 2024
JRNL REFN ISSN 0141-8130
JRNL PMID 39592048
JRNL DOI 10.1016/J.IJBIOMAC.2024.137999
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 86865
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4355
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 25.7700 - 5.8700 0.98 2792 141 0.1566 0.1693
REMARK 3 2 5.8700 - 4.6700 0.98 2793 136 0.1417 0.1655
REMARK 3 3 4.6700 - 4.0800 0.98 2756 165 0.1268 0.1681
REMARK 3 4 4.0800 - 3.7100 0.97 2785 136 0.1381 0.1849
REMARK 3 5 3.7100 - 3.4400 0.98 2752 169 0.1516 0.1823
REMARK 3 6 3.4400 - 3.2400 0.98 2790 122 0.1607 0.2138
REMARK 3 7 3.2400 - 3.0800 0.98 2757 160 0.1743 0.2171
REMARK 3 8 3.0800 - 2.9500 0.99 2828 145 0.1759 0.2384
REMARK 3 9 2.9500 - 2.8300 0.98 2780 153 0.1836 0.2351
REMARK 3 10 2.8300 - 2.7400 0.98 2790 143 0.1753 0.2399
REMARK 3 11 2.7400 - 2.6500 0.98 2784 142 0.1794 0.2258
REMARK 3 12 2.6500 - 2.5700 0.98 2731 169 0.1649 0.2351
REMARK 3 13 2.5700 - 2.5100 0.98 2803 143 0.1704 0.2615
REMARK 3 14 2.5100 - 2.4500 0.98 2803 138 0.1686 0.2107
REMARK 3 15 2.4500 - 2.3900 0.98 2691 137 0.1638 0.2405
REMARK 3 16 2.3900 - 2.3400 0.98 2820 161 0.1691 0.2450
REMARK 3 17 2.3400 - 2.2900 0.97 2776 144 0.1664 0.2334
REMARK 3 18 2.2900 - 2.2500 0.97 2736 147 0.1702 0.2434
REMARK 3 19 2.2500 - 2.2100 0.97 2753 163 0.1632 0.2267
REMARK 3 20 2.2100 - 2.1700 0.97 2744 139 0.1680 0.2310
REMARK 3 21 2.1700 - 2.1400 0.97 2730 152 0.1790 0.2390
REMARK 3 22 2.1400 - 2.1000 0.97 2803 161 0.1827 0.2604
REMARK 3 23 2.1000 - 2.0700 0.97 2742 132 0.1878 0.2480
REMARK 3 24 2.0700 - 2.0400 0.97 2687 141 0.1894 0.2736
REMARK 3 25 2.0400 - 2.0200 0.97 2833 135 0.1852 0.2704
REMARK 3 26 2.0200 - 1.9900 0.96 2683 137 0.1867 0.2418
REMARK 3 27 1.9900 - 1.9600 0.96 2705 158 0.1990 0.2494
REMARK 3 28 1.9600 - 1.9400 0.96 2706 147 0.1938 0.2565
REMARK 3 29 1.9400 - 1.9200 0.96 2769 136 0.2009 0.2394
REMARK 3 30 1.9200 - 1.9000 0.84 2388 103 0.2135 0.2851
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) : 0.187
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.896
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.30
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 9812
REMARK 3 ANGLE : 0.798 13294
REMARK 3 CHIRALITY : 0.053 1479
REMARK 3 PLANARITY : 0.005 1711
REMARK 3 DIHEDRAL : 10.061 1294
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.1385 13.4408 81.7371
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1619
REMARK 3 T33: 0.1273 T12: 0.0311
REMARK 3 T13: -0.0160 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 3.3412 L22: 2.7490
REMARK 3 L33: 2.1873 L12: 0.6970
REMARK 3 L13: 0.2286 L23: 0.5312
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: -0.0585 S13: -0.2409
REMARK 3 S21: 0.2108 S22: 0.0145 S23: -0.2458
REMARK 3 S31: 0.3290 S32: 0.2196 S33: 0.0233
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7658 11.5066 87.6441
REMARK 3 T TENSOR
REMARK 3 T11: 0.2007 T22: 0.1242
REMARK 3 T33: 0.1115 T12: 0.0266
REMARK 3 T13: 0.0048 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 4.7362 L22: 1.9602
REMARK 3 L33: 4.5098 L12: -0.2663
REMARK 3 L13: 0.3323 L23: 2.1904
REMARK 3 S TENSOR
REMARK 3 S11: -0.0593 S12: -0.3290 S13: -0.2703
REMARK 3 S21: 0.2890 S22: -0.0791 S23: 0.1503
REMARK 3 S31: 0.4187 S32: 0.1173 S33: 0.1447
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.2196 24.3422 74.5788
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.1608
REMARK 3 T33: 0.1033 T12: -0.0110
REMARK 3 T13: 0.0155 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 6.4267 L22: 7.2130
REMARK 3 L33: 0.4213 L12: -0.9291
REMARK 3 L13: 0.9071 L23: 1.3035
REMARK 3 S TENSOR
REMARK 3 S11: 0.2363 S12: 0.3995 S13: -0.0088
REMARK 3 S21: -0.1614 S22: -0.0649 S23: -0.1469
