HEADER ISOMERASE/DNA 20-DEC-09 3L4J
TITLE TOPOISOMERASE II-DNA CLEAVAGE COMPLEX, APO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 421-1177;
COMPND 5 SYNONYM: DNA TOPOISOMERASE II;
COMPND 6 EC: 5.99.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(P*CP*CP*TP*AP*CP*TP*GP*CP*TP*AP*C)-3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*GP*TP*AP*GP*CP*AP*GP*TP*AP*GP*G)-
COMPND 14 3');
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: DNA (5'-D(P*GP*GP*AP*TP*GP*AP*CP*GP*AP*TP*)-3');
COMPND 19 CHAIN: D;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*AP*AP*TP*CP*GP*TP*CP*AP*TP*CP*C)-
COMPND 23 3');
COMPND 24 CHAIN: E;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: N2244, TOP2, TOR3, YNL088W;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BCY123;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGAL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 MOL_ID: 4;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 MOL_ID: 5;
SOURCE 18 SYNTHETIC: YES
KEYWDS TOPOISOMERASE, PROTEIN-DNA COMPLEX, COVALENTLY LINKED COMPLEX, DNA
KEYWDS 2 SUPERCOILING, DNA REPLICATION, ATP-BINDING, DNA-BINDING, ISOMERASE,
KEYWDS 3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, ISOMERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.SCHMIDT,A.B.BURGIN,J.E.DEWEESE,N.OSHEROFF,J.M.BERGER
REVDAT 7 22-NOV-23 3L4J 1 REMARK
REVDAT 6 06-SEP-23 3L4J 1 REMARK
REVDAT 5 31-JUL-19 3L4J 1 LINK
REVDAT 4 13-SEP-17 3L4J 1 REMARK
REVDAT 3 16-JUN-10 3L4J 1 JRNL
REVDAT 2 09-JUN-10 3L4J 1 JRNL
REVDAT 1 26-MAY-10 3L4J 0
JRNL AUTH B.H.SCHMIDT,A.B.BURGIN,J.E.DEWEESE,N.OSHEROFF,J.M.BERGER
JRNL TITL A NOVEL AND UNIFIED TWO-METAL MECHANISM FOR DNA CLEAVAGE BY
JRNL TITL 2 TYPE II AND IA TOPOISOMERASES.
JRNL REF NATURE V. 465 641 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20485342
JRNL DOI 10.1038/NATURE08974
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 33330
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 1630
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 43.0289 - 5.6876 1.00 2833 142 0.2014 0.2120
REMARK 3 2 5.6876 - 4.5160 1.00 2696 129 0.1934 0.1809
REMARK 3 3 4.5160 - 3.9456 1.00 2678 145 0.1818 0.2226
REMARK 3 4 3.9456 - 3.5850 1.00 2608 147 0.2186 0.2143
REMARK 3 5 3.5850 - 3.3282 1.00 2643 146 0.2591 0.2552
REMARK 3 6 3.3282 - 3.1320 1.00 2620 140 0.2787 0.3086
REMARK 3 7 3.1320 - 2.9752 1.00 2634 117 0.3019 0.3343
REMARK 3 8 2.9752 - 2.8457 1.00 2628 137 0.2999 0.3935
REMARK 3 9 2.8457 - 2.7362 1.00 2609 132 0.3084 0.3653
REMARK 3 10 2.7362 - 2.6418 1.00 2612 135 0.3094 0.3671
REMARK 3 11 2.6418 - 2.5592 1.00 2617 132 0.3245 0.3721
REMARK 3 12 2.5592 - 2.4800 0.97 2522 128 0.3210 0.4057
