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HEADER HYDROLASE 12-MAR-24 8YNV
TITLE POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE PHAZ FROM 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
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 3HB, DEPOLYMERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.L.WANG,L.C.YE,S.C.CHEN,C.H.HSU
REVDAT 1 11-DEC-24 8YNV 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. 1.42 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) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 200717
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2009
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 28.4000 - 3.4200 0.99 14884 146 0.1374 0.1566
REMARK 3 2 3.4100 - 2.7100 0.93 13950 141 0.1623 0.2034
REMARK 3 3 2.7100 - 2.3700 0.95 14383 146 0.1629 0.2162
REMARK 3 4 2.3700 - 2.1500 0.95 14350 149 0.1570 0.1926
REMARK 3 5 2.1500 - 2.0000 0.95 14405 143 0.1599 0.1822
REMARK 3 6 2.0000 - 1.8800 0.95 14303 145 0.1563 0.1822
REMARK 3 7 1.8800 - 1.7900 0.95 14243 146 0.1599 0.1821
REMARK 3 8 1.7900 - 1.7100 0.95 14267 140 0.1593 0.1783
REMARK 3 9 1.7100 - 1.6400 0.94 14224 145 0.1652 0.1958
REMARK 3 10 1.6400 - 1.5900 0.94 14212 141 0.1678 0.1817
REMARK 3 11 1.5900 - 1.5400 0.94 14045 146 0.1743 0.1862
REMARK 3 12 1.5400 - 1.4900 0.93 14120 144 0.2023 0.2332
REMARK 3 13 1.4900 - 1.4500 0.93 14001 133 0.2209 0.2361
REMARK 3 14 1.4500 - 1.4200 0.89 13321 144 0.2523 0.2647
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) : 0.127
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.051
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.16
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 : 0.005 9860
REMARK 3 ANGLE : 0.752 13338
REMARK 3 CHIRALITY : 0.075 1476
REMARK 3 PLANARITY : 0.005 1708
REMARK 3 DIHEDRAL : 13.856 1331
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 36
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7379 15.4031 83.7246
REMARK 3 T TENSOR
REMARK 3 T11: 0.1533 T22: 0.1438
REMARK 3 T33: 0.1048 T12: 0.0445
REMARK 3 T13: -0.0316 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.9304 L22: 1.3700
REMARK 3 L33: 1.6866 L12: 0.4206
REMARK 3 L13: 0.0746 L23: -0.2646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0112 S12: -0.0623 S13: -0.1684
REMARK 3 S21: 0.1514 S22: 0.0056 S23: -0.2019
REMARK 3 S31: 0.2801 S32: 0.2507 S33: 0.0096
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.3379 13.4331 89.6295
REMARK 3 T TENSOR
REMARK 3 T11: 0.1252 T22: 0.1188
REMARK 3 T33: 0.0766 T12: 0.0274
REMARK 3 T13: -0.0207 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 2.8690 L22: 5.9060
REMARK 3 L33: 3.4788 L12: 0.1014
REMARK 3 L13: 0.0060 L23: 0.7873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: -0.1978 S13: -0.1502
REMARK 3 S21: 0.1289 S22: -0.1113 S23: 0.2123
REMARK 3 S31: 0.2224 S32: -0.0756 S33: 0.0642
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.8698 26.2723 76.5591
REMARK 3 T TENSOR
REMARK 3 T11: 0.0568 T22: 0.1517
REMARK 3 T33: 0.1008 T12: 0.0086
REMARK 3 T13: 0.0041 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 5.3911 L22: 3.6722
REMARK 3 L33: 0.5672 L12: -0.2913
REMARK 3 L13: 0.4384 L23: 0.5162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: 0.3586 S13: 0.1728
REMARK 3 S21: -0.1826 S22: -0.0109 S23: -0.1365
REMARK 3 S31: 0.0324 S32: 0.4160 S33: 0.0191
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7647 14.3620 72.3509
REMARK 3 T TENSOR
REMARK 3 T11: 0.1310 T22: 0.1369
REMARK 3 T33: 0.0690 T12: 0.0191
REMARK 3 T13: -0.0361 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 5.0344 L22: 6.1195
REMARK 3 L33: 3.5301 L12: -0.0030
REMARK 3 L13: -0.8171 L23: -0.4137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0338 S12: -0.0111 S13: -0.3200
