HEADER TRANSFERASE 11-FEB-11 3QOX
TITLE DOT1L STRUCTURE IN COMPLEX WITH SAH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE;
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 H3K79 METHYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JIN
REVDAT 3 21-FEB-24 3QOX 1 REMARK SEQADV
REVDAT 2 10-AUG-11 3QOX 1 JRNL VERSN
REVDAT 1 25-MAY-11 3QOX 0
JRNL AUTH V.M.RICHON,D.JOHNSTON,C.J.SNEERINGER,L.JIN,C.R.MAJER,
JRNL AUTH 2 K.ELLISTON,L.F.JERVA,M.P.SCOTT,R.A.COPELAND
JRNL TITL CHEMOGENETIC ANALYSIS OF HUMAN PROTEIN METHYLTRANSFERASES.
JRNL REF CHEM.BIOL.DRUG DES. V. 78 199 2011
JRNL REFN ISSN 1747-0277
JRNL PMID 21564555
JRNL DOI 10.1111/J.1747-0285.2011.01135.X
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29158
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1549
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2133
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2625
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.37000
REMARK 3 B12 (A**2) : -0.12000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.837
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2739 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3720 ; 1.185 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 5.426 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;34.156 ;24.091
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 459 ;15.542 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;15.745 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 398 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2083 ; 0.005 ; 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): 1635 ; 0.748 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2647 ; 1.445 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1104 ; 1.802 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1073 ; 3.115 ; 4.500
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 : 1.40
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 3QOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063918.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 30726
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 44.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.37600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 2 MM TCEP, 0.1 M
REMARK 280 SODIUM ACETATE, PH 5.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 34.20667
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 17.10333
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 25.65500
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 8.55167
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 42.75833
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 MET A -9
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 TYR A 58
REMARK 465 VAL A 59
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 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 GLU A 56 CG CD OE1 OE2
REMARK 470 LEU A 60 CG CD1 CD2
REMARK 470 ILE A 61 CG1 CG2 CD1
REMARK 470 TYR A 63 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 66 CG CD CE NZ
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 THR A 306 OG1 CG2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 421
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QOW RELATED DB: PDB
REMARK 900 DOT1L STRUCTURE IN COMPLEX WITH SAM
DBREF 3QOX A 1 416 UNP Q8TEK3 DOT1L_HUMAN 1 416
SEQADV 3QOX MET A -9 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -8 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -7 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -6 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -5 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -4 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX HIS A -3 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX SER A -2 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX SER A -1 UNP Q8TEK3 EXPRESSION TAG
