HEADER DNA BINDING PROTEIN/DNA 11-NOV-17 6BLW
TITLE ZINC FINGER DOMAIN OF WT1(+KTS FORM) WITH M342R MUTATION AND 17+1MER
TITLE 2 OLIGONUCLEOTIDE WITH TRIPLET GGT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WILMS TUMOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: WT33;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(P*GP*CP*GP*AP*AP*AP*TP*GP*GP*GP*AP*GP*GP*GP*TP*T)-3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-
COMPND 14 D(*TP*AP*AP*CP*CP*CP*TP*CP*CP*CP*AP*TP*TP*TP*CP*GP*C)-3');
COMPND 15 CHAIN: C;
COMPND 16 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: WT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS PROTEIN-DNA COMPLEX WILMS TUMOR SUPPRESSOR PROTEIN ZINC-FINGERS, DNA
KEYWDS 2 BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.HORTON,X.CHENG
REVDAT 3 16-MAY-18 6BLW 1 JRNL
REVDAT 2 17-JAN-18 6BLW 1 JRNL
REVDAT 1 03-JAN-18 6BLW 0
JRNL AUTH D.WANG,J.R.HORTON,Y.ZHENG,R.M.BLUMENTHAL,X.ZHANG,X.CHENG
JRNL TITL ROLE FOR FIRST ZINC FINGER OF WT1 IN DNA SEQUENCE
JRNL TITL 2 SPECIFICITY: DENYS-DRASH SYNDROME-ASSOCIATED WT1 MUTANT IN
JRNL TITL 3 ZF1 ENHANCES AFFINITY FOR A SUBSET OF WT1 BINDING SITES.
JRNL REF NUCLEIC ACIDS RES. V. 46 3864 2018
JRNL REFN ESSN 1362-4962
JRNL PMID 29294058
JRNL DOI 10.1093/NAR/GKX1274
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 21595
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1079
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 29.6949 - 4.4190 0.99 2893 154 0.1803 0.2076
REMARK 3 2 4.4190 - 3.5093 1.00 2923 150 0.1787 0.2152
REMARK 3 3 3.5093 - 3.0662 1.00 2901 156 0.1983 0.2054
REMARK 3 4 3.0662 - 2.7861 1.00 2926 147 0.2756 0.2910
REMARK 3 5 2.7861 - 2.5865 1.00 2884 157 0.2688 0.2886
REMARK 3 6 2.5865 - 2.4341 1.00 2932 153 0.2597 0.3202
REMARK 3 7 2.4341 - 2.3123 1.00 2902 151 0.2829 0.3350
REMARK 3 8 2.3123 - 2.2116 1.00 2907 150 0.2838 0.2353
REMARK 3 9 2.2116 - 2.1265 1.00 2896 152 0.2905 0.3179
REMARK 3 10 2.1265 - 2.0532 0.99 2874 159 0.3091 0.3081
REMARK 3 11 2.0532 - 1.9890 0.95 2761 148 0.3366 0.3245
REMARK 3 12 1.9890 - 1.9321 0.88 2561 132 0.3395 0.3927
REMARK 3 13 1.9321 - 1.8813 0.81 2357 125 0.3640 0.4081
REMARK 3 14 1.8813 - 1.8354 0.59 1683 93 0.3635 0.4110
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 1672
REMARK 3 ANGLE : 0.523 2358
REMARK 3 CHIRALITY : 0.030 248
REMARK 3 PLANARITY : 0.003 189
REMARK 3 DIHEDRAL : 19.261 863
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 336 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5749 -10.1096 30.4837
REMARK 3 T TENSOR
REMARK 3 T11: 0.4418 T22: 0.7645
REMARK 3 T33: 0.4348 T12: -0.1685
REMARK 3 T13: 0.0304 T23: 0.1095
REMARK 3 L TENSOR
REMARK 3 L11: 0.3512 L22: 1.0192
REMARK 3 L33: 0.4332 L12: -0.4737
REMARK 3 L13: 0.3354 L23: -0.2368
REMARK 3 S TENSOR
REMARK 3 S11: 0.3158 S12: -0.3579 S13: -0.1978
REMARK 3 S21: 0.3615 S22: -0.4444 S23: -0.3704
REMARK 3 S31: 0.2019 S32: -0.6836 S33: 0.0007
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 337 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6925 -4.4615 24.9237
REMARK 3 T TENSOR
REMARK 3 T11: 0.4652 T22: 0.8128
REMARK 3 T33: 0.3112 T12: 0.0972
REMARK 3 T13: 0.0484 T23: -0.1272
REMARK 3 L TENSOR
REMARK 3 L11: 2.2225 L22: 7.5165
REMARK 3 L33: 1.5884 L12: 1.9436
REMARK 3 L13: 0.0053 L23: -3.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1183 S12: 0.2342 S13: -0.3819
REMARK 3 S21: 0.2033 S22: -0.4847 S23: -0.3867
