HEADER TRANSFERASE 31-AUG-10 3OPE
TITLE STRUCTURAL BASIS OF AUTO-INHIBITORY MECHANISM OF HISTONE
TITLE 2 METHYLTRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SET DOMAIN (UNP RESIDUES 2074-2293);
COMPND 5 SYNONYM: ABSENT SMALL AND HOMEOTIC DISKS PROTEIN 1 HOMOLOG, ASH1-LIKE
COMPND 6 PROTEIN, HUASH1, LYSINE N-METHYLTRANSFERASE 2H;
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: ASH1L, KIAA1420, KMT2H;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A(MODIFIED)
KEYWDS SET, METHYLTRANSFERASE, NUCLEUS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.AN,J.SONG
REVDAT 4 20-MAR-24 3OPE 1 REMARK LINK
REVDAT 3 11-DEC-19 3OPE 1 REMARK SEQADV SSBOND
REVDAT 2 14-AUG-13 3OPE 1 JRNL VERSN
REVDAT 1 12-JAN-11 3OPE 0
JRNL AUTH S.AN,K.J.YEO,Y.H.JEON,J.SONG
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN HISTONE METHYLTRANSFERASE
JRNL TITL 2 ASH1L CATALYTIC DOMAIN AND ITS IMPLICATIONS FOR THE
JRNL TITL 3 REGULATORY MECHANISM
JRNL REF J.BIOL.CHEM. V. 286 8369 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21239497
JRNL DOI 10.1074/JBC.M110.203380
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 18803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 963
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 27
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 4
REMARK 4 3OPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061406.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2827
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19766
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.62000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BISTRISPROFANE, PEG, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 155.86933
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 77.93467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.93467
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 155.86933
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 2067
REMARK 465 GLY A 2281
REMARK 465 LYS A 2282
REMARK 465 SER A 2283
REMARK 465 GLN A 2284
REMARK 465 ARG A 2285
REMARK 465 VAL A 2286
REMARK 465 ASN A 2287
REMARK 465 GLY A 2288
REMARK 465 GLY B 2067
REMARK 465 GLY B 2085
REMARK 465 TYR B 2086
REMARK 465 GLU B 2087
REMARK 465 ALA B 2088
REMARK 465 THR B 2089
REMARK 465 THR B 2090
REMARK 465 CYS B 2091
REMARK 465 ASN B 2092
REMARK 465 CYS B 2093
REMARK 465 LYS B 2094
REMARK 465 LYS B 2095
REMARK 465 PRO B 2096
REMARK 465 ASP B 2097
REMARK 465 ASP B 2098
REMARK 465 ASP B 2099
REMARK 465 THR B 2100
REMARK 465 ARG B 2101
REMARK 465 LYS B 2102
REMARK 465 GLY B 2103
REMARK 465 GLY B 2280
REMARK 465 GLY B 2281
REMARK 465 LYS B 2282
REMARK 465 SER B 2283
REMARK 465 GLN B 2284
REMARK 465 ARG B 2285
REMARK 465 VAL B 2286
REMARK 465 ASN B 2287
REMARK 465 GLY B 2288
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 SG CYS B 2220 SG CYS B 2270 1.96
REMARK 500 SG CYS A 2104 SG CYS A 2108 1.99
REMARK 500 SG CYS B 2122 SG CYS B 2128 2.04
REMARK 500 SG CYS B 2268 SG CYS B 2275 2.05
REMARK 500 SG CYS A 2093 SG CYS A 2108 2.05
REMARK 500 SG CYS A 2093 SG CYS A 2104 2.06
REMARK 500 SG CYS B 2268 SG CYS B 2270 2.08