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 : 0.30
REMARK 3 B_SOL : 40.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.77900
REMARK 3 B22 (A**2) : -2.56790
REMARK 3 B33 (A**2) : 8.34690
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 7268
REMARK 3 ANGLE : 1.216 10022
REMARK 3 CHIRALITY : 0.097 1079
REMARK 3 PLANARITY : 0.008 1096
REMARK 3 DIHEDRAL : 19.282 2797
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 421:506)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9450 -32.3326 5.3623
REMARK 3 T TENSOR
REMARK 3 T11: 0.6277 T22: 0.4189
REMARK 3 T33: 0.7269 T12: -0.0374
REMARK 3 T13: 0.2626 T23: 0.1101
REMARK 3 L TENSOR
REMARK 3 L11: 0.1545 L22: 0.7977
REMARK 3 L33: 0.6517 L12: 0.0837
REMARK 3 L13: 0.2857 L23: -0.2323
REMARK 3 S TENSOR
REMARK 3 S11: -0.3584 S12: -0.3824 S13: -0.6374
REMARK 3 S21: 0.2437 S22: -0.1359 S23: -0.3910
REMARK 3 S31: 0.9415 S32: 0.1256 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 507:563)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4580 -29.2392 -1.7062
REMARK 3 T TENSOR
REMARK 3 T11: 0.4947 T22: 0.5823
REMARK 3 T33: 0.7124 T12: -0.1846
REMARK 3 T13: 0.2484 T23: -0.1374
REMARK 3 L TENSOR
REMARK 3 L11: 0.3806 L22: 0.1023
REMARK 3 L33: 0.9408 L12: -0.1750
REMARK 3 L13: 0.1780 L23: -0.0727
REMARK 3 S TENSOR
REMARK 3 S11: -0.5263 S12: 0.1915 S13: -0.8296
REMARK 3 S21: 0.0949 S22: -0.1520 S23: -0.1085
REMARK 3 S31: 0.5697 S32: -0.7785 S33: -0.0035
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 564:609)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2165 1.5941 1.4028
REMARK 3 T TENSOR
REMARK 3 T11: 1.5959 T22: 1.1217
REMARK 3 T33: 1.2328 T12: -0.0403
REMARK 3 T13: 0.3327 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.1602 L22: 0.1160
REMARK 3 L33: 0.1506 L12: 0.1292
REMARK 3 L13: -0.0198 L23: 0.0367
REMARK 3 S TENSOR
REMARK 3 S11: 0.7918 S12: 0.1990 S13: 1.1832
REMARK 3 S21: 0.2025 S22: 0.1995 S23: 0.7348
REMARK 3 S31: -1.7012 S32: -0.0551 S33: 0.0054
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 610:680)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0263 -19.4832 -8.3922
REMARK 3 T TENSOR
REMARK 3 T11: 0.3406 T22: 0.7065
REMARK 3 T33: 0.5711 T12: -0.0947
REMARK 3 T13: 0.0779 T23: -0.2375
REMARK 3 L TENSOR
REMARK 3 L11: 1.0668 L22: 0.7217
REMARK 3 L33: 0.8957 L12: -0.2762
REMARK 3 L13: -0.0886 L23: -0.7383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0582 S12: 0.2316 S13: -0.1724
REMARK 3 S21: 0.0644 S22: -0.2120 S23: 0.4405
REMARK 3 S31: -0.3443 S32: -1.0805 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 681:988)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8433 -14.7667 -24.6190
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.2195
