HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-APR-12 4EK9
TITLE CRYSTAL STRUCTURE OF DOT1L IN COMPLEX WITH EPZ000004
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-416;
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: 562
KEYWDS METHYLTRANSFERASE, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JIN
REVDAT 3 13-SEP-23 4EK9 1 REMARK SEQADV
REVDAT 2 09-JAN-13 4EK9 1 JRNL
REVDAT 1 17-OCT-12 4EK9 0
JRNL AUTH A.BASAVAPATHRUNI,L.JIN,S.R.DAIGLE,C.R.MAJER,C.A.THERKELSEN,
JRNL AUTH 2 T.J.WIGLE,K.W.KUNTZ,R.CHESWORTH,R.M.POLLOCK,M.P.SCOTT,
JRNL AUTH 3 M.P.MOYER,V.M.RICHON,R.A.COPELAND,E.J.OLHAVA
JRNL TITL CONFORMATIONAL ADAPTATION DRIVES POTENT, SELECTIVE AND
JRNL TITL 2 DURABLE INHIBITION OF THE HUMAN PROTEIN METHYLTRANSFERASE
JRNL TITL 3 DOT1L.
JRNL REF CHEM.BIOL.DRUG DES. V. 80 971 2012
JRNL REFN ISSN 1747-0277
JRNL PMID 22978415
JRNL DOI 10.1111/CBDD.12050
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 22063
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1189
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1274
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.02000
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): 0.265
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.238
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.201
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.572
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2753 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3734 ; 1.334 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 323 ; 5.930 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 134 ;35.793 ;24.030
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;19.305 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.829 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 400 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2091 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4EK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071723.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : CHANNEL-CUT SI(111)CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23264
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 11.50
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1NW3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 1.8-2.0 M
REMARK 280 AMMONIUM SULFATE, 5 MM TCEP, PH 5.5, VAPOR DIFFUSION, HANGING
REMARK 280 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 34.24667
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 17.12333
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 25.68500
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 8.56167
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 42.80833
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: MONOMERIC
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 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 VAL A 59
REMARK 465 LEU A 60
REMARK 465 ILE A 61
REMARK 465 LYS A 333
REMARK 465 LEU A 334
REMARK 465 ARG A 335
REMARK 465 GLU A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 GLU A 339
REMARK 465 ALA A 340
REMARK 465 ALA A 341
REMARK 465 ARG A 342
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 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 ASN A 99 83.70 -150.65
REMARK 500 SER A 103 156.83 -49.12
REMARK 500 ILE A 151 42.91 -107.25
REMARK 500 LYS A 152 123.92 -25.24
REMARK 500 SER A 302 102.75 -164.73
REMARK 500 SER A 304 -159.80 -80.92
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 EP4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QOW RELATED DB: PDB
REMARK 900 DOT1L STRCUTRE IN COMPLEX WITH SAM
REMARK 900 RELATED ID: 4EKG RELATED DB: PDB
REMARK 900 RELATED ID: 4EKI RELATED DB: PDB
DBREF 4EK9 A 1 416 UNP Q8TEK3 DOT1L_HUMAN 1 416
