HEADER REPLICATION 06-JAN-15 4XHT
TITLE CRYSTAL STRUCTURE OF TIMELESS_PAB DOMAIN NATIVE FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TIMELESS HOMOLOG;
COMPND 3 CHAIN: A, C, B, D;
COMPND 4 FRAGMENT: PAB DOMAIN (UNP RESIDUES 1000-1098);
COMPND 5 SYNONYM: HTIM;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TIMELESS, TIM, TIM1, TIMELESS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA DAMAGE RESPONSE, REPLICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XIE,C.QIAN
REVDAT 3 08-NOV-23 4XHT 1 JRNL REMARK
REVDAT 2 14-OCT-15 4XHT 1 JRNL
REVDAT 1 30-SEP-15 4XHT 0
JRNL AUTH S.XIE,O.MORTUSEWICZ,H.T.MA,P.HERR,R.R.POON,T.HELLEDAY,C.QIAN
JRNL TITL TIMELESS INTERACTS WITH PARP-1 TO PROMOTE HOMOLOGOUS
JRNL TITL 2 RECOMBINATION REPAIR.
JRNL REF MOL.CELL V. 60 163 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26344098
JRNL DOI 10.1016/J.MOLCEL.2015.07.031
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 59606
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.350
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 26.3414 - 3.9758 0.89 3918 136 0.1735 0.1888
REMARK 3 2 3.9758 - 3.1574 0.99 4199 145 0.1673 0.1786
REMARK 3 3 3.1574 - 2.7587 1.00 4224 147 0.2145 0.2426
REMARK 3 4 2.7587 - 2.5067 1.00 4198 146 0.2009 0.2426
REMARK 3 5 2.5067 - 2.3272 1.00 4168 144 0.1905 0.2200
REMARK 3 6 2.3272 - 2.1900 1.00 4178 144 0.1787 0.1984
REMARK 3 7 2.1900 - 2.0804 1.00 4131 144 0.1779 0.1845
REMARK 3 8 2.0804 - 1.9899 1.00 4178 145 0.1867 0.2188
REMARK 3 9 1.9899 - 1.9133 1.00 4153 144 0.1835 0.1946
REMARK 3 10 1.9133 - 1.8473 1.00 4145 145 0.1859 0.2123
REMARK 3 11 1.8473 - 1.7895 1.00 4140 144 0.1874 0.1876
REMARK 3 12 1.7895 - 1.7384 1.00 4118 143 0.2027 0.2452
REMARK 3 13 1.7384 - 1.6926 1.00 4144 143 0.2108 0.2285
REMARK 3 14 1.6926 - 1.6514 0.90 3714 128 0.2260 0.2676
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.53
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 2981
REMARK 3 ANGLE : 1.090 4052
REMARK 3 CHIRALITY : 0.046 447
REMARK 3 PLANARITY : 0.007 550
REMARK 3 DIHEDRAL : 14.916 1147
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1005 THROUGH 1015 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1363 -31.9990 -27.8762
REMARK 3 T TENSOR
REMARK 3 T11: 0.6831 T22: 0.3484
REMARK 3 T33: 0.4371 T12: 0.1199
REMARK 3 T13: 0.0093 T23: -0.1534
REMARK 3 L TENSOR
REMARK 3 L11: 0.0695 L22: 0.3288
REMARK 3 L33: 0.3782 L12: -0.0562
REMARK 3 L13: 0.0959 L23: -0.2216
REMARK 3 S TENSOR
REMARK 3 S11: 0.2993 S12: 0.3339 S13: -0.3082
REMARK 3 S21: -0.8970 S22: 0.1488 S23: -0.0662
REMARK 3 S31: 0.9360 S32: 0.2924 S33: 0.2591
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 1016 THROUGH 1034 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9918 -15.4917 -24.5928
REMARK 3 T TENSOR
REMARK 3 T11: 0.2209 T22: 0.3155
REMARK 3 T33: 0.2685 T12: 0.0235
REMARK 3 T13: 0.0009 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.3091 L22: 0.0546
REMARK 3 L33: 0.3088 L12: -0.1022
REMARK 3 L13: 0.1146 L23: -0.1477
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 0.2318 S13: 0.1839
REMARK 3 S21: -0.0924 S22: -0.1129 S23: -0.0221
REMARK 3 S31: 0.0039 S32: 0.1893 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 1035 THROUGH 1048 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9308 -11.9145 -16.3621