REMARK 500 SG CYS B 2220 SG CYS B 2268 2.08
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 PRO B2246 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 CYS B2275 CA - CB - SG ANGL. DEV. = 10.3 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 VAL A2078 -84.26 -75.82
REMARK 500 PRO A2082 39.59 -82.72
REMARK 500 LEU A2083 109.10 -56.00
REMARK 500 GLU A2087 87.52 -69.34
REMARK 500 CYS A2091 -8.05 -53.01
REMARK 500 ASN A2092 -29.92 52.24
REMARK 500 PRO A2096 -141.66 -54.32
REMARK 500 ASP A2097 -24.18 -159.45
REMARK 500 VAL A2105 -162.21 -51.05
REMARK 500 ASP A2107 -112.69 -120.41
REMARK 500 CYS A2108 96.77 51.68
REMARK 500 LEU A2109 -36.99 -24.66
REMARK 500 ASN A2120 30.02 -71.34
REMARK 500 THR A2121 -22.70 -167.79
REMARK 500 GLU A2126 -25.63 -34.35
REMARK 500 GLN A2127 77.91 -106.74
REMARK 500 CYS A2128 -158.95 -118.46
REMARK 500 CYS A2129 9.59 -163.82
REMARK 500 ARG A2135 12.95 -58.27
REMARK 500 HIS A2136 53.94 39.75
REMARK 500 CYS A2141 -38.08 -142.69
REMARK 500 LEU A2142 139.25 -37.97
REMARK 500 GLU A2148 -100.22 5.20
REMARK 500 PRO A2159 171.68 -58.40
REMARK 500 ILE A2167 151.87 179.49
REMARK 500 GLN A2186 -40.71 -140.61
REMARK 500 TYR A2187 33.56 -85.87
REMARK 500 HIS A2188 -84.02 -48.38
REMARK 500 TYR A2194 79.67 -104.61
REMARK 500 CYS A2195 141.59 -177.30
REMARK 500 LEU A2198 -72.71 -106.17
REMARK 500 ASP A2199 143.27 -173.24
REMARK 500 ASN A2211 -165.79 -115.71
REMARK 500 HIS A2258 -59.05 -121.50
REMARK 500 PHE A2260 174.56 -54.62
REMARK 500 GLU A2263 4.55 -66.48
REMARK 500 GLU A2273 -71.57 -41.92
REMARK 500 VAL B2078 -79.34 -79.09
REMARK 500 ASP B2106 -63.87 -132.55
REMARK 500 CYS B2108 107.29 -167.66
REMARK 500 LEU B2109 -8.54 -47.06
REMARK 500 PHE B2114 55.92 71.39
REMARK 500 THR B2121 -16.07 -43.59
REMARK 500 ASN B2130 68.49 -105.30
REMARK 500 GLN B2131 27.81 -160.53
REMARK 500 ARG B2135 26.94 -76.84
REMARK 500 HIS B2136 35.08 28.58
REMARK 500 GLU B2137 53.82 -69.77
REMARK 500 TRP B2138 -160.13 -71.53
REMARK 500 LYS B2150 44.19 -157.10
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
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 ZN A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2220 SG
REMARK 620 2 CYS A2268 SG 115.6
REMARK 620 3 CYS A2270 SG 92.7 105.5
REMARK 620 4 CYS A2275 SG 104.9 111.2 126.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2117 SG
REMARK 620 2 CYS A2122 SG 125.7
REMARK 620 3 CYS A2128 SG 133.9 94.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 4 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2091 SG
REMARK 620 2 CYS A2093 SG 125.8
REMARK 620 3 CYS A2104 SG 113.3 50.3
REMARK 620 4 CYS A2108 SG 157.1 44.6 43.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 3 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2220 SG
REMARK 620 2 CYS B2268 SG 44.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 5 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2117 SG
REMARK 620 2 CYS B2122 SG 109.9
REMARK 620 3 CYS B2128 SG 84.5 52.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 6 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B2104 SG
REMARK 620 2 CYS B2108 SG 126.3
REMARK 620 N 1
