HEADER TRANSFERASE 23-NOV-17 6BPI
TITLE CRYSTAL STRUCTURE OF SETDB1 TUDOR DOMAIN WITH ARYL TRIAZOLE FRAGMENT
TITLE 2 PEPTIDE CONJUGATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TUDOR DOMAIN;
COMPND 5 SYNONYM: ERG-ASSOCIATED PROTEIN WITH SET DOMAIN,ESET,HISTONE H3-K9
COMPND 6 METHYLTRANSFERASE 4,H3-K9-HMTASE 4,LYSINE N-METHYLTRANSFERASE 1E,SET
COMPND 7 DOMAIN BIFURCATED 1;
COMPND 8 EC: 2.1.1.43;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: MLY-SER-THR-E2G;
COMPND 12 CHAIN: B;
COMPND 13 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: SETDB1, KIAA0067, KMT1E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS SETDB1 TUDOR, FRAGMENT HITS, EPIGENETICS, METHYL LYSINE READER,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MADER,R.MENDOZA-SANCHEZ,A.DONG,E.DOBROVETSKY,A.IQBAL,V.CORLESS,
AUTHOR 2 W.TEMPEL,S.K.LIEW,D.SMIL,C.C.DELA SENA,S.KENNEDY,D.B.DIAZ,
AUTHOR 3 M.SCHAPIRA,M.VEDADI,P.J.BROWN,V.SANTHAKUMAR,S.FRYE,C.BOUNTRA,
AUTHOR 4 A.M.EDWARDS,A.K.YUDIN,C.H.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 5 (SGC)
REVDAT 1 27-DEC-17 6BPI 0
JRNL AUTH P.MADER,R.MENDOZA-SANCHEZ,A.DONG,E.DOBROVETSKY,A.IQBAL,
JRNL AUTH 2 V.CORLESS,W.TEMPEL,S.K.LIEW,D.SMIL,C.C.DELA SENA,S.KENNEDY,
JRNL AUTH 3 D.B.DIAZ,M.SCHAPIRA,M.VEDADI,P.J.BROWN,V.SANTHAKUMAR,S.FRYE,
JRNL AUTH 4 C.BOUNTRA,A.M.EDWARDS,A.K.YUDIN,C.H.ARROWSMITH,
JRNL AUTH 5 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF SETDB1 TUDOR DOMAIN WITH ARYL TRIAZOLE
JRNL TITL 2 FRAGMENT PEPTIDE CONJUGATES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29574
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 917
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2158
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.3580
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1715
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.71000
REMARK 3 B33 (A**2) : 0.69000
REMARK 3 B12 (A**2) : 0.00000
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.793
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1959 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1790 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2673 ; 1.355 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4138 ; 0.876 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 241 ; 6.702 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;30.554 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 326 ;11.715 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.128 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 279 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2219 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 455 ; 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): 916 ; 1.533 ; 2.385
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 917 ; 1.532 ; 2.385
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1163 ; 2.501 ; 3.565
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1164 ; 2.500 ; 3.565
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1043 ; 1.924 ; 2.644
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1044 ; 1.924 ; 2.644
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1507 ; 3.099 ; 3.891
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2177 ; 5.454 ;27.685
