HEADER TRANSCRIPTION/DNA 22-JUN-16 5KKQ
TITLE HOMO SAPIENS CCCTC-BINDING FACTOR (CTCF) ZNF3-7 AND DNA COMPLEX
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR CTCF;
COMPND 3 CHAIN: A, D;
COMPND 4 SYNONYM: 11-ZINC FINGER PROTEIN,CCCTC-BINDING FACTOR,CTCFL PARALOG;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(*TP*AP*GP*CP*GP*CP*CP*CP*CP*CP*TP*GP*CP*TP*GP*GP*C)-3');
COMPND 9 CHAIN: B, E;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DNA (5'-
COMPND 13 D(*GP*CP*CP*AP*GP*CP*AP*GP*GP*GP*GP*GP*CP*GP*CP*TP*A)-3');
COMPND 14 CHAIN: C, F;
COMPND 15 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: CTCF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RIL-CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-6P-1;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PXC1551;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630
KEYWDS CTCF, ZINC FINGER, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HASHIMOTO,D.WANG,X.CHENG
REVDAT 6 06-MAR-24 5KKQ 1 REMARK
REVDAT 5 25-DEC-19 5KKQ 1 REMARK
REVDAT 4 20-SEP-17 5KKQ 1 REMARK
REVDAT 3 14-JUN-17 5KKQ 1 JRNL
REVDAT 2 07-JUN-17 5KKQ 1 JRNL
REVDAT 1 24-MAY-17 5KKQ 0
JRNL AUTH H.HASHIMOTO,D.WANG,J.R.HORTON,X.ZHANG,V.G.CORCES,X.CHENG
JRNL TITL STRUCTURAL BASIS FOR THE VERSATILE AND METHYLATION-DEPENDENT
JRNL TITL 2 BINDING OF CTCF TO DNA.
JRNL REF MOL. CELL V. 66 711 2017
JRNL REFN ISSN 1097-4164
JRNL PMID 28529057
JRNL DOI 10.1016/J.MOLCEL.2017.05.004
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2257: ???)
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 110863
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.490
REMARK 3 FREE R VALUE TEST SET COUNT : 3864
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 28.9398 - 5.2862 0.96 4092 151 0.1345 0.1373
REMARK 3 2 5.2862 - 4.2000 0.97 4181 150 0.1174 0.1376
REMARK 3 3 4.2000 - 3.6703 0.96 4124 149 0.1350 0.1489
REMARK 3 4 3.6703 - 3.3352 0.97 4135 154 0.1446 0.1616
REMARK 3 5 3.3352 - 3.0965 0.95 4082 146 0.1833 0.2410
REMARK 3 6 3.0965 - 2.9141 0.97 4132 147 0.1941 0.3239
REMARK 3 7 2.9141 - 2.7683 0.97 4136 150 0.1978 0.2275
REMARK 3 8 2.7683 - 2.6478 0.97 4109 148 0.1830 0.2368
REMARK 3 9 2.6478 - 2.5460 0.97 4148 152 0.1784 0.2360
REMARK 3 10 2.5460 - 2.4582 0.96 4191 150 0.1837 0.2157
REMARK 3 11 2.4582 - 2.3813 0.97 4143 150 0.1831 0.1972
REMARK 3 12 2.3813 - 2.3133 0.96 4094 148 0.1769 0.1771
REMARK 3 13 2.3133 - 2.2524 0.95 4036 146 0.1734 0.2304
REMARK 3 14 2.2524 - 2.1975 0.96 4150 152 0.1844 0.2481
REMARK 3 15 2.1975 - 2.1475 0.95 4001 144 0.1846 0.1933
REMARK 3 16 2.1475 - 2.1019 0.96 4149 148 0.2007 0.2561
REMARK 3 17 2.1019 - 2.0598 0.95 3977 146 0.2213 0.2881
REMARK 3 18 2.0598 - 2.0210 0.95 4127 148 0.2314 0.2544
REMARK 3 19 2.0210 - 1.9849 0.94 4022 146 0.2407 0.2632
REMARK 3 20 1.9849 - 1.9512 0.94 3943 142 0.2443 0.2500
REMARK 3 21 1.9512 - 1.9198 0.93 4045 146 0.2443 0.3006
REMARK 3 22 1.9198 - 1.8902 0.91 3967 141 0.2616 0.2625
REMARK 3 23 1.8902 - 1.8624 0.89 3740 135 0.2692 0.2629
REMARK 3 24 1.8624 - 1.8362 0.86 3818 141 0.2785 0.2605
REMARK 3 25 1.8362 - 1.8114 0.79 3314 114 0.2878 0.3430
REMARK 3 26 1.8114 - 1.7879 0.66 2791 97 0.2948 0.2926
REMARK 3 27 1.7879 - 1.7655 0.46 1972 72 0.3088 0.3104
REMARK 3 28 1.7655 - 1.7443 0.32 1380 51 0.2947 0.2852
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.540