REMARK 3 T33: 0.1885 T12: -0.0104
REMARK 3 T13: 0.0349 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 0.8591 L22: 1.1725
REMARK 3 L33: 0.8059 L12: -0.1462
REMARK 3 L13: -0.5101 L23: -0.0158
REMARK 3 S TENSOR
REMARK 3 S11: -0.1333 S12: 0.0125 S13: -0.0875
REMARK 3 S21: -0.0412 S22: 0.0002 S23: 0.0161
REMARK 3 S31: 0.0992 S32: -0.0215 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 989:1035)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3262 19.5797 -24.2233
REMARK 3 T TENSOR
REMARK 3 T11: 0.4177 T22: 0.4174
REMARK 3 T33: 0.3616 T12: -0.0063
REMARK 3 T13: -0.0958 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.3343 L22: 0.4428
REMARK 3 L33: 0.1851 L12: -0.3723
REMARK 3 L13: 0.2431 L23: -0.2945
REMARK 3 S TENSOR
REMARK 3 S11: -0.1022 S12: 0.2173 S13: 0.2341
REMARK 3 S21: -0.0627 S22: -0.2708 S23: 0.3649
REMARK 3 S31: -0.1234 S32: -0.0087 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1036:1069)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0315 37.3389 -6.1671
REMARK 3 T TENSOR
REMARK 3 T11: 0.7511 T22: 0.4525
REMARK 3 T33: 0.6816 T12: 0.0886
REMARK 3 T13: -0.2933 T23: -0.1277
REMARK 3 L TENSOR
REMARK 3 L11: 0.3222 L22: 0.0589
REMARK 3 L33: 0.5305 L12: -0.0865
REMARK 3 L13: -0.3514 L23: 0.1708
REMARK 3 S TENSOR
REMARK 3 S11: -0.4064 S12: -0.2520 S13: 0.3152
REMARK 3 S21: 0.3229 S22: -0.0030 S23: 0.6733
REMARK 3 S31: -0.3263 S32: -0.3101 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1107:1124)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2084 31.1294 -4.9761
REMARK 3 T TENSOR
REMARK 3 T11: 0.6536 T22: 0.3743
REMARK 3 T33: 0.4830 T12: -0.0812
REMARK 3 T13: -0.2027 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 0.0029 L22: 0.0705
REMARK 3 L33: 0.3784 L12: -0.0117
REMARK 3 L13: 0.0301 L23: -0.1687
REMARK 3 S TENSOR
REMARK 3 S11: -0.1683 S12: -0.3639 S13: -0.2323
REMARK 3 S21: 0.2937 S22: -0.2377 S23: -0.0009
REMARK 3 S31: -0.3625 S32: -0.0829 S33: 0.0028
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1125:1150)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4754 30.9880 -21.0912
REMARK 3 T TENSOR
REMARK 3 T11: 0.6018 T22: 0.5030
REMARK 3 T33: 0.5532 T12: -0.0564
REMARK 3 T13: -0.1125 T23: 0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 0.0430 L22: 0.3419
REMARK 3 L33: 0.2465 L12: -0.0633
REMARK 3 L13: 0.1051 L23: -0.2672
REMARK 3 S TENSOR
REMARK 3 S11: -0.1396 S12: 0.0180 S13: 0.1138
REMARK 3 S21: 0.2835 S22: 0.0504 S23: -0.6001
REMARK 3 S31: -0.2990 S32: 0.5716 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1151:1177)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4741 2.7732 -30.4148
REMARK 3 T TENSOR
REMARK 3 T11: 0.3541 T22: 0.3715
