HEADER TRANSFERASE 02-DEC-11 3UWP
TITLE CRYSTAL STRUCTURE OF DOT1L IN COMPLEX WITH 5-IODOTUBERCIDIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-420;
COMPND 5 SYNONYM: DOT1-LIKE PROTEIN, HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-
COMPND 6 HMTASE, LYSINE N-METHYLTRANSFERASE 4;
COMPND 7 EC: 2.1.1.43;
COMPND 8 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: DOT1L, KIAA1814, KMT4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS HISTONE, METHYLTRANSFERASE, EPIGENETICS, TUBERCIDIN, STRUCTURAL
KEYWDS 2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.YU,W.TEMPEL,D.SMIL,M.SCHAPIRA,Y.LI,M.VEDADI,K.T.NGUYEN,
AUTHOR 2 A.K.WERNIMONT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,
AUTHOR 3 P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 28-FEB-24 3UWP 1 REMARK SEQADV LINK
REVDAT 3 16-MAY-18 3UWP 1 JRNL
REVDAT 2 08-NOV-17 3UWP 1 REMARK
REVDAT 1 14-MAR-12 3UWP 0
JRNL AUTH W.YU,E.J.CHORY,A.K.WERNIMONT,W.TEMPEL,A.SCOPTON,
JRNL AUTH 2 A.FEDERATION,J.J.MARINEAU,J.QI,D.BARSYTE-LOVEJOY,J.YI,
JRNL AUTH 3 R.MARCELLUS,R.E.IACOB,J.R.ENGEN,C.GRIFFIN,A.AMAN,
JRNL AUTH 4 E.WIENHOLDS,F.LI,J.PINEDA,G.ESTIU,T.SHATSEVA,T.HAJIAN,
JRNL AUTH 5 R.AL-AWAR,J.E.DICK,M.VEDADI,P.J.BROWN,C.H.ARROWSMITH,
JRNL AUTH 6 J.E.BRADNER,M.SCHAPIRA
JRNL TITL CATALYTIC SITE REMODELLING OF THE DOT1L METHYLTRANSFERASE BY
JRNL TITL 2 SELECTIVE INHIBITORS.
JRNL REF NAT COMMUN V. 3 1288 2012
JRNL REFN ESSN 2041-1723
JRNL PMID 23250418
JRNL DOI 10.1038/NCOMMS2304
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 43105
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : FROM PDB ENTRY 3QOW
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.853
REMARK 3 FREE R VALUE TEST SET COUNT : 2092
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2785
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2669
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.95900
REMARK 3 B22 (A**2) : -1.95900
REMARK 3 B33 (A**2) : 2.93900
REMARK 3 B12 (A**2) : -0.98000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.927
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2808 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1851 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3839 ; 1.327 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4498 ; 0.879 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 352 ; 5.435 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;32.233 ;23.769
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 439 ;13.411 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.800 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3161 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 588 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 344
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1790 58.3140 3.2350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0182 T22: 0.0205
REMARK 3 T33: 0.0396 T12: 0.0071
REMARK 3 T13: 0.0015 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 3.6851 L22: 1.2583
REMARK 3 L33: 0.4925 L12: -1.4903
REMARK 3 L13: 0.0403 L23: -0.1079
REMARK 3 S TENSOR
REMARK 3 S11: -0.0168 S12: 0.0761 S13: -0.0151
REMARK 3 S21: -0.0469 S22: -0.0137 S23: 0.0620
REMARK 3 S31: 0.0572 S32: -0.0295 S33: 0.0305