REMARK 3 T TENSOR
REMARK 3 T11: 0.2960 T22: 0.2814
REMARK 3 T33: 0.3411 T12: -0.0108
REMARK 3 T13: 0.0134 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.0219 L22: 0.0912
REMARK 3 L33: 0.7014 L12: 0.1448
REMARK 3 L13: 0.0596 L23: 0.3750
REMARK 3 S TENSOR
REMARK 3 S11: -0.1704 S12: 0.0289 S13: 0.3985
REMARK 3 S21: -0.2810 S22: 0.1842 S23: 0.1749
REMARK 3 S31: -0.1880 S32: 0.2650 S33: -0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 1049 THROUGH 1057 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0151 -27.3220 -15.4156
REMARK 3 T TENSOR
REMARK 3 T11: 0.3808 T22: 0.2101
REMARK 3 T33: 0.3121 T12: -0.0001
REMARK 3 T13: 0.0345 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 0.1142 L22: 0.2046
REMARK 3 L33: 0.1201 L12: -0.0266
REMARK 3 L13: 0.1159 L23: -0.0055
REMARK 3 S TENSOR
REMARK 3 S11: -0.0133 S12: -0.0241 S13: 0.0743
REMARK 3 S21: 0.2463 S22: 0.0242 S23: 0.1486
REMARK 3 S31: 0.5785 S32: -0.0915 S33: 0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 1058 THROUGH 1067 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4001 -29.3815 -19.5315
REMARK 3 T TENSOR
REMARK 3 T11: 0.4261 T22: 0.2967
REMARK 3 T33: 0.3392 T12: 0.1565
REMARK 3 T13: 0.0012 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 0.7261 L22: 0.1057
REMARK 3 L33: 0.3377 L12: -0.0361
REMARK 3 L13: 0.4426 L23: -0.0662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: 0.3062 S13: -0.5378
REMARK 3 S21: -0.0474 S22: -0.0645 S23: -0.1842
REMARK 3 S31: 0.7912 S32: 0.9194 S33: 0.0017
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 1068 THROUGH 1087 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2790 -18.9889 -11.9401
REMARK 3 T TENSOR
REMARK 3 T11: 0.2416 T22: 0.3281
REMARK 3 T33: 0.2397 T12: 0.0411
REMARK 3 T13: 0.0145 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.2165 L22: 0.3553
REMARK 3 L33: 0.2358 L12: -0.1433
REMARK 3 L13: 0.1396 L23: 0.1881
REMARK 3 S TENSOR
REMARK 3 S11: 0.0838 S12: 0.0383 S13: -0.0681
REMARK 3 S21: 0.1735 S22: -0.0248 S23: -0.1109
REMARK 3 S31: -0.0258 S32: 0.4438 S33: 0.0002
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESID 1088 THROUGH 1098 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0612 -17.8458 -28.8332
REMARK 3 T TENSOR
REMARK 3 T11: 0.2216 T22: 0.4657
REMARK 3 T33: 0.2216 T12: 0.0425
REMARK 3 T13: 0.0329 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.0087 L22: 0.0709
REMARK 3 L33: 0.1743 L12: 0.0421
REMARK 3 L13: 0.0905 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0714 S12: 0.6052 S13: -0.1022
REMARK 3 S21: -0.1426 S22: 0.1169 S23: -0.3679
REMARK 3 S31: -0.0468 S32: 0.2882 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND (RESID 1005 THROUGH 1015 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2909 -9.1885 -12.7443
REMARK 3 T TENSOR
REMARK 3 T11: 0.3099 T22: 0.7800
REMARK 3 T33: 0.4570 T12: 0.0945
REMARK 3 T13: 0.1158 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 0.0665 L22: 0.3338
REMARK 3 L33: 0.0775 L12: -0.1142
REMARK 3 L13: -0.0039 L23: -0.1229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0935 S12: -0.9107 S13: -0.2632
REMARK 3 S21: -0.0447 S22: 0.0930 S23: 0.7684