REMARK 3 S21: -0.1331 S22: -0.0475 S23: -0.5400
REMARK 3 S31: 0.4202 S32: 0.2873 S33: -0.0075
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2987 19.1055 75.8622
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: 0.0947
REMARK 3 T33: 0.0756 T12: -0.0105
REMARK 3 T13: -0.0128 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 1.4127 L22: 3.4218
REMARK 3 L33: 3.1716 L12: -0.6871
REMARK 3 L13: -0.4706 L23: 1.0662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: 0.0269 S13: 0.0288
REMARK 3 S21: 0.0524 S22: -0.0100 S23: 0.0358
REMARK 3 S31: 0.1454 S32: -0.0317 S33: 0.0104
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3556 45.7116 76.9953
REMARK 3 T TENSOR
REMARK 3 T11: 0.1792 T22: 0.1106
REMARK 3 T33: 0.1329 T12: 0.0073
REMARK 3 T13: -0.0213 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.2580 L22: 6.1450
REMARK 3 L33: 0.6970 L12: 0.6325
REMARK 3 L13: 0.3681 L23: 1.1982
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: -0.0187 S13: 0.0373
REMARK 3 S21: 0.0650 S22: 0.0044 S23: -0.0271
REMARK 3 S31: -0.1316 S32: -0.0711 S33: 0.0544
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.5665 42.3762 82.6011
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.1630
REMARK 3 T33: 0.2027 T12: -0.0325
REMARK 3 T13: -0.0092 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 5.6950 L22: 3.5140
REMARK 3 L33: 2.9447 L12: -1.0739
REMARK 3 L13: 3.9960 L23: -1.0535
REMARK 3 S TENSOR
REMARK 3 S11: -0.2196 S12: -0.1624 S13: 0.5649
REMARK 3 S21: -0.0703 S22: -0.0853 S23: -0.2926
REMARK 3 S31: -0.4989 S32: 0.0892 S33: 0.4120
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4677 32.4249 86.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0981 T22: 0.0940
REMARK 3 T33: 0.1011 T12: 0.0098
REMARK 3 T13: -0.0146 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 0.2857 L22: 0.7197
REMARK 3 L33: 2.8427 L12: 0.0814
REMARK 3 L13: 0.2773 L23: -0.4379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0168 S12: -0.0898 S13: 0.0738
REMARK 3 S21: 0.1197 S22: -0.0180 S23: -0.0174
REMARK 3 S31: -0.1267 S32: 0.0884 S33: 0.0061
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1718 25.6362 76.0327
REMARK 3 T TENSOR
REMARK 3 T11: 0.0767 T22: 0.1330
REMARK 3 T33: 0.1327 T12: 0.0097
REMARK 3 T13: -0.0171 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.8979 L22: 1.4877
REMARK 3 L33: 2.8095 L12: 0.5064
REMARK 3 L13: -0.3993 L23: -1.1628
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: -0.0471 S13: 0.0399
REMARK 3 S21: -0.1879 S22: 0.0200 S23: 0.1342
REMARK 3 S31: 0.1443 S32: -0.2809 S33: 0.0442
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 256 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9922 23.8756 78.0941
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.2070
REMARK 3 T33: 0.1388 T12: -0.0091
REMARK 3 T13: -0.0026 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 2.4275 L22: 1.8766
REMARK 3 L33: 6.0773 L12: -0.7055
REMARK 3 L13: 0.5231 L23: 0.4002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0940 S12: -0.0623 S13: 0.0283
REMARK 3 S21: -0.0963 S22: 0.0024 S23: 0.2691
REMARK 3 S31: 0.1093 S32: -0.4830 S33: -0.0764
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 275 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9782 17.9171 90.7783
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.1922
REMARK 3 T33: 0.1128 T12: -0.0464
REMARK 3 T13: 0.0151 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 2.9059 L22: 3.8175
REMARK 3 L33: 3.5745 L12: -0.2276
REMARK 3 L13: 0.0983 L23: 0.1280
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.2257 S13: -0.2326
REMARK 3 S21: 0.1139 S22: -0.0539 S23: 0.3143
REMARK 3 S31: 0.4862 S32: -0.4985 S33: 0.0524
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4151 62.2965 25.4852