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 : 0.017 4139
REMARK 3 ANGLE : 1.489 5844
REMARK 3 CHIRALITY : 0.080 636
REMARK 3 PLANARITY : 0.011 494
REMARK 3 DIHEDRAL : 21.642 2255
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7358 -18.2625 -23.3722
REMARK 3 T TENSOR
REMARK 3 T11: 0.4433 T22: 0.4329
REMARK 3 T33: 0.2961 T12: -0.1068
REMARK 3 T13: 0.0713 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 2.8081 L22: 4.6291
REMARK 3 L33: 5.3858 L12: -1.6544
REMARK 3 L13: -1.3487 L23: 4.2398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: 0.2533 S13: -0.1503
REMARK 3 S21: -0.5515 S22: 0.3739 S23: -0.5040
REMARK 3 S31: -0.4614 S32: 0.9493 S33: -0.3797
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 375 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9550 -25.5524 -13.2481
REMARK 3 T TENSOR
REMARK 3 T11: 0.3059 T22: 0.2114
REMARK 3 T33: 0.2518 T12: -0.0016
REMARK 3 T13: -0.0684 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 2.3167 L22: 7.9062
REMARK 3 L33: 2.8013 L12: -2.7179
REMARK 3 L13: 1.5034 L23: -1.7525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0626 S12: -0.0444 S13: -0.0335
REMARK 3 S21: -0.8235 S22: 0.0040 S23: 0.7131
REMARK 3 S31: -0.0022 S32: -0.1242 S33: -0.0689
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 439 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7477 -40.0621 -1.6047
REMARK 3 T TENSOR
REMARK 3 T11: 0.2214 T22: 0.2219
REMARK 3 T33: 0.2574 T12: 0.0280
REMARK 3 T13: 0.0084 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 2.7061 L22: 2.4172
REMARK 3 L33: 7.2167 L12: 0.5467
REMARK 3 L13: 2.2001 L23: 2.2784
REMARK 3 S TENSOR
REMARK 3 S11: 0.2190 S12: 0.0300 S13: -0.0885
REMARK 3 S21: -0.0410 S22: 0.1590 S23: -0.2020
REMARK 3 S31: 0.5179 S32: 0.4988 S33: -0.3438
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 440 THROUGH 463 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2798 -31.6500 13.1996
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.3106
REMARK 3 T33: 0.2626 T12: -0.0012
REMARK 3 T13: 0.0443 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 7.7143 L22: 3.5531
REMARK 3 L33: 7.0453 L12: -0.0729
REMARK 3 L13: 0.0092 L23: 2.6087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0661 S12: -0.5192 S13: 0.7263
REMARK 3 S21: 0.4977 S22: -0.0237 S23: 0.0435
REMARK 3 S31: -0.0937 S32: -0.0564 S33: -0.0347
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7668 -13.8419 -28.1851
REMARK 3 T TENSOR
REMARK 3 T11: 0.7106 T22: 0.5282
REMARK 3 T33: 0.4851 T12: 0.0078
REMARK 3 T13: 0.1220 T23: 0.1464
REMARK 3 L TENSOR
REMARK 3 L11: 7.8610 L22: 6.9767
REMARK 3 L33: 3.6279 L12: -4.1896
REMARK 3 L13: 0.1314 L23: 3.6847
REMARK 3 S TENSOR
REMARK 3 S11: 0.0959 S12: -0.6219 S13: -0.4658
REMARK 3 S21: 0.2426 S22: -0.0841 S23: 0.5942
REMARK 3 S31: -1.3210 S32: -0.0698 S33: -0.0468
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6364 -27.4657 -17.2677
REMARK 3 T TENSOR
REMARK 3 T11: 0.3764 T22: 0.3844
REMARK 3 T33: 0.3440 T12: -0.0539
REMARK 3 T13: 0.0321 T23: 0.1542
REMARK 3 L TENSOR
REMARK 3 L11: 2.6486 L22: 7.7036
REMARK 3 L33: 6.9160 L12: 0.0437
REMARK 3 L13: 0.4641 L23: 1.4709
REMARK 3 S TENSOR
REMARK 3 S11: 0.1734 S12: 0.2952 S13: 0.1094
REMARK 3 S21: -0.4442 S22: 0.5408 S23: 0.2770
REMARK 3 S31: 0.7351 S32: -0.1653 S33: -0.7307
