HEADER TRANSFERASE 30-AUG-17 6AU2
TITLE CRYSTAL STRUCTURE OF SETDB1 TUDOR DOMAIN WITH ARYL TRIAZOLE FRAGMENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TUDOR DOMAIN (196-402);
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
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)-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL
KEYWDS SETDB1 TUDOR, FRAGMENT HITS, EPIGENETICS, METHYLLYSINE READER,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MADER,R.MENDOZA-SANCHEZ,A.IQBAL,A.DONG,E.DOBROVETSKY,V.B.CORLESS,
AUTHOR 2 S.K.LIEW,W.TEMPEL,D.SMIL,C.C.DELA SENA,S.KENNEDY,D.DIAZ,A.HOLOWNIA,
AUTHOR 3 M.VEDADI,P.J.BROWN,V.SANTHAKUMAR,C.BOUNTRA,A.M.EDWARDS,A.K.YUDIN,
AUTHOR 4 C.H.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 16-OCT-19 6AU2 1 JRNL
REVDAT 1 11-OCT-17 6AU2 0
JRNL AUTH P.MADER,R.MENDOZA-SANCHEZ,A.IQBAL,A.DONG,E.DOBROVETSKY,
JRNL AUTH 2 V.B.CORLESS,S.K.LIEW,S.R.HOULISTON,R.F.DE FREITAS,D.SMIL,
JRNL AUTH 3 C.C.D.SENA,S.KENNEDY,D.B.DIAZ,H.WU,L.DOMBROVSKI,
JRNL AUTH 4 A.ALLALI-HASSANI,J.MIN,M.SCHAPIRA,M.VEDADI,P.J.BROWN,
JRNL AUTH 5 V.SANTHAKUMAR,A.K.YUDIN,C.H.ARROWSMITH
JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF THE FIRST FRAGMENT
JRNL TITL 2 HITS FOR SETDB1 TUDOR DOMAIN.
JRNL REF BIOORG.MED.CHEM. V. 27 3866 2019
JRNL REFN ESSN 1464-3391
JRNL PMID 31327677
JRNL DOI 10.1016/J.BMC.2019.07.020
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30025
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 949
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2142
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1704
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : -0.03000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.703
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1916 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1769 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2602 ; 1.463 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4097 ; 0.914 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 235 ; 6.537 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;28.296 ;22.771
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 327 ;10.981 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.662 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 275 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2153 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 427 ; 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): 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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6AU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000229741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-14
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31031
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
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 : 6.800
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.77300
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 (%): 49.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M LISO4, 0.1M BIS-TRIS
REMARK 280 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 27.60100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.92950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.63650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.92950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.60100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.63650
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: 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 ASP A 270
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 CE NZ