REMARK 3 T TENSOR
REMARK 3 T11: 0.1081 T22: 0.1581
REMARK 3 T33: 0.1652 T12: -0.0222
REMARK 3 T13: 0.0079 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 3.3734 L22: 3.4133
REMARK 3 L33: 3.1870 L12: -1.2193
REMARK 3 L13: 1.7404 L23: -1.3078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.1621 S13: 0.0568
REMARK 3 S21: -0.1050 S22: 0.0362 S23: -0.1621
REMARK 3 S31: 0.0001 S32: 0.2649 S33: 0.0837
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.7078 66.7979 21.1933
REMARK 3 T TENSOR
REMARK 3 T11: 0.0982 T22: 0.0829
REMARK 3 T33: 0.0774 T12: 0.0016
REMARK 3 T13: 0.0115 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 2.0189 L22: 3.8166
REMARK 3 L33: 2.3597 L12: 0.3104
REMARK 3 L13: 0.1469 L23: 0.3671
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: 0.1203 S13: 0.2231
REMARK 3 S21: -0.1613 S22: 0.0206 S23: -0.0566
REMARK 3 S31: -0.3020 S32: 0.0098 S33: 0.0214
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.5952 58.5195 33.0822
REMARK 3 T TENSOR
REMARK 3 T11: 0.0510 T22: 0.0991
REMARK 3 T33: 0.0716 T12: -0.0063
REMARK 3 T13: -0.0104 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 2.7864 L22: 3.5297
REMARK 3 L33: 2.7965 L12: -0.3315
REMARK 3 L13: -0.5471 L23: 0.9705
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: -0.0697 S13: 0.0186
REMARK 3 S21: 0.1206 S22: -0.0213 S23: -0.1864
REMARK 3 S31: -0.0365 S32: 0.1593 S33: 0.0035
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 97 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.8037 61.0959 32.9335
REMARK 3 T TENSOR
REMARK 3 T11: 0.0795 T22: 0.0883
REMARK 3 T33: 0.0837 T12: 0.0241
REMARK 3 T13: 0.0157 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.6542 L22: 1.6342
REMARK 3 L33: 2.5036 L12: 0.8100
REMARK 3 L13: 0.7837 L23: 0.5864
REMARK 3 S TENSOR
REMARK 3 S11: -0.0110 S12: -0.0381 S13: 0.0467
REMARK 3 S21: 0.0343 S22: -0.0014 S23: 0.0511
REMARK 3 S31: -0.0829 S32: -0.0135 S33: 0.0205
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.6120 34.6729 28.6321
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.0895
REMARK 3 T33: 0.0990 T12: -0.0048
REMARK 3 T13: 0.0162 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.3412 L22: 3.9922
REMARK 3 L33: 3.2176 L12: -0.0336
REMARK 3 L13: -0.1295 L23: 2.6859
REMARK 3 S TENSOR
REMARK 3 S11: 0.0929 S12: 0.0378 S13: 0.0432
REMARK 3 S21: -0.2124 S22: 0.0621 S23: -0.2519
REMARK 3 S31: -0.0448 S32: -0.2684 S33: -0.1542
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 151 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.7372 36.7852 23.9379
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.1111
REMARK 3 T33: 0.1729 T12: 0.0069
REMARK 3 T13: -0.0007 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.8034 L22: 1.8359
REMARK 3 L33: 6.2880 L12: 1.0146
REMARK 3 L13: -1.8641 L23: -1.1334
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: -0.0188 S13: -0.2364
REMARK 3 S21: 0.0377 S22: -0.0686 S23: -0.1962
REMARK 3 S31: 0.3929 S32: 0.1644 S33: 0.1983
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.4925 48.2819 20.1657
REMARK 3 T TENSOR
REMARK 3 T11: 0.0810 T22: 0.0698
REMARK 3 T33: 0.0800 T12: -0.0124
REMARK 3 T13: 0.0175 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.4403 L22: 1.1063
REMARK 3 L33: 2.0437 L12: -0.1625
REMARK 3 L13: -0.1063 L23: -0.0975
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: 0.1035 S13: -0.0220
REMARK 3 S21: -0.1189 S22: 0.0051 S23: 0.0109
REMARK 3 S31: 0.0706 S32: 0.0069 S33: -0.0188
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 229 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6689 55.6140 32.9218
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: 0.1211
REMARK 3 T33: 0.1123 T12: 0.0033
REMARK 3 T13: 0.0237 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.5998 L22: 1.6659
