HEADER TRANSFERASE 26-FEB-15 4YH2
TITLE GLUTATHIONE TRANSFERASE E6 FROM DROSOPHILA MELANOGASTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S TRANSFERASE E6;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.5.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: GSTE6, CG17530, DMEL_CG17530;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS TRANSFERASE, DROSOPHILA
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WONGSANTICHON,R.C.ROBINSON,A.J.KETTERMAN
REVDAT 3 20-MAR-24 4YH2 1 REMARK
REVDAT 2 05-FEB-20 4YH2 1 JRNL REMARK
REVDAT 1 10-FEB-16 4YH2 0
JRNL AUTH J.WONGSANTICHON,R.C.ROBINSON,A.J.KETTERMAN
JRNL TITL EPSILON GLUTATHIONE TRANSFERASES POSSESS A UNIQUE
JRNL TITL 2 CLASS-CONSERVED SUBUNIT INTERFACE MOTIF THAT DIRECTLY
JRNL TITL 3 INTERACTS WITH GLUTATHIONE IN THE ACTIVE SITE
JRNL REF BIOSCI.REP. V. 35 2015
JRNL REFN ISSN 0144-8463
JRNL PMID 26487708
JRNL DOI 10.1042/BSR20150183
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.SAISAWANG,J.WONGSANTICHON,A.J.KETTERMAN
REMARK 1 TITL A PRELIMINARY CHARACTERIZATION OF THE CYTOSOLIC GLUTATHIONE
REMARK 1 TITL 2 TRANSFERASE PROTEOME FROM DROSOPHILA MELANOGASTER
REMARK 1 REF BIOCHEM.J. V. 442 181 2012
REMARK 1 REFN ESSN 1470-8728
REMARK 1 PMID 22082028
REMARK 1 DOI 10.1042/BJ20111747
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 105000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5247
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 96.5967 - 5.3442 0.99 3427 178 0.1311 0.1449
REMARK 3 2 5.3442 - 4.2418 1.00 3367 192 0.1191 0.1348
REMARK 3 3 4.2418 - 3.7056 0.99 3331 190 0.1267 0.1371
REMARK 3 4 3.7056 - 3.3667 0.99 3346 174 0.1480 0.1951
REMARK 3 5 3.3667 - 3.1254 0.99 3300 191 0.1622 0.1958
REMARK 3 6 3.1254 - 2.9411 1.00 3332 173 0.1627 0.2224
REMARK 3 7 2.9411 - 2.7938 1.00 3339 158 0.1674 0.1872
REMARK 3 8 2.7938 - 2.6722 1.00 3332 164 0.1716 0.1986
REMARK 3 9 2.6722 - 2.5693 1.00 3378 161 0.1613 0.2016
REMARK 3 10 2.5693 - 2.4807 1.00 3338 166 0.1485 0.1943
REMARK 3 11 2.4807 - 2.4031 1.00 3324 191 0.1537 0.2128
REMARK 3 12 2.4031 - 2.3344 1.00 3312 201 0.1505 0.1770
REMARK 3 13 2.3344 - 2.2729 1.00 3253 184 0.1562 0.1898
REMARK 3 14 2.2729 - 2.2175 1.00 3365 176 0.1567 0.1950
REMARK 3 15 2.2175 - 2.1671 1.00 3285 177 0.1534 0.1777
REMARK 3 16 2.1671 - 2.1209 1.00 3318 184 0.1593 0.2043
REMARK 3 17 2.1209 - 2.0785 1.00 3338 165 0.1714 0.2100
REMARK 3 18 2.0785 - 2.0393 1.00 3339 175 0.1724 0.2155
REMARK 3 19 2.0393 - 2.0029 1.00 3303 182 0.1751 0.2094
REMARK 3 20 2.0029 - 1.9689 1.00 3344 157 0.1744 0.2198
REMARK 3 21 1.9689 - 1.9371 1.00 3275 181 0.1797 0.2081
REMARK 3 22 1.9371 - 1.9073 1.00 3286 204 0.1846 0.2406
REMARK 3 23 1.9073 - 1.8793 1.00 3356 154 0.2006 0.2245
REMARK 3 24 1.8793 - 1.8528 1.00 3306 164 0.2024 0.2730
REMARK 3 25 1.8528 - 1.8278 1.00 3350 160 0.2035 0.2617
REMARK 3 26 1.8278 - 1.8040 1.00 3326 160 0.2217 0.2570
REMARK 3 27 1.8040 - 1.7815 1.00 3240 180 0.2230 0.2482
REMARK 3 28 1.7815 - 1.7600 1.00 3385 170 0.2328 0.2687
REMARK 3 29 1.7600 - 1.7395 1.00 3292 167 0.2382 0.2693
REMARK 3 30 1.7395 - 1.7200 1.00 3266 168 0.2479 0.3323
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.54
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 : 0.006 7284
REMARK 3 ANGLE : 1.057 9904
REMARK 3 CHIRALITY : 0.044 1123
REMARK 3 PLANARITY : 0.006 1261
REMARK 3 DIHEDRAL : 12.658 2646
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 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.6388 -3.2408 25.1474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1215 T22: 0.1110
REMARK 3 T33: 0.1652 T12: 0.0123
REMARK 3 T13: 0.0205 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.1679 L22: 0.1507
REMARK 3 L33: 0.0718 L12: -0.1570
REMARK 3 L13: -0.1021 L23: -0.0325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0229 S13: 0.1119
REMARK 3 S21: 0.0611 S22: 0.0375 S23: 0.1064
REMARK 3 S31: -0.1436 S32: -0.0704 S33: 0.0020
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8082 -14.6113 36.7596
REMARK 3 T TENSOR
REMARK 3 T11: 0.2591 T22: 0.2677
REMARK 3 T33: 0.2089 T12: -0.0002
REMARK 3 T13: 0.0644 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0203