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3UWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91963
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43269
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.97300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.68067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.84033
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 26.76050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.92017
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.60083
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 MET A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 345
REMARK 465 GLN A 346
REMARK 465 ARG A 347
REMARK 465 GLU A 348
REMARK 465 SER A 349
REMARK 465 LYS A 350
REMARK 465 SER A 351
REMARK 465 ASN A 352
REMARK 465 ALA A 353
REMARK 465 ALA A 354
REMARK 465 THR A 355
REMARK 465 PRO A 356
REMARK 465 THR A 357
REMARK 465 LYS A 358
REMARK 465 GLY A 359
REMARK 465 PRO A 360
REMARK 465 GLU A 361
REMARK 465 GLY A 362
REMARK 465 LYS A 363
REMARK 465 VAL A 364
REMARK 465 ALA A 365
REMARK 465 GLY A 366
REMARK 465 PRO A 367
REMARK 465 ALA A 368
REMARK 465 ASP A 369
REMARK 465 ALA A 370
REMARK 465 PRO A 371
REMARK 465 MET A 372
REMARK 465 ASP A 373
REMARK 465 SER A 374
REMARK 465 GLY A 375
REMARK 465 ALA A 376
REMARK 465 GLU A 377
REMARK 465 GLU A 378
REMARK 465 GLU A 379
REMARK 465 LYS A 380
REMARK 465 ALA A 381
REMARK 465 GLY A 382
REMARK 465 ALA A 383
REMARK 465 ALA A 384
REMARK 465 THR A 385
REMARK 465 VAL A 386
REMARK 465 LYS A 387
REMARK 465 LYS A 388
REMARK 465 PRO A 389
REMARK 465 SER A 390
REMARK 465 PRO A 391
REMARK 465 SER A 392
REMARK 465 LYS A 393
REMARK 465 ALA A 394
REMARK 465 ARG A 395
REMARK 465 LYS A 396
REMARK 465 LYS A 397
REMARK 465 LYS A 398
REMARK 465 LEU A 399
REMARK 465 ASN A 400
REMARK 465 LYS A 401
REMARK 465 LYS A 402
REMARK 465 GLY A 403
REMARK 465 ARG A 404
REMARK 465 LYS A 405
REMARK 465 MET A 406
REMARK 465 ALA A 407
REMARK 465 GLY A 408
REMARK 465 ARG A 409
REMARK 465 LYS A 410
REMARK 465 ARG A 411
REMARK 465 GLY A 412
REMARK 465 ARG A 413
REMARK 465 PRO A 414
REMARK 465 LYS A 415
REMARK 465 LYS A 416
REMARK 465 MET A 417
REMARK 465 ASN A 418
REMARK 465 THR A 419
REMARK 465 ALA A 420
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 LYS A 4 CG CD CE NZ
REMARK 470 LYS A 29 CD CE NZ
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 ILE A 61 CG1 CG2 CD1
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 LYS A 77 CD CE NZ
REMARK 470 GLN A 94 CG CD OE1 NE2
REMARK 470 LYS A 97 CD CE NZ
REMARK 470 ASN A 99 CG OD1 ND2
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 LYS A 152 CE NZ
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 LYS A 187 CE NZ
REMARK 470 ASP A 189 CG OD1 OD2
REMARK 470 LYS A 193 CD CE NZ
REMARK 470 LYS A 207 CD CE NZ
REMARK 470 LYS A 212 CD CE NZ
REMARK 470 GLU A 227 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLU A 248 CD OE1 OE2
REMARK 470 LYS A 261 NZ
REMARK 470 ARG A 278 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 282 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LYS A 308 CE NZ
REMARK 470 LYS A 333 NZ
REMARK 470 GLU A 336 CD OE1 OE2
REMARK 470 GLU A 337 CG CD OE1 OE2
REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 343 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 344 CG CD NE CZ NH1 NH2