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0982 -28.7428 2.4513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1813 T22: 0.2724
REMARK 3 T33: 0.3304 T12: 0.0265
REMARK 3 T13: -0.0039 T23: 0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 6.7433 L22: 5.5362
REMARK 3 L33: 6.8344 L12: 5.0466
REMARK 3 L13: -5.5201 L23: -2.3816
REMARK 3 S TENSOR
REMARK 3 S11: 0.2465 S12: -0.3863 S13: 0.9730
REMARK 3 S21: -0.0105 S22: 0.1528 S23: 0.8018
REMARK 3 S31: -0.2110 S32: 0.2357 S33: -0.4010
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7234 -28.2710 -3.4408
REMARK 3 T TENSOR
REMARK 3 T11: 0.1611 T22: 0.2447
REMARK 3 T33: 0.1772 T12: 0.0264
REMARK 3 T13: 0.0276 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.5361 L22: 5.3190
REMARK 3 L33: 3.7472 L12: 1.5285
REMARK 3 L13: -0.3779 L23: -3.2301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.1883 S13: -0.0487
REMARK 3 S21: -0.2130 S22: 0.0169 S23: 0.1229
REMARK 3 S31: 0.0799 S32: 0.1590 S33: -0.0005
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 11 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3557 -23.2358 -24.7968
REMARK 3 T TENSOR
REMARK 3 T11: 0.4264 T22: 0.3994
REMARK 3 T33: 0.2916 T12: -0.0417
REMARK 3 T13: 0.0409 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 5.9877 L22: 8.6332
REMARK 3 L33: 4.2439 L12: -2.2345
REMARK 3 L13: 0.3122 L23: 2.0597
REMARK 3 S TENSOR
REMARK 3 S11: 0.4087 S12: 0.3915 S13: -0.2843
REMARK 3 S21: -0.4919 S22: 0.1832 S23: 0.3954
REMARK 3 S31: -0.0069 S32: 0.5574 S33: -0.5679
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6304 -16.0897 -37.2381
REMARK 3 T TENSOR
REMARK 3 T11: 0.6771 T22: 0.7961
REMARK 3 T33: 0.5424 T12: -0.0663
REMARK 3 T13: 0.1005 T23: 0.0882
REMARK 3 L TENSOR
REMARK 3 L11: 5.1292 L22: 2.0008
REMARK 3 L33: 8.3121 L12: 2.9136
REMARK 3 L13: 4.7805 L23: -2.9677
REMARK 3 S TENSOR
REMARK 3 S11: 0.9514 S12: 0.7595 S13: 1.6274
REMARK 3 S21: -1.0540 S22: -0.2308 S23: 1.6684
REMARK 3 S31: 0.1625 S32: 0.9105 S33: -0.7930
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 321 THROUGH 374 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5305 -16.6062 36.5516
REMARK 3 T TENSOR
REMARK 3 T11: 0.4181 T22: 0.5114
REMARK 3 T33: 0.3388 T12: -0.0588
REMARK 3 T13: 0.0845 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 3.4787 L22: 3.4276
REMARK 3 L33: 4.8811 L12: -0.0734
REMARK 3 L13: 0.7343 L23: 3.2104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: -0.1943 S13: -0.2587
REMARK 3 S21: 0.3685 S22: -0.3069 S23: 0.4913
REMARK 3 S31: 0.6480 S32: -0.3541 S33: 0.3194
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 375 THROUGH 402 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1603 -6.6880 36.4043
REMARK 3 T TENSOR
REMARK 3 T11: 0.2369 T22: 0.5479
REMARK 3 T33: 0.2441 T12: -0.0097
REMARK 3 T13: 0.0045 T23: 0.0765
REMARK 3 L TENSOR
REMARK 3 L11: 5.4617 L22: 6.7497
REMARK 3 L33: 4.9430 L12: -2.7180
REMARK 3 L13: -2.0733 L23: 3.2539
REMARK 3 S TENSOR
REMARK 3 S11: 0.0507 S12: -0.6314 S13: 0.1130
REMARK 3 S21: 0.4870 S22: 0.0260 S23: 0.0731
REMARK 3 S31: 0.0570 S32: -0.0814 S33: -0.0451
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 403 THROUGH 430 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1941 -12.5063 15.3683
REMARK 3 T TENSOR
REMARK 3 T11: 0.3505 T22: 0.1929
REMARK 3 T33: 0.2064 T12: -0.0169