REMARK 3 L33: 0.0031 L12: -0.0256
REMARK 3 L13: 0.0126 L23: -0.0060
REMARK 3 S TENSOR
REMARK 3 S11: 0.0573 S12: -0.2086 S13: -0.0496
REMARK 3 S21: 0.2074 S22: 0.1435 S23: 0.2612
REMARK 3 S31: -0.0006 S32: -0.1983 S33: -0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8898 -14.4670 25.8728
REMARK 3 T TENSOR
REMARK 3 T11: 0.1506 T22: 0.1655
REMARK 3 T33: 0.1823 T12: -0.0154
REMARK 3 T13: 0.0249 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.0300 L22: 0.0491
REMARK 3 L33: 0.0855 L12: -0.0303
REMARK 3 L13: -0.0322 L23: -0.0072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0559 S12: -0.0569 S13: -0.1081
REMARK 3 S21: 0.0117 S22: -0.0006 S23: 0.1784
REMARK 3 S31: 0.1328 S32: -0.1242 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3379 -9.0064 10.4495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.2131
REMARK 3 T33: 0.1428 T12: 0.0087
REMARK 3 T13: -0.0237 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 0.1473 L22: 0.4798
REMARK 3 L33: 0.0830 L12: 0.0574
REMARK 3 L13: 0.0265 L23: 0.1020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0370 S12: 0.2727 S13: -0.0485
REMARK 3 S21: -0.0400 S22: -0.0616 S23: 0.2034
REMARK 3 S31: 0.0855 S32: 0.0482 S33: -0.0214
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 90 THROUGH 104 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6223 -8.7759 10.8480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.2002
REMARK 3 T33: 0.1179 T12: 0.0173
REMARK 3 T13: -0.0107 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0637 L22: 0.1256
REMARK 3 L33: 0.0195 L12: 0.0390
REMARK 3 L13: -0.0198 L23: -0.0348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0944 S12: 0.1773 S13: 0.0017
REMARK 3 S21: 0.0165 S22: -0.1000 S23: -0.0020
REMARK 3 S31: -0.0488 S32: 0.0541 S33: 0.0040
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0768 -3.6928 34.3988
REMARK 3 T TENSOR
REMARK 3 T11: 0.2236 T22: 0.1875
REMARK 3 T33: 0.1408 T12: -0.0084
REMARK 3 T13: -0.0250 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.0279 L22: 0.0689
REMARK 3 L33: 0.0224 L12: 0.0119
REMARK 3 L13: 0.0012 L23: 0.0116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0780 S12: -0.0758 S13: -0.0596
REMARK 3 S21: 0.2152 S22: 0.0366 S23: -0.0795
REMARK 3 S31: 0.0554 S32: -0.0177 S33: -0.0025
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4037 1.0075 21.8927
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.2180
REMARK 3 T33: 0.2331 T12: -0.0250
REMARK 3 T13: -0.0203 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.0605 L22: 0.0363
REMARK 3 L33: 0.0260 L12: 0.0180
REMARK 3 L13: -0.0436 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0737 S12: 0.0257 S13: 0.1663
REMARK 3 S21: 0.0585 S22: -0.0070 S23: -0.2509
REMARK 3 S31: -0.0587 S32: 0.2781 S33: 0.0001
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3843 4.1668 15.6007
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.1851
REMARK 3 T33: 0.2046 T12: -0.0141
REMARK 3 T13: -0.0023 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.1087 L22: 0.1677
REMARK 3 L33: 0.0193 L12: -0.1406
REMARK 3 L13: 0.0653 L23: -0.0624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: 0.1604 S13: 0.2922
REMARK 3 S21: 0.0029 S22: -0.0689 S23: -0.0645
REMARK 3 S31: -0.0166 S32: 0.0490 S33: -0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4387 8.9663 15.8346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1773 T22: 0.1474
REMARK 3 T33: 0.2671 T12: 0.0009
REMARK 3 T13: -0.0048 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 0.0351 L22: 0.1276
REMARK 3 L33: 0.3691 L12: 0.0278
REMARK 3 L13: 0.0935 L23: 0.2010
REMARK 3 S TENSOR
REMARK 3 S11: -0.1102 S12: 0.1304 S13: 0.3811
REMARK 3 S21: 0.0222 S22: -0.0456 S23: -0.0166
REMARK 3 S31: -0.2046 S32: -0.0456 S33: -0.0645
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 222 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0484 6.8772 34.4903
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1884
REMARK 3 T33: 0.2765 T12: 0.0231
REMARK 3 T13: -0.0483 T23: -0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 0.0445 L22: 0.2225
REMARK 3 L33: 0.1625 L12: 0.1022