REMARK 3 S31: -0.0599 S32: 0.2390 S33: -0.0810
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.1976 12.4228 70.4266
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.2021
REMARK 3 T33: 0.1414 T12: -0.0079
REMARK 3 T13: -0.0546 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 5.0073 L22: 2.4344
REMARK 3 L33: 3.9172 L12: 0.3339
REMARK 3 L13: -1.2598 L23: 1.2268
REMARK 3 S TENSOR
REMARK 3 S11: 0.1148 S12: 0.1732 S13: -0.2898
REMARK 3 S21: -0.2887 S22: 0.0463 S23: -0.4791
REMARK 3 S31: 0.2401 S32: 0.1872 S33: -0.1298
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7039 17.0602 73.8229
REMARK 3 T TENSOR
REMARK 3 T11: 0.1098 T22: 0.1123
REMARK 3 T33: 0.0822 T12: -0.0170
REMARK 3 T13: -0.0042 T23: 0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 2.1400 L22: 3.6593
REMARK 3 L33: 4.3466 L12: -1.4136
REMARK 3 L13: -0.5413 L23: 3.0421
REMARK 3 S TENSOR
REMARK 3 S11: 0.0744 S12: -0.0178 S13: 0.0055
REMARK 3 S21: 0.0757 S22: -0.0716 S23: -0.0105
REMARK 3 S31: 0.1958 S32: -0.0414 S33: 0.0105
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6703 43.7754 74.9244
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.1053
REMARK 3 T33: 0.1402 T12: -0.0044
REMARK 3 T13: 0.0190 T23: 0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 3.3198 L22: 8.8915
REMARK 3 L33: 4.3055 L12: 0.1392
REMARK 3 L13: 1.0252 L23: 5.3658
REMARK 3 S TENSOR
REMARK 3 S11: -0.0313 S12: 0.0277 S13: 0.0133
REMARK 3 S21: 0.2159 S22: -0.0176 S23: -0.1857
REMARK 3 S31: 0.0345 S32: -0.1245 S33: 0.0780
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8162 40.4188 80.6113
REMARK 3 T TENSOR
REMARK 3 T11: 0.2141 T22: 0.1588
REMARK 3 T33: 0.2536 T12: -0.0188
REMARK 3 T13: 0.0386 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 7.0231 L22: 5.4235
REMARK 3 L33: 7.0415 L12: -1.3342
REMARK 3 L13: 4.8467 L23: -1.6095
REMARK 3 S TENSOR
REMARK 3 S11: -0.2906 S12: 0.1145 S13: 0.5751
REMARK 3 S21: -0.1591 S22: -0.2374 S23: -0.5259
REMARK 3 S31: -0.7059 S32: 0.2506 S33: 0.4155
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0757 28.3580 81.5202
REMARK 3 T TENSOR
REMARK 3 T11: 0.1089 T22: 0.1300
REMARK 3 T33: 0.1323 T12: 0.0210
REMARK 3 T13: 0.0019 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.2833 L22: 1.2646
REMARK 3 L33: 1.9679 L12: 0.2179
REMARK 3 L13: 0.2548 L23: -0.0273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0334 S12: -0.0701 S13: 0.1220
REMARK 3 S21: 0.0591 S22: -0.0566 S23: 0.0500
REMARK 3 S31: -0.0969 S32: -0.0987 S33: 0.0887
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4299 21.9276 76.0656
REMARK 3 T TENSOR
REMARK 3 T11: 0.0902 T22: 0.2438
REMARK 3 T33: 0.1955 T12: -0.0204
REMARK 3 T13: 0.0176 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 2.4379 L22: 1.6316
REMARK 3 L33: 6.3873 L12: -0.1462
REMARK 3 L13: 1.6328 L23: 1.9890
REMARK 3 S TENSOR
REMARK 3 S11: -0.1880 S12: -0.1171 S13: 0.1395
REMARK 3 S21: -0.0731 S22: -0.0243 S23: 0.3603
REMARK 3 S31: -0.0258 S32: -0.4571 S33: 0.2247
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 275 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4078 15.8617 88.7397
REMARK 3 T TENSOR
REMARK 3 T11: 0.2447 T22: 0.2634
REMARK 3 T33: 0.1499 T12: -0.0741
REMARK 3 T13: 0.0126 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.0148 L22: 3.0782
REMARK 3 L33: 4.2431 L12: 0.4372
REMARK 3 L13: 1.2980 L23: 0.8558
REMARK 3 S TENSOR
REMARK 3 S11: 0.0906 S12: -0.4051 S13: -0.2438
REMARK 3 S21: 0.3843 S22: -0.2092 S23: 0.2086
REMARK 3 S31: 0.6825 S32: -0.5860 S33: 0.0288
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7558 73.2936 57.2840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.0873
REMARK 3 T33: 0.0773 T12: 0.0135
REMARK 3 T13: 0.0157 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 3.1401 L22: 1.8161