REMARK 3 S31: -0.4411 S32: -0.3257 S33: -0.0024
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND (RESID 1016 THROUGH 1034 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4217 -8.2360 -14.2976
REMARK 3 T TENSOR
REMARK 3 T11: 0.2710 T22: 0.1993
REMARK 3 T33: 0.2570 T12: 0.0337
REMARK 3 T13: 0.0209 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2431 L22: 0.8467
REMARK 3 L33: 0.3740 L12: -0.4299
REMARK 3 L13: 0.2964 L23: -0.2431
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.1600 S13: -0.0475
REMARK 3 S21: 0.0635 S22: -0.0553 S23: -0.0545
REMARK 3 S31: -0.1070 S32: -0.2755 S33: -0.0012
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN C AND (RESID 1035 THROUGH 1048 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5765 -5.5675 -21.6186
REMARK 3 T TENSOR
REMARK 3 T11: 0.3127 T22: 0.2818
REMARK 3 T33: 0.3601 T12: 0.0194
REMARK 3 T13: -0.0217 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.2466 L22: 0.3154
REMARK 3 L33: 0.7440 L12: -0.1551
REMARK 3 L13: -0.3660 L23: -0.1259
REMARK 3 S TENSOR
REMARK 3 S11: 0.2563 S12: -0.3731 S13: -0.4238
REMARK 3 S21: 0.1106 S22: -0.2252 S23: -0.6361
REMARK 3 S31: -0.2629 S32: -0.0593 S33: -0.0008
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND (RESID 1049 THROUGH 1057 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0739 -12.7554 -24.7085
REMARK 3 T TENSOR
REMARK 3 T11: 0.2432 T22: 0.4337
REMARK 3 T33: 0.3181 T12: 0.0390
REMARK 3 T13: -0.0036 T23: -0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 0.1140 L22: 0.0728
REMARK 3 L33: 0.1093 L12: -0.0970
REMARK 3 L13: 0.0672 L23: -0.0426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: 0.3158 S13: -0.3727
REMARK 3 S21: 0.1368 S22: 0.0071 S23: 0.1189
REMARK 3 S31: -0.0526 S32: -0.9029 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND (RESID 1058 THROUGH 1067 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7239 -2.0875 -20.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.3135 T22: 0.4155
REMARK 3 T33: 0.3224 T12: 0.3730
REMARK 3 T13: 0.0569 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 0.1335 L22: 0.4359
REMARK 3 L33: 3.9242 L12: 0.1374
REMARK 3 L13: 0.4710 L23: -0.1707
REMARK 3 S TENSOR
REMARK 3 S11: 0.2487 S12: -0.0604 S13: 0.2529
REMARK 3 S21: 0.2672 S22: 0.1900 S23: 0.4828
REMARK 3 S31: -0.3908 S32: -2.3548 S33: 0.4896
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESID 1068 THROUGH 1087 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3426 -0.2071 -26.2655
REMARK 3 T TENSOR
REMARK 3 T11: 0.3781 T22: 0.2498
REMARK 3 T33: 0.2356 T12: 0.0725
REMARK 3 T13: -0.0066 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.2825 L22: 0.4009
REMARK 3 L33: 0.2939 L12: 0.1956
REMARK 3 L13: -0.3158 L23: 0.0214
REMARK 3 S TENSOR
REMARK 3 S11: -0.1374 S12: 0.1748 S13: 0.1027
REMARK 3 S21: -0.2050 S22: 0.2000 S23: -0.0588
REMARK 3 S31: -0.5523 S32: -0.0830 S33: 0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN C AND (RESID 1088 THROUGH 1098 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6590 -0.7723 -9.6145
REMARK 3 T TENSOR
REMARK 3 T11: 0.3983 T22: 0.2831
REMARK 3 T33: 0.2519 T12: 0.0591
REMARK 3 T13: -0.0023 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.5839 L22: 0.0295
REMARK 3 L33: 0.4999 L12: 0.1205