REMARK 3 L33: 2.3283 L12: -0.1632
REMARK 3 L13: 0.1674 L23: -0.3736
REMARK 3 S TENSOR
REMARK 3 S11: -0.0523 S12: 0.0184 S13: 0.0365
REMARK 3 S21: 0.0784 S22: 0.0195 S23: 0.1116
REMARK 3 S31: -0.1086 S32: -0.1589 S33: -0.0184
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.8979 62.0968 24.2725
REMARK 3 T TENSOR
REMARK 3 T11: 0.0725 T22: 0.1523
REMARK 3 T33: 0.1134 T12: 0.0410
REMARK 3 T13: -0.0167 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.7910 L22: 1.5593
REMARK 3 L33: 2.7617 L12: 0.0775
REMARK 3 L13: -0.5150 L23: -0.0298
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: -0.0186 S13: 0.0873
REMARK 3 S21: -0.0600 S22: 0.0208 S23: 0.1757
REMARK 3 S31: -0.1940 S32: -0.2634 S33: 0.0017
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0315 74.7340 57.5431
REMARK 3 T TENSOR
REMARK 3 T11: 0.0644 T22: 0.1042
REMARK 3 T33: 0.0781 T12: 0.0263
REMARK 3 T13: 0.0094 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 5.5966 L22: 2.8091
REMARK 3 L33: 3.2335 L12: 1.2378
REMARK 3 L13: 0.4390 L23: -1.3041
REMARK 3 S TENSOR
REMARK 3 S11: -0.0927 S12: -0.0348 S13: 0.1155
REMARK 3 S21: -0.0255 S22: 0.0823 S23: 0.0814
REMARK 3 S31: -0.1465 S32: -0.2963 S33: 0.0559
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 24 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3428 73.6095 58.2302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0240 T22: 0.0470
REMARK 3 T33: 0.0770 T12: 0.0071
REMARK 3 T13: -0.0049 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 2.3042 L22: 4.9709
REMARK 3 L33: 4.2054 L12: 1.7691
REMARK 3 L13: -1.5252 L23: -3.0729
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: 0.0565 S13: 0.1919
REMARK 3 S21: 0.0049 S22: 0.1122 S23: 0.1719
REMARK 3 S31: -0.0306 S32: -0.0501 S33: -0.0660
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.8809 76.8355 61.9056
REMARK 3 T TENSOR
REMARK 3 T11: 0.0675 T22: 0.0389
REMARK 3 T33: 0.0896 T12: 0.0050
REMARK 3 T13: 0.0073 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 2.3722 L22: 1.8270
REMARK 3 L33: 4.1160 L12: 0.4322
REMARK 3 L13: -1.4943 L23: -2.3947
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.1354 S13: 0.1626
REMARK 3 S21: 0.1068 S22: -0.0028 S23: -0.0256
REMARK 3 S31: -0.1514 S32: 0.1043 S33: -0.0200
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 61 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9400 65.6987 54.3401
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: 0.0791
REMARK 3 T33: 0.0796 T12: -0.0050
REMARK 3 T13: -0.0193 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 3.3955 L22: 2.2700
REMARK 3 L33: 2.5826 L12: 0.4557
REMARK 3 L13: -0.9884 L23: -0.7706
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.1395 S13: -0.0148
REMARK 3 S21: -0.1355 S22: 0.0764 S23: 0.0766
REMARK 3 S31: 0.0799 S32: -0.0907 S33: -0.0469
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 97 THROUGH 130 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4939 62.1529 55.2182
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0548
REMARK 3 T33: 0.0779 T12: 0.0018
REMARK 3 T13: 0.0140 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 1.6532 L22: 1.8238
REMARK 3 L33: 4.5468 L12: -0.3034
REMARK 3 L13: 0.9585 L23: -0.9978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.0861 S13: -0.1183
REMARK 3 S21: -0.0769 S22: -0.0361 S23: -0.0023
REMARK 3 S31: 0.0359 S32: 0.0065 S33: 0.0375
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 131 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4931 42.6691 73.3602
REMARK 3 T TENSOR
REMARK 3 T11: 0.1478 T22: 0.1151
REMARK 3 T33: 0.1847 T12: 0.0346
REMARK 3 T13: 0.0099 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 4.8256 L22: 4.9165
REMARK 3 L33: 5.6907 L12: 0.4004