REMARK 3 L13: -0.0844 L23: -0.2133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0751 S12: -0.0415 S13: 0.3809
REMARK 3 S21: 0.1946 S22: 0.1343 S23: -0.0151
REMARK 3 S31: -0.1259 S32: 0.2185 S33: 0.0402
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7160 7.8364 26.5699
REMARK 3 T TENSOR
REMARK 3 T11: 0.1399 T22: 0.1280
REMARK 3 T33: 0.1553 T12: 0.0142
REMARK 3 T13: -0.0099 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0479
REMARK 3 L33: 0.0301 L12: -0.0324
REMARK 3 L13: 0.0017 L23: 0.0304
REMARK 3 S TENSOR
REMARK 3 S11: 0.0296 S12: -0.0049 S13: 0.1321
REMARK 3 S21: -0.0318 S22: 0.0048 S23: 0.2328
REMARK 3 S31: -0.0567 S32: -0.0340 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5463 1.1111 21.1866
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.2124
REMARK 3 T33: 0.2053 T12: 0.0095
REMARK 3 T13: -0.0343 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.1843 L22: 0.1276
REMARK 3 L33: 0.5308 L12: 0.0451
REMARK 3 L13: -0.1935 L23: 0.0862
REMARK 3 S TENSOR
REMARK 3 S11: -0.0671 S12: 0.1428 S13: 0.0790
REMARK 3 S21: -0.1393 S22: 0.0042 S23: 0.1707
REMARK 3 S31: -0.0399 S32: -0.2793 S33: -0.0276
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8756 6.8242 20.3559
REMARK 3 T TENSOR
REMARK 3 T11: 0.1436 T22: 0.1470
REMARK 3 T33: 0.1560 T12: -0.0069
REMARK 3 T13: -0.0136 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 0.1419 L22: 0.1718
REMARK 3 L33: 0.0801 L12: -0.0654
REMARK 3 L13: -0.0160 L23: 0.0040
REMARK 3 S TENSOR
REMARK 3 S11: -0.0002 S12: 0.0559 S13: 0.1515
REMARK 3 S21: -0.0605 S22: -0.0003 S23: -0.0063
REMARK 3 S31: -0.0335 S32: -0.0393 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2275 -5.6917 35.9426
REMARK 3 T TENSOR
REMARK 3 T11: 0.1204 T22: 0.1110
REMARK 3 T33: 0.1048 T12: -0.0218
REMARK 3 T13: 0.0120 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.0793 L22: 0.3365
REMARK 3 L33: 0.3322 L12: -0.1760
REMARK 3 L13: 0.0195 L23: 0.1988
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: 0.0094 S13: 0.1178
REMARK 3 S21: 0.0057 S22: -0.0181 S23: 0.1106
REMARK 3 S31: 0.0798 S32: -0.1072 S33: 0.0001
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4374 -5.8815 46.4295
REMARK 3 T TENSOR
REMARK 3 T11: 0.2268 T22: 0.1560
REMARK 3 T33: 0.1425 T12: 0.0008
REMARK 3 T13: 0.0337 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.0680 L22: 0.0490
REMARK 3 L33: 0.0503 L12: -0.0679
REMARK 3 L13: -0.0014 L23: 0.0038
REMARK 3 S TENSOR
REMARK 3 S11: -0.0285 S12: -0.1570 S13: -0.1879
REMARK 3 S21: 0.1869 S22: 0.0388 S23: -0.1128
REMARK 3 S31: 0.0447 S32: 0.0993 S33: -0.0003
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 146 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3020 9.3172 39.3961
REMARK 3 T TENSOR
REMARK 3 T11: 0.1918 T22: 0.1485
REMARK 3 T33: 0.1607 T12: -0.0315
REMARK 3 T13: -0.0419 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.0171 L22: 0.0006
REMARK 3 L33: 0.0168 L12: 0.0082
REMARK 3 L13: 0.0086 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0935 S12: 0.0895 S13: 0.2099
REMARK 3 S21: 0.0999 S22: -0.0979 S23: -0.2531
REMARK 3 S31: -0.2891 S32: 0.2197 S33: 0.0002
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4231 3.1064 43.5464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1475 T22: 0.1236
REMARK 3 T33: 0.1247 T12: -0.0216
REMARK 3 T13: 0.0162 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.0112 L22: 0.1046
REMARK 3 L33: 0.0489 L12: 0.0694
REMARK 3 L13: -0.0205 L23: 0.0478
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: 0.0017 S13: 0.1484
REMARK 3 S21: 0.0311 S22: -0.0405 S23: 0.0274
REMARK 3 S31: -0.0099 S32: -0.0984 S33: 0.0018
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0485 12.9387 40.7954
REMARK 3 T TENSOR
REMARK 3 T11: 0.1913 T22: 0.1385
REMARK 3 T33: 0.1641 T12: -0.0041
REMARK 3 T13: 0.0299 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.0475 L22: 0.0755
REMARK 3 L33: 0.0548 L12: -0.0016
REMARK 3 L13: -0.0506 L23: 0.0289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: -0.0529 S13: 0.0820
REMARK 3 S21: 0.1812 S22: 0.0293 S23: 0.1562
REMARK 3 S31: -0.1032 S32: -0.0226 S33: 0.0003