REMARK 3 T13: 0.0322 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 8.6010 L22: 6.9035
REMARK 3 L33: 2.5124 L12: 0.6794
REMARK 3 L13: 1.4945 L23: 3.2331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0082 S12: 0.0955 S13: -0.3716
REMARK 3 S21: -0.4911 S22: 0.0890 S23: 0.0531
REMARK 3 S31: 0.4920 S32: 0.0918 S33: -0.0619
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 431 THROUGH 459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3918 6.7350 9.4789
REMARK 3 T TENSOR
REMARK 3 T11: 0.1731 T22: 0.2644
REMARK 3 T33: 0.2620 T12: -0.0220
REMARK 3 T13: 0.0442 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 5.3254 L22: 8.0489
REMARK 3 L33: 6.5983 L12: -1.0559
REMARK 3 L13: 1.5925 L23: 2.3871
REMARK 3 S TENSOR
REMARK 3 S11: 0.3132 S12: 0.0880 S13: -0.0604
REMARK 3 S21: -0.0594 S22: -0.3481 S23: 0.1971
REMARK 3 S31: 0.2436 S32: -0.2262 S33: 0.0279
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 460 THROUGH 465 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7578 20.8153 14.8208
REMARK 3 T TENSOR
REMARK 3 T11: 0.4662 T22: 0.3636
REMARK 3 T33: 0.6192 T12: 0.0189
REMARK 3 T13: 0.1168 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 6.0103 L22: 5.0320
REMARK 3 L33: 8.3596 L12: 5.3687
REMARK 3 L13: 7.0423 L23: 6.4525
REMARK 3 S TENSOR
REMARK 3 S11: 0.1851 S12: -0.9370 S13: 1.4612
REMARK 3 S21: 1.1620 S22: -0.2397 S23: 1.9930
REMARK 3 S31: -0.0779 S32: -0.4630 S33: 0.0380
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1245 -18.7108 44.6373
REMARK 3 T TENSOR
REMARK 3 T11: 0.6117 T22: 0.6890
REMARK 3 T33: 0.3955 T12: -0.1134
REMARK 3 T13: 0.0479 T23: 0.1107
REMARK 3 L TENSOR
REMARK 3 L11: 1.5828 L22: 6.9060
REMARK 3 L33: 6.5588 L12: -1.7422
REMARK 3 L13: 2.5233 L23: 0.7868
REMARK 3 S TENSOR
REMARK 3 S11: -0.6406 S12: -0.7239 S13: 0.7578
REMARK 3 S21: 0.3116 S22: 0.1570 S23: -0.2881
REMARK 3 S31: -0.4893 S32: 0.8845 S33: 0.4188
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 6 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6964 -2.9976 22.7319
REMARK 3 T TENSOR
REMARK 3 T11: 0.2164 T22: 0.3357
REMARK 3 T33: 0.1455 T12: 0.0105
REMARK 3 T13: 0.0201 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 4.5254 L22: 4.7922
REMARK 3 L33: 2.9634 L12: 3.5903
REMARK 3 L13: -3.3382 L23: -3.7551
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.3250 S13: 0.3949
REMARK 3 S21: -0.1370 S22: 0.0408 S23: 0.2786
REMARK 3 S31: 0.1715 S32: 0.2215 S33: -0.0929
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6082 -0.2158 13.5746
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.2563
REMARK 3 T33: 0.2314 T12: 0.0014
REMARK 3 T13: 0.0436 T23: 0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 2.6766 L22: 4.7690
REMARK 3 L33: 5.9948 L12: 0.2392
REMARK 3 L13: 1.7936 L23: -3.9330
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: -0.0983 S13: 0.0473
REMARK 3 S21: -0.1525 S22: -0.0646 S23: -0.0503
REMARK 3 S31: 0.1616 S32: 0.0057 S33: -0.0964
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 6 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4313 -12.2376 31.9386
REMARK 3 T TENSOR
REMARK 3 T11: 0.2969 T22: 0.3787
REMARK 3 T33: 0.1885 T12: 0.0244
REMARK 3 T13: 0.0299 T23: 0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 4.6280 L22: 4.4023
REMARK 3 L33: 2.9965 L12: 2.4174
