HEADER TRANSFERASE/PEPTIDE 13-FEB-13 4J7I
TITLE SET7/9Y335F IN COMPLEX WITH TAF10 PEPTIDE AND ADOHCY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE SETD7, H3-K4-HMTASE SETD7,
COMPND 5 LYSINE N-METHYLTRANSFERASE 7, SET DOMAIN-CONTAINING PROTEIN 7,
COMPND 6 SET7/9;
COMPND 7 EC: 2.1.1.43;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 10;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: STAF28, TRANSCRIPTION INITIATION FACTOR TFIID 30 KDA
COMPND 14 SUBUNIT, TAF(II)30, TAFII-30, TAFII30;
COMPND 15 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: SETD7, KIAA1717, KMT7, SET7, SET9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 OTHER_DETAILS: SYNTHETICALLY PRODUCED PEPTIDE
KEYWDS SET DOMAIN, LYSINE METHYLTRANSFERASE, TRANSFERASE-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HOROWITZ,R.C.TRIEVEL
REVDAT 2 28-FEB-24 4J7I 1 REMARK SEQADV
REVDAT 1 08-JAN-14 4J7I 0
JRNL AUTH S.HOROWITZ,L.M.DIRK,J.D.YESSELMAN,J.S.NIMTZ,U.ADHIKARI,
JRNL AUTH 2 R.A.MEHL,S.SCHEINER,R.L.HOUTZ,H.M.AL-HASHIMI,R.C.TRIEVEL
JRNL TITL CONSERVATION AND FUNCTIONAL IMPORTANCE OF CARBON-OXYGEN
JRNL TITL 2 HYDROGEN BONDING IN ADOMET-DEPENDENT METHYLTRANSFERASES.
JRNL REF J.AM.CHEM.SOC. V. 135 15536 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 24093804
JRNL DOI 10.1021/JA407140K
REMARK 2
REMARK 2 RESOLUTION. 2.56 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) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 11539
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 584
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) : 2.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 613
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 40
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1834
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.88000
REMARK 3 B22 (A**2) : 1.88000
REMARK 3 B33 (A**2) : -2.82000
REMARK 3 B12 (A**2) : 0.94000
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): 0.359
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.923
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1913 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2616 ; 1.378 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 247 ; 7.657 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;38.063 ;23.919
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 249 ;14.909 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ; 9.103 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 293 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1477 ; 0.008 ; 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 4J7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11539
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
REMARK 200 RESOLUTION RANGE LOW (A) : 71.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 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 (%): 60.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, IMIDAZOLE, NICKEL
REMARK 280 CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 63.51200
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 31.75600
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 31.75600
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 63.51200
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -31.75600
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 106
REMARK 465 ALA A 107
REMARK 465 MET A 108
REMARK 465 GLY A 109
REMARK 465 TYR A 110
REMARK 465 LYS A 111
REMARK 465 ASP A 112
REMARK 465 ASN A 113
REMARK 465 ILE A 114
REMARK 465 ARG A 115
REMARK 465 HIS A 116
REMARK 465 PRO A 342
REMARK 465 GLY A 343
REMARK 465 LYS A 344
REMARK 465 SER A 345
REMARK 465 GLY A 346
REMARK 465 LYS A 366
REMARK 465 ACE B 185
REMARK 465 LYS B 192
REMARK 465 TYR B 193
REMARK 465 THR B 194
REMARK 465 LEU B 195
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 135 CG CD OE1 OE2
REMARK 470 ASP A 136 CG OD1 OD2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 166 CG CD OE1 OE2
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 THR A 175 OG1 CG2
REMARK 470 SER A 189 OG
REMARK 470 HIS A 192 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 198 CA CB OG
REMARK 470 SER A 213 OG
REMARK 470 GLU A 214 CG CD OE1 OE2
REMARK 470 VAL A 218 CG1 CG2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 SER A 224 OG
REMARK 470 SER A 225 OG
REMARK 470 SER A 232 OG
REMARK 470 GLN A 253 CG CD OE1 NE2
REMARK 470 SER A 257 OG
REMARK 470 ASP A 259 CG OD1 OD2
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 GLU A 272 CG CD OE1 OE2
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 ARG A 323 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 326 CG CD OE1 OE2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 HIS A 339 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 351 CG CD OE1 OE2
REMARK 470 GLN A 354 CG CD OE1 NE2