REMARK 3 T33: 0.3771 T12: -0.0438
REMARK 3 T13: 0.0749 T23: -0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 0.2423 L22: 0.3000
REMARK 3 L33: 0.1181 L12: 0.1925
REMARK 3 L13: 0.1782 L23: 0.1719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0712 S12: 0.0996 S13: -0.0846
REMARK 3 S21: -0.3121 S22: -0.0036 S23: -0.7056
REMARK 3 S31: -0.1126 S32: 0.4494 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7450 -28.9253 -19.7904
REMARK 3 T TENSOR
REMARK 3 T11: 0.8463 T22: 0.2327
REMARK 3 T33: 1.0966 T12: -0.1282
REMARK 3 T13: 0.2615 T23: -0.3867
REMARK 3 L TENSOR
REMARK 3 L11: 0.5500 L22: 0.1019
REMARK 3 L33: 0.0540 L12: -0.0016
REMARK 3 L13: 0.0310 L23: -0.0351
REMARK 3 S TENSOR
REMARK 3 S11: -0.5875 S12: -0.2115 S13: -0.8344
REMARK 3 S21: -0.2983 S22: 0.0013 S23: -0.0373
REMARK 3 S31: 0.7926 S32: -0.2577 S33: -0.0235
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4294 -29.2148 -17.0105
REMARK 3 T TENSOR
REMARK 3 T11: 0.3260 T22: 1.1728
REMARK 3 T33: 0.5176 T12: -0.0633
REMARK 3 T13: 0.0833 T23: 0.1285
REMARK 3 L TENSOR
REMARK 3 L11: 0.5071 L22: 1.0199
REMARK 3 L33: 0.6603 L12: -0.5556
REMARK 3 L13: 0.1941 L23: -0.7160
REMARK 3 S TENSOR
REMARK 3 S11: 0.1977 S12: 0.0031 S13: -0.7905
REMARK 3 S21: -0.2067 S22: -0.4814 S23: -0.1266
REMARK 3 S31: 0.2878 S32: 1.9136 S33: 0.0405
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6406 -29.1328 -19.8773
REMARK 3 T TENSOR
REMARK 3 T11: 0.4677 T22: 0.4976
REMARK 3 T33: 0.3141 T12: -0.0482
REMARK 3 T13: 0.1522 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 1.8236 L22: 0.1768
REMARK 3 L33: 2.1669 L12: 0.0220
REMARK 3 L13: -0.4757 L23: -0.6043
REMARK 3 S TENSOR
REMARK 3 S11: -0.2904 S12: 0.2318 S13: -1.1130
REMARK 3 S21: -0.2041 S22: -0.1236 S23: 0.1143
REMARK 3 S31: 1.2642 S32: -0.4193 S33: -0.0186
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5191 -28.9667 -16.7402
REMARK 3 T TENSOR
REMARK 3 T11: 0.4720 T22: 0.3238
REMARK 3 T33: 0.8166 T12: 0.2000
REMARK 3 T13: 0.2649 T23: -0.5399
REMARK 3 L TENSOR
REMARK 3 L11: 0.7725 L22: 0.3572
REMARK 3 L33: 0.6225 L12: -0.4217
REMARK 3 L13: 0.6857 L23: -0.3816
REMARK 3 S TENSOR
REMARK 3 S11: 0.6415 S12: 0.4139 S13: -0.5204
REMARK 3 S21: -0.4034 S22: -0.1090 S23: -0.1021
REMARK 3 S31: -0.1080 S32: 0.6178 S33: -0.5709
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 3L4J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33390
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.64200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2RGR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% 1,4-BUTANEDIOL, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 43.02250