REMARK 3 L13: -1.5982 L23: 0.3454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: 0.0825 S13: 0.0237
REMARK 3 S21: 0.3738 S22: -0.0461 S23: 0.2688
REMARK 3 S31: 0.4329 S32: -0.0590 S33: 0.0881
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 16 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8111 -27.0098 47.3473
REMARK 3 T TENSOR
REMARK 3 T11: 0.8180 T22: 0.7444
REMARK 3 T33: 0.5287 T12: -0.1573
REMARK 3 T13: 0.1916 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 5.8550 L22: 8.5412
REMARK 3 L33: 6.7424 L12: -3.6074
REMARK 3 L13: 5.1365 L23: -5.3119
REMARK 3 S TENSOR
REMARK 3 S11: 1.5216 S12: -1.5607 S13: 1.3851
REMARK 3 S21: -0.0455 S22: -0.3121 S23: -0.9144
REMARK 3 S31: 1.8426 S32: -0.0256 S33: -0.9517
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 5KKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222097.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.27046
REMARK 200 MONOCHROMATOR : SI (111)
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 : 110968
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 28.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
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) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.54900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 3350, 0.2 M NACL, 0.1 M
REMARK 280 BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 6150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 316
REMARK 465 GLU A 464
REMARK 465 GLN A 465
REMARK 465 GLY D 316
REMARK 465 PRO D 317
REMARK 465 LEU D 318
REMARK 465 GLY D 319
REMARK 465 SER D 320
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 ILE A 463 CG1 CG2 CD1
REMARK 470 GLN D 465 CG CD OE1 NE2
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 HH TYR D 343 OE2 GLU D 362 1.56
REMARK 500 OP2 DG B 15 O HOH B 101 1.75
REMARK 500 OP2 DG B 12 O HOH B 102 1.88
REMARK 500 OP1 DC E 10 O HOH E 101 2.04
REMARK 500 O HOH D 660 O HOH D 679 2.05
REMARK 500 OP2 DA C 4 O HOH C 101 2.05
REMARK 500 O HOH E 139 O HOH E 141 2.10
REMARK 500 O HOH A 603 O HOH C 138 2.11
REMARK 500 O HOH D 674 O HOH D 678 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT B 1 O3' DT B 1 C3' -0.054
REMARK 500 DG B 5 O3' DG B 5 C3' 0.094
REMARK 500 DC B 7 O3' DC B 7 C3' -0.050
REMARK 500 DG B 12 O3' DG B 12 C3' -0.063
REMARK 500 DC B 13 O3' DC B 13 C3' -0.055
REMARK 500 DG B 16 O3' DG B 16 C3' -0.038
REMARK 500 DC B 17 O3' DC B 17 C3' -0.044
REMARK 500 DA C 7 O3' DA C 7 C3' -0.044
REMARK 500 DC E 9 O3' DC E 9 C3' -0.047
REMARK 500 DG E 12 O3' DG E 12 C3' -0.044
REMARK 500 DC E 13 O3' DC E 13 C3' -0.062
REMARK 500 DG E 15 O3' DG E 15 C3' -0.036
REMARK 500 DC F 6 O3' DC F 6 C3' -0.073
REMARK 500 DA F 7 P DA F 7 OP1 -0.104
REMARK 500 DG F 8 O3' DG F 8 C3' -0.057
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 CYS A 327 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 399 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 399 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 DC B 4 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG B 5 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG B 5 O4' - C1' - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DC B 6 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DT B 11 OP1 - P - OP2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 DT B 11 O5' - P - OP2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DG