HEADER HYDROLASE 04-FEB-16 5I0J
TITLE CRYSTAL STRUCTURE OF DR2231_E47A MUTANT IN COMPLEX WITH DUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DR2231;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DR_2231;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET151/D-TOPO
KEYWDS ALPHA HELIX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.MOTA,A.M.D.GONCALVES,D.DE SANCTIS
REVDAT 4 10-JAN-24 5I0J 1 REMARK
REVDAT 3 04-APR-18 5I0J 1 AUTHOR
REVDAT 2 14-DEC-16 5I0J 1 JRNL
REVDAT 1 26-OCT-16 5I0J 0
JRNL AUTH C.S.MOTA,A.M.GONCALVES,D.DE SANCTIS
JRNL TITL DEINOCOCCUS RADIODURANS DR2231 IS A TWO-METAL-ION MECHANISM
JRNL TITL 2 HYDROLASE WITH EXCLUSIVE ACTIVITY ON DUTP.
JRNL REF FEBS J. V. 283 4274 2016
JRNL REFN ISSN 1742-4658
JRNL PMID 27739259
JRNL DOI 10.1111/FEBS.13923
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.260
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 57787
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 5568
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 43.5434 - 5.5892 0.99 3437 209 0.1938 0.2067
REMARK 3 2 5.5892 - 4.4377 0.99 3453 192 0.1641 0.2047
REMARK 3 3 4.4377 - 3.8772 0.99 3467 182 0.1470 0.1518
REMARK 3 4 3.8772 - 3.5229 1.00 3486 142 0.1420 0.1825
REMARK 3 5 3.5229 - 3.2704 1.00 3456 184 0.1431 0.1680
REMARK 3 6 3.2704 - 3.0777 1.00 3466 188 0.1477 0.2049
REMARK 3 7 3.0777 - 2.9236 0.99 3473 181 0.1420 0.1651
REMARK 3 8 2.9236 - 2.7963 0.99 3449 213 0.1490 0.1874
REMARK 3 9 2.7963 - 2.6887 1.00 3463 178 0.1577 0.2133
REMARK 3 10 2.6887 - 2.5959 0.99 3480 178 0.1611 0.2152
REMARK 3 11 2.5959 - 2.5148 0.99 3437 187 0.1656 0.2323
REMARK 3 12 2.5148 - 2.4429 1.00 3549 165 0.1687 0.2352
REMARK 3 13 2.4429 - 2.3786 0.99 3416 171 0.1643 0.2325
REMARK 3 14 2.3786 - 2.3206 1.00 3535 189 0.1547 0.1941
REMARK 3 15 2.3206 - 2.2678 0.99 3409 203 0.1546 0.2027
REMARK 3 16 2.2678 - 2.2196 0.99 3479 185 0.1622 0.2034
REMARK 3 17 2.2196 - 2.1752 0.99 3466 151 0.1707 0.2140
REMARK 3 18 2.1752 - 2.1341 1.00 3486 197 0.1738 0.1913
REMARK 3 19 2.1341 - 2.0960 1.00 3442 184 0.1852 0.2402
REMARK 3 20 2.0960 - 2.0605 1.00 3487 170 0.1867 0.1988
REMARK 3 21 2.0605 - 2.0272 1.00 3469 206 0.2039 0.2660
REMARK 3 22 2.0272 - 1.9960 1.00 3472 184 0.2053 0.2632
REMARK 3 23 1.9960 - 1.9667 1.00 3446 177 0.2126 0.2405
REMARK 3 24 1.9667 - 1.9390 1.00 3443 201 0.2278 0.2984
REMARK 3 25 1.9390 - 1.9128 1.00 3492 197 0.2421 0.2872
REMARK 3 26 1.9128 - 1.8879 1.00 3497 164 0.2577 0.2789
REMARK 3 27 1.8879 - 1.8643 1.00 3424 212 0.2650 0.3044
REMARK 3 28 1.8643 - 1.8419 1.00 3468 202 0.2830 0.2832
REMARK 3 29 1.8419 - 1.8205 1.00 3469 179 0.3034 0.3424
REMARK 3 30 1.8205 - 1.8000 1.00 3509 197 0.3152 0.3219
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.64
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 4273
REMARK 3 ANGLE : 0.788 5825
REMARK 3 CHIRALITY : 0.042 650
REMARK 3 PLANARITY : 0.006 783
REMARK 3 DIHEDRAL : 18.581 1602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5435 -37.6201 25.1917
REMARK 3 T TENSOR
REMARK 3 T11: -0.3822 T22: 0.3898
REMARK 3 T33: 0.2311 T12: -0.3945
REMARK 3 T13: 0.1486 T23: 0.0962
REMARK 3 L TENSOR
REMARK 3 L11: 0.0187 L22: 0.0322
REMARK 3 L33: 0.0275 L12: 0.0246
REMARK 3 L13: -0.0276 L23: -0.0333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: -0.0144 S13: -0.0563
REMARK 3 S21: 0.0163 S22: 0.0652 S23: 0.0385