REMARK 3 S31: -1.3161 S32: -1.1785 S33: -0.6139
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 349 THROUGH 353 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1232 -1.6488 16.8791
REMARK 3 T TENSOR
REMARK 3 T11: 0.4803 T22: 1.1658
REMARK 3 T33: 0.5251 T12: 0.1844
REMARK 3 T13: 0.1332 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.1731 L22: 1.3232
REMARK 3 L33: 0.6032 L12: 0.4154
REMARK 3 L13: -0.1160 L23: 0.0810
REMARK 3 S TENSOR
REMARK 3 S11: -0.3030 S12: -1.0220 S13: -0.2720
REMARK 3 S21: 0.1689 S22: 0.0417 S23: 0.2260
REMARK 3 S31: 0.1189 S32: -0.8924 S33: -0.1039
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 354 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.1073 -3.9824 8.5063
REMARK 3 T TENSOR
REMARK 3 T11: 0.3589 T22: 0.6984
REMARK 3 T33: 0.4577 T12: -0.0127
REMARK 3 T13: 0.0536 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 0.3025 L22: 0.1632
REMARK 3 L33: 0.1644 L12: 0.2443
REMARK 3 L13: -0.0520 L23: -0.0643
REMARK 3 S TENSOR
REMARK 3 S11: 0.1772 S12: -0.5181 S13: 0.1406
REMARK 3 S21: 0.0445 S22: 0.0489 S23: 0.4456
REMARK 3 S31: 0.5360 S32: -0.8766 S33: 0.0003
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 367 THROUGH 383 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2531 -5.2705 3.2448
REMARK 3 T TENSOR
REMARK 3 T11: 0.3429 T22: 0.4240
REMARK 3 T33: 0.3494 T12: -0.0324
REMARK 3 T13: 0.0178 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.5316 L22: 0.5572
REMARK 3 L33: 0.0566 L12: 0.0488
REMARK 3 L13: -0.1748 L23: -0.0460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1702 S12: -0.2710 S13: -0.1423
REMARK 3 S21: -0.0511 S22: 0.0614 S23: -0.0258
REMARK 3 S31: 0.0762 S32: -0.2378 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8416 -13.4687 -5.4663
REMARK 3 T TENSOR
REMARK 3 T11: 0.4197 T22: 0.4766
REMARK 3 T33: 0.4480 T12: 0.0213
REMARK 3 T13: 0.0663 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.1432 L22: 0.3842
REMARK 3 L33: 0.1716 L12: -0.1114
REMARK 3 L13: 0.0435 L23: 0.1862
REMARK 3 S TENSOR
REMARK 3 S11: 0.1175 S12: 0.5514 S13: -0.1424
REMARK 3 S21: -0.2302 S22: -0.0689 S23: -0.3728
REMARK 3 S31: 0.1452 S32: 0.1080 S33: 0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 395 THROUGH 407 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3631 -19.9254 -0.1867
REMARK 3 T TENSOR
REMARK 3 T11: 0.3977 T22: 0.3519
REMARK 3 T33: 0.4948 T12: 0.0198
REMARK 3 T13: -0.0082 T23: -0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 0.0596 L22: 0.0821
REMARK 3 L33: 0.1776 L12: 0.0121
REMARK 3 L13: -0.0170 L23: 0.1889
REMARK 3 S TENSOR
REMARK 3 S11: 0.1496 S12: -0.2951 S13: -0.5312
REMARK 3 S21: -0.0466 S22: -0.3813 S23: 0.8231
REMARK 3 S31: 0.3071 S32: 0.2850 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 408 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4761 -22.8347 -14.7810
REMARK 3 T TENSOR
REMARK 3 T11: 1.2069 T22: 1.1543
REMARK 3 T33: 0.7482 T12: 0.2433
REMARK 3 T13: 0.0908 T23: -0.3822
REMARK 3 L TENSOR
REMARK 3 L11: 4.2357 L22: 0.2989
REMARK 3 L33: 0.3267 L12: 0.7929
REMARK 3 L13: -0.6018 L23: -0.3089
REMARK 3 S TENSOR
REMARK 3 S11: -0.2850 S12: 1.2447 S13: 0.3837
REMARK 3 S21: 1.2343 S22: 0.5972 S23: -1.0860
REMARK 3 S31: 0.9259 S32: -1.0902 S33: 0.0400
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 431 THROUGH 436 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2191 -14.8580 -16.8258
REMARK 3 T TENSOR
REMARK 3 T11: 0.9696 T22: 1.0494