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 203 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8965 -0.2589 43.3830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1858 T22: 0.2479
REMARK 3 T33: 0.3354 T12: -0.0002
REMARK 3 T13: 0.0873 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.0243 L22: 0.0329
REMARK 3 L33: 0.0837 L12: -0.0027
REMARK 3 L13: -0.0408 L23: 0.0508
REMARK 3 S TENSOR
REMARK 3 S11: -0.0468 S12: -0.0336 S13: 0.0244
REMARK 3 S21: 0.0223 S22: -0.0113 S23: 0.2252
REMARK 3 S31: 0.0116 S32: -0.2794 S33: -0.0006
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4734 -22.9794 10.0308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1522 T22: 0.2659
REMARK 3 T33: 0.0871 T12: 0.0754
REMARK 3 T13: -0.0014 T23: -0.0688
REMARK 3 L TENSOR
REMARK 3 L11: 0.0675 L22: 0.0850
REMARK 3 L33: 0.1663 L12: -0.0087
REMARK 3 L13: -0.0588 L23: -0.0252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0638 S12: 0.3110 S13: -0.1601
REMARK 3 S21: -0.0091 S22: -0.2057 S23: -0.0447
REMARK 3 S31: 0.0865 S32: 0.1648 S33: -0.2154
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8256 -14.6771 8.9963
REMARK 3 T TENSOR
REMARK 3 T11: 0.0748 T22: 0.4246
REMARK 3 T33: -0.0746 T12: 0.0768
REMARK 3 T13: 0.1117 T23: -0.0570
REMARK 3 L TENSOR
REMARK 3 L11: 0.0536 L22: 0.0426
REMARK 3 L33: 0.0819 L12: 0.0703
REMARK 3 L13: -0.0837 L23: 0.0578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: 0.5450 S13: 0.4457
REMARK 3 S21: 0.1407 S22: -0.4226 S23: -0.5086
REMARK 3 S31: -0.0630 S32: 0.6236 S33: -0.1079
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 57 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8618 -13.3336 3.1428
REMARK 3 T TENSOR
REMARK 3 T11: 0.2080 T22: 0.3535
REMARK 3 T33: 0.1010 T12: 0.0132
REMARK 3 T13: 0.0074 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.0150 L22: 0.0286
REMARK 3 L33: 0.0199 L12: -0.0210
REMARK 3 L13: -0.0035 L23: 0.0119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0471 S12: 0.2048 S13: -0.0085
REMARK 3 S21: -0.0990 S22: -0.0181 S23: 0.1132
REMARK 3 S31: 0.0377 S32: 0.1043 S33: -0.0248
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 68 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8048 -21.5147 6.5480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.2597
REMARK 3 T33: 0.1359 T12: 0.0391
REMARK 3 T13: -0.0287 T23: -0.0703
REMARK 3 L TENSOR
REMARK 3 L11: 0.0375 L22: 0.0468
REMARK 3 L33: 0.0357 L12: 0.0006
REMARK 3 L13: 0.0069 L23: 0.0359
REMARK 3 S TENSOR
REMARK 3 S11: 0.1113 S12: 0.1514 S13: -0.0091
REMARK 3 S21: 0.0128 S22: -0.1192 S23: 0.1463
REMARK 3 S31: 0.0751 S32: -0.0391 S33: 0.0001
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 90 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3433 -15.7325 24.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.1403
REMARK 3 T33: 0.0964 T12: -0.0136
REMARK 3 T13: -0.0058 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.0819 L22: 0.2418
REMARK 3 L33: -0.0131 L12: -0.2676
REMARK 3 L13: 0.0603 L23: -0.0329
REMARK 3 S TENSOR
REMARK 3 S11: -0.0505 S12: 0.0509 S13: 0.0782
REMARK 3 S21: 0.0337 S22: -0.0698 S23: 0.0137
REMARK 3 S31: -0.0436 S32: 0.0748 S33: -0.0008
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4638 -20.5574 34.1291
REMARK 3 T TENSOR
REMARK 3 T11: 0.1987 T22: 0.1670
REMARK 3 T33: 0.1445 T12: 0.0005
REMARK 3 T13: -0.0110 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.0513 L22: 0.0522
REMARK 3 L33: 0.0443 L12: -0.0332
REMARK 3 L13: -0.0141 L23: -0.0477
REMARK 3 S TENSOR
REMARK 3 S11: -0.0306 S12: -0.2433 S13: -0.0929
REMARK 3 S21: 0.0795 S22: -0.0171 S23: 0.0761
REMARK 3 S31: -0.0798 S32: -0.0705 S33: -0.0001
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 146 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7624 -28.1804 24.7884
REMARK 3 T TENSOR
REMARK 3 T11: 0.1958 T22: 0.1533
REMARK 3 T33: 0.1881 T12: -0.0133
REMARK 3 T13: -0.0182 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.0646 L22: 0.1910
REMARK 3 L33: 0.0730 L12: 0.0420
REMARK 3 L13: -0.0347 L23: 0.0083
REMARK 3 S TENSOR
REMARK 3 S11: 0.1106 S12: 0.0381 S13: -0.2047
REMARK 3 S21: 0.0037 S22: -0.0523 S23: 0.0195
REMARK 3 S31: 0.1425 S32: 0.0772 S33: 0.0003