REMARK 3 L33: 1.7917 L12: 0.1840
REMARK 3 L13: 0.0460 L23: -0.4398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.0151 S13: 0.1890
REMARK 3 S21: -0.0533 S22: 0.0081 S23: -0.0516
REMARK 3 S31: -0.1076 S32: -0.1040 S33: 0.0353
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9974 62.1553 52.4956
REMARK 3 T TENSOR
REMARK 3 T11: 0.1038 T22: 0.0834
REMARK 3 T33: 0.0897 T12: -0.0132
REMARK 3 T13: 0.0109 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 2.9871 L22: 1.3957
REMARK 3 L33: 1.5960 L12: -0.2805
REMARK 3 L13: 0.5326 L23: -0.4104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: 0.1037 S13: -0.1654
REMARK 3 S21: -0.1172 S22: -0.0394 S23: 0.0309
REMARK 3 S31: 0.0623 S32: -0.0849 S33: 0.0422
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7357 46.6346 72.2857
REMARK 3 T TENSOR
REMARK 3 T11: 0.1752 T22: 0.1640
REMARK 3 T33: 0.2180 T12: -0.0170
REMARK 3 T13: 0.0197 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 2.2801 L22: 4.2117
REMARK 3 L33: 2.2121 L12: -1.3263
REMARK 3 L13: -0.3296 L23: 1.3513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0790 S12: -0.2228 S13: -0.4050
REMARK 3 S21: 0.3421 S22: 0.1170 S23: 0.1864
REMARK 3 S31: 0.3228 S32: -0.0995 S33: -0.0100
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.3364 57.7568 66.3869
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.0746
REMARK 3 T33: 0.1172 T12: 0.0023
REMARK 3 T13: -0.0022 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.1489 L22: 0.5891
REMARK 3 L33: 0.8036 L12: 0.2595
REMARK 3 L13: -0.1073 L23: -0.2505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: -0.0135 S13: -0.1528
REMARK 3 S21: 0.0160 S22: 0.0211 S23: -0.0562
REMARK 3 S31: -0.0487 S32: 0.0298 S33: -0.0109
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.1329 62.3503 60.8099
REMARK 3 T TENSOR
REMARK 3 T11: 0.0556 T22: 0.1393
REMARK 3 T33: 0.1760 T12: -0.0025
REMARK 3 T13: -0.0093 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.1514 L22: 2.9624
REMARK 3 L33: 3.1774 L12: -0.2243
REMARK 3 L13: -0.3657 L23: 0.9663
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: -0.0382 S13: 0.0227
REMARK 3 S21: 0.0066 S22: 0.0026 S23: -0.3556
REMARK 3 S31: -0.0339 S32: 0.3186 S33: -0.0092
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 85.1105 60.6314 24.0363
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.1095
REMARK 3 T33: 0.1097 T12: -0.0128
REMARK 3 T13: 0.0235 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 2.0827 L22: 2.2715
REMARK 3 L33: 1.9430 L12: -0.2448
REMARK 3 L13: 0.6832 L23: 0.2337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: 0.0919 S13: 0.1481
REMARK 3 S21: 0.0027 S22: 0.0407 S23: -0.1176
REMARK 3 S31: -0.1253 S32: 0.1397 S33: -0.0102
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 97 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 74.0831 59.2141 30.7381
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.0905
REMARK 3 T33: 0.0923 T12: 0.0083
REMARK 3 T13: 0.0207 T23: 0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 3.5610 L22: 2.5337
REMARK 3 L33: 3.9962 L12: 0.7820
REMARK 3 L13: 1.4408 L23: 1.9931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0346 S12: -0.1457 S13: 0.0725
REMARK 3 S21: 0.0200 S22: -0.0634 S23: 0.0496
REMARK 3 S31: -0.0449 S32: -0.0198 S33: 0.0345
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 131 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.6380 32.8057 27.2561
REMARK 3 T TENSOR
REMARK 3 T11: 0.1920 T22: 0.1190
REMARK 3 T33: 0.1685 T12: 0.0148
REMARK 3 T13: 0.0233 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 3.0452 L22: 4.7195
REMARK 3 L33: 2.3852 L12: 1.6030
REMARK 3 L13: 0.3541 L23: 2.4022
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.2285 S13: 0.1586