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2177 ; 5.449 ;27.668
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6BPI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30573
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.64500
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M LISO4, 0.1M BIS
REMARK 280 -TRIS PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 27.36550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.79500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.87800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.79500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.36550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.87800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 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 271
REMARK 465 ASN A 272
REMARK 465 GLN A 273
REMARK 465 SER A 400
REMARK 465 MET A 401
REMARK 465 LYS A 402
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 215 CD CE NZ
REMARK 470 VAL A 224 CG1
REMARK 470 LYS A 231 NZ
REMARK 470 LYS A 233 NZ
REMARK 470 ASN A 236 CG OD1 ND2
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 LYS A 239 CE NZ
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 ASP A 270 CA C O CB CG OD1 OD2
REMARK 470 VAL A 274 CG1 CG2
REMARK 470 LYS A 288 CD CE NZ
REMARK 470 LYS A 290 CE NZ
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 LYS A 364 CD CE NZ
REMARK 470 MET A 398 CG SD CE
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 ARG A 315 NE - CZ - NH2 ANGL. DEV. = -3.0 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 SER A 201 -12.58 94.09
REMARK 500 SER A 201 -11.00 94.09
REMARK 500 LYS A 211 1.23 80.14
REMARK 500 ASN A 236 -79.41 -88.64
REMARK 500 ASP A 250 53.40 -90.41
REMARK 500 MET A 398 57.92 -103.71
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 SO4 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 SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand E2G B 4 bound to THR B 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6AU2 RELATED DB: PDB
REMARK 900 RELATED ID: 6AU3 RELATED DB: PDB
DBREF 6BPI A 196 402 UNP Q15047 SETB1_HUMAN 196 402
DBREF 6BPI B 1 4 PDB 6BPI 6BPI 1 4
SEQADV 6BPI GLU A 190 UNP Q15047 EXPRESSION TAG
SEQADV 6BPI ASN A 191 UNP Q15047 EXPRESSION TAG
SEQADV 6BPI LEU A 192 UNP Q15047 EXPRESSION TAG
SEQADV 6BPI TYR A 193 UNP Q15047 EXPRESSION TAG
SEQADV 6BPI PHE A 194 UNP Q15047 EXPRESSION TAG
SEQADV 6BPI GLN A 195 UNP Q15047 EXPRESSION TAG
SEQRES 1 A 213 GLU ASN LEU TYR PHE GLN GLY ASP LEU ILE VAL SER MET
SEQRES 2 A 213 ARG ILE LEU GLY LYS LYS ARG THR LYS THR TRP HIS LYS
SEQRES 3 A 213 GLY THR LEU ILE ALA ILE GLN THR VAL GLY PRO GLY LYS
SEQRES 4 A 213 LYS TYR LYS VAL LYS PHE ASP ASN LYS GLY LYS SER LEU
SEQRES 5 A 213 LEU SER GLY ASN HIS ILE ALA TYR ASP TYR HIS PRO PRO
SEQRES 6 A 213 ALA ASP LYS LEU TYR VAL GLY SER ARG VAL VAL ALA LYS
SEQRES 7 A 213 TYR LYS ASP GLY ASN GLN VAL TRP LEU TYR ALA GLY ILE
SEQRES 8 A 213 VAL ALA GLU THR PRO ASN VAL LYS ASN LYS LEU ARG PHE
SEQRES 9 A 213 LEU ILE PHE PHE ASP ASP GLY TYR ALA SER TYR VAL THR
SEQRES 10 A 213 GLN SER GLU LEU TYR PRO ILE CYS ARG PRO LEU LYS LYS
SEQRES 11 A 213 THR TRP GLU ASP ILE GLU ASP ILE SER CYS ARG ASP PHE