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 183 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4724 -34.2569 19.9173
REMARK 3 T TENSOR
REMARK 3 T11: 0.2392 T22: 0.1816
REMARK 3 T33: 0.2548 T12: 0.0308
REMARK 3 T13: -0.0203 T23: -0.0558
REMARK 3 L TENSOR
REMARK 3 L11: 0.0544 L22: -0.0099
REMARK 3 L33: 0.0554 L12: -0.0104
REMARK 3 L13: 0.0572 L23: 0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0893 S12: 0.0089 S13: -0.3460
REMARK 3 S21: 0.0425 S22: -0.0445 S23: 0.0723
REMARK 3 S31: 0.2111 S32: 0.1490 S33: 0.0051
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 203 THROUGH 222 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4822 -24.5251 28.6851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1776 T22: 0.2222
REMARK 3 T33: 0.1933 T12: 0.0469
REMARK 3 T13: -0.0199 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0364 L22: 0.0918
REMARK 3 L33: 0.0461 L12: -0.0031
REMARK 3 L13: -0.0105 L23: -0.0740
REMARK 3 S TENSOR
REMARK 3 S11: 0.1451 S12: -0.0844 S13: -0.1479
REMARK 3 S21: 0.0106 S22: -0.0801 S23: -0.1983
REMARK 3 S31: 0.0532 S32: 0.1659 S33: -0.0010
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2231 -14.7320 28.4158
REMARK 3 T TENSOR
REMARK 3 T11: 0.1423 T22: 0.0930
REMARK 3 T33: 0.1656 T12: -0.0172
REMARK 3 T13: -0.0053 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.0975 L22: 0.0732
REMARK 3 L33: 0.0568 L12: -0.0893
REMARK 3 L13: -0.0124 L23: -0.0253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: 0.0257 S13: -0.0714
REMARK 3 S21: 0.0895 S22: -0.0472 S23: -0.1162
REMARK 3 S31: -0.0372 S32: 0.0278 S33: 0.0010
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 25 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4855 -13.7040 38.4407
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.1909
REMARK 3 T33: 0.2130 T12: -0.0140
REMARK 3 T13: -0.0359 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 0.2239 L22: 0.1129
REMARK 3 L33: 0.0314 L12: -0.0413
REMARK 3 L13: 0.0062 L23: 0.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: -0.1838 S13: -0.1405
REMARK 3 S21: 0.1163 S22: -0.0384 S23: -0.2049
REMARK 3 S31: 0.0238 S32: 0.0042 S33: -0.0001
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 57 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8619 -4.2195 25.0165
REMARK 3 T TENSOR
REMARK 3 T11: 0.1372 T22: 0.1086
REMARK 3 T33: 0.1364 T12: -0.0090
REMARK 3 T13: -0.0061 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.1307 L22: 0.1831
REMARK 3 L33: 0.1085 L12: 0.0700
REMARK 3 L13: -0.0089 L23: 0.0284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0214 S12: 0.0316 S13: 0.0928
REMARK 3 S21: 0.0320 S22: -0.0164 S23: -0.1467
REMARK 3 S31: -0.0431 S32: 0.0153 S33: -0.0001
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 90 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2643 -14.0559 30.6931
REMARK 3 T TENSOR
REMARK 3 T11: 0.1479 T22: 0.0889
REMARK 3 T33: 0.1134 T12: -0.0235
REMARK 3 T13: 0.0034 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.2216 L22: 0.2101
REMARK 3 L33: 0.0664 L12: -0.0265
REMARK 3 L13: -0.0152 L23: 0.1525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0684 S12: 0.0372 S13: -0.0154
REMARK 3 S21: 0.1254 S22: -0.0643 S23: 0.0302
REMARK 3 S31: -0.0730 S32: 0.0365 S33: -0.0069
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 129 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6815 -18.9447 25.1536
REMARK 3 T TENSOR
REMARK 3 T11: 0.1429 T22: 0.1598
REMARK 3 T33: 0.1709 T12: -0.0238
REMARK 3 T13: 0.0143 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.0454 L22: 0.0540
REMARK 3 L33: 0.0147 L12: -0.0139
REMARK 3 L13: 0.0340 L23: -0.0020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0188 S12: 0.0684 S13: -0.0641
REMARK 3 S21: -0.0461 S22: 0.0767 S23: 0.2383
REMARK 3 S31: -0.0218 S32: -0.2561 S33: 0.0006
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 146 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2203 -11.7517 10.9406
REMARK 3 T TENSOR
REMARK 3 T11: 0.2071 T22: 0.2446
REMARK 3 T33: 0.1409 T12: -0.0063
REMARK 3 T13: -0.0119 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.0231 L22: 0.0071
REMARK 3 L33: 0.0020 L12: 0.0030