REMARK 3 S21: -0.2424 S22: 0.1719 S23: -0.2064
REMARK 3 S31: -0.2413 S32: -0.2632 S33: -0.0877
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.1883 50.1027 21.6657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0975 T22: 0.1030
REMARK 3 T33: 0.1147 T12: -0.0218
REMARK 3 T13: 0.0163 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.8160 L22: 1.2017
REMARK 3 L33: 1.4499 L12: -0.2210
REMARK 3 L13: -0.0247 L23: 0.1464
REMARK 3 S TENSOR
REMARK 3 S11: 0.0147 S12: 0.0735 S13: -0.0252
REMARK 3 S21: -0.0246 S22: -0.0140 S23: 0.0750
REMARK 3 S31: -0.0016 S32: -0.1088 S33: 0.0048
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8736 7.4933 44.5139
REMARK 3 T TENSOR
REMARK 3 T11: 0.1023 T22: 0.0890
REMARK 3 T33: 0.0970 T12: -0.0201
REMARK 3 T13: -0.0209 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.3243 L22: 2.2280
REMARK 3 L33: 1.7966 L12: -0.7521
REMARK 3 L13: -0.5017 L23: -0.1195
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: 0.0158 S13: -0.1641
REMARK 3 S21: -0.0096 S22: 0.0196 S23: 0.1173
REMARK 3 S31: 0.0802 S32: -0.0238 S33: 0.0234
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 77 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9057 14.1126 51.8840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1388 T22: 0.0910
REMARK 3 T33: 0.0987 T12: -0.0134
REMARK 3 T13: -0.0271 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 3.2094 L22: 1.2282
REMARK 3 L33: 2.2262 L12: 0.5262
REMARK 3 L13: -1.3454 L23: 0.1873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: -0.2822 S13: -0.0125
REMARK 3 S21: 0.1348 S22: -0.1054 S23: 0.0133
REMARK 3 S31: 0.0526 S32: 0.0612 S33: 0.0234
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 126 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.3955 24.1803 31.8156
REMARK 3 T TENSOR
REMARK 3 T11: 0.1282 T22: 0.1443
REMARK 3 T33: 0.1221 T12: 0.0027
REMARK 3 T13: 0.0068 T23: 0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 1.7556 L22: 2.0303
REMARK 3 L33: 1.5035 L12: 0.0855
REMARK 3 L13: 0.2650 L23: 0.4866
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: 0.2406 S13: 0.2254
REMARK 3 S21: -0.1295 S22: -0.0262 S23: 0.0912
REMARK 3 S31: -0.1573 S32: -0.1058 S33: 0.0264
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 229 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1139 22.2265 43.8036
REMARK 3 T TENSOR
REMARK 3 T11: 0.0973 T22: 0.1048
REMARK 3 T33: 0.1377 T12: -0.0580
REMARK 3 T13: 0.0006 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.4196 L22: 3.5423
REMARK 3 L33: 1.0177 L12: -1.0932
REMARK 3 L13: 0.1477 L23: -0.4492
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0785 S13: 0.0613
REMARK 3 S21: 0.3034 S22: 0.0347 S23: -0.1603
REMARK 3 S31: -0.0441 S32: 0.1007 S33: -0.0346
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 256 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.3336 12.6813 39.4823
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: 0.1420
REMARK 3 T33: 0.1467 T12: 0.0063
REMARK 3 T13: 0.0094 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 2.5915 L22: 3.3900
REMARK 3 L33: 3.1840 L12: 0.7235
REMARK 3 L13: 0.7255 L23: 0.2919
REMARK 3 S TENSOR
REMARK 3 S11: 0.0755 S12: 0.0106 S13: -0.1338
REMARK 3 S21: -0.0104 S22: -0.1009 S23: -0.3349
REMARK 3 S31: 0.1465 S32: 0.3101 S33: 0.0021
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 8YNW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300045482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-15
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 : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91138
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 8YNV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 6.5, 0.2 M AMMONIUM