REMARK 3 S31: 0.0127 S32: -0.0696 S33: 0.0264
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1812 -27.6683 12.7579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1297 T22: 0.3041
REMARK 3 T33: 0.1529 T12: -0.0230
REMARK 3 T13: -0.0310 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.0696 L22: 0.0752
REMARK 3 L33: 0.0605 L12: -0.0202
REMARK 3 L13: -0.0387 L23: -0.0244
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.1561 S13: -0.0995
REMARK 3 S21: -0.0608 S22: -0.0842 S23: 0.0580
REMARK 3 S31: 0.0456 S32: -0.3641 S33: -0.0159
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0427 -12.5254 23.4895
REMARK 3 T TENSOR
REMARK 3 T11: 0.1532 T22: 0.0954
REMARK 3 T33: 0.1818 T12: 0.0638
REMARK 3 T13: -0.0210 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.6008 L22: 0.3245
REMARK 3 L33: 0.1613 L12: -0.0391
REMARK 3 L13: -0.2286 L23: -0.0312
REMARK 3 S TENSOR
REMARK 3 S11: -0.0521 S12: 0.0372 S13: 0.2229
REMARK 3 S21: -0.0159 S22: 0.0082 S23: -0.0547
REMARK 3 S31: -0.2471 S32: -0.3598 S33: 0.0282
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0830 -17.8025 29.6659
REMARK 3 T TENSOR
REMARK 3 T11: 0.0783 T22: 0.1926
REMARK 3 T33: 0.1144 T12: 0.0436
REMARK 3 T13: -0.0099 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.1608 L22: 0.2535
REMARK 3 L33: 0.1313 L12: 0.0312
REMARK 3 L13: -0.0619 L23: -0.2377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0636 S12: -0.0516 S13: 0.0897
REMARK 3 S21: -0.0667 S22: -0.0104 S23: -0.0046
REMARK 3 S31: -0.2435 S32: -0.4359 S33: 0.0659
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 94 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7635 -34.5936 24.1771
REMARK 3 T TENSOR
REMARK 3 T11: 0.1284 T22: 0.0974
REMARK 3 T33: 0.1255 T12: -0.0294
REMARK 3 T13: -0.0133 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.0900 L22: -0.0032
REMARK 3 L33: 0.0859 L12: -0.0144
REMARK 3 L13: -0.1272 L23: -0.0059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.0678 S13: 0.0344
REMARK 3 S21: -0.0186 S22: -0.0674 S23: -0.0573
REMARK 3 S31: 0.2277 S32: -0.0088 S33: -0.0011
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1966 -31.9109 27.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0932 T22: 0.1064
REMARK 3 T33: 0.0923 T12: 0.0106
REMARK 3 T13: -0.0238 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 0.0555 L22: 0.0700
REMARK 3 L33: 0.0899 L12: 0.0775
REMARK 3 L13: 0.0863 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.1159 S13: -0.0924
REMARK 3 S21: -0.0585 S22: 0.1620 S23: -0.1282
REMARK 3 S31: 0.0230 S32: 0.2487 S33: 0.0056
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3906 -39.0072 9.5509
REMARK 3 T TENSOR
REMARK 3 T11: 0.2026 T22: 0.1422
REMARK 3 T33: 0.1066 T12: 0.0047
REMARK 3 T13: -0.0325 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.0192 L22: 0.0103
REMARK 3 L33: 0.0219 L12: -0.0122
REMARK 3 L13: 0.0148 L23: 0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.2204 S13: -0.1758
REMARK 3 S21: 0.0118 S22: -0.0072 S23: -0.0591
REMARK 3 S31: -0.0048 S32: -0.0375 S33: -0.0027
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0529 -25.7846 7.2701
REMARK 3 T TENSOR
REMARK 3 T11: 0.1199 T22: 0.1727
REMARK 3 T33: 0.1484 T12: 0.0207
REMARK 3 T13: -0.0282 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0551 L22: -0.0018
REMARK 3 L33: -0.0088 L12: 0.0359