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 8
DBREF 3OPE A 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
DBREF 3OPE B 2069 2288 UNP Q9NR48 ASH1L_HUMAN 2074 2293
SEQADV 3OPE GLY A 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 3OPE SER A 2068 UNP Q9NR48 EXPRESSION TAG
SEQADV 3OPE GLY B 2067 UNP Q9NR48 EXPRESSION TAG
SEQADV 3OPE SER B 2068 UNP Q9NR48 EXPRESSION TAG
SEQRES 1 A 222 GLY SER TYR LYS LYS ILE ARG SER ASN VAL TYR VAL ASP
SEQRES 2 A 222 VAL LYS PRO LEU SER GLY TYR GLU ALA THR THR CYS ASN
SEQRES 3 A 222 CYS LYS LYS PRO ASP ASP ASP THR ARG LYS GLY CYS VAL
SEQRES 4 A 222 ASP ASP CYS LEU ASN ARG MET ILE PHE ALA GLU CYS SER
SEQRES 5 A 222 PRO ASN THR CYS PRO CYS GLY GLU GLN CYS CYS ASN GLN
SEQRES 6 A 222 ARG ILE GLN ARG HIS GLU TRP VAL GLN CYS LEU GLU ARG
SEQRES 7 A 222 PHE ARG ALA GLU GLU LYS GLY TRP GLY ILE ARG THR LYS
SEQRES 8 A 222 GLU PRO LEU LYS ALA GLY GLN PHE ILE ILE GLU TYR LEU
SEQRES 9 A 222 GLY GLU VAL VAL SER GLU GLN GLU PHE ARG ASN ARG MET
SEQRES 10 A 222 ILE GLU GLN TYR HIS ASN HIS SER ASP HIS TYR CYS LEU
SEQRES 11 A 222 ASN LEU ASP SER GLY MET VAL ILE ASP SER TYR ARG MET
SEQRES 12 A 222 GLY ASN GLU ALA ARG PHE ILE ASN HIS SER CYS ASP PRO
SEQRES 13 A 222 ASN CYS GLU MET GLN LYS TRP SER VAL ASN GLY VAL TYR
SEQRES 14 A 222 ARG ILE GLY LEU TYR ALA LEU LYS ASP MET PRO ALA GLY
SEQRES 15 A 222 THR GLU LEU THR TYR ASP TYR ASN PHE HIS SER PHE ASN
SEQRES 16 A 222 VAL GLU LYS GLN GLN LEU CYS LYS CYS GLY PHE GLU LYS
SEQRES 17 A 222 CYS ARG GLY ILE ILE GLY GLY LYS SER GLN ARG VAL ASN
SEQRES 18 A 222 GLY
SEQRES 1 B 222 GLY SER TYR LYS LYS ILE ARG SER ASN VAL TYR VAL ASP
SEQRES 2 B 222 VAL LYS PRO LEU SER GLY TYR GLU ALA THR THR CYS ASN
SEQRES 3 B 222 CYS LYS LYS PRO ASP ASP ASP THR ARG LYS GLY CYS VAL
SEQRES 4 B 222 ASP ASP CYS LEU ASN ARG MET ILE PHE ALA GLU CYS SER
SEQRES 5 B 222 PRO ASN THR CYS PRO CYS GLY GLU GLN CYS CYS ASN GLN
SEQRES 6 B 222 ARG ILE GLN ARG HIS GLU TRP VAL GLN CYS LEU GLU ARG
SEQRES 7 B 222 PHE ARG ALA GLU GLU LYS GLY TRP GLY ILE ARG THR LYS
SEQRES 8 B 222 GLU PRO LEU LYS ALA GLY GLN PHE ILE ILE GLU TYR LEU
SEQRES 9 B 222 GLY GLU VAL VAL SER GLU GLN GLU PHE ARG ASN ARG MET
SEQRES 10 B 222 ILE GLU GLN TYR HIS ASN HIS SER ASP HIS TYR CYS LEU
SEQRES 11 B 222 ASN LEU ASP SER GLY MET VAL ILE ASP SER TYR ARG MET
SEQRES 12 B 222 GLY ASN GLU ALA ARG PHE ILE ASN HIS SER CYS ASP PRO
SEQRES 13 B 222 ASN CYS GLU MET GLN LYS TRP SER VAL ASN GLY VAL TYR
SEQRES 14 B 222 ARG ILE GLY LEU TYR ALA LEU LYS ASP MET PRO ALA GLY
SEQRES 15 B 222 THR GLU LEU THR TYR ASP TYR ASN PHE HIS SER PHE ASN
SEQRES 16 B 222 VAL GLU LYS GLN GLN LEU CYS LYS CYS GLY PHE GLU LYS
SEQRES 17 B 222 CYS ARG GLY ILE ILE GLY GLY LYS SER GLN ARG VAL ASN
SEQRES 18 B 222 GLY
HET ZN A 1 1
HET ZN A 2 1
HET ZN A 4 1
HET SAM A 7 27
HET ZN B 3 1
HET ZN B 5 1
HET ZN B 6 1
HET SAM B 8 27
HETNAM ZN ZINC ION
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 3 ZN 6(ZN 2+)
FORMUL 6 SAM 2(C15 H22 N6 O5 S)
FORMUL 11 HOH *27(H2 O)
HELIX 1 1 ASN A 2110 PHE A 2114 5 5
HELIX 2 2 SER A 2175 GLN A 2186 1 12
HELIX 3 3 ASN A 2211 ILE A 2216 5 6
HELIX 4 4 CYS B 2124 CYS B 2128 5 5