REMARK 3 T33: 0.9292 T12: 0.1330
REMARK 3 T13: 0.1584 T23: -0.1867
REMARK 3 L TENSOR
REMARK 3 L11: 0.3362 L22: 0.0486
REMARK 3 L33: 0.2624 L12: -0.0005
REMARK 3 L13: 0.2855 L23: -0.0292
REMARK 3 S TENSOR
REMARK 3 S11: -1.5429 S12: 0.7255 S13: 0.8376
REMARK 3 S21: -0.1133 S22: -0.1052 S23: 0.1163
REMARK 3 S31: -0.7351 S32: 0.6737 S33: -0.0251
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 6 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5821 -31.7985 -2.4905
REMARK 3 T TENSOR
REMARK 3 T11: 0.8194 T22: 0.4873
REMARK 3 T33: 0.4877 T12: -0.1931
REMARK 3 T13: 0.1312 T23: -0.2513
REMARK 3 L TENSOR
REMARK 3 L11: 0.2536 L22: 1.6616
REMARK 3 L33: 0.7174 L12: 0.1411
REMARK 3 L13: -0.1589 L23: -1.0493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.8885 S13: -0.1005
REMARK 3 S21: 0.2914 S22: -0.8197 S23: -0.0280
REMARK 3 S31: 0.1415 S32: -0.4123 S33: -0.6360
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9261 -10.7879 12.3153
REMARK 3 T TENSOR
REMARK 3 T11: 0.4551 T22: 0.4170
REMARK 3 T33: 0.4833 T12: -0.0516
REMARK 3 T13: -0.0014 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.4437 L22: 1.1667
REMARK 3 L33: 1.0382 L12: -0.5612
REMARK 3 L13: -0.4039 L23: -0.9091
REMARK 3 S TENSOR
REMARK 3 S11: -0.1337 S12: -0.2112 S13: 0.0170
REMARK 3 S21: -0.1410 S22: -0.0253 S23: -0.2449
REMARK 3 S31: -0.1464 S32: -0.0822 S33: 0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 6 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1481 1.9577 15.5227
REMARK 3 T TENSOR
REMARK 3 T11: 0.4530 T22: 0.4583
REMARK 3 T33: 0.4320 T12: 0.0190
REMARK 3 T13: -0.0706 T23: -0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 0.1211 L22: 0.4725
REMARK 3 L33: 0.2149 L12: 0.1114
REMARK 3 L13: 0.0051 L23: -0.2970
REMARK 3 S TENSOR
REMARK 3 S11: 0.2580 S12: -0.0705 S13: -0.2180
REMARK 3 S21: 0.0358 S22: -0.3146 S23: -0.4852
REMARK 3 S31: -0.4993 S32: -0.8203 S33: -0.0001
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 7 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5472 -16.3520 11.8290
REMARK 3 T TENSOR
REMARK 3 T11: 0.4373 T22: 0.3514
REMARK 3 T33: 0.4906 T12: -0.0228
REMARK 3 T13: -0.0282 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.3555 L22: 0.1010
REMARK 3 L33: 0.0374 L12: -0.1906
REMARK 3 L13: 0.1248 L23: -0.0681
REMARK 3 S TENSOR
REMARK 3 S11: 0.3295 S12: -0.2664 S13: -0.3252
REMARK 3 S21: -0.4250 S22: -0.2825 S23: 0.0978
REMARK 3 S31: 0.2390 S32: -0.0124 S33: 0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 12 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8553 -22.9753 2.1647
REMARK 3 T TENSOR
REMARK 3 T11: 0.5763 T22: 0.5091
REMARK 3 T33: 0.4520 T12: -0.2204
REMARK 3 T13: 0.0267 T23: -0.0995
REMARK 3 L TENSOR
REMARK 3 L11: 0.7934 L22: 0.1774
REMARK 3 L33: 0.1019 L12: 0.0607
REMARK 3 L13: -0.1516 L23: -0.0724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0857 S12: 0.1709 S13: -0.5277
REMARK 3 S21: 0.0518 S22: -0.1054 S23: 0.1303
REMARK 3 S31: 0.4231 S32: -0.9145 S33: 0.0183
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 18 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9156 -28.9779 -10.5210
REMARK 3 T TENSOR
REMARK 3 T11: 0.7986 T22: 0.4637
REMARK 3 T33: 0.5395 T12: -0.2104
REMARK 3 T13: 0.2095 T23: -0.1697
REMARK 3 L TENSOR
REMARK 3 L11: 2.1275 L22: 0.0213
REMARK 3 L33: 0.8660 L12: -0.2066
REMARK 3 L13: 1.3510 L23: -0.1239
REMARK 3 S TENSOR
REMARK 3 S11: 1.3395 S12: -0.3994 S13: -0.1318
