HEADER TRANSFERASE/TRANSFERASE INHIBITOR 19-APR-12 4ER7
TITLE CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR SGC0947
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DOT1-LIKE PROTEIN, HISTONE H3-K79 METHYLTRANSFERASE, H3-K79-
COMPND 5 HMTASE, LYSINE N-METHYLTRANSFERASE 4;
COMPND 6 EC: 2.1.1.43;
COMPND 7 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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 V2R PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS HISTONE, METHYLTRANSFERASE, EPIGENETICS, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.WERNIMONT,W.TEMPEL,W.YU,A.SCOPTON,Y.LI,K.T.NGUYEN,M.VEDADI,
AUTHOR 2 J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 3 P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 16-MAY-12 4ER7 0
JRNL AUTH A.K.WERNIMONT,W.TEMPEL,W.YU,A.SCOPTON,Y.LI,K.T.NGUYEN,
JRNL AUTH 2 M.VEDADI,J.E.BRADNER,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 3 C.BOUNTRA,P.J.BROWN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN DOT1L IN COMPLEX WITH INHIBITOR
JRNL TITL 2 SGC0947
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 34923
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1722
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2407
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 132
REMARK 3 BIN FREE R VALUE : 0.3930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2540
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.64000
REMARK 3 B22 (A**2) : -0.64000
REMARK 3 B33 (A**2) : 0.96000
REMARK 3 B12 (A**2) : -0.32000
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): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.670
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2775 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1838 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3790 ; 1.380 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4482 ; 0.971 ; 3.011
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 341 ; 5.455 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;32.692 ;23.884
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 437 ;14.180 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.020 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 414 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3103 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 570 ; 0.002 ; 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): 1682 ; 0.926 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 668 ; 0.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2723 ; 1.756 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1093 ; 2.097 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1067 ; 3.447 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 4ER7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071968.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-11
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 : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979310
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34959
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.233
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.40
REMARK 200 R MERGE FOR SHELL (I) : 0.83500
REMARK 200 R SYM FOR SHELL (I) : 0.83500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: RIGID BODY REFINEMENT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5 M NAFORMATE, 0.1 M NAACET, PH 4.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 35.20000
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 17.60000
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 26.40000
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 8.80000
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 44.00000
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL MOLECULE IS UNKNOWN.
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 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 56
REMARK 465 ASN A 57
REMARK 465 TYR A 58
REMARK 465 VAL A 59
REMARK 465 LEU A 60
REMARK 465 PRO A 130
REMARK 465 PHE A 131
REMARK 465 SER A 132
REMARK 465 PRO A 133
REMARK 465 GLU A 134
REMARK 465 VAL A 135
REMARK 465 TYR A 136
REMARK 465 GLY A 137
REMARK 465 ARG A 343
REMARK 465 ARG A 344
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 ILE A 61 CG1 CG2 CD1
REMARK 470 ASP A 62 CG OD1 OD2
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 ARG A 73 CG CD NE CZ NH1 NH2
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 CD CE NZ
REMARK 470 ASN A 127 CG OD1 ND2
REMARK 470 TYR A 128 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 THR A 139 OG1 CG2
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 ASP A 156 CG OD1 OD2
REMARK 470 GLN A 168 OE1 NE2
REMARK 470 LYS A 180 CD CE NZ
REMARK 470 LYS A 187 CE NZ