REMARK 3 L13: 0.4435 L23: 0.0419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1288 S12: -0.8660 S13: 0.2388
REMARK 3 S21: 0.3768 S22: -0.2774 S23: 0.1890
REMARK 3 S31: -0.1178 S32: -0.6481 S33: -0.0155
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN B AND (RESID 1004 THROUGH 1015 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9037 -12.8362 12.8531
REMARK 3 T TENSOR
REMARK 3 T11: 0.5787 T22: 0.3639
REMARK 3 T33: 0.2942 T12: -0.0263
REMARK 3 T13: -0.0549 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.0365 L22: 0.2998
REMARK 3 L33: 0.5029 L12: -0.0709
REMARK 3 L13: 0.0972 L23: -0.0641
REMARK 3 S TENSOR
REMARK 3 S11: 0.3561 S12: -0.7211 S13: 0.1476
REMARK 3 S21: 1.0650 S22: 0.2163 S23: -0.1614
REMARK 3 S31: 0.4934 S32: 0.6081 S33: 0.0107
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND (RESID 1016 THROUGH 1034 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2371 -12.4536 1.1170
REMARK 3 T TENSOR
REMARK 3 T11: 0.3132 T22: 0.2287
REMARK 3 T33: 0.3229 T12: 0.0087
REMARK 3 T13: 0.0570 T23: 0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 0.9346 L22: 0.5016
REMARK 3 L33: 0.3857 L12: 0.4373
REMARK 3 L13: -0.5668 L23: -0.0966
REMARK 3 S TENSOR
REMARK 3 S11: 0.1364 S12: 0.5426 S13: 0.5418
REMARK 3 S21: 0.0865 S22: 0.1722 S23: 0.3197
REMARK 3 S31: -0.3975 S32: -0.1708 S33: 0.0389
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND (RESID 1035 THROUGH 1048 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4584 -18.5656 -5.7775
REMARK 3 T TENSOR
REMARK 3 T11: 0.3041 T22: 0.2956
REMARK 3 T33: 0.2542 T12: -0.0631
REMARK 3 T13: 0.0021 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.1550 L22: 0.1986
REMARK 3 L33: 0.3813 L12: -0.2340
REMARK 3 L13: -0.1659 L23: 0.0541
REMARK 3 S TENSOR
REMARK 3 S11: -0.2837 S12: 0.2296 S13: -0.0110
REMARK 3 S21: -0.3411 S22: 0.1309 S23: 0.0374
REMARK 3 S31: 0.0061 S32: -0.3859 S33: -0.0007
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND (RESID 1049 THROUGH 1057 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7795 -15.8108 -0.4385
REMARK 3 T TENSOR
REMARK 3 T11: 0.3128 T22: 0.2784
REMARK 3 T33: 0.2825 T12: -0.0219
REMARK 3 T13: 0.0282 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.0578 L22: 0.1549
REMARK 3 L33: 0.1076 L12: -0.0330
REMARK 3 L13: 0.0034 L23: 0.0205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: -0.0811 S13: 0.0738
REMARK 3 S21: -0.0290 S22: 0.1599 S23: -0.3225
REMARK 3 S31: -0.0897 S32: 0.5092 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN B AND (RESID 1058 THROUGH 1067 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6477 -22.3325 8.1362
REMARK 3 T TENSOR
REMARK 3 T11: 0.4194 T22: 0.2491
REMARK 3 T33: 0.2811 T12: 0.0331
REMARK 3 T13: 0.0240 T23: 0.0646
REMARK 3 L TENSOR
REMARK 3 L11: 0.7025 L22: 0.0982
REMARK 3 L33: 0.1408 L12: 0.1666
REMARK 3 L13: 0.2265 L23: 0.1015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: -0.8363 S13: -0.2854
REMARK 3 S21: 0.4943 S22: -0.1836 S23: -0.0558
REMARK 3 S31: 0.4912 S32: 0.1316 S33: -0.0195
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN B AND (RESID 1068 THROUGH 1077 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0415 -29.1007 -3.9134
REMARK 3 T TENSOR