REMARK 3 L13: -0.6524 L23: -1.1514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: -0.4771 S13: -0.1502
REMARK 3 S21: 0.4202 S22: 0.0944 S23: 0.2743
REMARK 3 S31: 0.1724 S32: -0.1653 S33: -0.0479
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2737 54.3928 75.5167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0931 T22: 0.1391
REMARK 3 T33: 0.1689 T12: -0.0045
REMARK 3 T13: 0.0314 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 1.1446 L22: 7.8576
REMARK 3 L33: 6.7190 L12: -0.8203
REMARK 3 L13: -0.8183 L23: 4.6647
REMARK 3 S TENSOR
REMARK 3 S11: -0.0898 S12: -0.0825 S13: -0.1879
REMARK 3 S21: 0.3133 S22: -0.0485 S23: 0.4837
REMARK 3 S31: 0.3049 S32: -0.1509 S33: 0.1355
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 175 THROUGH 206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2487 68.0092 78.5777
REMARK 3 T TENSOR
REMARK 3 T11: 0.1183 T22: 0.0833
REMARK 3 T33: 0.0540 T12: 0.0114
REMARK 3 T13: 0.0161 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 2.5215 L22: 1.4665
REMARK 3 L33: 1.7011 L12: -0.2575
REMARK 3 L13: 0.3646 L23: -0.2612
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: -0.1262 S13: 0.0655
REMARK 3 S21: 0.1437 S22: -0.0001 S23: 0.0361
REMARK 3 S31: -0.0592 S32: -0.0123 S33: -0.0357
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 207 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7037 51.4103 62.4384
REMARK 3 T TENSOR
REMARK 3 T11: 0.0659 T22: 0.0490
REMARK 3 T33: 0.1034 T12: -0.0073
REMARK 3 T13: -0.0091 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.5660 L22: 2.8981
REMARK 3 L33: 2.2691 L12: -0.7966
REMARK 3 L13: -0.9575 L23: 1.1285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.1114 S13: -0.1109
REMARK 3 S21: -0.0865 S22: 0.0822 S23: -0.0985
REMARK 3 S31: 0.1107 S32: 0.0847 S33: -0.0499
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 229 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4568 55.2697 59.8280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.0824
REMARK 3 T33: 0.1340 T12: 0.0232
REMARK 3 T13: 0.0126 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.9545 L22: 1.0636
REMARK 3 L33: 0.4271 L12: 0.6326
REMARK 3 L13: -0.3092 L23: -0.5889
REMARK 3 S TENSOR
REMARK 3 S11: -0.0437 S12: 0.0495 S13: -0.1836
REMARK 3 S21: -0.0751 S22: 0.0220 S23: -0.1100
REMARK 3 S31: 0.0633 S32: 0.0403 S33: 0.0208
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 256 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2054 55.7239 60.0921
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.0917
REMARK 3 T33: 0.1193 T12: 0.0373
REMARK 3 T13: 0.0058 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 2.0653 L22: 1.0850
REMARK 3 L33: 7.6153 L12: -0.2389
REMARK 3 L13: 0.2417 L23: 0.2772
REMARK 3 S TENSOR
REMARK 3 S11: -0.0316 S12: 0.0036 S13: -0.1983
REMARK 3 S21: -0.1104 S22: -0.0226 S23: -0.0572
REMARK 3 S31: 0.2686 S32: 0.1904 S33: 0.0334
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 275 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.5848 69.9269 64.6813
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.0727
REMARK 3 T33: 0.1240 T12: 0.0044
REMARK 3 T13: 0.0047 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.3392 L22: 2.9918
REMARK 3 L33: 4.2661 L12: 0.8630
REMARK 3 L13: -0.0185 L23: -1.3203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.0749 S13: 0.1004
REMARK 3 S21: 0.0034 S22: -0.1269 S23: -0.3116
REMARK 3 S31: -0.1046 S32: 0.3610 S33: 0.0830
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 4 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.3719 6.6395 46.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0668 T22: 0.0517
REMARK 3 T33: 0.0897 T12: -0.0074
REMARK 3 T13: -0.0101 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.4550 L22: 1.6167
REMARK 3 L33: 1.5049 L12: 0.0680