SEQADV 4EK9 HIS A -8 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 HIS A -7 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 HIS A -6 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 HIS A -5 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 HIS A -4 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 HIS A -3 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 SER A -2 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 SER A -1 UNP Q8TEK3 EXPRESSION TAG
SEQADV 4EK9 GLY A 0 UNP Q8TEK3 EXPRESSION TAG
SEQRES 1 A 425 HIS HIS HIS HIS HIS HIS SER SER GLY MET GLY GLU LYS
SEQRES 2 A 425 LEU GLU LEU ARG LEU LYS SER PRO VAL GLY ALA GLU PRO
SEQRES 3 A 425 ALA VAL TYR PRO TRP PRO LEU PRO VAL TYR ASP LYS HIS
SEQRES 4 A 425 HIS ASP ALA ALA HIS GLU ILE ILE GLU THR ILE ARG TRP
SEQRES 5 A 425 VAL CYS GLU GLU ILE PRO ASP LEU LYS LEU ALA MET GLU
SEQRES 6 A 425 ASN TYR VAL LEU ILE ASP TYR ASP THR LYS SER PHE GLU
SEQRES 7 A 425 SER MET GLN ARG LEU CYS ASP LYS TYR ASN ARG ALA ILE
SEQRES 8 A 425 ASP SER ILE HIS GLN LEU TRP LYS GLY THR THR GLN PRO
SEQRES 9 A 425 MET LYS LEU ASN THR ARG PRO SER THR GLY LEU LEU ARG
SEQRES 10 A 425 HIS ILE LEU GLN GLN VAL TYR ASN HIS SER VAL THR ASP
SEQRES 11 A 425 PRO GLU LYS LEU ASN ASN TYR GLU PRO PHE SER PRO GLU
SEQRES 12 A 425 VAL TYR GLY GLU THR SER PHE ASP LEU VAL ALA GLN MET
SEQRES 13 A 425 ILE ASP GLU ILE LYS MET THR ASP ASP ASP LEU PHE VAL
SEQRES 14 A 425 ASP LEU GLY SER GLY VAL GLY GLN VAL VAL LEU GLN VAL
SEQRES 15 A 425 ALA ALA ALA THR ASN CYS LYS HIS HIS TYR GLY VAL GLU
SEQRES 16 A 425 LYS ALA ASP ILE PRO ALA LYS TYR ALA GLU THR MET ASP
SEQRES 17 A 425 ARG GLU PHE ARG LYS TRP MET LYS TRP TYR GLY LYS LYS
SEQRES 18 A 425 HIS ALA GLU TYR THR LEU GLU ARG GLY ASP PHE LEU SER
SEQRES 19 A 425 GLU GLU TRP ARG GLU ARG ILE ALA ASN THR SER VAL ILE
SEQRES 20 A 425 PHE VAL ASN ASN PHE ALA PHE GLY PRO GLU VAL ASP HIS
SEQRES 21 A 425 GLN LEU LYS GLU ARG PHE ALA ASN MET LYS GLU GLY GLY
SEQRES 22 A 425 ARG ILE VAL SER SER LYS PRO PHE ALA PRO LEU ASN PHE
SEQRES 23 A 425 ARG ILE ASN SER ARG ASN LEU SER ASP ILE GLY THR ILE
SEQRES 24 A 425 MET ARG VAL VAL GLU LEU SER PRO LEU LYS GLY SER VAL
SEQRES 25 A 425 SER TRP THR GLY LYS PRO VAL SER TYR TYR LEU HIS THR
SEQRES 26 A 425 ILE ASP ARG THR ILE LEU GLU ASN TYR PHE SER SER LEU
SEQRES 27 A 425 LYS ASN PRO LYS LEU ARG GLU GLU GLN GLU ALA ALA ARG
SEQRES 28 A 425 ARG ARG GLN GLN ARG GLU SER LYS SER ASN ALA ALA THR
SEQRES 29 A 425 PRO THR LYS GLY PRO GLU GLY LYS VAL ALA GLY PRO ALA
SEQRES 30 A 425 ASP ALA PRO MET ASP SER GLY ALA GLU GLU GLU LYS ALA
SEQRES 31 A 425 GLY ALA ALA THR VAL LYS LYS PRO SER PRO SER LYS ALA
SEQRES 32 A 425 ARG LYS LYS LYS LEU ASN LYS LYS GLY ARG LYS MET ALA
SEQRES 33 A 425 GLY ARG LYS ARG GLY ARG PRO LYS LYS
HET EP4 A 501 21
HET SO4 A 502 5
HET SO4 A 503 5
HET GOL A 504 6
HETNAM EP4 5'-DEOXY-5'-(DIMETHYLAMINO)ADENOSINE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EP4 C12 H18 N6 O3
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *42(H2 O)
HELIX 1 1 ALA A 33 ILE A 48 1 16
HELIX 2 2 ILE A 48 ASN A 57 1 10
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 5 7
HELIX 6 6 SER A 140 ILE A 151 1 12
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 ASN A 234 1 10
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 SER A 328 1 10
HELIX 13 13 LEU A 329 ASN A 331 5 3
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 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 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 TYR A 313 N SER A 268
SHEET 7 C 7 MET A 291 GLU A 295 -1 N ARG A 292 O THR A 316
CISPEP 1 TRP A 22 PRO A 23 0 -5.97
SITE 1 AC1 12 PRO A 133 GLU A 134 VAL A 135 GLY A 137
SITE 2 AC1 12 GLY A 163 GLU A 186 LYS A 187 GLY A 221
SITE 3 AC1 12 ASP A 222 PHE A 223 ASN A 241 HOH A 641
SITE 1 AC2 3 SER A 140 PHE A 141 ASP A 142
SITE 1 AC3 1 THR A 104
SITE 1 AC4 5 VAL A 160 TYR A 183 ARG A 231 ASN A 234
SITE 2 AC4 5 THR A 235
CRYST1 152.810 152.810 51.370 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 0.006544 0.003778 0.000000 0.00000
SCALE2 0.000000 0.007556 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019467 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