REMARK 3 T11: 0.5459 T22: 0.1929
REMARK 3 T33: 0.3824 T12: -0.0609
REMARK 3 T13: 0.1118 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 0.6560 L22: 1.3647
REMARK 3 L33: 2.5105 L12: -0.7157
REMARK 3 L13: -0.9603 L23: 1.5589
REMARK 3 S TENSOR
REMARK 3 S11: -0.2367 S12: 0.3583 S13: -0.6319
REMARK 3 S21: 0.1371 S22: -0.3907 S23: 0.1657
REMARK 3 S31: 0.7691 S32: -0.6161 S33: -0.0745
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN B AND (RESID 1078 THROUGH 1087 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1301 -24.0908 -1.3333
REMARK 3 T TENSOR
REMARK 3 T11: 0.3092 T22: 0.2507
REMARK 3 T33: 0.3042 T12: -0.0580
REMARK 3 T13: 0.0424 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: -0.0067 L22: 0.1531
REMARK 3 L33: 0.1109 L12: -0.0334
REMARK 3 L13: -0.0272 L23: -0.2056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0823 S12: 0.2432 S13: -0.1915
REMARK 3 S21: -0.0290 S22: 0.0489 S23: 0.2481
REMARK 3 S31: 0.3349 S32: -0.4265 S33: 0.0001
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN B AND (RESID 1088 THROUGH 1098 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4675 -15.8670 8.4357
REMARK 3 T TENSOR
REMARK 3 T11: 0.3961 T22: 0.3202
REMARK 3 T33: 0.3195 T12: -0.0079
REMARK 3 T13: 0.1207 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0767 L22: 0.1629
REMARK 3 L33: 0.1091 L12: -0.1163
REMARK 3 L13: -0.0065 L23: -0.0360
REMARK 3 S TENSOR
REMARK 3 S11: 0.1191 S12: -0.6999 S13: 0.2839
REMARK 3 S21: 0.5230 S22: -0.1111 S23: 0.5735
REMARK 3 S31: 0.2169 S32: -0.2654 S33: -0.0011
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN D AND (RESID 1006 THROUGH 1015 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7298 -10.5948 -50.8804
REMARK 3 T TENSOR
REMARK 3 T11: 0.3814 T22: 0.7770
REMARK 3 T33: 0.3376 T12: 0.0416
REMARK 3 T13: 0.0366 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.5258 L22: 3.5299
REMARK 3 L33: 0.7128 L12: 0.2246
REMARK 3 L13: 0.5810 L23: -0.0926
REMARK 3 S TENSOR
REMARK 3 S11: 0.0309 S12: 1.6702 S13: 0.0764
REMARK 3 S21: -0.9641 S22: 0.1540 S23: 0.1421
REMARK 3 S31: -0.4080 S32: -0.3561 S33: -0.0411
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN D AND (RESID 1016 THROUGH 1033 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7173 -22.8019 -40.3535
REMARK 3 T TENSOR
REMARK 3 T11: 0.2330 T22: 0.3487
REMARK 3 T33: 0.3843 T12: 0.0400
REMARK 3 T13: 0.0328 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 0.2438 L22: 0.1339
REMARK 3 L33: 0.4842 L12: -0.0393
REMARK 3 L13: 0.0684 L23: 0.0429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0414 S13: -0.4633
REMARK 3 S21: 0.0377 S22: -0.1010 S23: -0.0452
REMARK 3 S31: 0.1325 S32: 0.3360 S33: -0.0101
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN D AND (RESID 1034 THROUGH 1048 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9827 -21.7835 -34.6572
REMARK 3 T TENSOR
REMARK 3 T11: 0.3018 T22: 0.3001
REMARK 3 T33: 0.3727 T12: 0.0245
REMARK 3 T13: 0.0267 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.2458 L22: 0.2373
REMARK 3 L33: 0.5703 L12: 0.1432
REMARK 3 L13: 0.0407 L23: 0.2693
REMARK 3 S TENSOR
REMARK 3 S11: -0.0491 S12: -0.0236 S13: -0.4557
REMARK 3 S21: 0.2106 S22: -0.0820 S23: 0.2057
REMARK 3 S31: 0.3617 S32: 0.4078 S33: -0.0827