REMARK 3 L13: 0.0132 L23: -0.0149
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: 0.3622 S13: 0.1768
REMARK 3 S21: -0.2483 S22: 0.0056 S23: 0.0777
REMARK 3 S31: 0.0005 S32: -0.0277 S33: -0.0001
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 159 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7489 -21.5792 21.8375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1497 T22: 0.1432
REMARK 3 T33: 0.1348 T12: -0.0202
REMARK 3 T13: 0.0020 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0092
REMARK 3 L33: 0.0524 L12: 0.0087
REMARK 3 L13: -0.0731 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.1156 S13: -0.0730
REMARK 3 S21: -0.0591 S22: 0.0514 S23: -0.0825
REMARK 3 S31: 0.0854 S32: -0.0315 S33: -0.0000
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 183 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2273 -25.7596 23.7461
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.1295
REMARK 3 T33: 0.1856 T12: -0.0107
REMARK 3 T13: 0.0043 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.0979 L22: 0.2478
REMARK 3 L33: 0.1539 L12: -0.0763
REMARK 3 L13: 0.0393 L23: 0.0107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: 0.1042 S13: -0.2540
REMARK 3 S21: -0.0394 S22: -0.0049 S23: -0.0385
REMARK 3 S31: 0.1095 S32: -0.0216 S33: -0.0005
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 4YH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-13
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105003
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 96.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: XIA2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM THIOCYANATE, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 88.17500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 88.17500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.43000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 1
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 ALA B 222
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 ALA D 222
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 A 431 O HOH A 482 2.16
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 HIS A 53 56.09 37.80
REMARK 500 ASP A 67 119.80 72.57
REMARK 500 TYR A 86 73.35 -152.73
REMARK 500 ASP B 67 117.66 74.08
REMARK 500 TYR B 86 74.74 -152.48
REMARK 500 ASP C 67 117.65 72.53
REMARK 500 TYR C 86 73.16 -151.92
REMARK 500 ASP D 61 64.04 35.67
REMARK 500 ASP D 67 117.44 73.15
REMARK 500 TYR D 86 73.00 -155.79
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 A 610 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A 611 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 615 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A 627 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 566 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C 618 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH D 573 DISTANCE = 6.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSH D 301
DBREF 4YH2 A 1 222 UNP A1ZB71 A1ZB71_DROME 1 222
DBREF 4YH2 B 1 222 UNP A1ZB71 A1ZB71_DROME 1 222
DBREF 4YH2 C 1 222 UNP A1ZB71 A1ZB71_DROME 1 222
DBREF 4YH2 D 1 222 UNP A1ZB71 A1ZB71_DROME 1 222
SEQRES 1 A 222 MET VAL LYS LEU THR LEU TYR GLY LEU ASP PRO SER PRO
SEQRES 2 A 222 PRO VAL ARG ALA VAL LYS LEU THR LEU ALA ALA LEU ASN
SEQRES 3 A 222 LEU THR TYR GLU TYR VAL ASN VAL ASP ILE VAL ALA ARG
SEQRES 4 A 222 ALA GLN LEU SER PRO GLU TYR LEU GLU LYS ASN PRO GLN
SEQRES 5 A 222 HIS THR VAL PRO THR LEU GLU ASP ASP GLY HIS TYR ILE
SEQRES 6 A 222 TRP ASP SER HIS ALA ILE ILE ALA TYR LEU VAL SER LYS
SEQRES 7 A 222 TYR ALA ASP SER ASP ALA LEU TYR PRO LYS ASP PRO LEU
SEQRES 8 A 222 LYS ARG ALA VAL VAL ASP GLN ARG LEU HIS PHE GLU SER
SEQRES 9 A 222 GLY VAL VAL PHE ALA ASN GLY ILE ARG SER ILE SER LYS
SEQRES 10 A 222 SER VAL LEU PHE GLN GLY GLN THR LYS VAL PRO LYS GLU
SEQRES 11 A 222 ARG TYR ASP ALA ILE ILE GLU ILE TYR ASP PHE VAL GLU
SEQRES 12 A 222 THR PHE LEU LYS GLY GLN ASP TYR ILE ALA GLY ASN GLN
SEQRES 13 A 222 LEU THR ILE ALA ASP PHE SER LEU VAL SER SER VAL ALA
SEQRES 14 A 222 SER LEU GLU ALA PHE VAL ALA LEU ASP THR THR LYS TYR
SEQRES 15 A 222 PRO ARG ILE GLY ALA TRP ILE LYS LYS LEU GLU GLN LEU