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 ARG A 220 CD NE CZ NH1 NH2
REMARK 470 GLU A 230 CD OE1 OE2
REMARK 470 GLU A 248 CD OE1 OE2
REMARK 470 GLU A 255 CD OE1 OE2
REMARK 470 LYS A 261 CE NZ
REMARK 470 ARG A 278 CD NE CZ NH1 NH2
REMARK 470 ARG A 282 CD NE CZ NH1 NH2
REMARK 470 LYS A 300 CD CE NZ
REMARK 470 LYS A 308 CE NZ
REMARK 470 GLU A 337 CD OE1 OE2
REMARK 470 ARG A 342 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 -169.44 -160.35
REMARK 500 ASP A 62 32.25 -89.85
REMARK 500 ASN A 99 11.56 57.59
REMARK 500 ASN A 127 5.58 -68.72
REMARK 500 ASN A 276 69.59 -111.91
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 AW3 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EQZ RELATED DB: PDB
REMARK 900 RELATED ID: 4ER0 RELATED DB: PDB
REMARK 900 RELATED ID: 4ER3 RELATED DB: PDB
REMARK 900 RELATED ID: 4ER5 RELATED DB: PDB
REMARK 900 RELATED ID: 4ER6 RELATED DB: PDB
DBREF 4ER7 A 1 420 UNP Q8TEK3 DOT1L_HUMAN 1 420
SEQADV 4ER7 GLY A 0 UNP Q8TEK3 EXPRESSION TAG
SEQRES 1 A 421 GLY MET GLY GLU LYS LEU GLU LEU ARG LEU LYS SER PRO
SEQRES 2 A 421 VAL GLY ALA GLU PRO ALA VAL TYR PRO TRP PRO LEU PRO
SEQRES 3 A 421 VAL TYR ASP LYS HIS HIS ASP ALA ALA HIS GLU ILE ILE
SEQRES 4 A 421 GLU THR ILE ARG TRP VAL CYS GLU GLU ILE PRO ASP LEU
SEQRES 5 A 421 LYS LEU ALA MET GLU ASN TYR VAL LEU ILE ASP TYR ASP
SEQRES 6 A 421 THR LYS SER PHE GLU SER MET GLN ARG LEU CYS ASP LYS
SEQRES 7 A 421 TYR ASN ARG ALA ILE ASP SER ILE HIS GLN LEU TRP LYS
SEQRES 8 A 421 GLY THR THR GLN PRO MET LYS LEU ASN THR ARG PRO SER
SEQRES 9 A 421 THR GLY LEU LEU ARG HIS ILE LEU GLN GLN VAL TYR ASN
SEQRES 10 A 421 HIS SER VAL THR ASP PRO GLU LYS LEU ASN ASN TYR GLU
SEQRES 11 A 421 PRO PHE SER PRO GLU VAL TYR GLY GLU THR SER PHE ASP
SEQRES 12 A 421 LEU VAL ALA GLN MET ILE ASP GLU ILE LYS MET THR ASP
SEQRES 13 A 421 ASP ASP LEU PHE VAL ASP LEU GLY SER GLY VAL GLY GLN
SEQRES 14 A 421 VAL VAL LEU GLN VAL ALA ALA ALA THR ASN CYS LYS HIS
SEQRES 15 A 421 HIS TYR GLY VAL GLU LYS ALA ASP ILE PRO ALA LYS TYR
SEQRES 16 A 421 ALA GLU THR MET ASP ARG GLU PHE ARG LYS TRP MET LYS
SEQRES 17 A 421 TRP TYR GLY LYS LYS HIS ALA GLU TYR THR LEU GLU ARG
SEQRES 18 A 421 GLY ASP PHE LEU SER GLU GLU TRP ARG GLU ARG ILE ALA
SEQRES 19 A 421 ASN THR SER VAL ILE PHE VAL ASN ASN PHE ALA PHE GLY
SEQRES 20 A 421 PRO GLU VAL ASP HIS GLN LEU LYS GLU ARG PHE ALA ASN
SEQRES 21 A 421 MET LYS GLU GLY GLY ARG ILE VAL SER SER LYS PRO PHE
SEQRES 22 A 421 ALA PRO LEU ASN PHE ARG ILE ASN SER ARG ASN LEU SER
SEQRES 23 A 421 ASP ILE GLY THR ILE MET ARG VAL VAL GLU LEU SER PRO
SEQRES 24 A 421 LEU LYS GLY SER VAL SER TRP THR GLY LYS PRO VAL SER
SEQRES 25 A 421 TYR TYR LEU HIS THR ILE ASP ARG THR ILE LEU GLU ASN
SEQRES 26 A 421 TYR PHE SER SER LEU LYS ASN PRO LYS LEU ARG GLU GLU
SEQRES 27 A 421 GLN GLU ALA ALA ARG ARG ARG GLN GLN ARG GLU SER LYS
SEQRES 28 A 421 SER ASN ALA ALA THR PRO THR LYS GLY PRO GLU GLY LYS
SEQRES 29 A 421 VAL ALA GLY PRO ALA ASP ALA PRO MET ASP SER GLY ALA
SEQRES 30 A 421 GLU GLU GLU LYS ALA GLY ALA ALA THR VAL LYS LYS PRO
SEQRES 31 A 421 SER PRO SER LYS ALA ARG LYS LYS LYS LEU ASN LYS LYS
SEQRES 32 A 421 GLY ARG LYS MET ALA GLY ARG LYS ARG GLY ARG PRO LYS
SEQRES 33 A 421 LYS MET ASN THR ALA
HET AW3 A 501 74
HET GOL A 502 6
HETNAM AW3 5-BROMO-7-{5-[(3-{[(4-TERT-BUTYLPHENYL)
HETNAM 2 AW3 CARBAMOYL]AMINO}PROPYL)AMINO]-5-DEOXY-BETA-D-
HETNAM 3 AW3 RIBOFURANOSYL}-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 AW3 C25 H34 BR N7 O4
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *57(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 SER A 67 GLY A 91 1 25
HELIX 4 4 SER A 103 VAL A 119 1 17
HELIX 5 5 ASP A 121 ASN A 127 1 7
HELIX 6 6 THR A 139 ILE A 151 1 13
HELIX 7 7 GLY A 167 THR A 177 1 11
HELIX 8 8 ALA A 188 GLY A 210 1 23
HELIX 9 9 SER A 225 THR A 235 1 11
HELIX 10 10 GLY A 246 ALA A 258 1 13
HELIX 11 11 ASP A 286 THR A 289 5 4
HELIX 12 12 ARG A 319 ASN A 331 1 13
HELIX 13 13 ASN A 331 ARG A 342 1 12
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 ASP A 28
SHEET 1 C 7 TYR A 216 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 PHE A 159 O HIS A 181
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
CISPEP 1 TRP A 22 PRO A 23 0 -4.46
SITE 1 AC1 13 ASP A 161 GLY A 163 SER A 164 VAL A 169
SITE 2 AC1 13 GLU A 186 LYS A 187 GLY A 221 ASP A 222
SITE 3 AC1 13 PHE A 223 PHE A 239 ASN A 241 SER A 268
SITE 4 AC1 13 HOH A 651
SITE 1 AC2 6 ALA A 18 VAL A 19 TYR A 20 HIS A 117
SITE 2 AC2 6 LYS A 204 HOH A 650
CRYST1 150.617 150.617 52.800 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 0.006639 0.003833 0.000000 0.00000
SCALE2 0.000000 0.007666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018939 0.00000
(ATOM LINES ARE NOT SHOWN.)
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