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 LYS A 257 CE NZ
REMARK 470 LYS A 267 CD CE NZ
REMARK 470 LYS A 269 CG CD CE NZ
REMARK 470 LYS A 288 CD CE NZ
REMARK 470 GLU A 325 CD OE1 OE2
REMARK 470 LYS A 355 CE NZ
REMARK 470 LYS A 364 CE NZ
REMARK 470 SER A 400 O
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 -16.77 96.50
REMARK 500 SER A 201 0.87 90.86
REMARK 500 LYS A 237 -13.86 81.77
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 CGJ A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BME A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BME 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 SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 514
DBREF 6AU2 A 196 402 UNP Q15047 SETB1_HUMAN 196 402
SEQADV 6AU2 GLU A 190 UNP Q15047 EXPRESSION TAG
SEQADV 6AU2 ASN A 191 UNP Q15047 EXPRESSION TAG
SEQADV 6AU2 LEU A 192 UNP Q15047 EXPRESSION TAG
SEQADV 6AU2 TYR A 193 UNP Q15047 EXPRESSION TAG
SEQADV 6AU2 PHE A 194 UNP Q15047 EXPRESSION TAG
SEQADV 6AU2 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
HET CGJ A 501 15
HET BME A 502 4
HET BME A 503 4
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 4
HET EDO A 514 4
HET UNX A 515 1
HET UNX A 516 1
HET UNX A 517 1
HET UNX A 518 1
HET UNX A 519 1
HET UNX A 520 1
HET UNX A 521 1
HET UNX A 522 1
HET UNX A 523 1
HET UNX A 524 1
HET UNX A 525 1
HET UNX A 526 1
HET UNX A 527 1
HETNAM CGJ 1-METHYL-4H,6H-[1,2,4]TRIAZOLO[4,3-A][4,1]BENZOXAZEPINE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CGJ C11 H11 N3 O
FORMUL 3 BME 2(C2 H6 O S)
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 10 EDO 6(C2 H6 O2)
FORMUL 16 UNX 13(X)
FORMUL 29 HOH *180(H2 O)
HELIX 1 AA1 SER A 243 ASN A 245 5 3
HELIX 2 AA2 PRO A 254 LEU A 258 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
HELIX 6 AA6 LEU A 395 SER A 400 1 6
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 229 N GLN A 222
SHEET 4 AA1 4 LYS A 239 LEU A 242 -1 O SER A 240 N VAL A 232
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 GLY A 206 O HIS A 214
SHEET 4 AA2 4 ILE A 247 TYR A 249 -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 4 LEU A 353 TRP A 358 0
SHEET 2 AA5 4 THR A 361 ASP A 371 -1 O TRP A 363 N THR A 356
SHEET 3 AA5 4 LEU A 374 PHE A 379 -1 O ARG A 376 N GLU A 369
SHEET 4 AA5 4 ARG A 384 TYR A 389 -1 O GLU A 386 N ILE A 377
LINK SG CYS A 329 S2 BME A 502 1555 1555 2.17
LINK SG CYS A 385 S2 BME A 503 1555 1555 2.20
CISPEP 1 TYR A 340 PRO A 341 0 11.87
SITE 1 AC1 12 PHE A 296 PHE A 297 GLY A 300 ALA A 302
SITE 2 AC1 12 CYS A 329 PHE A 332 ILE A 333 TYR A 389
SITE 3 AC1 12 SER A 392 BME A 502 HOH A 689 HOH A 707
SITE 1 AC2 3 SER A 328 CYS A 329 CGJ A 501
SITE 1 AC3 3 TYR A 251 ARG A 376 CYS A 385
SITE 1 AC4 4 ARG A 203 LYS A 215 ASP A 250 LYS A 383
SITE 1 AC5 6 ARG A 209 TRP A 363 LYS A 364 ASP A 381
SITE 2 AC5 6 HOH A 610 HOH A 680
SITE 1 AC6 6 LEU A 242 SER A 243 HIS A 246 EDO A 510
SITE 2 AC6 6 HOH A 608 HOH A 643
SITE 1 AC7 4 THR A 306 GLN A 307 SER A 308 ARG A 384
SITE 1 AC8 5 HIS A 214 LYS A 215 HOH A 605 HOH A 642
SITE 2 AC8 5 HOH A 743
SITE 1 AC9 6 TYR A 193 SER A 262 THR A 320 HOH A 618
SITE 2 AC9 6 HOH A 621 HOH A 694
SITE 1 AD1 8 LYS A 207 LYS A 208 ARG A 209 LYS A 211
SITE 2 AD1 8 LEU A 242 HIS A 246 SO4 A 506 EDO A 512
SITE 1 AD2 4 PRO A 254 ALA A 255 GLN A 307 HOH A 718
SITE 1 AD3 4 LYS A 207 LYS A 211 HIS A 246 EDO A 510
SITE 1 AD4 4 ASN A 191 ASP A 256 LEU A 258 ASN A 272
SITE 1 AD5 4 GLU A 357 TRP A 358 GLU A 359 ARG A 394
CRYST1 55.202 63.273 69.859 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 0.018115 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015805 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