SEQRES 16 A 222 PRO TYR TYR GLU GLU ALA ASN GLY LYS GLY VAL ARG GLN
SEQRES 17 A 222 LEU VAL ALA ILE PHE LYS LYS THR ASN PHE THR PHE GLU
SEQRES 18 A 222 ALA
SEQRES 1 B 222 MET VAL LYS LEU THR LEU TYR GLY LEU ASP PRO SER PRO
SEQRES 2 B 222 PRO VAL ARG ALA VAL LYS LEU THR LEU ALA ALA LEU ASN
SEQRES 3 B 222 LEU THR TYR GLU TYR VAL ASN VAL ASP ILE VAL ALA ARG
SEQRES 4 B 222 ALA GLN LEU SER PRO GLU TYR LEU GLU LYS ASN PRO GLN
SEQRES 5 B 222 HIS THR VAL PRO THR LEU GLU ASP ASP GLY HIS TYR ILE
SEQRES 6 B 222 TRP ASP SER HIS ALA ILE ILE ALA TYR LEU VAL SER LYS
SEQRES 7 B 222 TYR ALA ASP SER ASP ALA LEU TYR PRO LYS ASP PRO LEU
SEQRES 8 B 222 LYS ARG ALA VAL VAL ASP GLN ARG LEU HIS PHE GLU SER
SEQRES 9 B 222 GLY VAL VAL PHE ALA ASN GLY ILE ARG SER ILE SER LYS
SEQRES 10 B 222 SER VAL LEU PHE GLN GLY GLN THR LYS VAL PRO LYS GLU
SEQRES 11 B 222 ARG TYR ASP ALA ILE ILE GLU ILE TYR ASP PHE VAL GLU
SEQRES 12 B 222 THR PHE LEU LYS GLY GLN ASP TYR ILE ALA GLY ASN GLN
SEQRES 13 B 222 LEU THR ILE ALA ASP PHE SER LEU VAL SER SER VAL ALA
SEQRES 14 B 222 SER LEU GLU ALA PHE VAL ALA LEU ASP THR THR LYS TYR
SEQRES 15 B 222 PRO ARG ILE GLY ALA TRP ILE LYS LYS LEU GLU GLN LEU
SEQRES 16 B 222 PRO TYR TYR GLU GLU ALA ASN GLY LYS GLY VAL ARG GLN
SEQRES 17 B 222 LEU VAL ALA ILE PHE LYS LYS THR ASN PHE THR PHE GLU
SEQRES 18 B 222 ALA
SEQRES 1 C 222 MET VAL LYS LEU THR LEU TYR GLY LEU ASP PRO SER PRO
SEQRES 2 C 222 PRO VAL ARG ALA VAL LYS LEU THR LEU ALA ALA LEU ASN
SEQRES 3 C 222 LEU THR TYR GLU TYR VAL ASN VAL ASP ILE VAL ALA ARG
SEQRES 4 C 222 ALA GLN LEU SER PRO GLU TYR LEU GLU LYS ASN PRO GLN
SEQRES 5 C 222 HIS THR VAL PRO THR LEU GLU ASP ASP GLY HIS TYR ILE
SEQRES 6 C 222 TRP ASP SER HIS ALA ILE ILE ALA TYR LEU VAL SER LYS
SEQRES 7 C 222 TYR ALA ASP SER ASP ALA LEU TYR PRO LYS ASP PRO LEU
SEQRES 8 C 222 LYS ARG ALA VAL VAL ASP GLN ARG LEU HIS PHE GLU SER
SEQRES 9 C 222 GLY VAL VAL PHE ALA ASN GLY ILE ARG SER ILE SER LYS
SEQRES 10 C 222 SER VAL LEU PHE GLN GLY GLN THR LYS VAL PRO LYS GLU
SEQRES 11 C 222 ARG TYR ASP ALA ILE ILE GLU ILE TYR ASP PHE VAL GLU
SEQRES 12 C 222 THR PHE LEU LYS GLY GLN ASP TYR ILE ALA GLY ASN GLN
SEQRES 13 C 222 LEU THR ILE ALA ASP PHE SER LEU VAL SER SER VAL ALA
SEQRES 14 C 222 SER LEU GLU ALA PHE VAL ALA LEU ASP THR THR LYS TYR
SEQRES 15 C 222 PRO ARG ILE GLY ALA TRP ILE LYS LYS LEU GLU GLN LEU
SEQRES 16 C 222 PRO TYR TYR GLU GLU ALA ASN GLY LYS GLY VAL ARG GLN
SEQRES 17 C 222 LEU VAL ALA ILE PHE LYS LYS THR ASN PHE THR PHE GLU
SEQRES 18 C 222 ALA
SEQRES 1 D 222 MET VAL LYS LEU THR LEU TYR GLY LEU ASP PRO SER PRO
SEQRES 2 D 222 PRO VAL ARG ALA VAL LYS LEU THR LEU ALA ALA LEU ASN
SEQRES 3 D 222 LEU THR TYR GLU TYR VAL ASN VAL ASP ILE VAL ALA ARG
SEQRES 4 D 222 ALA GLN LEU SER PRO GLU TYR LEU GLU LYS ASN PRO GLN
SEQRES 5 D 222 HIS THR VAL PRO THR LEU GLU ASP ASP GLY HIS TYR ILE
SEQRES 6 D 222 TRP ASP SER HIS ALA ILE ILE ALA TYR LEU VAL SER LYS
SEQRES 7 D 222 TYR ALA ASP SER ASP ALA LEU TYR PRO LYS ASP PRO LEU
SEQRES 8 D 222 LYS ARG ALA VAL VAL ASP GLN ARG LEU HIS PHE GLU SER
SEQRES 9 D 222 GLY VAL VAL PHE ALA ASN GLY ILE ARG SER ILE SER LYS
SEQRES 10 D 222 SER VAL LEU PHE GLN GLY GLN THR LYS VAL PRO LYS GLU
SEQRES 11 D 222 ARG TYR ASP ALA ILE ILE GLU ILE TYR ASP PHE VAL GLU
SEQRES 12 D 222 THR PHE LEU LYS GLY GLN ASP TYR ILE ALA GLY ASN GLN
SEQRES 13 D 222 LEU THR ILE ALA ASP PHE SER LEU VAL SER SER VAL ALA
SEQRES 14 D 222 SER LEU GLU ALA PHE VAL ALA LEU ASP THR THR LYS TYR
SEQRES 15 D 222 PRO ARG ILE GLY ALA TRP ILE LYS LYS LEU GLU GLN LEU
SEQRES 16 D 222 PRO TYR TYR GLU GLU ALA ASN GLY LYS GLY VAL ARG GLN
SEQRES 17 D 222 LEU VAL ALA ILE PHE LYS LYS THR ASN PHE THR PHE GLU
SEQRES 18 D 222 ALA
HET GSH A 301 20
HET GSH B 301 20
HET GSH C 301 20
HET GSH D 301 20
HETNAM GSH GLUTATHIONE
FORMUL 5 GSH 4(C10 H17 N3 O6 S)
FORMUL 9 HOH *979(H2 O)
HELIX 1 AA1 SER A 12 LEU A 25 1 14
HELIX 2 AA2 ASP A 35 LEU A 42 5 8
HELIX 3 AA3 SER A 43 ASN A 50 1 8
HELIX 4 AA4 ASP A 67 ALA A 80 1 14
HELIX 5 AA5 ASP A 89 GLY A 105 1 17
HELIX 6 AA6 VAL A 107 ILE A 112 1 6
HELIX 7 AA7 ILE A 112 PHE A 121 1 10
HELIX 8 AA8 PRO A 128 LEU A 146 1 19
HELIX 9 AA9 THR A 158 ALA A 169 1 12