REMARK 280 ACETATE, 25 % PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -10
REMARK 465 ARG A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 LYS A 300
REMARK 465 MET B -10
REMARK 465 ARG B -9
REMARK 465 GLY B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ILE B 2
REMARK 465 LYS B 3
REMARK 465 MET C -10
REMARK 465 ARG C -9
REMARK 465 GLY C -8
REMARK 465 SER C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 LYS C 300
REMARK 465 MET D -10
REMARK 465 ARG D -9
REMARK 465 GLY D -8
REMARK 465 SER D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 ILE D 2
REMARK 465 LYS D 3
REMARK 465 LYS D 300
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 NZ LYS D 291 O HOH D 501 2.12
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 SER A 40 -164.57 -124.48
REMARK 500 ALA A 102 -118.87 63.49
REMARK 500 ILE A 186 -56.92 -130.36
REMARK 500 ASN A 221 93.22 -160.13
REMARK 500 CYS A 285 67.48 -158.94
REMARK 500 ALA B 102 -122.38 59.35
REMARK 500 ILE B 186 -60.98 -121.84
REMARK 500 ASN B 268 53.79 -146.20
REMARK 500 CYS B 285 61.12 -161.42
REMARK 500 ALA C 102 -121.27 60.19
REMARK 500 ILE C 186 -58.01 -127.77
REMARK 500 CYS C 285 67.53 -154.86
REMARK 500 ALA D 102 -120.81 51.87
REMARK 500 ILE D 186 -63.72 -123.62
REMARK 500 CYS D 285 66.30 -159.77
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 B 759 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 633 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH C 634 DISTANCE = 7.15 ANGSTROMS
DBREF1 8YNW A 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNW A A0A9X6EQW5 2 300
DBREF1 8YNW B 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNW B A0A9X6EQW5 2 300
DBREF1 8YNW C 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNW C A0A9X6EQW5 2 300
DBREF1 8YNW D 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNW D A0A9X6EQW5 2 300
SEQADV 8YNW MET A -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNW ARG A -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY A -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER A -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS A -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY A 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER A 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW ALA A 102 UNP A0A9X6EQW SER 102 ENGINEERED MUTATION
SEQADV 8YNW MET B -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNW ARG B -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY B -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER B -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS B -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY B 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER B 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW ALA B 102 UNP A0A9X6EQW SER 102 ENGINEERED MUTATION
SEQADV 8YNW MET C -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNW ARG C -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY C -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER C -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS C -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY C 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER C 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW ALA C 102 UNP A0A9X6EQW SER 102 ENGINEERED MUTATION
SEQADV 8YNW MET D -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNW ARG D -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY D -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER D -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW HIS D -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW GLY D 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW SER D 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNW ALA D 102 UNP A0A9X6EQW SER 102 ENGINEERED MUTATION