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.36600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.02250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.36600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CZ ARG A1120 LIES ON A SPECIAL POSITION.
REMARK 375 NH2 ARG A1120 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 181 LIES ON A SPECIAL POSITION.
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 A 1071
REMARK 465 ASN A 1072
REMARK 465 ASP A 1073
REMARK 465 GLU A 1074
REMARK 465 ILE A 1075
REMARK 465 ALA A 1076
REMARK 465 GLU A 1077
REMARK 465 GLN A 1078
REMARK 465 ILE A 1079
REMARK 465 ASN A 1080
REMARK 465 ASP A 1081
REMARK 465 VAL A 1082
REMARK 465 LYS A 1083
REMARK 465 GLY A 1084
REMARK 465 ALA A 1085
REMARK 465 THR A 1086
REMARK 465 SER A 1087
REMARK 465 ASP A 1088
REMARK 465 GLU A 1089
REMARK 465 GLU A 1090
REMARK 465 ASP A 1091
REMARK 465 GLU A 1092
REMARK 465 GLU A 1093
REMARK 465 SER A 1094
REMARK 465 SER A 1095
REMARK 465 HIS A 1096
REMARK 465 GLU A 1097
REMARK 465 ASP A 1098
REMARK 465 THR A 1099
REMARK 465 GLU A 1100
REMARK 465 ASN A 1101
REMARK 465 VAL A 1102
REMARK 465 ILE A 1103
REMARK 465 ASN A 1104
REMARK 465 GLY A 1105
REMARK 465 PRO A 1106
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 DC C 1 O5'
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 THR A 437 N GLU A 439 2.05
REMARK 500 O SER A 592 NE1 TRP A 597 2.13
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 PRO A 571 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 GLY A1069 N - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG A1120 NH1 - CZ - NH2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A1120 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 DT B 9 C3' - O3' - P ANGL. DEV. = 7.7 DEGREES
REMARK 500 DA B 10 O4' - C4' - C3' ANGL. DEV. = -2.8 DEGREES
REMARK 500 DC C 1 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC C 1 C3' - O3' - P ANGL. DEV. = -8.4 DEGREES
REMARK 500 DG D 2 O3' - P - OP2 ANGL. DEV. = -19.9 DEGREES
REMARK 500 DG D 2 O3' - P - OP1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 DA D 6 O4' - C4' - C3' ANGL. DEV. = -2.5 DEGREES
REMARK 500 DT D 10 O4' - C4' - C3' ANGL. DEV. = -3.5 DEGREES
REMARK 500 DT D 10 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG E 2 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC E 11 O4' - C1' - N1 ANGL. DEV. = 2.0 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 LYS A 438 -17.50 -47.43
REMARK 500 GLU A 483 8.63 93.37
REMARK 500 LYS A 508 -134.27 60.11
REMARK 500 PRO A 571 -90.99 -113.14
REMARK 500 GLU A 591 -29.76 -147.19
REMARK 500 THR A 607 -61.19 -141.38
REMARK 500 SER A 608 138.32 -31.91
REMARK 500 TYR A 657 141.66 -38.65
REMARK 500 LEU A 667 -39.40 -131.70
REMARK 500 GLU A 679 -53.61 -121.16