B 12 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC B 13 O5' - P - OP1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 DC B 13 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC C 6 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG C 10 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 399 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 DG E 5 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC E 7 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA F 4 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG F 5 O3' - P - OP2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 DA F 7 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG F 9 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG F 10 O5' - P - OP2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 DG F 10 O4' - C1' - N9 ANGL. DEV. = 3.9 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 345 -50.94 -122.01
REMARK 500 SER A 461 56.10 39.84
REMARK 500 HIS D 345 -53.23 -120.10
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 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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 324 SG
REMARK 620 2 CYS A 327 SG 128.2
REMARK 620 3 HIS A 340 NE2 107.2 102.2
REMARK 620 4 HIS A 345 NE2 97.6 117.3 101.3
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 353 SG
REMARK 620 2 CYS A 356 SG 123.4
REMARK 620 3 HIS A 369 NE2 107.1 101.1
REMARK 620 4 HIS A 373 NE2 103.2 118.6 100.6
REMARK 620 N 1 2 3
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 381 SG
REMARK 620 2 CYS A 384 SG 123.8
REMARK 620 3 HIS A 397 NE2 111.2 98.4
REMARK 620 4 HIS A 401 NE2 108.3 114.6 96.6
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 409 SG
REMARK 620 2 CYS A 412 SG 118.4
REMARK 620 3 HIS A 425 NE2 110.2 105.3
REMARK 620 4 HIS A 430 NE2 103.6 116.1 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 439 SG
REMARK 620 2 CYS A 442 SG 122.2
REMARK 620 3 HIS A 455 NE2 106.1 101.7
REMARK 620 4 HIS A 460 NE2 102.5 120.1 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 324 SG
REMARK 620 2 CYS D 327 SG 120.7
REMARK 620 3 HIS D 340 NE2 108.1 99.7
REMARK 620 4 HIS D 345 NE2 96.5 124.9 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 353 SG
REMARK 620 2 CYS D 356 SG 125.7
REMARK 620 3 HIS D 369 NE2 108.4 97.7
REMARK 620 4 HIS D 373 NE2 106.1 114.5 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 381 SG
REMARK 620 2 CYS D 384 SG 122.6
REMARK 620 3 HIS D 397 NE2 108.1 99.9
REMARK 620 4 HIS D 401 NE2 110.2 112.5 100.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 409 SG
REMARK 620 2 CYS D 412 SG 116.4
REMARK 620 3 HIS D 425 NE2 109.3 106.0
REMARK 620 4 HIS D 430 NE2 100.6 120.4 103.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 439 SG
REMARK 620 2 CYS D 442 SG 123.2
REMARK 620 3 HIS D 455 NE2 103.4 107.3
REMARK 620 4 HIS D 460 NE2 98.5 122.6 97.7
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 ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 505
DBREF 5KKQ A 321 465 UNP P49711 CTCF_HUMAN 321 465
DBREF 5KKQ B 1 17 PDB 5KKQ 5KKQ 1 17
DBREF 5KKQ C 1 17 PDB 5KKQ 5KKQ 1 17
DBREF 5KKQ D 321 465 UNP P49711 CTCF_HUMAN 321 465
DBREF 5KKQ E 1 17 PDB 5KKQ 5KKQ 1 17
DBREF 5KKQ F 1 17 PDB 5KKQ 5KKQ 1 17