REMARK 3 L13: -0.3293 L23: -0.3586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0257 S12: -0.0312 S13: -0.1856
REMARK 3 S21: -0.0240 S22: -0.0409 S23: 0.0209
REMARK 3 S31: 0.1266 S32: 0.0059 S33: 0.0668
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 61 THROUGH 150 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.1858 22.3428 47.4999
REMARK 3 T TENSOR
REMARK 3 T11: 0.0817 T22: 0.0639
REMARK 3 T33: 0.0795 T12: -0.0085
REMARK 3 T13: -0.0033 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.9413 L22: 0.9434
REMARK 3 L33: 0.7214 L12: 0.2679
REMARK 3 L13: -0.2896 L23: -0.2733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0442 S12: 0.0571 S13: 0.1753
REMARK 3 S21: 0.0738 S22: -0.0347 S23: 0.0425
REMARK 3 S31: -0.0974 S32: 0.0428 S33: -0.0085
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5868 30.4794 32.6743
REMARK 3 T TENSOR
REMARK 3 T11: 0.1307 T22: 0.1976
REMARK 3 T33: 0.2177 T12: 0.0363
REMARK 3 T13: -0.0079 T23: 0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 1.2836 L22: 2.7038
REMARK 3 L33: 2.5088 L12: 0.4949
REMARK 3 L13: 0.3409 L23: 1.2782
REMARK 3 S TENSOR
REMARK 3 S11: -0.1164 S12: 0.3141 S13: 0.3203
REMARK 3 S21: -0.2329 S22: 0.0370 S23: 0.3922
REMARK 3 S31: -0.2409 S32: 0.1143 S33: -0.0077
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 175 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5169 19.1844 39.0505
REMARK 3 T TENSOR
REMARK 3 T11: 0.0727 T22: 0.0716
REMARK 3 T33: 0.0792 T12: -0.0084
REMARK 3 T13: 0.0002 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.7739 L22: 0.9340
REMARK 3 L33: 0.6973 L12: 0.0547
REMARK 3 L13: -0.1245 L23: -0.1100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0296 S12: 0.0277 S13: -0.0209
REMARK 3 S21: 0.0078 S22: -0.0365 S23: -0.0902
REMARK 3 S31: -0.0066 S32: 0.0769 S33: 0.0106
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 8YNV 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_1300045481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-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 : 200742
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.420
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 (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1A88
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% POLYETHYLENE GLYCOL 3350, 200 MM
REMARK 280 AMMONIUM ACETATE, AND 100 MM BIS-TRIS (PH 5.6), VAPOR DIFFUSION,
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 LYS B 300
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 ILE C 2
REMARK 465 LYS C 3
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 O HOH B 746 O HOH B 747 2.18
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 C 571 O HOH D 599 1465 2.07
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 -165.46 -125.29
REMARK 500 SER A 102 -123.76 65.53
REMARK 500 ILE A 163 -61.01 -120.09
REMARK 500 ILE A 186 -57.62 -127.03
REMARK 500 CYS A 285 63.98 -160.01
REMARK 500 SER B 102 -122.04 63.92
REMARK 500 ILE B 186 -58.06 -129.38
REMARK 500 CYS B 285 66.21 -159.76
REMARK 500 SER C 102 -125.12 63.14
REMARK 500 ILE C 186 -61.26 -125.31
REMARK 500 ASN C 268 58.71 -148.72
REMARK 500 CYS C 285 62.34 -161.63
REMARK 500 SER D 102 -123.18 65.10
REMARK 500 ILE D 186 -59.84 -126.47
REMARK 500 ASN D 221 97.66 -162.71
REMARK 500 CYS D 285 60.01 -163.67
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 774 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH D 779 DISTANCE = 9.38 ANGSTROMS
DBREF1 8YNV A 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNV A A0A9X6EQW5 2 300
DBREF1 8YNV B 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNV B A0A9X6EQW5 2 300
DBREF1 8YNV C 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNV C A0A9X6EQW5 2 300
DBREF1 8YNV D 2 300 UNP A0A9X6EQW5_BACTU
DBREF2 8YNV D A0A9X6EQW5 2 300