REMARK 3 L13: -0.0127 L23: 0.0062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0395 S12: -0.0368 S13: -0.1027
REMARK 3 S21: 0.0614 S22: 0.0076 S23: -0.0851
REMARK 3 S31: -0.0171 S32: 0.1818 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 22 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3855 -27.1585 19.6628
REMARK 3 T TENSOR
REMARK 3 T11: 0.2722 T22: 0.1790
REMARK 3 T33: 0.1968 T12: -0.0441
REMARK 3 T13: -0.0315 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.0059 L22: 0.0094
REMARK 3 L33: -0.0094 L12: 0.0070
REMARK 3 L13: -0.0065 L23: 0.0073
REMARK 3 S TENSOR
REMARK 3 S11: 0.1275 S12: -0.2189 S13: -0.0967
REMARK 3 S21: 0.0481 S22: -0.0833 S23: -0.0559
REMARK 3 S31: -0.0921 S32: -0.0743 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9674 -11.3926 3.0856
REMARK 3 T TENSOR
REMARK 3 T11: 0.1807 T22: 0.1051
REMARK 3 T33: 0.1435 T12: -0.0085
REMARK 3 T13: -0.0225 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.1243 L22: 0.0019
REMARK 3 L33: 0.0196 L12: 0.1603
REMARK 3 L13: -0.0031 L23: -0.1258
REMARK 3 S TENSOR
REMARK 3 S11: -0.0294 S12: -0.0591 S13: 0.1448
REMARK 3 S21: 0.1278 S22: -0.0084 S23: 0.0329
REMARK 3 S31: -0.3096 S32: 0.0290 S33: 0.0144
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9273 -23.3183 -0.1976
REMARK 3 T TENSOR
REMARK 3 T11: 0.1005 T22: 0.0871
REMARK 3 T33: 0.1018 T12: -0.0138
REMARK 3 T13: -0.0209 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.1596 L22: 0.3041
REMARK 3 L33: 0.3907 L12: -0.0954
REMARK 3 L13: 0.0810 L23: 0.0390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.0438 S13: 0.0381
REMARK 3 S21: 0.0120 S22: 0.0038 S23: -0.0279
REMARK 3 S31: 0.0703 S32: 0.0720 S33: 0.0423
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2315 -29.9298 -6.0249
REMARK 3 T TENSOR
REMARK 3 T11: 0.1315 T22: 0.0953
REMARK 3 T33: 0.1041 T12: -0.0385
REMARK 3 T13: -0.0160 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0486 L22: 0.0203
REMARK 3 L33: 0.0440 L12: -0.0326
REMARK 3 L13: 0.0435 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0643 S12: -0.0367 S13: -0.0597
REMARK 3 S21: -0.0098 S22: -0.0563 S23: 0.1362
REMARK 3 S31: 0.0155 S32: -0.1049 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 128 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3738 -37.8195 12.8719
REMARK 3 T TENSOR
REMARK 3 T11: 0.2152 T22: 0.1392
REMARK 3 T33: 0.1378 T12: -0.0604
REMARK 3 T13: -0.0559 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 0.0153 L22: 0.0827
REMARK 3 L33: 0.0327 L12: 0.0159
REMARK 3 L13: -0.0012 L23: -0.0366
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: -0.1931 S13: -0.2749
REMARK 3 S21: 0.0648 S22: 0.0713 S23: 0.0098
REMARK 3 S31: 0.0558 S32: -0.1797 S33: -0.0019
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 7 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0430 -29.5618 -10.7572
REMARK 3 T TENSOR
REMARK 3 T11: 0.1208 T22: 0.0818
REMARK 3 T33: 0.1143 T12: 0.0176
REMARK 3 T13: -0.0124 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.0906 L22: 0.1486
REMARK 3 L33: 0.0144 L12: 0.1040
REMARK 3 L13: 0.0753 L23: 0.0561
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: 0.0505 S13: -0.0342
REMARK 3 S21: -0.0464 S22: 0.0264 S23: -0.0356
REMARK 3 S31: 0.1160 S32: 0.0449 S33: 0.0253
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0884 -19.4157 9.0010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0938 T22: 0.0909