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN D AND (RESID 1049 THROUGH 1057 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3964 -7.7420 -38.0197
REMARK 3 T TENSOR
REMARK 3 T11: 0.2957 T22: 0.3680
REMARK 3 T33: 0.2432 T12: 0.0283
REMARK 3 T13: 0.0320 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.0937 L22: 0.0973
REMARK 3 L33: 0.1613 L12: -0.0504
REMARK 3 L13: -0.0487 L23: -0.1355
REMARK 3 S TENSOR
REMARK 3 S11: 0.2031 S12: -0.1940 S13: -0.0489
REMARK 3 S21: -0.0616 S22: 0.0301 S23: -0.0517
REMARK 3 S31: -0.5086 S32: -0.2042 S33: 0.0002
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN D AND (RESID 1058 THROUGH 1082 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7385 -14.0842 -40.8290
REMARK 3 T TENSOR
REMARK 3 T11: 0.1745 T22: 0.4192
REMARK 3 T33: 0.2497 T12: 0.0236
REMARK 3 T13: -0.0256 T23: -0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 0.4185 L22: 0.4571
REMARK 3 L33: 0.1839 L12: -0.3863
REMARK 3 L13: 0.1075 L23: 0.0331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: 0.3312 S13: 0.0321
REMARK 3 S21: -0.0716 S22: -0.1445 S23: 0.1575
REMARK 3 S31: -0.1933 S32: -0.4740 S33: 0.0004
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN D AND (RESID 1083 THROUGH 1098 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0331 -26.9987 -46.7888
REMARK 3 T TENSOR
REMARK 3 T11: 0.4616 T22: 0.4438
REMARK 3 T33: 0.5180 T12: -0.0426
REMARK 3 T13: 0.0714 T23: -0.1973
REMARK 3 L TENSOR
REMARK 3 L11: 0.0159 L22: 0.1570
REMARK 3 L33: 0.1693 L12: -0.0638
REMARK 3 L13: -0.0296 L23: 0.1220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0819 S12: 1.0150 S13: -0.4718
REMARK 3 S21: -0.6385 S22: -0.0966 S23: 0.2014
REMARK 3 S31: 0.2787 S32: -0.6119 S33: -0.0016
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 1732
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 1732
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 1732
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.06997
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59619
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 26.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.6500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.43100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4XHW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200MM SODIUM ACETATE, PH
REMARK 280 8.0, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 74.77700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.77700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.33400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.29800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.33400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.29800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 74.77700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.33400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.29800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.77700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.33400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.29800
REMARK 290 SMTRY3 8 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 996
REMARK 465 SER A 997
REMARK 465 HIS A 998
REMARK 465 MET A 999