REMARK 500 LEU A 715 63.61 -104.05
REMARK 500 SER A 755 -92.49 -102.31
REMARK 500 VAL A 813 -155.53 -133.53
REMARK 500 ASP A 938 -88.75 -112.18
REMARK 500 ASN A1042 -152.64 63.90
REMARK 500 LYS A1043 79.25 63.59
REMARK 500 ARG A1045 -39.89 -35.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSP D 11
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L4K RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH ZINC IONS SOAKED IN
DBREF 3L4J A 421 1177 UNP P06786 TOP2_YEAST 421 1177
DBREF 3L4J B 1 11 PDB 3L4J 3L4J 1 11
DBREF 3L4J C 1 15 PDB 3L4J 3L4J 1 15
DBREF 3L4J D 1 10 PDB 3L4J 3L4J 1 10
DBREF 3L4J E 1 15 PDB 3L4J 3L4J 1 15
SEQADV 3L4J PTR A 782 UNP P06786 TYR 782 MICROHETEROGENEITY
SEQRES 1 A 757 SER ARG ILE THR ASN TYR PRO LYS LEU GLU ASP ALA ASN
SEQRES 2 A 757 LYS ALA GLY THR LYS GLU GLY TYR LYS CYS THR LEU VAL
SEQRES 3 A 757 LEU THR GLU GLY ASP SER ALA LEU SER LEU ALA VAL ALA
SEQRES 4 A 757 GLY LEU ALA VAL VAL GLY ARG ASP TYR TYR GLY CYS TYR
SEQRES 5 A 757 PRO LEU ARG GLY LYS MET LEU ASN VAL ARG GLU ALA SER
SEQRES 6 A 757 ALA ASP GLN ILE LEU LYS ASN ALA GLU ILE GLN ALA ILE
SEQRES 7 A 757 LYS LYS ILE MET GLY LEU GLN HIS ARG LYS LYS TYR GLU
SEQRES 8 A 757 ASP THR LYS SER LEU ARG TYR GLY HIS LEU MET ILE MET
SEQRES 9 A 757 THR ASP GLN ASP HIS ASP GLY SER HIS ILE LYS GLY LEU
SEQRES 10 A 757 ILE ILE ASN PHE LEU GLU SER SER PHE PRO GLY LEU LEU
SEQRES 11 A 757 ASP ILE GLN GLY PHE LEU LEU GLU PHE ILE THR PRO ILE
SEQRES 12 A 757 ILE LYS VAL SER ILE THR LYS PRO THR LYS ASN THR ILE
SEQRES 13 A 757 ALA PHE TYR ASN MET PRO ASP TYR GLU LYS TRP ARG GLU
SEQRES 14 A 757 GLU GLU SER HIS LYS PHE THR TRP LYS GLN LYS TYR TYR
SEQRES 15 A 757 LYS GLY LEU GLY THR SER LEU ALA GLN GLU VAL ARG GLU
SEQRES 16 A 757 TYR PHE SER ASN LEU ASP ARG HIS LEU LYS ILE PHE HIS
SEQRES 17 A 757 SER LEU GLN GLY ASN ASP LYS ASP TYR ILE ASP LEU ALA
SEQRES 18 A 757 PHE SER LYS LYS LYS ALA ASP ASP ARG LYS GLU TRP LEU
SEQRES 19 A 757 ARG GLN TYR GLU PRO GLY THR VAL LEU ASP PRO THR LEU
SEQRES 20 A 757 LYS GLU ILE PRO ILE SER ASP PHE ILE ASN LYS GLU LEU
SEQRES 21 A 757 ILE LEU PHE SER LEU ALA ASP ASN ILE ARG SER ILE PRO
SEQRES 22 A 757 ASN VAL LEU ASP GLY PHE LYS PRO GLY GLN ARG LYS VAL
SEQRES 23 A 757 LEU TYR GLY CYS PHE LYS LYS ASN LEU LYS SER GLU LEU
SEQRES 24 A 757 LYS VAL ALA GLN LEU ALA PRO TYR VAL SER GLU CYS THR
SEQRES 25 A 757 ALA TYR HIS HIS GLY GLU GLN SER LEU ALA GLN THR ILE
SEQRES 26 A 757 ILE GLY LEU ALA GLN ASN PHE VAL GLY SER ASN ASN ILE
SEQRES 27 A 757 TYR LEU LEU LEU PRO ASN GLY ALA PHE GLY THR ARG ALA
SEQRES 28 A 757 THR GLY GLY LYS ASP ALA ALA ALA ALA ARG PTR ILE TYR
SEQRES 29 A 757 THR GLU LEU ASN LYS LEU THR ARG LYS ILE PHE HIS PRO