REMARK 3 S21: -0.8962 S22: -0.6074 S23: -0.2245
REMARK 3 S31: -0.0437 S32: -0.4381 S33: 0.1123
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 6BLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000229846.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21595
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.835
REMARK 200 RESOLUTION RANGE LOW (A) : 29.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 32.70
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.5
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : 0.93700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 300 0.1M CHES:NAOH, PH 9.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
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 41.67000
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 41.67000
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 31.77600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.78600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.77600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.78600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.67000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.77600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.78600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 41.67000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.77600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.78600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 THR A 409
REMARK 465 SER A 410
REMARK 465 GLU A 411
REMARK 465 LYS A 412
REMARK 465 PRO A 413
REMARK 465 PHE A 414
REMARK 465 LYS A 423
REMARK 465 LYS A 424
REMARK 465 PHE A 425
REMARK 465 ALA A 426
REMARK 465 ARG A 427
REMARK 465 SER A 428
REMARK 465 ASP A 429
REMARK 465 GLU A 430
REMARK 465 ARG A 440
REMARK 465 DA B 1
REMARK 465 DA B 18
REMARK 465 DT C 1
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 HIS A 317 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 318 CG SD CE
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 MET A 324 CG SD CE
REMARK 470 ASN A 331 CG OD1 ND2
REMARK 470 GLU A 350 CG CD OE1 OE2
REMARK 470 PHE A 357 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 GLU A 361 CG CD OE1 OE2
REMARK 470 LYS A 386 CG CD CE NZ
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 LYS A 408 CG CD CE NZ
REMARK 470 GLN A 422 CG CD OE1 NE2
REMARK 470 LEU A 431 CG CD1 CD2
REMARK 470 VAL A 432 CG1 CG2
REMARK 470 ARG A 433 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 436 CG OD1 ND2
REMARK 470 MET A 437 CG SD CE
REMARK 470 GLN A 439 CG CD OE1 NE2
REMARK 470 DT C 2 P OP1 OP2
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 CYS A 360 -70.19 -117.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 325 SG
REMARK 620 2 CYS A 330 SG 116.2
REMARK 620 3 HIS A 343 NE2 111.9 109.7
REMARK 620 4 HIS A 347 NE2 107.3 110.6 99.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 355 SG
REMARK 620 2 CYS A 360 SG 112.6
REMARK 620 3 HIS A 373 NE2 109.0 105.8
REMARK 620 4 HIS A 377 NE2 110.7 116.3 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 385 SG
REMARK 620 2 CYS A 388 SG 114.0
REMARK 620 3 HIS A 401 NE2 113.6 95.9
REMARK 620 4 HIS A 405 NE2 111.1 114.1 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 416 SG
REMARK 620 2 CYS A 421 SG 107.2
REMARK 620 3 HIS A 434 NE2 48.7 111.5
REMARK 620 4 HIS A 438 NE2 113.1 133.8 81.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 509