REMARK 3 T33: 0.0767 T12: -0.0134
REMARK 3 T13: 0.0047 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.1953 L22: 0.1111
REMARK 3 L33: 0.0631 L12: 0.1024
REMARK 3 L13: -0.0875 L23: -0.0469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: -0.0688 S13: 0.0558
REMARK 3 S21: 0.0160 S22: 0.0045 S23: 0.0522
REMARK 3 S31: 0.0033 S32: -0.1245 S33: -0.0046
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0528 -23.2237 1.6302
REMARK 3 T TENSOR
REMARK 3 T11: 0.0663 T22: 0.0665
REMARK 3 T33: 0.0757 T12: -0.0212
REMARK 3 T13: -0.0178 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0879 L22: 0.3222
REMARK 3 L33: 0.2373 L12: -0.0702
REMARK 3 L13: 0.0998 L23: -0.0581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: -0.0086 S13: -0.0050
REMARK 3 S21: 0.0216 S22: -0.0474 S23: -0.0430
REMARK 3 S31: 0.0465 S32: 0.0458 S33: -0.0878
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 115 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.7116 -10.1783 2.6213
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.2178
REMARK 3 T33: 0.2932 T12: -0.0472
REMARK 3 T13: -0.0458 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.0113 L22: 0.0138
REMARK 3 L33: 0.0081 L12: -0.0044
REMARK 3 L13: -0.0075 L23: -0.0018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.0805 S13: 0.1021
REMARK 3 S21: 0.1251 S22: 0.0813 S23: -0.1891
REMARK 3 S31: -0.1874 S32: 0.0066 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 134 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6680 -18.6319 -15.2569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1184 T22: 0.2415
REMARK 3 T33: 0.1182 T12: -0.0187
REMARK 3 T13: 0.0223 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: -0.0061 L22: 0.0085
REMARK 3 L33: 0.0073 L12: 0.0006
REMARK 3 L13: -0.0012 L23: -0.0078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0291 S12: 0.2860 S13: 0.1992
REMARK 3 S21: -0.0465 S22: 0.0893 S23: -0.0512
REMARK 3 S31: -0.1071 S32: 0.0564 S33: -0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 5 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9098 -31.6959 36.3797
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.1645
REMARK 3 T33: 0.1324 T12: -0.0541
REMARK 3 T13: 0.0046 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.0994 L22: 0.1581
REMARK 3 L33: 0.1150 L12: -0.1247
REMARK 3 L13: 0.1017 L23: -0.1202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: -0.2142 S13: -0.0489
REMARK 3 S21: 0.1492 S22: 0.0937 S23: 0.0710
REMARK 3 S31: 0.2045 S32: -0.1967 S33: 0.0565
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 34 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7291 -20.2215 17.1000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1090 T22: 0.0881
REMARK 3 T33: 0.1052 T12: 0.0008
REMARK 3 T13: 0.0006 T23: 0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.2441 L22: -0.0123
REMARK 3 L33: 0.1004 L12: -0.0516
REMARK 3 L13: -0.2162 L23: -0.0202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0489 S12: 0.0822 S13: 0.0574
REMARK 3 S21: -0.0179 S22: 0.0269 S23: -0.0610
REMARK 3 S31: 0.0069 S32: 0.0194 S33: 0.0291
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 71 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2176 -22.3941 25.2277
REMARK 3 T TENSOR
REMARK 3 T11: 0.0595 T22: 0.1677
REMARK 3 T33: 0.0917 T12: 0.0175