SEQRES 1 A 311 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE
SEQRES 2 A 311 LYS PRO ALA THR MET GLU PHE VAL SER LEU SER ASN GLY
SEQRES 3 A 311 GLU THR ILE ALA TYR GLN GLU VAL GLY ARG ARG ASN THR
SEQRES 4 A 311 ASP ILE LEU VAL LEU ILE HIS GLY ASN MET THR SER SER
SEQRES 5 A 311 GLN HIS TRP ASP LEU VAL ILE GLU LYS LEU GLN ASP GLN
SEQRES 6 A 311 TYR HIS ILE TYR ALA LEU ASP LEU ARG GLY PHE GLY GLN
SEQRES 7 A 311 SER THR TYR ASN GLN SER ILE ASP SER LEU GLN ASP PHE
SEQRES 8 A 311 ALA GLU ASP VAL LYS LEU PHE ILE ASP GLU LEU LYS LEU
SEQRES 9 A 311 GLU LYS PHE SER LEU MET GLY TRP ALA MET GLY GLY GLY
SEQRES 10 A 311 VAL ALA MET GLN PHE THR ALA ASN HIS PRO THR PHE VAL
SEQRES 11 A 311 GLU LYS LEU ILE LEU VAL GLU SER VAL GLY MET LYS GLY
SEQRES 12 A 311 TYR PRO ILE PHE LYS LYS ASP THR ASN GLY GLN PRO ILE
SEQRES 13 A 311 VAL SER SER LEU VAL LYS THR LYS GLU GLU ILE ALA GLN
SEQRES 14 A 311 ASP PRO VAL GLN ILE ALA PRO VAL LEU ASP ALA ILE LYS
SEQRES 15 A 311 ASN MET ASN LYS LEU TYR TYR ARG THR VAL TRP ASN LEU
SEQRES 16 A 311 LEU ILE TYR THR HIS ASN GLN PRO GLU PRO ASP ARG TYR
SEQRES 17 A 311 GLU LYS TYR LEU ASP ASP MET LEU THR GLN ARG ASN PHE
SEQRES 18 A 311 VAL ASP VAL ASN TYR ALA LEU ILE THR PHE ASN ILE SER
SEQRES 19 A 311 ASP GLU HIS ASN GLY VAL VAL GLY GLY SER LYS GLN ILE
SEQRES 20 A 311 HIS ARG ILE LYS ALA PRO THR LEU VAL ILE GLN GLY ASP
SEQRES 21 A 311 ARG ASP TYR VAL VAL PRO GLN VAL VAL GLY GLU GLU LEU
SEQRES 22 A 311 ALA LYS HIS LEU PRO ASN ALA GLU LEU LYS VAL LEU GLU
SEQRES 23 A 311 ASP CYS GLY HIS SER PRO PHE ILE ASP CYS LEU ASP VAL
SEQRES 24 A 311 PHE ILE LYS HIS VAL GLU ASP TRP LEU GLU GLN LYS
SEQRES 1 B 311 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE
SEQRES 2 B 311 LYS PRO ALA THR MET GLU PHE VAL SER LEU SER ASN GLY
SEQRES 3 B 311 GLU THR ILE ALA TYR GLN GLU VAL GLY ARG ARG ASN THR
SEQRES 4 B 311 ASP ILE LEU VAL LEU ILE HIS GLY ASN MET THR SER SER
SEQRES 5 B 311 GLN HIS TRP ASP LEU VAL ILE GLU LYS LEU GLN ASP GLN
SEQRES 6 B 311 TYR HIS ILE TYR ALA LEU ASP LEU ARG GLY PHE GLY GLN
SEQRES 7 B 311 SER THR TYR ASN GLN SER ILE ASP SER LEU GLN ASP PHE
SEQRES 8 B 311 ALA GLU ASP VAL LYS LEU PHE ILE ASP GLU LEU LYS LEU
SEQRES 9 B 311 GLU LYS PHE SER LEU MET GLY TRP ALA MET GLY GLY GLY
SEQRES 10 B 311 VAL ALA MET GLN PHE THR ALA ASN HIS PRO THR PHE VAL
SEQRES 11 B 311 GLU LYS LEU ILE LEU VAL GLU SER VAL GLY MET LYS GLY
SEQRES 12 B 311 TYR PRO ILE PHE LYS LYS ASP THR ASN GLY GLN PRO ILE
SEQRES 13 B 311 VAL SER SER LEU VAL LYS THR LYS GLU GLU ILE ALA GLN
SEQRES 14 B 311 ASP PRO VAL GLN ILE ALA PRO VAL LEU ASP ALA ILE LYS
SEQRES 15 B 311 ASN MET ASN LYS LEU TYR TYR ARG THR VAL TRP ASN LEU
SEQRES 16 B 311 LEU ILE TYR THR HIS ASN GLN PRO GLU PRO ASP ARG TYR
SEQRES 17 B 311 GLU LYS TYR LEU ASP ASP MET LEU THR GLN ARG ASN PHE
SEQRES 18 B 311 VAL ASP VAL ASN TYR ALA LEU ILE THR PHE ASN ILE SER
SEQRES 19 B 311 ASP GLU HIS ASN GLY VAL VAL GLY GLY SER LYS GLN ILE
SEQRES 20 B 311 HIS ARG ILE LYS ALA PRO THR LEU VAL ILE GLN GLY ASP
SEQRES 21 B 311 ARG ASP TYR VAL VAL PRO GLN VAL VAL GLY GLU GLU LEU
SEQRES 22 B 311 ALA LYS HIS LEU PRO ASN ALA GLU LEU LYS VAL LEU GLU
SEQRES 23 B 311 ASP CYS GLY HIS SER PRO PHE ILE ASP CYS LEU ASP VAL
SEQRES 24 B 311 PHE ILE LYS HIS VAL GLU ASP TRP LEU GLU GLN LYS
SEQRES 1 C 311 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE
SEQRES 2 C 311 LYS PRO ALA THR MET GLU PHE VAL SER LEU SER ASN GLY
SEQRES 3 C 311 GLU THR ILE ALA TYR GLN GLU VAL GLY ARG ARG ASN THR
SEQRES 4 C 311 ASP ILE LEU VAL LEU ILE HIS GLY ASN MET THR SER SER
SEQRES 5 C 311 GLN HIS TRP ASP LEU VAL ILE GLU LYS LEU GLN ASP GLN
SEQRES 6 C 311 TYR HIS ILE TYR ALA LEU ASP LEU ARG GLY PHE GLY GLN