HELIX 5 5 SER B 2175 GLN B 2186 1 12
HELIX 6 6 ASN B 2211 ILE B 2216 5 6
HELIX 7 7 ASP B 2254 SER B 2259 1 6
SHEET 1 A 2 LYS A2070 LYS A2071 0
SHEET 2 A 2 MET A2209 GLY A2210 1 O GLY A2210 N LYS A2070
SHEET 1 B 4 VAL A2076 TYR A2077 0
SHEET 2 B 4 GLU A2172 VAL A2174 1 O VAL A2173 N VAL A2076
SHEET 3 B 4 MET A2202 ASP A2205 -1 O ASP A2205 N GLU A2172
SHEET 4 B 4 CYS A2195 ASP A2199 -1 N LEU A2196 O ILE A2204
SHEET 1 C 2 GLU A2143 ARG A2146 0
SHEET 2 C 2 TRP A2152 ARG A2155 -1 O ARG A2155 N GLU A2143
SHEET 1 D 3 PHE A2165 GLU A2168 0
SHEET 2 D 3 VAL A2234 ALA A2241 -1 O LEU A2239 N ILE A2166
SHEET 3 D 3 CYS A2224 VAL A2231 -1 N GLN A2227 O GLY A2238
SHEET 1 E 2 ASN A2217 HIS A2218 0
SHEET 2 E 2 THR A2252 TYR A2253 1 O TYR A2253 N ASN A2217
SHEET 1 F 2 LYS B2070 LYS B2071 0
SHEET 2 F 2 MET B2209 GLY B2210 1 O GLY B2210 N LYS B2070
SHEET 1 G 3 VAL B2076 TYR B2077 0
SHEET 2 G 3 GLU B2172 VAL B2174 1 O VAL B2173 N VAL B2076
SHEET 3 G 3 VAL B2203 ASP B2205 -1 O ASP B2205 N GLU B2172
SHEET 1 H 4 LEU B2142 ARG B2146 0
SHEET 2 H 4 TRP B2152 THR B2156 -1 O ARG B2155 N GLU B2143
SHEET 3 H 4 GLU B2250 TYR B2253 -1 O LEU B2251 N ILE B2154
SHEET 4 H 4 ASN B2217 HIS B2218 1 N ASN B2217 O TYR B2253
SHEET 1 I 3 PHE B2165 GLU B2168 0
SHEET 2 I 3 VAL B2234 ALA B2241 -1 O LEU B2239 N ILE B2167
SHEET 3 I 3 CYS B2224 VAL B2231 -1 N VAL B2231 O VAL B2234
LINK ZN ZN A 1 SG CYS A2220 1555 1555 2.41
LINK ZN ZN A 1 SG CYS A2268 1555 1555 2.52
LINK ZN ZN A 1 SG CYS A2270 1555 1555 2.73
LINK ZN ZN A 1 SG CYS A2275 1555 1555 2.63
LINK ZN ZN A 2 SG CYS A2117 1555 1555 2.55
LINK ZN ZN A 2 SG CYS A2122 1555 1555 2.34
LINK ZN ZN A 2 SG CYS A2128 1555 1555 2.67
LINK ZN ZN A 4 SG CYS A2091 1555 1555 2.77
LINK ZN ZN A 4 SG CYS A2093 1555 1555 2.49
LINK ZN ZN A 4 SG CYS A2104 1555 1555 2.34
LINK ZN ZN A 4 SG CYS A2108 1555 1555 2.85
LINK ZN ZN B 3 SG CYS B2220 1555 1555 2.20
LINK ZN ZN B 3 SG CYS B2268 1555 1555 2.95
LINK ZN ZN B 5 SG CYS B2117 1555 1555 2.75
LINK ZN ZN B 5 SG CYS B2122 1555 1555 2.13
LINK ZN ZN B 5 SG CYS B2128 1555 1555 2.44
LINK ZN ZN B 6 SG CYS B2104 1555 1555 2.78
LINK ZN ZN B 6 SG CYS B2108 1555 1555 2.61
SITE 1 AC1 4 CYS A2220 CYS A2268 CYS A2270 CYS A2275
SITE 1 AC2 5 CYS A2091 CYS A2104 CYS A2117 CYS A2122
SITE 2 AC2 5 CYS A2128
SITE 1 AC3 4 CYS A2091 CYS A2093 CYS A2104 CYS A2108
SITE 1 AC4 13 LYS A2150 GLY A2151 TRP A2152 ASP A2192
SITE 2 AC4 13 HIS A2193 TYR A2194 ARG A2214 ASN A2217
SITE 3 AC4 13 HIS A2218 GLN A2266 LEU A2267 CYS A2268
SITE 4 AC4 13 LYS A2269
SITE 1 AC5 4 CYS B2220 CYS B2268 CYS B2275 GLY B2277
SITE 1 AC6 4 ZN B 6 CYS B2117 CYS B2122 CYS B2128
SITE 1 AC7 3 ZN B 5 CYS B2104 CYS B2108
SITE 1 AC8 15 LYS B2150 GLY B2151 TRP B2152 ASP B2192
SITE 2 AC8 15 HIS B2193 TYR B2194 ARG B2214 PHE B2215
SITE 3 AC8 15 ASN B2217 HIS B2218 TYR B2255 GLN B2266
SITE 4 AC8 15 LEU B2267 LYS B2269 ILE B2279
CRYST1 59.530 59.530 233.804 90.00 90.00 120.00 P 32 2 1 12
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 0.016798 0.009698 0.000000 0.00000
SCALE2 0.000000 0.019397 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004277 0.00000
(ATOM LINES ARE NOT SHOWN.)
END