REMARK 3 T13: -0.0025 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.1751 L22: 0.1539
REMARK 3 L33: 0.2015 L12: -0.0173
REMARK 3 L13: 0.2322 L23: 0.0661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0605 S12: -0.0758 S13: 0.0076
REMARK 3 S21: -0.0268 S22: -0.0661 S23: 0.0127
REMARK 3 S31: -0.0088 S32: -0.2030 S33: 0.0159
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 134 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8274 -21.3659 41.3491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.4725
REMARK 3 T33: 0.1662 T12: 0.0841
REMARK 3 T13: 0.0656 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 0.0589 L22: -0.0005
REMARK 3 L33: 0.0372 L12: -0.0031
REMARK 3 L13: 0.0319 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0779 S12: -0.1064 S13: 0.1186
REMARK 3 S21: 0.0848 S22: -0.1100 S23: 0.1740
REMARK 3 S31: 0.1025 S32: -0.0583 S33: -0.0428
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 5I0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 43.531
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.88300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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: PDBID 2YFC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM ACETATE, PEG3350, PH 7.5,
REMARK 280 EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+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 74.86550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.03500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.86550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.03500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 PRO B 5
REMARK 465 CYS B 6
REMARK 465 PRO C 5
REMARK 465 CYS C 6
REMARK 465 PRO C 116
REMARK 465 ARG C 117
REMARK 465 ARG C 118
REMARK 465 ALA C 119
REMARK 465 ASP C 120
REMARK 465 GLY C 121
REMARK 465 PRO D 116
REMARK 465 ARG D 117
REMARK 465 ARG D 118
REMARK 465 ALA D 119
REMARK 465 ASP D 120
REMARK 465 GLY D 121
REMARK 465 LYS D 122
REMARK 465 GLN D 123
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 C 290 O HOH C 339 2.03
REMARK 500 O HOH C 228 O HOH C 245 2.08
REMARK 500 O HOH A 349 O HOH A 397 2.10
REMARK 500 O HOH D 205 O HOH D 288 2.11
REMARK 500 O HOH B 399 O HOH B 462 2.12
REMARK 500 O HOH C 364 O HOH C 385 2.13
REMARK 500 O HOH A 351 O HOH A 445 2.14
REMARK 500 OD2 ASP B 45 O HOH B 301 2.15
REMARK 500 O HOH D 274 O HOH D 303 2.15
REMARK 500 OD2 ASP B 56 O HOH B 302 2.16
REMARK 500 O HOH A 402 O HOH A 419 2.16
REMARK 500 O HOH C 202 O HOH C 204 2.16
REMARK 500 O HOH C 214 O HOH C 270 2.16
REMARK 500 O HOH B 374 O HOH B 429 2.16
REMARK 500 O HOH B 417 O HOH C 312 2.16
REMARK 500 O ALA B 23 O HOH B 303 2.17
REMARK 500 O HOH A 487 O HOH A 489 2.17
REMARK 500 O HOH A 483 O HOH C 373 2.17
REMARK 500 O HOH C 248 O HOH C 345 2.17
REMARK 500 N GLY C 128 O HOH C 201 2.18
REMARK 500 O GLY C 115 O HOH C 202 2.18
REMARK 500 O HOH B 476 O HOH C 382 2.19
REMARK 500 O HOH B 436 O HOH B 461 2.19
REMARK 500 O HOH B 361 O HOH B 447 2.19
REMARK 500 O HOH D 203 O HOH D 318 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 19 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
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 143 -64.68 -92.66
REMARK 500 THR B 25 82.40 -156.37
REMARK 500 ASP C 97 104.64 -57.12
REMARK 500 ASP C 133 75.22 -107.26
REMARK 500 THR D 25 74.74 -152.83