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 ASP A 28 -167.93 -163.29
REMARK 500 THR A 139 -85.47 -138.76
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 NA A 424 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 52 O
REMARK 620 2 LEU A 53 O 79.0
REMARK 620 3 MET A 55 O 85.6 89.5
REMARK 620 4 ASN A 57 OD1 84.0 162.2 84.0
REMARK 620 5 HOH A 480 O 174.1 100.1 88.6 96.2
REMARK 620 6 HOH A 481 O 100.1 89.0 173.7 99.2 85.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5ID A 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 424
DBREF 3UWP A 1 420 UNP Q8TEK3 DOT1L_HUMAN 1 420
SEQADV 3UWP MET A -17 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -16 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -15 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -14 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -13 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -12 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP HIS A -11 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP SER A -10 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP SER A -9 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP GLY A -8 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP ARG A -7 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP GLU A -6 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP ASN A -5 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP LEU A -4 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP TYR A -3 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP PHE A -2 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP GLN A -1 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3UWP GLY A 0 UNP Q8TEK3 EXPRESSION TAG
SEQRES 1 A 438 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 438 LEU TYR PHE GLN GLY MET GLY GLU LYS LEU GLU LEU ARG
SEQRES 3 A 438 LEU LYS SER PRO VAL GLY ALA GLU PRO ALA VAL TYR PRO
SEQRES 4 A 438 TRP PRO LEU PRO VAL TYR ASP LYS HIS HIS ASP ALA ALA
SEQRES 5 A 438 HIS GLU ILE ILE GLU THR ILE ARG TRP VAL CYS GLU GLU
SEQRES 6 A 438 ILE PRO ASP LEU LYS LEU ALA MET GLU ASN TYR VAL LEU
SEQRES 7 A 438 ILE ASP TYR ASP THR LYS SER PHE GLU SER MET GLN ARG
SEQRES 8 A 438 LEU CYS ASP LYS TYR ASN ARG ALA ILE ASP SER ILE HIS
SEQRES 9 A 438 GLN LEU TRP LYS GLY THR THR GLN PRO MET LYS LEU ASN
SEQRES 10 A 438 THR ARG PRO SER THR GLY LEU LEU ARG HIS ILE LEU GLN
SEQRES 11 A 438 GLN VAL TYR ASN HIS SER VAL THR ASP PRO GLU LYS LEU
SEQRES 12 A 438 ASN ASN TYR GLU PRO PHE SER PRO GLU VAL TYR GLY GLU
SEQRES 13 A 438 THR SER PHE ASP LEU VAL ALA GLN MET ILE ASP GLU ILE
SEQRES 14 A 438 LYS MET THR ASP ASP ASP LEU PHE VAL ASP LEU GLY SER
SEQRES 15 A 438 GLY VAL GLY GLN VAL VAL LEU GLN VAL ALA ALA ALA THR
SEQRES 16 A 438 ASN CYS LYS HIS HIS TYR GLY VAL GLU LYS ALA ASP ILE
SEQRES 17 A 438 PRO ALA LYS TYR ALA GLU THR MET ASP ARG GLU PHE ARG
SEQRES 18 A 438 LYS TRP MET LYS TRP TYR GLY LYS LYS HIS ALA GLU TYR
SEQRES 19 A 438 THR LEU GLU ARG GLY ASP PHE LEU SER GLU GLU TRP ARG
SEQRES 20 A 438 GLU ARG ILE ALA ASN THR SER VAL ILE PHE VAL ASN ASN
SEQRES 21 A 438 PHE ALA PHE GLY PRO GLU VAL ASP HIS GLN LEU LYS GLU
SEQRES 22 A 438 ARG PHE ALA ASN MET LYS GLU GLY GLY ARG ILE VAL SER
SEQRES 23 A 438 SER LYS PRO PHE ALA PRO LEU ASN PHE ARG ILE ASN SER