REMARK 465 VAL A 1000
REMARK 465 LEU A 1001
REMARK 465 SER A 1002
REMARK 465 ASN A 1003
REMARK 465 GLU A 1004
REMARK 465 GLY C 996
REMARK 465 SER C 997
REMARK 465 HIS C 998
REMARK 465 MET C 999
REMARK 465 VAL C 1000
REMARK 465 LEU C 1001
REMARK 465 SER C 1002
REMARK 465 ASN C 1003
REMARK 465 GLU C 1004
REMARK 465 GLY B 996
REMARK 465 SER B 997
REMARK 465 HIS B 998
REMARK 465 MET B 999
REMARK 465 VAL B 1000
REMARK 465 LEU B 1001
REMARK 465 SER B 1002
REMARK 465 ASN B 1003
REMARK 465 ASP B 1036
REMARK 465 GLY B 1037
REMARK 465 CYS B 1038
REMARK 465 GLY D 996
REMARK 465 SER D 997
REMARK 465 HIS D 998
REMARK 465 MET D 999
REMARK 465 VAL D 1000
REMARK 465 LEU D 1001
REMARK 465 SER D 1002
REMARK 465 ASN D 1003
REMARK 465 GLU D 1004
REMARK 465 ASN D 1005
REMARK 465 GLU D 1035
REMARK 465 ASP D 1036
REMARK 465 GLY D 1037
REMARK 465 CYS D 1038
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A1005 CG OD1 ND2
REMARK 470 GLU A1035 CD OE1 OE2
REMARK 470 ASP A1036 CG OD1 OD2
REMARK 470 ASN C1005 CG OD1 ND2
REMARK 470 GLN C1008 CG CD OE1 NE2
REMARK 470 ASP C1036 CG OD1 OD2
REMARK 470 GLU C1049 CD OE1 OE2
REMARK 470 GLN C1076 CD OE1 NE2
REMARK 470 GLU B1004 CG CD OE1 OE2
REMARK 470 ASN B1005 CG OD1 ND2
REMARK 470 GLU B1035 CG CD OE1 OE2
REMARK 470 LEU D1006 CG CD1 CD2
REMARK 470 GLN D1062 CG CD OE1 NE2
REMARK 470 LYS D1066 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLN D 1008 O HOH D 1101 2.19
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 GLN A1076 -40.79 -130.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XHW RELATED DB: PDB
REMARK 900 RELATED ID: 4XHU RELATED DB: PDB
DBREF 4XHT A 1000 1098 UNP Q9UNS1 TIM_HUMAN 1000 1098
DBREF 4XHT C 1000 1098 UNP Q9UNS1 TIM_HUMAN 1000 1098
DBREF 4XHT B 1000 1098 UNP Q9UNS1 TIM_HUMAN 1000 1098
DBREF 4XHT D 1000 1098 UNP Q9UNS1 TIM_HUMAN 1000 1098
SEQADV 4XHT GLY A 996 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT SER A 997 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT HIS A 998 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT MET A 999 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT GLY C 996 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT SER C 997 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT HIS C 998 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT MET C 999 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT GLY B 996 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT SER B 997 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT HIS B 998 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT MET B 999 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT GLY D 996 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT SER D 997 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT HIS D 998 UNP Q9UNS1 EXPRESSION TAG
SEQADV 4XHT MET D 999 UNP Q9UNS1 EXPRESSION TAG
SEQRES 1 A 103 GLY SER HIS MET VAL LEU SER ASN GLU ASN LEU GLY GLN
SEQRES 2 A 103 SER LEU HIS GLN GLU GLY PHE SER ILE PRO LEU LEU TRP
SEQRES 3 A 103 LEU GLN ASN CYS LEU ILE ARG ALA ALA ASP ASP ARG GLU
SEQRES 4 A 103 GLU ASP GLY CYS SER GLN ALA VAL PRO LEU VAL PRO LEU
SEQRES 5 A 103 THR GLU GLU ASN GLU GLU ALA MET GLU ASN GLU GLN PHE
SEQRES 6 A 103 GLN GLN LEU LEU ARG LYS LEU GLY VAL ARG PRO PRO ALA