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 487 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 488 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 489 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH A 490 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH B 478 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B 479 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B 480 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B 481 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B 482 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH B 483 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH B 484 DISTANCE = 7.86 ANGSTROMS
REMARK 525 HOH B 485 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH C 403 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH C 404 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C 405 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH C 406 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH C 407 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH C 408 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH D 391 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH D 392 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH D 393 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH D 394 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH D 395 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH D 396 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH D 397 DISTANCE = 8.68 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UMP B 201
DBREF 5I0J A 5 144 UNP Q9RS96 Q9RS96_DEIRA 5 144
DBREF 5I0J B 5 144 UNP Q9RS96 Q9RS96_DEIRA 5 144
DBREF 5I0J C 5 144 UNP Q9RS96 Q9RS96_DEIRA 5 144
DBREF 5I0J D 5 144 UNP Q9RS96 Q9RS96_DEIRA 5 144
SEQADV 5I0J ALA A 47 UNP Q9RS96 GLU 47 ENGINEERED MUTATION
SEQADV 5I0J ALA B 47 UNP Q9RS96 GLU 47 ENGINEERED MUTATION
SEQADV 5I0J ALA C 47 UNP Q9RS96 GLU 47 ENGINEERED MUTATION
SEQADV 5I0J ALA D 47 UNP Q9RS96 GLU 47 ENGINEERED MUTATION
SEQRES 1 A 140 PRO CYS PRO PRO THR ASN ALA GLU ARG LEU HIS GLU PHE
SEQRES 2 A 140 HIS ARG ALA ILE GLY ALA ALA THR PRO GLU ARG PRO THR
SEQRES 3 A 140 PRO PRO PRO PRO GLU LEU LEU ARG LEU ARG GLN THR LEU
SEQRES 4 A 140 LEU ASP GLU ALA SER ALA GLU VAL ARG ALA GLU ILE ASP
SEQRES 5 A 140 HIS LEU LEU ALA ARG GLN ALA ALA GLY GLU ALA LEU SER
SEQRES 6 A 140 ALA GLY ASP LEU ALA PRO LEU ALA HIS GLU LEU ALA ASP
SEQRES 7 A 140 LEU LEU TYR VAL THR TYR GLY ALA LEU ASP GLN LEU GLY
SEQRES 8 A 140 ILE ASP ALA ASP ALA VAL PHE ALA GLU VAL HIS ARG ALA
SEQRES 9 A 140 ASN LEU SER LYS ALA SER GLY PRO ARG ARG ALA ASP GLY
SEQRES 10 A 140 LYS GLN LEU LYS PRO GLU GLY TRP ARG PRO ALA ASP VAL
SEQRES 11 A 140 ARG GLY VAL ILE GLU ARG LEU GLN HIS ALA
SEQRES 1 B 140 PRO CYS PRO PRO THR ASN ALA GLU ARG LEU HIS GLU PHE
SEQRES 2 B 140 HIS ARG ALA ILE GLY ALA ALA THR PRO GLU ARG PRO THR
SEQRES 3 B 140 PRO PRO PRO PRO GLU LEU LEU ARG LEU ARG GLN THR LEU
SEQRES 4 B 140 LEU ASP GLU ALA SER ALA GLU VAL ARG ALA GLU ILE ASP
SEQRES 5 B 140 HIS LEU LEU ALA ARG GLN ALA ALA GLY GLU ALA LEU SER
SEQRES 6 B 140 ALA GLY ASP LEU ALA PRO LEU ALA HIS GLU LEU ALA ASP
SEQRES 7 B 140 LEU LEU TYR VAL THR TYR GLY ALA LEU ASP GLN LEU GLY
SEQRES 8 B 140 ILE ASP ALA ASP ALA VAL PHE ALA GLU VAL HIS ARG ALA
SEQRES 9 B 140 ASN LEU SER LYS ALA SER GLY PRO ARG ARG ALA ASP GLY