SEQADV 3QOX GLY A 0 UNP Q8TEK3 EXPRESSION TAG
SEQRES 1 A 426 MET HIS HIS HIS HIS HIS HIS SER SER GLY MET GLY GLU
SEQRES 2 A 426 LYS LEU GLU LEU ARG LEU LYS SER PRO VAL GLY ALA GLU
SEQRES 3 A 426 PRO ALA VAL TYR PRO TRP PRO LEU PRO VAL TYR ASP LYS
SEQRES 4 A 426 HIS HIS ASP ALA ALA HIS GLU ILE ILE GLU THR ILE ARG
SEQRES 5 A 426 TRP VAL CYS GLU GLU ILE PRO ASP LEU LYS LEU ALA MET
SEQRES 6 A 426 GLU ASN TYR VAL LEU ILE ASP TYR ASP THR LYS SER PHE
SEQRES 7 A 426 GLU SER MET GLN ARG LEU CYS ASP LYS TYR ASN ARG ALA
SEQRES 8 A 426 ILE ASP SER ILE HIS GLN LEU TRP LYS GLY THR THR GLN
SEQRES 9 A 426 PRO MET LYS LEU ASN THR ARG PRO SER THR GLY LEU LEU
SEQRES 10 A 426 ARG HIS ILE LEU GLN GLN VAL TYR ASN HIS SER VAL THR
SEQRES 11 A 426 ASP PRO GLU LYS LEU ASN ASN TYR GLU PRO PHE SER PRO
SEQRES 12 A 426 GLU VAL TYR GLY GLU THR SER PHE ASP LEU VAL ALA GLN
SEQRES 13 A 426 MET ILE ASP GLU ILE LYS MET THR ASP ASP ASP LEU PHE
SEQRES 14 A 426 VAL ASP LEU GLY SER GLY VAL GLY GLN VAL VAL LEU GLN
SEQRES 15 A 426 VAL ALA ALA ALA THR ASN CYS LYS HIS HIS TYR GLY VAL
SEQRES 16 A 426 GLU LYS ALA ASP ILE PRO ALA LYS TYR ALA GLU THR MET
SEQRES 17 A 426 ASP ARG GLU PHE ARG LYS TRP MET LYS TRP TYR GLY LYS
SEQRES 18 A 426 LYS HIS ALA GLU TYR THR LEU GLU ARG GLY ASP PHE LEU
SEQRES 19 A 426 SER GLU GLU TRP ARG GLU ARG ILE ALA ASN THR SER VAL
SEQRES 20 A 426 ILE PHE VAL ASN ASN PHE ALA PHE GLY PRO GLU VAL ASP
SEQRES 21 A 426 HIS GLN LEU LYS GLU ARG PHE ALA ASN MET LYS GLU GLY
SEQRES 22 A 426 GLY ARG ILE VAL SER SER LYS PRO PHE ALA PRO LEU ASN
SEQRES 23 A 426 PHE ARG ILE ASN SER ARG ASN LEU SER ASP ILE GLY THR
SEQRES 24 A 426 ILE MET ARG VAL VAL GLU LEU SER PRO LEU LYS GLY SER
SEQRES 25 A 426 VAL SER TRP THR GLY LYS PRO VAL SER TYR TYR LEU HIS
SEQRES 26 A 426 THR ILE ASP ARG THR ILE LEU GLU ASN TYR PHE SER SER
SEQRES 27 A 426 LEU LYS ASN PRO LYS LEU ARG GLU GLU GLN GLU ALA ALA
SEQRES 28 A 426 ARG ARG ARG GLN GLN ARG GLU SER LYS SER ASN ALA ALA
SEQRES 29 A 426 THR PRO THR LYS GLY PRO GLU GLY LYS VAL ALA GLY PRO
SEQRES 30 A 426 ALA ASP ALA PRO MET ASP SER GLY ALA GLU GLU GLU LYS
SEQRES 31 A 426 ALA GLY ALA ALA THR VAL LYS LYS PRO SER PRO SER LYS
SEQRES 32 A 426 ALA ARG LYS LYS LYS LEU ASN LYS LYS GLY ARG LYS MET
SEQRES 33 A 426 ALA GLY ARG LYS ARG GLY ARG PRO LYS LYS
HET SAH A 417 26
HET SO4 A 418 5
HET SO4 A 419 5
HET SO4 A 420 5
HET SO4 A 421 5
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM SO4 SULFATE ION
FORMUL 2 SAH C14 H20 N6 O5 S
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *102(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 TRP A 89 1 23
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 LEU A 329 1 11
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 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 TYR A 313 N SER A 268
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 -0.72
SITE 1 AC1 20 PRO A 133 GLY A 137 GLU A 138 THR A 139
SITE 2 AC1 20 ASP A 161 GLY A 163 SER A 164 GLN A 168
SITE 3 AC1 20 GLU A 186 LYS A 187 GLY A 221 ASP A 222
SITE 4 AC1 20 PHE A 223 PHE A 239 ASN A 241 PHE A 245
SITE 5 AC1 20 HOH A 426 HOH A 473 HOH A 482 HOH A 486
SITE 1 AC2 4 ARG A 203 LYS A 207 HIS A 213 HOH A 441
SITE 1 AC3 4 HIS A 117 GLU A 201 LYS A 204 HOH A 514
SITE 1 AC4 2 THR A 100 ARG A 101
SITE 1 AC5 4 ARG A 229 GLN A 252 GLU A 255 ARG A 256
CRYST1 152.710 152.710 51.310 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 0.006548 0.003781 0.000000 0.00000
SCALE2 0.000000 0.007561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END