SEQADV 5KKQ GLY A 316 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ PRO A 317 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ LEU A 318 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ GLY A 319 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ SER A 320 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ GLY D 316 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ PRO D 317 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ LEU D 318 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ GLY D 319 UNP P49711 EXPRESSION TAG
SEQADV 5KKQ SER D 320 UNP P49711 EXPRESSION TAG
SEQRES 1 A 150 GLY PRO LEU GLY SER PRO HIS LYS CYS PRO ASP CYS ASP
SEQRES 2 A 150 MET ALA PHE VAL THR SER GLY GLU LEU VAL ARG HIS ARG
SEQRES 3 A 150 ARG TYR LYS HIS THR HIS GLU LYS PRO PHE LYS CYS SER
SEQRES 4 A 150 MET CYS ASP TYR ALA SER VAL GLU VAL SER LYS LEU LYS
SEQRES 5 A 150 ARG HIS ILE ARG SER HIS THR GLY GLU ARG PRO PHE GLN
SEQRES 6 A 150 CYS SER LEU CYS SER TYR ALA SER ARG ASP THR TYR LYS
SEQRES 7 A 150 LEU LYS ARG HIS MET ARG THR HIS SER GLY GLU LYS PRO
SEQRES 8 A 150 TYR GLU CYS TYR ILE CYS HIS ALA ARG PHE THR GLN SER
SEQRES 9 A 150 GLY THR MET LYS MET HIS ILE LEU GLN LYS HIS THR GLU
SEQRES 10 A 150 ASN VAL ALA LYS PHE HIS CYS PRO HIS CYS ASP THR VAL
SEQRES 11 A 150 ILE ALA ARG LYS SER ASP LEU GLY VAL HIS LEU ARG LYS
SEQRES 12 A 150 GLN HIS SER TYR ILE GLU GLN
SEQRES 1 B 17 DT DA DG DC DG DC DC DC DC DC DT DG DC
SEQRES 2 B 17 DT DG DG DC
SEQRES 1 C 17 DG DC DC DA DG DC DA DG DG DG DG DG DC
SEQRES 2 C 17 DG DC DT DA
SEQRES 1 D 150 GLY PRO LEU GLY SER PRO HIS LYS CYS PRO ASP CYS ASP
SEQRES 2 D 150 MET ALA PHE VAL THR SER GLY GLU LEU VAL ARG HIS ARG
SEQRES 3 D 150 ARG TYR LYS HIS THR HIS GLU LYS PRO PHE LYS CYS SER
SEQRES 4 D 150 MET CYS ASP TYR ALA SER VAL GLU VAL SER LYS LEU LYS
SEQRES 5 D 150 ARG HIS ILE ARG SER HIS THR GLY GLU ARG PRO PHE GLN
SEQRES 6 D 150 CYS SER LEU CYS SER TYR ALA SER ARG ASP THR TYR LYS
SEQRES 7 D 150 LEU LYS ARG HIS MET ARG THR HIS SER GLY GLU LYS PRO
SEQRES 8 D 150 TYR GLU CYS TYR ILE CYS HIS ALA ARG PHE THR GLN SER
SEQRES 9 D 150 GLY THR MET LYS MET HIS ILE LEU GLN LYS HIS THR GLU
SEQRES 10 D 150 ASN VAL ALA LYS PHE HIS CYS PRO HIS CYS ASP THR VAL
SEQRES 11 D 150 ILE ALA ARG LYS SER ASP LEU GLY VAL HIS LEU ARG LYS
SEQRES 12 D 150 GLN HIS SER TYR ILE GLU GLN
SEQRES 1 E 17 DT DA DG DC DG DC DC DC DC DC DT DG DC
SEQRES 2 E 17 DT DG DG DC
SEQRES 1 F 17 DG DC DC DA DG DC DA DG DG DG DG DG DC
SEQRES 2 F 17 DG DC DT DA
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET ZN A 504 1
HET ZN A 505 1
HET ZN D 501 1
HET ZN D 502 1
HET ZN D 503 1
HET ZN D 504 1
HET ZN D 505 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 10(ZN 2+)
FORMUL 17 HOH *327(H2 O)
HELIX 1 AA1 THR A 333 HIS A 345 1 13
HELIX 2 AA2 GLU A 362 GLY A 375 1 14
HELIX 3 AA3 ASP A 390 GLY A 403 1 14
HELIX 4 AA4 GLN A 418 HIS A 430 1 13
HELIX 5 AA5 ARG A 448 HIS A 460 1 13
HELIX 6 AA6 THR D 333 HIS D 345 1 13
HELIX 7 AA7 GLU D 362 GLY D 375 1 14
HELIX 8 AA8 ASP D 390 GLY D 403 1 14
HELIX 9 AA9 GLN D 418 THR D 431 1 14
HELIX 10 AB1 ARG D 448 HIS D 460 1 13
SHEET 1 AA1 2 HIS A 322 LYS A 323 0
SHEET 2 AA1 2 ALA A 330 PHE A 331 -1 O PHE A 331 N HIS A 322
SHEET 1 AA2 2 PHE A 351 LYS A 352 0
SHEET 2 AA2 2 ALA A 359 SER A 360 -1 O SER A 360 N PHE A 351
SHEET 1 AA3 2 PHE A 379 GLN A 380 0
SHEET 2 AA3 2 ALA A 387 SER A 388 -1 O SER A 388 N PHE A 379