REMARK 470 GLU A 356 CG CD OE1 OE2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 GLN A 361 CG CD OE1 NE2
REMARK 470 THR A 363 OG1 CG2
REMARK 470 GLN A 364 CG CD OE1 NE2
REMARK 470 GLN A 365 CG CD OE1 NE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 ARG B 191 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 283 CG HIS A 283 CD2 0.054
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 ARG A 152 -55.38 -121.96
REMARK 500 SER A 174 -179.04 -178.98
REMARK 500 SER A 189 89.59 -68.07
REMARK 500 ASP A 194 50.17 -144.87
REMARK 500 SER A 199 -23.60 -153.93
REMARK 500 LEU A 269 -61.26 -95.14
REMARK 500 ASP A 270 -159.05 -141.14
REMARK 500 CYS A 288 23.94 -147.79
REMARK 500 THR A 300 62.91 -117.77
REMARK 500 ILE A 316 -157.18 -134.69
REMARK 500 LYS B 187 51.16 -91.46
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 SAH A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M53 RELATED DB: PDB
REMARK 900 RELATED ID: 4J7F RELATED DB: PDB
REMARK 900 RELATED ID: 4J83 RELATED DB: PDB
REMARK 900 RELATED ID: 4J8O RELATED DB: PDB
DBREF 4J7I A 110 366 UNP Q8WTS6 SETD7_HUMAN 110 366
DBREF 4J7I B 186 195 UNP Q12962 TAF10_HUMAN 186 195
SEQADV 4J7I GLY A 106 UNP Q8WTS6 EXPRESSION TAG
SEQADV 4J7I ALA A 107 UNP Q8WTS6 EXPRESSION TAG
SEQADV 4J7I MET A 108 UNP Q8WTS6 EXPRESSION TAG
SEQADV 4J7I GLY A 109 UNP Q8WTS6 EXPRESSION TAG
SEQADV 4J7I PHE A 335 UNP Q8WTS6 TYR 335 ENGINEERED MUTATION
SEQADV 4J7I ACE B 185 UNP Q12962 EXPRESSION TAG
SEQRES 1 A 261 GLY ALA MET GLY TYR LYS ASP ASN ILE ARG HIS GLY VAL
SEQRES 2 A 261 CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY
SEQRES 3 A 261 GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU LYS ILE
SEQRES 4 A 261 ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY
SEQRES 5 A 261 LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS LEU ALA
SEQRES 6 A 261 THR LEU MET SER THR GLU GLU GLY ARG PRO HIS PHE GLU
SEQRES 7 A 261 LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER
SEQRES 8 A 261 THR SER SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP
SEQRES 9 A 261 PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU
SEQRES 10 A 261 ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA
SEQRES 11 A 261 VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN GLY VAL
SEQRES 12 A 261 ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA
SEQRES 13 A 261 LEU ASN GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL
SEQRES 14 A 261 ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR
SEQRES 15 A 261 CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR
SEQRES 16 A 261 PRO ASN CYS ILE TYR ASP MET PHE VAL HIS PRO ARG PHE
SEQRES 17 A 261 GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU
SEQRES 18 A 261 ALA ASP GLU GLU LEU THR VAL ALA PHE GLY TYR ASP HIS
SEQRES 19 A 261 SER PRO PRO GLY LYS SER GLY PRO GLU ALA PRO GLU TRP
SEQRES 20 A 261 TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA THR GLN GLN
SEQRES 21 A 261 LYS
SEQRES 1 B 11 ACE SER LYS SER LYS ASP ARG LYS TYR THR LEU
HET SAH A 800 26
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 3 SAH C14 H20 N6 O5 S
FORMUL 4 HOH *5(H2 O)
HELIX 1 1 ASP A 209 ARG A 215 1 7
HELIX 2 2 THR A 251 SER A 257 1 7
HELIX 3 3 ARG A 258 ASN A 263 5 6
HELIX 4 4 LEU A 291 ALA A 295 5 5
HELIX 5 5 PRO A 350 GLN A 365 1 16
SHEET 1 A 6 CYS A 119 TYR A 122 0
SHEET 2 A 6 SER A 128 GLY A 131 -1 O LEU A 129 N ILE A 121
SHEET 3 A 6 GLY A 141 VAL A 147 -1 O VAL A 147 N SER A 128
SHEET 4 A 6 THR A 153 ILE A 160 -1 O GLY A 157 N ILE A 144
SHEET 5 A 6 GLU A 163 GLU A 176 -1 O LYS A 168 N TYR A 156
SHEET 6 A 6 ARG A 179 LEU A 184 -1 O HIS A 181 N MET A 173
SHEET 1 B 6 CYS A 119 TYR A 122 0
SHEET 2 B 6 SER A 128 GLY A 131 -1 O LEU A 129 N ILE A 121
SHEET 3 B 6 GLY A 141 VAL A 147 -1 O VAL A 147 N SER A 128
SHEET 4 B 6 THR A 153 ILE A 160 -1 O GLY A 157 N ILE A 144
SHEET 5 B 6 GLU A 163 GLU A 176 -1 O LYS A 168 N TYR A 156
SHEET 6 B 6 VAL A 190 TYR A 191 -1 O TYR A 191 N GLY A 167
SHEET 1 C 4 VAL A 216 GLU A 220 0
SHEET 2 C 4 GLU A 228 SER A 232 -1 O GLY A 229 N ALA A 219
SHEET 3 C 4 GLU A 330 VAL A 333 -1 O LEU A 331 N LEU A 230
SHEET 4 C 4 ASN A 296 HIS A 297 1 N ASN A 296 O VAL A 333
SHEET 1 D 3 VAL A 241 TYR A 245 0
SHEET 2 D 3 GLY A 314 THR A 321 -1 O ILE A 319 N MET A 242
SHEET 3 D 3 CYS A 303 HIS A 310 -1 N PHE A 308 O ILE A 316
SHEET 1 E 3 VAL A 248 ILE A 250 0
SHEET 2 E 3 VAL A 274 ASP A 276 -1 O VAL A 274 N ILE A 250
SHEET 3 E 3 LEU A 267 SER A 268 -1 N LEU A 267 O ILE A 275
CISPEP 1 GLU A 279 PRO A 280 0 7.81
SITE 1 AC1 9 ALA A 226 GLU A 228 GLY A 264 ASN A 265
SITE 2 AC1 9 HIS A 293 LYS A 294 ASN A 296 HIS A 297
SITE 3 AC1 9 TRP A 352
CRYST1 82.305 82.305 95.268 90.00 90.00 120.00 P 32 2 1 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 0.012150 0.007015 0.000000 0.00000
SCALE2 0.000000 0.014030 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010497 0.00000
(ATOM LINES ARE NOT SHOWN.)
END