SEQRES 24 A 438 ARG ASN LEU SER ASP ILE GLY THR ILE MET ARG VAL VAL
SEQRES 25 A 438 GLU LEU SER PRO LEU LYS GLY SER VAL SER TRP THR GLY
SEQRES 26 A 438 LYS PRO VAL SER TYR TYR LEU HIS THR ILE ASP ARG THR
SEQRES 27 A 438 ILE LEU GLU ASN TYR PHE SER SER LEU LYS ASN PRO LYS
SEQRES 28 A 438 LEU ARG GLU GLU GLN GLU ALA ALA ARG ARG ARG GLN GLN
SEQRES 29 A 438 ARG GLU SER LYS SER ASN ALA ALA THR PRO THR LYS GLY
SEQRES 30 A 438 PRO GLU GLY LYS VAL ALA GLY PRO ALA ASP ALA PRO MET
SEQRES 31 A 438 ASP SER GLY ALA GLU GLU GLU LYS ALA GLY ALA ALA THR
SEQRES 32 A 438 VAL LYS LYS PRO SER PRO SER LYS ALA ARG LYS LYS LYS
SEQRES 33 A 438 LEU ASN LYS LYS GLY ARG LYS MET ALA GLY ARG LYS ARG
SEQRES 34 A 438 GLY ARG PRO LYS LYS MET ASN THR ALA
HET 5ID A 421 20
HET IOD A 422 1
HET IOD A 423 1
HET NA A 424 1
HET UNX A 425 1
HET UNX A 426 1
HET UNX A 427 1
HET UNX A 428 1
HET UNX A 429 1
HET UNX A 430 1
HETNAM 5ID (2R,3R,4S,5R)-2-(4-AMINO-5-IODO-7H-PYRROLO[2,3-
HETNAM 2 5ID D]PYRIMIDIN-7-YL)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-3,
HETNAM 3 5ID 4-DIOL
HETNAM IOD IODIDE ION
HETNAM NA SODIUM ION
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN 5ID 5-IODOTUBERCIDIN
FORMUL 2 5ID C11 H13 I N4 O4
FORMUL 3 IOD 2(I 1-)
FORMUL 5 NA NA 1+
FORMUL 6 UNX 6(X)
FORMUL 12 HOH *66(H2 O)
HELIX 1 1 ALA A 33 ILE A 48 1 16
HELIX 2 2 ILE A 48 MET A 55 1 8
HELIX 3 3 GLU A 56 TYR A 63 5 8
HELIX 4 4 SER A 67 GLY A 91 1 25
HELIX 5 5 SER A 103 VAL A 119 1 17
HELIX 6 6 ASP A 121 LEU A 125 5 5
HELIX 7 7 SER A 132 GLU A 138 5 7
HELIX 8 8 THR A 139 LYS A 152 1 14
HELIX 9 9 GLY A 167 THR A 177 1 11
HELIX 10 10 ALA A 188 GLY A 210 1 23
HELIX 11 11 SER A 225 ASN A 234 1 10
HELIX 12 12 GLY A 246 ALA A 258 1 13
HELIX 13 13 ASP A 286 THR A 289 5 4
HELIX 14 14 ARG A 319 ASN A 331 1 13
HELIX 15 15 ASN A 331 ARG A 343 1 13
SHEET 1 A 2 GLU A 6 LEU A 9 0
SHEET 2 A 2 ALA A 18 PRO A 21 -1 O TYR A 20 N LEU A 7
SHEET 1 B 2 VAL A 26 ASP A 28 0
SHEET 2 B 2 HIS A 31 ASP A 32 -1 O HIS A 31 N TYR A 27
SHEET 1 C 7 GLU A 215 ARG A 220 0
SHEET 2 C 7 HIS A 181 GLU A 186 1 N GLY A 184 O GLU A 219
SHEET 3 C 7 LEU A 158 LEU A 162 1 N ASP A 161 O TYR A 183
SHEET 4 C 7 VAL A 237 VAL A 240 1 O PHE A 239 N VAL A 160
SHEET 5 C 7 ARG A 265 SER A 268 1 O VAL A 267 N ILE A 238
SHEET 6 C 7 TYR A 313 ILE A 317 -1 O HIS A 315 N ILE A 266
SHEET 7 C 7 MET A 291 GLU A 295 -1 N VAL A 294 O LEU A 314
LINK O LYS A 52 NA NA A 424 1555 1555 2.57
LINK O LEU A 53 NA NA A 424 1555 1555 2.74
LINK O MET A 55 NA NA A 424 1555 1555 2.33
LINK OD1 ASN A 57 NA NA A 424 1555 1555 2.35
LINK NA NA A 424 O HOH A 480 1555 1555 2.37
LINK NA NA A 424 O HOH A 481 1555 1555 2.34
CISPEP 1 TRP A 22 PRO A 23 0 -0.12
SITE 1 AC1 10 TYR A 58 GLU A 129 GLY A 163 GLU A 186
SITE 2 AC1 10 LYS A 187 GLY A 221 ASP A 222 PHE A 223
SITE 3 AC1 10 ASN A 241 IOD A 422
SITE 1 AC2 1 5ID A 421
SITE 1 AC3 2 GLY A 246 VAL A 249
SITE 1 AC4 6 LYS A 52 LEU A 53 MET A 55 ASN A 57
SITE 2 AC4 6 HOH A 480 HOH A 481
CRYST1 149.784 149.784 53.521 90.00 90.00 120.00 P 65 6
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 0.006676 0.003855 0.000000 0.00000
SCALE2 0.000000 0.007709 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018684 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