SEQRES 30 A 757 ALA ASP ASP PRO LEU TYR LYS TYR ILE GLN GLU ASP GLU
SEQRES 31 A 757 LYS THR VAL GLU PRO GLU TRP TYR LEU PRO ILE LEU PRO
SEQRES 32 A 757 MET ILE LEU VAL ASN GLY ALA GLU GLY ILE GLY THR GLY
SEQRES 33 A 757 TRP SER THR TYR ILE PRO PRO PHE ASN PRO LEU GLU ILE
SEQRES 34 A 757 ILE LYS ASN ILE ARG HIS LEU MET ASN ASP GLU GLU LEU
SEQRES 35 A 757 GLU GLN MET HIS PRO TRP PHE ARG GLY TRP THR GLY THR
SEQRES 36 A 757 ILE GLU GLU ILE GLU PRO LEU ARG TYR ARG MET TYR GLY
SEQRES 37 A 757 ARG ILE GLU GLN ILE GLY ASP ASN VAL LEU GLU ILE THR
SEQRES 38 A 757 GLU LEU PRO ALA ARG THR TRP THR SER THR ILE LYS GLU
SEQRES 39 A 757 TYR LEU LEU LEU GLY LEU SER GLY ASN ASP LYS ILE LYS
SEQRES 40 A 757 PRO TRP ILE LYS ASP MET GLU GLU GLN HIS ASP ASP ASN
SEQRES 41 A 757 ILE LYS PHE ILE ILE THR LEU SER PRO GLU GLU MET ALA
SEQRES 42 A 757 LYS THR ARG LYS ILE GLY PHE TYR GLU ARG PHE LYS LEU
SEQRES 43 A 757 ILE SER PRO ILE SER LEU MET ASN MET VAL ALA PHE ASP
SEQRES 44 A 757 PRO HIS GLY LYS ILE LYS LYS TYR ASN SER VAL ASN GLU
SEQRES 45 A 757 ILE LEU SER GLU PHE TYR TYR VAL ARG LEU GLU TYR TYR
SEQRES 46 A 757 GLN LYS ARG LYS ASP HIS MET SER GLU ARG LEU GLN TRP
SEQRES 47 A 757 GLU VAL GLU LYS TYR SER PHE GLN VAL LYS PHE ILE LYS
SEQRES 48 A 757 MET ILE ILE GLU LYS GLU LEU THR VAL THR ASN LYS PRO
SEQRES 49 A 757 ARG ASN ALA ILE ILE GLN GLU LEU GLU ASN LEU GLY PHE
SEQRES 50 A 757 PRO ARG PHE ASN LYS GLU GLY LYS PRO TYR TYR GLY SER
SEQRES 51 A 757 PRO ASN ASP GLU ILE ALA GLU GLN ILE ASN ASP VAL LYS
SEQRES 52 A 757 GLY ALA THR SER ASP GLU GLU ASP GLU GLU SER SER HIS
SEQRES 53 A 757 GLU ASP THR GLU ASN VAL ILE ASN GLY PRO GLU GLU LEU
SEQRES 54 A 757 TYR GLY THR TYR GLU TYR LEU LEU GLY MET ARG ILE TRP
SEQRES 55 A 757 SER LEU THR LYS GLU ARG TYR GLN LYS LEU LEU LYS GLN
SEQRES 56 A 757 LYS GLN GLU LYS GLU THR GLU LEU GLU ASN LEU LEU LYS
SEQRES 57 A 757 LEU SER ALA LYS ASP ILE TRP ASN THR ASP LEU LYS ALA
SEQRES 58 A 757 PHE GLU VAL GLY TYR GLN GLU PHE LEU GLN ARG ASP ALA
SEQRES 59 A 757 GLU ALA ARG
SEQRES 1 B 11 DC DC DT DA DC DT DG DC DT DA DC
SEQRES 1 C 15 DC DG DC DG DG DT DA DG DC DA DG DT DA
SEQRES 2 C 15 DG DG
SEQRES 1 D 10 DG DG DA DT DG DA DC DG DA DT
SEQRES 1 E 15 DC DG DC DG DA DA DT DC DG DT DC DA DT
SEQRES 2 E 15 DC DC
MODRES 3L4J PTR A 782 TYR O-PHOSPHOTYROSINE
HET PTR A 782 16
HET TSP D 11 20
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM TSP 3'-THIO-THYMIDINE-5'-PHOSPHATE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 6 TSP C10 H15 N2 O7 P S
FORMUL 7 HOH *113(H2 O)
HELIX 1 1 GLY A 450 GLY A 465 1 16
HELIX 2 2 SER A 485 ASN A 492 1 8
HELIX 3 3 ASN A 492 MET A 502 1 11
HELIX 4 4 ASP A 512 LEU A 516 5 5
HELIX 5 5 ASP A 528 PHE A 546 1 19