SEQRES 7 C 311 SER THR TYR ASN GLN SER ILE ASP SER LEU GLN ASP PHE
SEQRES 8 C 311 ALA GLU ASP VAL LYS LEU PHE ILE ASP GLU LEU LYS LEU
SEQRES 9 C 311 GLU LYS PHE SER LEU MET GLY TRP ALA MET GLY GLY GLY
SEQRES 10 C 311 VAL ALA MET GLN PHE THR ALA ASN HIS PRO THR PHE VAL
SEQRES 11 C 311 GLU LYS LEU ILE LEU VAL GLU SER VAL GLY MET LYS GLY
SEQRES 12 C 311 TYR PRO ILE PHE LYS LYS ASP THR ASN GLY GLN PRO ILE
SEQRES 13 C 311 VAL SER SER LEU VAL LYS THR LYS GLU GLU ILE ALA GLN
SEQRES 14 C 311 ASP PRO VAL GLN ILE ALA PRO VAL LEU ASP ALA ILE LYS
SEQRES 15 C 311 ASN MET ASN LYS LEU TYR TYR ARG THR VAL TRP ASN LEU
SEQRES 16 C 311 LEU ILE TYR THR HIS ASN GLN PRO GLU PRO ASP ARG TYR
SEQRES 17 C 311 GLU LYS TYR LEU ASP ASP MET LEU THR GLN ARG ASN PHE
SEQRES 18 C 311 VAL ASP VAL ASN TYR ALA LEU ILE THR PHE ASN ILE SER
SEQRES 19 C 311 ASP GLU HIS ASN GLY VAL VAL GLY GLY SER LYS GLN ILE
SEQRES 20 C 311 HIS ARG ILE LYS ALA PRO THR LEU VAL ILE GLN GLY ASP
SEQRES 21 C 311 ARG ASP TYR VAL VAL PRO GLN VAL VAL GLY GLU GLU LEU
SEQRES 22 C 311 ALA LYS HIS LEU PRO ASN ALA GLU LEU LYS VAL LEU GLU
SEQRES 23 C 311 ASP CYS GLY HIS SER PRO PHE ILE ASP CYS LEU ASP VAL
SEQRES 24 C 311 PHE ILE LYS HIS VAL GLU ASP TRP LEU GLU GLN LYS
SEQRES 1 D 311 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE
SEQRES 2 D 311 LYS PRO ALA THR MET GLU PHE VAL SER LEU SER ASN GLY
SEQRES 3 D 311 GLU THR ILE ALA TYR GLN GLU VAL GLY ARG ARG ASN THR
SEQRES 4 D 311 ASP ILE LEU VAL LEU ILE HIS GLY ASN MET THR SER SER
SEQRES 5 D 311 GLN HIS TRP ASP LEU VAL ILE GLU LYS LEU GLN ASP GLN
SEQRES 6 D 311 TYR HIS ILE TYR ALA LEU ASP LEU ARG GLY PHE GLY GLN
SEQRES 7 D 311 SER THR TYR ASN GLN SER ILE ASP SER LEU GLN ASP PHE
SEQRES 8 D 311 ALA GLU ASP VAL LYS LEU PHE ILE ASP GLU LEU LYS LEU
SEQRES 9 D 311 GLU LYS PHE SER LEU MET GLY TRP ALA MET GLY GLY GLY
SEQRES 10 D 311 VAL ALA MET GLN PHE THR ALA ASN HIS PRO THR PHE VAL
SEQRES 11 D 311 GLU LYS LEU ILE LEU VAL GLU SER VAL GLY MET LYS GLY
SEQRES 12 D 311 TYR PRO ILE PHE LYS LYS ASP THR ASN GLY GLN PRO ILE
SEQRES 13 D 311 VAL SER SER LEU VAL LYS THR LYS GLU GLU ILE ALA GLN
SEQRES 14 D 311 ASP PRO VAL GLN ILE ALA PRO VAL LEU ASP ALA ILE LYS
SEQRES 15 D 311 ASN MET ASN LYS LEU TYR TYR ARG THR VAL TRP ASN LEU
SEQRES 16 D 311 LEU ILE TYR THR HIS ASN GLN PRO GLU PRO ASP ARG TYR
SEQRES 17 D 311 GLU LYS TYR LEU ASP ASP MET LEU THR GLN ARG ASN PHE
SEQRES 18 D 311 VAL ASP VAL ASN TYR ALA LEU ILE THR PHE ASN ILE SER
SEQRES 19 D 311 ASP GLU HIS ASN GLY VAL VAL GLY GLY SER LYS GLN ILE
SEQRES 20 D 311 HIS ARG ILE LYS ALA PRO THR LEU VAL ILE GLN GLY ASP
SEQRES 21 D 311 ARG ASP TYR VAL VAL PRO GLN VAL VAL GLY GLU GLU LEU
SEQRES 22 D 311 ALA LYS HIS LEU PRO ASN ALA GLU LEU LYS VAL LEU GLU
SEQRES 23 D 311 ASP CYS GLY HIS SER PRO PHE ILE ASP CYS LEU ASP VAL
SEQRES 24 D 311 PHE ILE LYS HIS VAL GLU ASP TRP LEU GLU GLN LYS
HET P33 B 401 22
HET P33 D 401 22
HET TRS D 402 8
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
HETSYN TRS TRIS BUFFER
FORMUL 5 P33 2(C14 H30 O8)
FORMUL 7 TRS C4 H12 N O3 1+
FORMUL 8 HOH *959(H2 O)
HELIX 1 AA1 SER A 40 HIS A 43 5 4
HELIX 2 AA2 TRP A 44 GLN A 52 1 9
HELIX 3 AA3 SER A 76 LEU A 91 1 16
HELIX 4 AA4 MET A 103 HIS A 115 1 13
HELIX 5 AA5 THR A 152 GLN A 158 1 7
HELIX 6 AA6 ILE A 163 MET A 173 1 11
HELIX 7 AA7 ASN A 174 ILE A 186 1 13
HELIX 8 AA8 GLU A 193 LEU A 205 1 13
HELIX 9 AA9 ASN A 209 THR A 219 1 11
HELIX 10 AB1 LYS A 234 ILE A 239 5 6
HELIX 11 AB2 PRO A 255 LEU A 266 1 12
HELIX 12 AB3 SER A 280 CYS A 285 1 6
HELIX 13 AB4 CYS A 285 GLN A 299 1 15
HELIX 14 AB5 SER B 40 HIS B 43 5 4
HELIX 15 AB6 TRP B 44 GLN B 52 1 9
HELIX 16 AB7 SER B 76 LEU B 91 1 16
HELIX 17 AB8 MET B 103 HIS B 115 1 13
HELIX 18 AB9 THR B 152 GLN B 158 1 7
HELIX 19 AC1 ILE B 163 ASN B 172 1 10