DBREF 6BLW A 319 440 UNP P19544 WT1_HUMAN 375 496
DBREF 6BLW B 1 18 PDB 6BLW 6BLW 1 18
DBREF 6BLW C 1 18 PDB 6BLW 6BLW 1 18
SEQADV 6BLW HIS A 317 UNP P19544 EXPRESSION TAG
SEQADV 6BLW MET A 318 UNP P19544 EXPRESSION TAG
SEQADV 6BLW ARG A 342 UNP P19544 MET 398 ENGINEERED MUTATION
SEQRES 1 A 124 HIS MET GLU LYS ARG PRO PHE MET CYS ALA TYR PRO GLY
SEQRES 2 A 124 CYS ASN LYS ARG TYR PHE LYS LEU SER HIS LEU GLN ARG
SEQRES 3 A 124 HIS SER ARG LYS HIS THR GLY GLU LYS PRO TYR GLN CYS
SEQRES 4 A 124 ASP PHE LYS ASP CYS GLU ARG ARG PHE SER ARG SER ASP
SEQRES 5 A 124 GLN LEU LYS ARG HIS GLN ARG ARG HIS THR GLY VAL LYS
SEQRES 6 A 124 PRO PHE GLN CYS LYS THR CYS GLN ARG LYS PHE SER ARG
SEQRES 7 A 124 SER ASP HIS LEU LYS THR HIS THR ARG THR HIS THR GLY
SEQRES 8 A 124 LYS THR SER GLU LYS PRO PHE SER CYS ARG TRP PRO SER
SEQRES 9 A 124 CYS GLN LYS LYS PHE ALA ARG SER ASP GLU LEU VAL ARG
SEQRES 10 A 124 HIS HIS ASN MET HIS GLN ARG
SEQRES 1 B 18 DA DG DC DG DA DA DA DT DG DG DG DA DG
SEQRES 2 B 18 DG DG DT DT DA
SEQRES 1 C 18 DT DT DA DA DC DC DC DT DC DC DC DA DT
SEQRES 2 C 18 DT DT DC DG DC
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET ZN A 504 1
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET GOL A 509 6
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 ZN 4(ZN 2+)
FORMUL 8 EDO 4(C2 H6 O2)
FORMUL 12 GOL C3 H8 O3
FORMUL 13 HOH *71(H2 O)
HELIX 1 AA1 LYS A 336 GLY A 349 1 14
HELIX 2 AA2 ARG A 366 GLY A 379 1 14
HELIX 3 AA3 ARG A 394 THR A 402 1 9
HELIX 4 AA4 THR A 402 LYS A 408 1 7
HELIX 5 AA5 VAL A 432 HIS A 438 1 7
SHEET 1 AA1 2 PHE A 323 MET A 324 0
SHEET 2 AA1 2 ARG A 333 TYR A 334 -1 O TYR A 334 N PHE A 323
SHEET 1 AA2 2 TYR A 353 GLN A 354 0
SHEET 2 AA2 2 ARG A 363 PHE A 364 -1 O PHE A 364 N TYR A 353
SHEET 1 AA3 2 PHE A 383 GLN A 384 0
SHEET 2 AA3 2 LYS A 391 PHE A 392 -1 O PHE A 392 N PHE A 383
LINK SG CYS A 325 ZN ZN A 503 1555 1555 2.29
LINK SG CYS A 330 ZN ZN A 503 1555 1555 2.28
LINK NE2 HIS A 343 ZN ZN A 503 1555 1555 2.03
LINK NE2 HIS A 347 ZN ZN A 503 1555 1555 2.01
LINK SG CYS A 355 ZN ZN A 501 1555 1555 2.26
LINK SG CYS A 360 ZN ZN A 501 1555 1555 2.26
LINK NE2 HIS A 373 ZN ZN A 501 1555 1555 2.02
LINK NE2 HIS A 377 ZN ZN A 501 1555 1555 2.03
LINK SG CYS A 385 ZN ZN A 502 1555 1555 2.34
LINK SG CYS A 388 ZN ZN A 502 1555 1555 2.27
LINK NE2 HIS A 401 ZN ZN A 502 1555 1555 2.03
LINK NE2 HIS A 405 ZN ZN A 502 1555 1555 2.03
LINK SG CYS A 416 NE2 HIS A 434 1555 1555 1.84
LINK SG CYS A 416 ZN ZN A 504 1555 1555 2.38
LINK SG CYS A 421 ZN ZN A 504 1555 1555 2.22
LINK NE2 HIS A 434 ZN ZN A 504 1555 1555 2.01
LINK NE2 HIS A 438 ZN ZN A 504 1555 1555 2.03
SITE 1 AC1 4 CYS A 355 CYS A 360 HIS A 373 HIS A 377
SITE 1 AC2 4 CYS A 385 CYS A 388 HIS A 401 HIS A 405
SITE 1 AC3 4 CYS A 325 CYS A 330 HIS A 343 HIS A 347
SITE 1 AC4 4 CYS A 416 CYS A 421 HIS A 434 HIS A 438
SITE 1 AC5 5 LYS A 381 SER A 393 HIS A 397 DT B 8
SITE 2 AC5 5 DG B 9
SITE 1 AC6 7 ARG A 372 SER A 393 ARG A 394 HIS A 397
SITE 2 AC6 7 DT B 8 DG B 9 HOH B 103
SITE 1 AC7 7 ARG A 366 ASP A 368 ARG A 372 DA B 12
SITE 2 AC7 7 DG B 13 HOH B 108 DC C 7
SITE 1 AC8 5 LYS A 371 LYS A 381 DC C 5 DC C 6
SITE 2 AC8 5 HOH C 108
SITE 1 AC9 2 LEU A 431 VAL A 432
CRYST1 63.552 95.572 83.340 90.00 90.00 90.00 C 2 2 21 8
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 0.015735 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011999 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