HELIX 10 AB1 SER A 170 PHE A 174 5 5
HELIX 11 AB2 TYR A 182 GLN A 194 1 13
HELIX 12 AB3 TYR A 197 ASN A 202 1 6
HELIX 13 AB4 ASN A 202 ASN A 217 1 16
HELIX 14 AB5 SER B 12 LEU B 25 1 14
HELIX 15 AB6 ARG B 39 LEU B 42 5 4
HELIX 16 AB7 SER B 43 ASN B 50 1 8
HELIX 17 AB8 ASP B 67 ALA B 80 1 14
HELIX 18 AB9 ASP B 89 VAL B 106 1 18
HELIX 19 AC1 VAL B 107 ILE B 112 1 6
HELIX 20 AC2 ILE B 112 PHE B 121 1 10
HELIX 21 AC3 PRO B 128 LEU B 146 1 19
HELIX 22 AC4 THR B 158 ALA B 169 1 12
HELIX 23 AC5 SER B 170 PHE B 174 5 5
HELIX 24 AC6 TYR B 182 GLN B 194 1 13
HELIX 25 AC7 TYR B 197 ASN B 202 1 6
HELIX 26 AC8 ASN B 202 THR B 216 1 15
HELIX 27 AC9 SER C 12 LEU C 25 1 14
HELIX 28 AD1 ARG C 39 LEU C 42 5 4
HELIX 29 AD2 SER C 43 ASN C 50 1 8
HELIX 30 AD3 ASP C 67 ALA C 80 1 14
HELIX 31 AD4 ASP C 89 VAL C 106 1 18
HELIX 32 AD5 VAL C 107 ILE C 112 1 6
HELIX 33 AD6 ILE C 112 LEU C 120 1 9
HELIX 34 AD7 PRO C 128 LEU C 146 1 19
HELIX 35 AD8 THR C 158 ALA C 169 1 12
HELIX 36 AD9 SER C 170 PHE C 174 5 5
HELIX 37 AE1 TYR C 182 GLN C 194 1 13
HELIX 38 AE2 TYR C 197 ASN C 202 1 6
HELIX 39 AE3 ASN C 202 ASN C 217 1 16
HELIX 40 AE4 SER D 12 LEU D 25 1 14
HELIX 41 AE5 ARG D 39 LEU D 42 5 4
HELIX 42 AE6 SER D 43 ASN D 50 1 8
HELIX 43 AE7 ASP D 67 ALA D 80 1 14
HELIX 44 AE8 ASP D 89 GLY D 105 1 17
HELIX 45 AE9 VAL D 107 ILE D 112 1 6
HELIX 46 AF1 ILE D 112 GLN D 122 1 11
HELIX 47 AF2 PRO D 128 LEU D 146 1 19
HELIX 48 AF3 THR D 158 ALA D 169 1 12
HELIX 49 AF4 SER D 170 PHE D 174 5 5
HELIX 50 AF5 TYR D 182 GLU D 193 1 12
HELIX 51 AF6 TYR D 197 ASN D 202 1 6
HELIX 52 AF7 ASN D 202 ASN D 217 1 16
SHEET 1 AA1 4 GLU A 30 ASN A 33 0
SHEET 2 AA1 4 LEU A 4 GLY A 8 1 N LEU A 6 O VAL A 32
SHEET 3 AA1 4 THR A 57 ASP A 60 -1 O GLU A 59 N THR A 5
SHEET 4 AA1 4 HIS A 63 TRP A 66 -1 O ILE A 65 N LEU A 58
SHEET 1 AA2 2 LYS A 126 VAL A 127 0
SHEET 2 AA2 2 THR A 219 PHE A 220 1 O THR A 219 N VAL A 127
SHEET 1 AA3 4 GLU B 30 ASN B 33 0
SHEET 2 AA3 4 LEU B 4 GLY B 8 1 N LEU B 6 O GLU B 30
SHEET 3 AA3 4 THR B 57 ASP B 60 -1 O THR B 57 N TYR B 7
SHEET 4 AA3 4 HIS B 63 TRP B 66 -1 O ILE B 65 N LEU B 58
SHEET 1 AA4 2 LYS B 126 VAL B 127 0
SHEET 2 AA4 2 THR B 219 PHE B 220 1 O THR B 219 N VAL B 127
SHEET 1 AA5 4 GLU C 30 ASN C 33 0
SHEET 2 AA5 4 LEU C 4 GLY C 8 1 N LEU C 6 O GLU C 30
SHEET 3 AA5 4 THR C 57 ASP C 60 -1 O GLU C 59 N THR C 5
SHEET 4 AA5 4 HIS C 63 TRP C 66 -1 O ILE C 65 N LEU C 58
SHEET 1 AA6 2 LYS C 126 VAL C 127 0
SHEET 2 AA6 2 THR C 219 PHE C 220 1 O THR C 219 N VAL C 127
SHEET 1 AA7 4 GLU D 30 ASN D 33 0
SHEET 2 AA7 4 LEU D 4 GLY D 8 1 N LEU D 6 O VAL D 32
SHEET 3 AA7 4 THR D 57 ASP D 60 -1 O THR D 57 N TYR D 7
SHEET 4 AA7 4 HIS D 63 TRP D 66 -1 O ILE D 65 N LEU D 58
SHEET 1 AA8 2 LYS D 126 VAL D 127 0
SHEET 2 AA8 2 THR D 219 PHE D 220 1 O THR D 219 N VAL D 127
CISPEP 1 VAL A 55 PRO A 56 0 4.52
CISPEP 2 VAL B 55 PRO B 56 0 3.11
CISPEP 3 VAL C 55 PRO C 56 0 3.23
CISPEP 4 VAL D 55 PRO D 56 0 2.09
SITE 1 AC1 18 SER A 12 PRO A 14 GLN A 41 HIS A 53
SITE 2 AC1 18 THR A 54 VAL A 55 PRO A 56 ASP A 67
SITE 3 AC1 18 SER A 68 HIS A 69 PHE A 108 ARG A 113
SITE 4 AC1 18 HOH A 447 HOH A 448 HOH A 449 HOH A 459
SITE 5 AC1 18 HOH A 514 HOH A 592
SITE 1 AC2 17 SER B 12 PRO B 14 GLN B 41 HIS B 53
SITE 2 AC2 17 THR B 54 VAL B 55 PRO B 56 ASP B 67
SITE 3 AC2 17 SER B 68 HIS B 69 PHE B 108 ARG B 113
SITE 4 AC2 17 HOH B 436 HOH B 443 HOH B 449 HOH B 455
SITE 5 AC2 17 HOH B 486
SITE 1 AC3 17 SER C 12 PRO C 14 GLN C 41 HIS C 53
SITE 2 AC3 17 THR C 54 VAL C 55 PRO C 56 ASP C 67
SITE 3 AC3 17 SER C 68 HIS C 69 PHE C 108 ARG C 113
SITE 4 AC3 17 HOH C 423 HOH C 427 HOH C 428 HOH C 433
SITE 5 AC3 17 HOH C 503
SITE 1 AC4 17 SER D 12 PRO D 14 GLN D 41 HIS D 53
SITE 2 AC4 17 THR D 54 VAL D 55 PRO D 56 ASP D 67
SITE 3 AC4 17 SER D 68 HIS D 69 PHE D 108 ARG D 113
SITE 4 AC4 17 HOH D 462 HOH D 464 HOH D 470 HOH D 487
SITE 5 AC4 17 HOH D 507
CRYST1 176.350 58.860 122.810 90.00 128.25 90.00 C 1 2 1 16
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 0.005671 0.000000 0.004470 0.00000
SCALE2 0.000000 0.016989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010369 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