SHEET 1 AA4 2 TYR A 407 GLU A 408 0
SHEET 2 AA4 2 ARG A 415 PHE A 416 -1 O PHE A 416 N TYR A 407
SHEET 1 AA5 2 PHE A 437 CYS A 439 0
SHEET 2 AA5 2 THR A 444 ILE A 446 -1 O THR A 444 N CYS A 439
SHEET 1 AA6 2 HIS D 322 LYS D 323 0
SHEET 2 AA6 2 ALA D 330 PHE D 331 -1 O PHE D 331 N HIS D 322
SHEET 1 AA7 2 PHE D 351 LYS D 352 0
SHEET 2 AA7 2 ALA D 359 SER D 360 -1 O SER D 360 N PHE D 351
SHEET 1 AA8 2 PHE D 379 GLN D 380 0
SHEET 2 AA8 2 ALA D 387 SER D 388 -1 O SER D 388 N PHE D 379
SHEET 1 AA9 2 TYR D 407 GLU D 408 0
SHEET 2 AA9 2 ARG D 415 PHE D 416 -1 O PHE D 416 N TYR D 407
SHEET 1 AB1 2 PHE D 437 HIS D 438 0
SHEET 2 AB1 2 VAL D 445 ILE D 446 -1 O ILE D 446 N PHE D 437
LINK SG CYS A 324 ZN ZN A 501 1555 1555 2.24
LINK SG CYS A 327 ZN ZN A 501 1555 1555 2.41
LINK NE2 HIS A 340 ZN ZN A 501 1555 1555 2.11
LINK NE2 HIS A 345 ZN ZN A 501 1555 1555 2.04
LINK SG CYS A 353 ZN ZN A 502 1555 1555 2.30
LINK SG CYS A 356 ZN ZN A 502 1555 1555 2.16
LINK NE2 HIS A 369 ZN ZN A 502 1555 1555 2.08
LINK NE2 HIS A 373 ZN ZN A 502 1555 1555 2.00
LINK SG CYS A 381 ZN ZN A 503 1555 1555 2.31
LINK SG CYS A 384 ZN ZN A 503 1555 1555 2.18
LINK NE2 HIS A 397 ZN ZN A 503 1555 1555 2.09
LINK NE2 HIS A 401 ZN ZN A 503 1555 1555 2.09
LINK SG CYS A 409 ZN ZN A 504 1555 1555 2.20
LINK SG CYS A 412 ZN ZN A 504 1555 1555 2.25
LINK NE2 HIS A 425 ZN ZN A 504 1555 1555 2.07
LINK NE2 HIS A 430 ZN ZN A 504 1555 1555 2.11
LINK SG CYS A 439 ZN ZN A 505 1555 1555 2.28
LINK SG CYS A 442 ZN ZN A 505 1555 1555 2.15
LINK NE2 HIS A 455 ZN ZN A 505 1555 1555 2.02
LINK NE2 HIS A 460 ZN ZN A 505 1555 1555 2.02
LINK SG CYS D 324 ZN ZN D 501 1555 1555 2.16
LINK SG CYS D 327 ZN ZN D 501 1555 1555 2.34
LINK NE2 HIS D 340 ZN ZN D 501 1555 1555 2.13
LINK NE2 HIS D 345 ZN ZN D 501 1555 1555 1.95
LINK SG CYS D 353 ZN ZN D 502 1555 1555 2.25
LINK SG CYS D 356 ZN ZN D 502 1555 1555 2.31
LINK NE2 HIS D 369 ZN ZN D 502 1555 1555 2.06
LINK NE2 HIS D 373 ZN ZN D 502 1555 1555 2.03
LINK SG CYS D 381 ZN ZN D 503 1555 1555 2.23
LINK SG CYS D 384 ZN ZN D 503 1555 1555 2.19
LINK NE2 HIS D 397 ZN ZN D 503 1555 1555 2.08
LINK NE2 HIS D 401 ZN ZN D 503 1555 1555 2.07
LINK SG CYS D 409 ZN ZN D 504 1555 1555 2.34
LINK SG CYS D 412 ZN ZN D 504 1555 1555 2.25
LINK NE2 HIS D 425 ZN ZN D 504 1555 1555 2.10
LINK NE2 HIS D 430 ZN ZN D 504 1555 1555 2.08
LINK SG CYS D 439 ZN ZN D 505 1555 1555 2.28
LINK SG CYS D 442 ZN ZN D 505 1555 1555 2.28
LINK NE2 HIS D 455 ZN ZN D 505 1555 1555 2.11
LINK NE2 HIS D 460 ZN ZN D 505 1555 1555 2.05
SITE 1 AC1 4 CYS A 324 CYS A 327 HIS A 340 HIS A 345
SITE 1 AC2 4 CYS A 353 CYS A 356 HIS A 369 HIS A 373
SITE 1 AC3 4 CYS A 381 CYS A 384 HIS A 397 HIS A 401
SITE 1 AC4 4 CYS A 409 CYS A 412 HIS A 425 HIS A 430
SITE 1 AC5 4 CYS A 439 CYS A 442 HIS A 455 HIS A 460
SITE 1 AC6 4 CYS D 324 CYS D 327 HIS D 340 HIS D 345
SITE 1 AC7 4 CYS D 353 CYS D 356 HIS D 369 HIS D 373
SITE 1 AC8 4 CYS D 381 CYS D 384 HIS D 397 HIS D 401
SITE 1 AC9 4 CYS D 409 CYS D 412 HIS D 425 HIS D 430
SITE 1 AD1 4 CYS D 439 CYS D 442 HIS D 455 HIS D 460
CRYST1 40.994 44.911 86.797 98.33 92.40 94.80 P 1 2
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 0.024394 0.002048 0.001344 0.00000
SCALE2 0.000000 0.022345 0.003369 0.00000
SCALE3 0.000000 0.000000 0.011662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