HELIX 6 6 ASN A 580 GLU A 591 1 12
HELIX 7 7 SER A 592 PHE A 595 5 4
HELIX 8 8 LEU A 609 ASN A 619 1 11
HELIX 9 9 ASN A 633 SER A 643 1 11
HELIX 10 10 LYS A 646 TYR A 657 1 12
HELIX 11 11 PRO A 671 GLU A 679 1 9
HELIX 12 12 GLU A 679 ILE A 692 1 14
HELIX 13 13 LYS A 700 LYS A 713 1 14
HELIX 14 14 VAL A 721 THR A 732 1 12
HELIX 15 15 GLY A 737 GLN A 750 1 14
HELIX 16 16 LEU A 790 PHE A 795 1 6
HELIX 17 17 HIS A 796 TYR A 803 5 8
HELIX 18 18 PRO A 823 GLY A 829 1 7
HELIX 19 19 ASN A 845 ASN A 858 1 14
HELIX 20 20 TRP A 908 GLY A 922 1 15
HELIX 21 21 SER A 948 GLY A 959 1 12
HELIX 22 22 GLY A 959 PHE A 964 1 6
HELIX 23 23 SER A 989 GLU A 1035 1 47
HELIX 24 24 PRO A 1044 LEU A 1055 1 12
HELIX 25 25 TYR A 1113 GLY A 1118 1 6
HELIX 26 26 ARG A 1120 LEU A 1124 5 5
HELIX 27 27 THR A 1125 LYS A 1148 1 24
HELIX 28 28 SER A 1150 ALA A 1176 1 27
SHEET 1 A 6 TYR A 469 LEU A 474 0
SHEET 2 A 6 THR A 444 GLU A 449 1 N THR A 448 O LEU A 474
SHEET 3 A 6 HIS A 520 MET A 524 1 O MET A 522 N LEU A 445
SHEET 4 A 6 LEU A 556 PHE A 559 1 O LEU A 557 N LEU A 521
SHEET 5 A 6 LEU A 624 PHE A 627 -1 O PHE A 627 N LEU A 556
SHEET 6 A 6 GLU A 669 ILE A 670 1 O ILE A 670 N ILE A 626
SHEET 1 B 3 THR A 575 PHE A 578 0
SHEET 2 B 3 ILE A 564 ILE A 568 -1 N ILE A 564 O PHE A 578
SHEET 3 B 3 TRP A 597 TYR A 601 -1 O LYS A 600 N LYS A 565
SHEET 1 C 2 LEU A 719 LYS A 720 0
SHEET 2 C 2 TYR A 784 THR A 785 -1 O THR A 785 N LEU A 719
SHEET 1 D 2 TYR A 805 GLN A 807 0
SHEET 2 D 2 THR A 812 PRO A 815 -1 O VAL A 813 N ILE A 806
SHEET 1 E 2 ALA A 830 ILE A 833 0
SHEET 2 E 2 SER A 838 ILE A 841 -1 O ILE A 841 N ALA A 830
SHEET 1 F 3 THR A 875 GLU A 880 0
SHEET 2 F 3 ARG A 883 TYR A 887 -1 O TYR A 887 N THR A 875
SHEET 3 F 3 ILE A 967 SER A 971 -1 O SER A 968 N MET A 886
SHEET 1 G 4 ARG A 889 GLY A 894 0
SHEET 2 G 4 VAL A 897 GLU A 902 -1 O GLU A 899 N GLU A 891
SHEET 3 G 4 PHE A 943 THR A 946 -1 O ILE A 945 N LEU A 898
SHEET 4 G 4 ASP A 932 GLU A 935 -1 N ASP A 932 O THR A 946
SHEET 1 H 2 VAL A 976 PHE A 978 0
SHEET 2 H 2 ILE A 984 LYS A 986 -1 O LYS A 985 N ALA A 977
SHEET 1 I 2 ARG A1059 PHE A1060 0
SHEET 2 I 2 PRO A1066 TYR A1067 -1 O TYR A1067 N ARG A1059
LINK C ARG A 781 N APTR A 782 1555 1555 1.25
LINK C APTR A 782 N ILE A 783 1555 1555 1.30
LINK O3'B DT D 10 P BTSP D 11 1555 1555 1.59
SITE 1 AC1 14 GLU A 449 LYS A 477 ASP A 530 HIS A 736
SITE 2 AC1 14 GLY A 737 PTR A 782 HOH B 202 DC C 1
SITE 3 AC1 14 DG C 5 DT C 6 DT D 10 DC E 1
SITE 4 AC1 14 DA E 5 DA E 6
CRYST1 86.045 92.416 116.732 90.00 90.00 90.00 P 21 2 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011622 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008567 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