SEQADV 8YNV MET A -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNV ARG A -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY A -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER A -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS A -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY A 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER A 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV MET B -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNV ARG B -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY B -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER B -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS B -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY B 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER B 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV MET C -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNV ARG C -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY C -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER C -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS C -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY C 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER C 1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV MET D -10 UNP A0A9X6EQW INITIATING METHIONINE
SEQADV 8YNV ARG D -9 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY D -8 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER D -7 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -6 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -5 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -4 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -3 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -2 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV HIS D -1 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV GLY D 0 UNP A0A9X6EQW EXPRESSION TAG
SEQADV 8YNV SER D 1 UNP A0A9X6EQW EXPRESSION TAG
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 SER 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 SER 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 SER 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 SER 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 A 401 22
HET P33 B 401 22
HET P33 C 401 22
HET P33 D 401 22
HET BTB D 402 14
HET BTB D 403 14
HETNAM P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETSYN P33 HEPTAETHYLENE GLYCOL; PEG330
HETSYN BTB BIS-TRIS BUFFER
FORMUL 5 P33 4(C14 H30 O8)
FORMUL 9 BTB 2(C8 H19 N O5)
FORMUL 11 HOH *1117(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 LYS B 92 1 17
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 LEU C 91 1 16
HELIX 30 AD3 MET C 103 HIS C 115 1 13
HELIX 31 AD4 THR C 152 ASP C 159 1 8
HELIX 32 AD5 GLN C 162 MET C 173 1 12
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 GLU C 298 1 14
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 MET D 173 1 11
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 31 O HIS A 56
SHEET 5 AA1 8 PHE A 96 TRP A 101 1 O SER A 97 N VAL A 32
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 SER B 97 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 MET C 99 N VAL C 32
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 TYR D 20 N GLU D 8
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 33 O TYR D 58
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 42.965 83.227 85.501 73.45 82.83 83.49 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 0.023275 -0.002656 -0.002286 0.00000
SCALE2 0.000000 0.012093 -0.003455 0.00000
SCALE3 0.000000 0.000000 0.012260 0.00000
TER 2396 GLN A 299
TER 4775 GLN B 299
TER 7163 LYS C 300
TER 9542 GLN D 299
MASTER 890 0 6 52 40 0 0 610771 4 116 96
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