SEQRES 12 A 213 ILE GLU GLU TYR VAL THR ALA TYR PRO ASN ARG PRO MET
SEQRES 13 A 213 VAL LEU LEU LYS SER GLY GLN LEU ILE LYS THR GLU TRP
SEQRES 14 A 213 GLU GLY THR TRP TRP LYS SER ARG VAL GLU GLU VAL ASP
SEQRES 15 A 213 GLY SER LEU VAL ARG ILE LEU PHE LEU ASP ASP LYS ARG
SEQRES 16 A 213 CYS GLU TRP ILE TYR ARG GLY SER THR ARG LEU GLU PRO
SEQRES 17 A 213 MET PHE SER MET LYS
SEQRES 1 B 4 MLY SER THR E2G
HET MLY B 1 11
HET E2G B 4 23
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET UNX A 508 1
HET UNX A 509 1
HET UNX A 510 1
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM E2G (2R)-N-[(4-{2-[(ACETYLAMINO)METHYL]PHENYL}-5-METHYL-4H-
HETNAM 2 E2G 1,2,4-TRIAZOL-3-YL)METHYL]-2-AMINO-2-HYDROXYACETAMIDE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MLY C8 H18 N2 O2
FORMUL 2 E2G C15 H20 N6 O3
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 EDO 3(C2 H6 O2)
FORMUL 10 UNX 3(X)
FORMUL 13 HOH *156(H2 O)
HELIX 1 AA1 PRO A 254 LEU A 258 5 5
HELIX 2 AA2 ASN A 286 LYS A 290 5 5
HELIX 3 AA3 THR A 306 SER A 308 5 3
HELIX 4 AA4 LYS A 319 ILE A 324 5 6
HELIX 5 AA5 ASP A 326 TYR A 340 1 15
SHEET 1 AA1 4 ASN A 191 LEU A 192 0
SHEET 2 AA1 4 TRP A 213 VAL A 224 -1 O ILE A 221 N LEU A 192
SHEET 3 AA1 4 GLY A 227 PHE A 234 -1 O LYS A 231 N ILE A 219
SHEET 4 AA1 4 LYS A 239 SER A 243 -1 O LEU A 242 N TYR A 230
SHEET 1 AA2 4 ASN A 191 LEU A 192 0
SHEET 2 AA2 4 TRP A 213 VAL A 224 -1 O ILE A 221 N LEU A 192
SHEET 3 AA2 4 ARG A 203 LYS A 207 -1 N ILE A 204 O GLY A 216
SHEET 4 AA2 4 ILE A 247 ALA A 248 -1 O ALA A 248 N LEU A 205
SHEET 1 AA3 2 PHE A 194 GLN A 195 0
SHEET 2 AA3 2 LEU A 198 ILE A 199 -1 O LEU A 198 N GLN A 195
SHEET 1 AA4 5 ALA A 302 VAL A 305 0
SHEET 2 AA4 5 PHE A 293 PHE A 297 -1 N ILE A 295 O SER A 303
SHEET 3 AA4 5 TRP A 275 GLU A 283 -1 N ALA A 282 O LEU A 294
SHEET 4 AA4 5 ARG A 263 TYR A 268 -1 N TYR A 268 O TRP A 275
SHEET 5 AA4 5 LEU A 310 PRO A 312 -1 O TYR A 311 N VAL A 265
SHEET 1 AA5 5 ARG A 384 TYR A 389 0
SHEET 2 AA5 5 LEU A 374 PHE A 379 -1 N ILE A 377 O GLU A 386
SHEET 3 AA5 5 THR A 361 ASP A 371 -1 N GLU A 368 O ARG A 376
SHEET 4 AA5 5 LEU A 353 TRP A 358 -1 N THR A 356 O TRP A 363
SHEET 5 AA5 5 LEU A 395 GLU A 396 -1 O GLU A 396 N LYS A 355
LINK C MLY B 1 N SER B 2 1555 1555 1.33
LINK C THR B 3 N E2G B 4 1555 1555 1.34
CISPEP 1 TYR A 340 PRO A 341 0 10.86
SITE 1 AC1 8 LYS A 229 LEU A 241 LEU A 242 SER A 243
SITE 2 AC1 8 HIS A 246 EDO A 506 HOH A 633 HOH A 726
SITE 1 AC2 5 HIS A 214 LYS A 215 HOH A 625 HOH A 629
SITE 2 AC2 5 HOH A 653
SITE 1 AC3 4 ARG A 203 ASP A 250 LYS A 383 HOH A 627
SITE 1 AC4 2 ARG A 384 MLY B 1
SITE 1 AC5 8 TYR A 193 SER A 262 PRO A 316 THR A 320
SITE 2 AC5 8 HOH A 630 HOH A 631 HOH A 677 HOH A 689
SITE 1 AC6 7 LYS A 207 LYS A 208 ARG A 209 LYS A 211
SITE 2 AC6 7 HIS A 246 SO4 A 501 HOH A 667
SITE 1 AC7 7 GLU A 322 ARG A 330 LEU A 348 LYS A 349
SITE 2 AC7 7 VAL A 370 HOH A 657 HOH A 659
SITE 1 AC8 14 GLY A 300 ALA A 302 CYS A 329 PHE A 332
SITE 2 AC8 14 GLU A 386 TRP A 387 ILE A 388 TYR A 389
SITE 3 AC8 14 SER A 392 ARG A 394 HOH A 636 SER B 2
SITE 4 AC8 14 THR B 3 HOH B 102
CRYST1 54.731 63.756 69.590 90.00 90.00 90.00 P 21 21 21 4
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 0.018271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