SEQRES 10 B 140 LYS GLN LEU LYS PRO GLU GLY TRP ARG PRO ALA ASP VAL
SEQRES 11 B 140 ARG GLY VAL ILE GLU ARG LEU GLN HIS ALA
SEQRES 1 C 140 PRO CYS PRO PRO THR ASN ALA GLU ARG LEU HIS GLU PHE
SEQRES 2 C 140 HIS ARG ALA ILE GLY ALA ALA THR PRO GLU ARG PRO THR
SEQRES 3 C 140 PRO PRO PRO PRO GLU LEU LEU ARG LEU ARG GLN THR LEU
SEQRES 4 C 140 LEU ASP GLU ALA SER ALA GLU VAL ARG ALA GLU ILE ASP
SEQRES 5 C 140 HIS LEU LEU ALA ARG GLN ALA ALA GLY GLU ALA LEU SER
SEQRES 6 C 140 ALA GLY ASP LEU ALA PRO LEU ALA HIS GLU LEU ALA ASP
SEQRES 7 C 140 LEU LEU TYR VAL THR TYR GLY ALA LEU ASP GLN LEU GLY
SEQRES 8 C 140 ILE ASP ALA ASP ALA VAL PHE ALA GLU VAL HIS ARG ALA
SEQRES 9 C 140 ASN LEU SER LYS ALA SER GLY PRO ARG ARG ALA ASP GLY
SEQRES 10 C 140 LYS GLN LEU LYS PRO GLU GLY TRP ARG PRO ALA ASP VAL
SEQRES 11 C 140 ARG GLY VAL ILE GLU ARG LEU GLN HIS ALA
SEQRES 1 D 140 PRO CYS PRO PRO THR ASN ALA GLU ARG LEU HIS GLU PHE
SEQRES 2 D 140 HIS ARG ALA ILE GLY ALA ALA THR PRO GLU ARG PRO THR
SEQRES 3 D 140 PRO PRO PRO PRO GLU LEU LEU ARG LEU ARG GLN THR LEU
SEQRES 4 D 140 LEU ASP GLU ALA SER ALA GLU VAL ARG ALA GLU ILE ASP
SEQRES 5 D 140 HIS LEU LEU ALA ARG GLN ALA ALA GLY GLU ALA LEU SER
SEQRES 6 D 140 ALA GLY ASP LEU ALA PRO LEU ALA HIS GLU LEU ALA ASP
SEQRES 7 D 140 LEU LEU TYR VAL THR TYR GLY ALA LEU ASP GLN LEU GLY
SEQRES 8 D 140 ILE ASP ALA ASP ALA VAL PHE ALA GLU VAL HIS ARG ALA
SEQRES 9 D 140 ASN LEU SER LYS ALA SER GLY PRO ARG ARG ALA ASP GLY
SEQRES 10 D 140 LYS GLN LEU LYS PRO GLU GLY TRP ARG PRO ALA ASP VAL
SEQRES 11 D 140 ARG GLY VAL ILE GLU ARG LEU GLN HIS ALA
HET UMP A 201 20
HET UMP B 201 20
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETSYN UMP DUMP
FORMUL 5 UMP 2(C9 H13 N2 O8 P)
FORMUL 7 HOH *780(H2 O)
HELIX 1 AA1 THR A 9 ILE A 21 1 13
HELIX 2 AA2 PRO A 33 ALA A 64 1 32
HELIX 3 AA3 ALA A 70 ASP A 72 5 3
HELIX 4 AA4 LEU A 73 LEU A 94 1 22
HELIX 5 AA5 ASP A 97 SER A 111 1 15
HELIX 6 AA6 ASP A 133 ALA A 144 1 12
HELIX 7 AA7 THR B 9 GLY B 22 1 14
HELIX 8 AA8 PRO B 33 ALA B 64 1 32
HELIX 9 AA9 ALA B 70 ASP B 72 5 3
HELIX 10 AB1 LEU B 73 LEU B 94 1 22
HELIX 11 AB2 ASP B 97 SER B 111 1 15
HELIX 12 AB3 ASP B 133 HIS B 143 1 11
HELIX 13 AB4 THR C 9 GLY C 22 1 14
HELIX 14 AB5 PRO C 33 ALA C 64 1 32
HELIX 15 AB6 SER C 69 ASP C 72 5 4
HELIX 16 AB7 LEU C 73 LEU C 94 1 22
HELIX 17 AB8 ASP C 97 ALA C 113 1 17
HELIX 18 AB9 ASP C 133 GLN C 142 1 10
HELIX 19 AC1 THR D 9 GLY D 22 1 14
HELIX 20 AC2 PRO D 33 ALA D 64 1 32
HELIX 21 AC3 ALA D 70 ASP D 72 5 3
HELIX 22 AC4 LEU D 73 LEU D 94 1 22
HELIX 23 AC5 ASP D 97 SER D 114 1 18
HELIX 24 AC6 ASP D 133 HIS D 143 1 11
SSBOND 1 CYS A 6 CYS D 6 1555 1555 2.04
SITE 1 AC1 18 ASN A 109 LYS A 112 LYS A 122 GLN A 123
SITE 2 AC1 18 LYS A 125 HOH A 317 HOH A 323 HOH A 326
SITE 3 AC1 18 HOH A 346 HOH A 354 HOH A 374 HOH A 406
SITE 4 AC1 18 HOH A 415 PHE D 17 ASP D 82 TYR D 85
SITE 5 AC1 18 VAL D 86 HOH D 256
SITE 1 AC2 18 ASN B 109 LYS B 112 LYS B 122 GLN B 123
SITE 2 AC2 18 LYS B 125 HOH B 309 HOH B 313 HOH B 319
SITE 3 AC2 18 HOH B 332 HOH B 366 HOH B 379 HOH B 400
SITE 4 AC2 18 PHE C 17 ASP C 82 TYR C 85 VAL C 86
SITE 5 AC2 18 HOH C 228 HOH C 259
CRYST1 149.731 78.070 52.439 90.00 90.00 90.00 P 21 21 2 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 0.006679 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012809 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