HELIX 20 AC2 ASN B 174 ILE B 186 1 13
HELIX 21 AC3 GLU B 193 LEU B 205 1 13
HELIX 22 AC4 ASN B 209 THR B 219 1 11
HELIX 23 AC5 LYS B 234 ILE B 239 5 6
HELIX 24 AC6 PRO B 255 LEU B 266 1 12
HELIX 25 AC7 SER B 280 CYS B 285 1 6
HELIX 26 AC8 CYS B 285 GLN B 299 1 15
HELIX 27 AC9 SER C 40 HIS C 43 5 4
HELIX 28 AD1 TRP C 44 GLN C 52 1 9
HELIX 29 AD2 SER C 76 LYS C 92 1 17
HELIX 30 AD3 MET C 103 HIS C 115 1 13
HELIX 31 AD4 THR C 152 GLN C 158 1 7
HELIX 32 AD5 ILE C 163 ASN C 172 1 10
HELIX 33 AD6 ASN C 174 ILE C 186 1 13
HELIX 34 AD7 GLU C 193 LEU C 205 1 13
HELIX 35 AD8 ASN C 209 THR C 219 1 11
HELIX 36 AD9 LYS C 234 ILE C 239 5 6
HELIX 37 AE1 PRO C 255 LEU C 266 1 12
HELIX 38 AE2 SER C 280 CYS C 285 1 6
HELIX 39 AE3 CYS C 285 GLN C 299 1 15
HELIX 40 AE4 SER D 40 HIS D 43 5 4
HELIX 41 AE5 TRP D 44 GLN D 52 1 9
HELIX 42 AE6 SER D 76 LEU D 91 1 16
HELIX 43 AE7 MET D 103 HIS D 115 1 13
HELIX 44 AE8 THR D 152 GLN D 158 1 7
HELIX 45 AE9 ILE D 163 ASN D 172 1 10
HELIX 46 AF1 ASN D 174 ILE D 186 1 13
HELIX 47 AF2 GLU D 193 LEU D 205 1 13
HELIX 48 AF3 ASN D 209 THR D 219 1 11
HELIX 49 AF4 LYS D 234 ILE D 239 5 6
HELIX 50 AF5 PRO D 255 LEU D 266 1 12
HELIX 51 AF6 SER D 280 CYS D 285 1 6
HELIX 52 AF7 CYS D 285 GLN D 299 1 15
SHEET 1 AA1 8 GLU A 8 SER A 11 0
SHEET 2 AA1 8 THR A 17 VAL A 23 -1 O TYR A 20 N GLU A 8
SHEET 3 AA1 8 HIS A 56 LEU A 60 -1 O ALA A 59 N GLN A 21
SHEET 4 AA1 8 ILE A 30 ILE A 34 1 N LEU A 33 O TYR A 58
SHEET 5 AA1 8 PHE A 96 TRP A 101 1 O SER A 97 N ILE A 30
SHEET 6 AA1 8 VAL A 119 VAL A 125 1 O VAL A 125 N GLY A 100
SHEET 7 AA1 8 THR A 243 GLY A 248 1 O ILE A 246 N LEU A 124
SHEET 8 AA1 8 ALA A 269 LEU A 274 1 O GLU A 270 N VAL A 245
SHEET 1 AA2 2 PHE A 136 LYS A 138 0
SHEET 2 AA2 2 PRO A 144 LEU A 149 -1 O ILE A 145 N LYS A 137
SHEET 1 AA3 8 GLU B 8 SER B 11 0
SHEET 2 AA3 8 THR B 17 VAL B 23 -1 O TYR B 20 N GLU B 8
SHEET 3 AA3 8 HIS B 56 LEU B 60 -1 O ALA B 59 N GLN B 21
SHEET 4 AA3 8 ILE B 30 ILE B 34 1 N LEU B 33 O TYR B 58
SHEET 5 AA3 8 PHE B 96 TRP B 101 1 O MET B 99 N VAL B 32
SHEET 6 AA3 8 VAL B 119 VAL B 125 1 O VAL B 125 N GLY B 100
SHEET 7 AA3 8 THR B 243 GLY B 248 1 O ILE B 246 N LEU B 124
SHEET 8 AA3 8 ALA B 269 LEU B 274 1 O GLU B 270 N VAL B 245
SHEET 1 AA4 2 PHE B 136 LYS B 138 0
SHEET 2 AA4 2 PRO B 144 LEU B 149 -1 O ILE B 145 N LYS B 137
SHEET 1 AA5 8 GLU C 8 SER C 11 0
SHEET 2 AA5 8 THR C 17 VAL C 23 -1 O TYR C 20 N GLU C 8
SHEET 3 AA5 8 HIS C 56 LEU C 60 -1 O ALA C 59 N GLN C 21
SHEET 4 AA5 8 ILE C 30 ILE C 34 1 N LEU C 31 O HIS C 56
SHEET 5 AA5 8 PHE C 96 TRP C 101 1 O SER C 97 N ILE C 30
SHEET 6 AA5 8 VAL C 119 VAL C 125 1 O VAL C 125 N GLY C 100
SHEET 7 AA5 8 THR C 243 GLY C 248 1 O ILE C 246 N LEU C 124
SHEET 8 AA5 8 ALA C 269 LEU C 274 1 O GLU C 270 N VAL C 245
SHEET 1 AA6 2 PHE C 136 LYS C 138 0
SHEET 2 AA6 2 PRO C 144 LEU C 149 -1 O ILE C 145 N LYS C 137
SHEET 1 AA7 8 GLU D 8 SER D 11 0
SHEET 2 AA7 8 THR D 17 VAL D 23 -1 O ILE D 18 N VAL D 10
SHEET 3 AA7 8 HIS D 56 LEU D 60 -1 O ALA D 59 N GLN D 21
SHEET 4 AA7 8 ILE D 30 ILE D 34 1 N LEU D 31 O HIS D 56
SHEET 5 AA7 8 PHE D 96 TRP D 101 1 O SER D 97 N ILE D 30
SHEET 6 AA7 8 VAL D 119 VAL D 125 1 O VAL D 125 N GLY D 100
SHEET 7 AA7 8 THR D 243 GLY D 248 1 O ILE D 246 N LEU D 124
SHEET 8 AA7 8 ALA D 269 LEU D 274 1 O GLU D 270 N VAL D 245
SHEET 1 AA8 2 PHE D 136 LYS D 138 0
SHEET 2 AA8 2 PRO D 144 LEU D 149 -1 O ILE D 145 N LYS D 137
CRYST1 42.989 83.552 85.729 73.48 82.84 83.62 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023262 -0.002602 -0.002297 0.00000
SCALE2 0.000000 0.012043 -0.003435 0.00000
SCALE3 0.000000 0.000000 0.012225 0.00000
TER 2395 GLN A 299
TER 4782 LYS B 300
TER 7177 GLN C 299
TER 9555 GLN D 299
MASTER 705 0 3 52 40 0 0 610562 4 52 96
END |