SEQRES 7 A 103 SER GLY GLN GLU THR PHE TRP ARG ILE PRO ALA LYS LEU
SEQRES 8 A 103 SER PRO THR GLN LEU ARG ARG ALA ALA ALA SER LEU
SEQRES 1 C 103 GLY SER HIS MET VAL LEU SER ASN GLU ASN LEU GLY GLN
SEQRES 2 C 103 SER LEU HIS GLN GLU GLY PHE SER ILE PRO LEU LEU TRP
SEQRES 3 C 103 LEU GLN ASN CYS LEU ILE ARG ALA ALA ASP ASP ARG GLU
SEQRES 4 C 103 GLU ASP GLY CYS SER GLN ALA VAL PRO LEU VAL PRO LEU
SEQRES 5 C 103 THR GLU GLU ASN GLU GLU ALA MET GLU ASN GLU GLN PHE
SEQRES 6 C 103 GLN GLN LEU LEU ARG LYS LEU GLY VAL ARG PRO PRO ALA
SEQRES 7 C 103 SER GLY GLN GLU THR PHE TRP ARG ILE PRO ALA LYS LEU
SEQRES 8 C 103 SER PRO THR GLN LEU ARG ARG ALA ALA ALA SER LEU
SEQRES 1 B 103 GLY SER HIS MET VAL LEU SER ASN GLU ASN LEU GLY GLN
SEQRES 2 B 103 SER LEU HIS GLN GLU GLY PHE SER ILE PRO LEU LEU TRP
SEQRES 3 B 103 LEU GLN ASN CYS LEU ILE ARG ALA ALA ASP ASP ARG GLU
SEQRES 4 B 103 GLU ASP GLY CYS SER GLN ALA VAL PRO LEU VAL PRO LEU
SEQRES 5 B 103 THR GLU GLU ASN GLU GLU ALA MET GLU ASN GLU GLN PHE
SEQRES 6 B 103 GLN GLN LEU LEU ARG LYS LEU GLY VAL ARG PRO PRO ALA
SEQRES 7 B 103 SER GLY GLN GLU THR PHE TRP ARG ILE PRO ALA LYS LEU
SEQRES 8 B 103 SER PRO THR GLN LEU ARG ARG ALA ALA ALA SER LEU
SEQRES 1 D 103 GLY SER HIS MET VAL LEU SER ASN GLU ASN LEU GLY GLN
SEQRES 2 D 103 SER LEU HIS GLN GLU GLY PHE SER ILE PRO LEU LEU TRP
SEQRES 3 D 103 LEU GLN ASN CYS LEU ILE ARG ALA ALA ASP ASP ARG GLU
SEQRES 4 D 103 GLU ASP GLY CYS SER GLN ALA VAL PRO LEU VAL PRO LEU
SEQRES 5 D 103 THR GLU GLU ASN GLU GLU ALA MET GLU ASN GLU GLN PHE
SEQRES 6 D 103 GLN GLN LEU LEU ARG LYS LEU GLY VAL ARG PRO PRO ALA
SEQRES 7 D 103 SER GLY GLN GLU THR PHE TRP ARG ILE PRO ALA LYS LEU
SEQRES 8 D 103 SER PRO THR GLN LEU ARG ARG ALA ALA ALA SER LEU
FORMUL 5 HOH *317(H2 O)
HELIX 1 AA1 GLY A 1007 GLU A 1013 1 7
HELIX 2 AA2 PHE A 1015 GLU A 1034 1 20
HELIX 3 AA3 THR A 1048 GLU A 1056 1 9
HELIX 4 AA4 ASN A 1057 GLY A 1068 1 12
HELIX 5 AA5 SER A 1087 SER A 1097 1 11
HELIX 6 AA6 GLY C 1007 GLU C 1013 1 7
HELIX 7 AA7 PHE C 1015 GLU C 1034 1 20
HELIX 8 AA8 THR C 1048 GLU C 1056 1 9
HELIX 9 AA9 ASN C 1057 GLY C 1068 1 12
HELIX 10 AB1 SER C 1087 SER C 1097 1 11
HELIX 11 AB2 ASN B 1005 GLU B 1013 1 9
HELIX 12 AB3 PHE B 1015 GLU B 1035 1 21
HELIX 13 AB4 THR B 1048 GLU B 1056 1 9
HELIX 14 AB5 ASN B 1057 GLY B 1068 1 12
HELIX 15 AB6 SER B 1087 SER B 1097 1 11
HELIX 16 AB7 GLY D 1007 GLU D 1013 1 7
HELIX 17 AB8 PHE D 1015 GLU D 1034 1 20
HELIX 18 AB9 THR D 1048 GLU D 1056 1 9
HELIX 19 AC1 ASN D 1057 GLY D 1068 1 12
HELIX 20 AC2 SER D 1087 SER D 1097 1 11
SHEET 1 AA1 2 VAL A1042 PRO A1043 0
SHEET 2 AA1 2 ARG A1081 ILE A1082 -1 O ILE A1082 N VAL A1042
SHEET 1 AA2 2 VAL C1042 PRO C1043 0
SHEET 2 AA2 2 ARG C1081 ILE C1082 -1 O ILE C1082 N VAL C1042
SHEET 1 AA3 2 VAL B1042 PRO B1043 0
SHEET 2 AA3 2 ARG B1081 ILE B1082 -1 O ILE B1082 N VAL B1042
SHEET 1 AA4 2 VAL D1042 PRO D1043 0
SHEET 2 AA4 2 ARG D1081 ILE D1082 -1 O ILE D1082 N VAL D1042
SSBOND 1 CYS A 1038 CYS C 1038 1555 1555 2.04
CRYST1 66.668 100.596 149.554 90.00 90.00 90.00 C 2 2 21 32
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009941 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006687 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
