HEADER TRANSFERASE 06-JUN-16 5KCO
TITLE SETDB1 IN COMPLEX WITH AN EARLY STAGE, LOW AFFINITY FRAGMENT CANDIDATE
TITLE 2 MODELLED AT REDUCED OCCUPANCY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 196-403;
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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS FRAGMENT SCREENING, DIAMOND I04-1 XCHEM, PANDDA, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.TEMPEL,R.J.HARDING,P.MADER,E.DOBROVETSKY,J.R.WALKER,P.J.BROWN,
AUTHOR 2 M.SCHAPIRA,P.COLLINS,N.PEARCE,J.BRANDAO-NETO,A.DOUANGAMATH,F.VON
AUTHOR 3 DELFT,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,V.SANTHAKUMAR,STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (SGC)
REVDAT 2 27-SEP-23 5KCO 1 REMARK
REVDAT 1 27-JUL-16 5KCO 0
JRNL AUTH W.TEMPEL,R.J.HARDING,P.MADER,E.DOBROVETSKY,J.R.WALKER,
JRNL AUTH 2 P.J.BROWN,M.SCHAPIRA,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 3 S.SANTHAKUMAR,STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL SETDB1 IN COMPLEX WITH AN EARLY STAGE, LOW AFFINITY FRAGMENT
JRNL TITL 2 CANDIDATE MODELLED AT REDUCED OCCUPANCY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 41091
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2204
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) : 1.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2907
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 156
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1711
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : -0.86000
REMARK 3 B33 (A**2) : -0.04000
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): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.422
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
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): 1882 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1780 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2568 ; 1.761 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4094 ; 1.008 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 6.744 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;28.206 ;22.530
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 326 ;10.409 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.620 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2135 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 454 ; 0.001 ; 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): 880 ; 2.347 ; 1.865
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 881 ; 2.346 ; 1.865
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1110 ; 3.305 ; 2.790
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: USERS OF THIS CRYSTAL STRUCTURE: VERIFY
REMARK 3 OUR INTEPRETION OF THE ELECTRON DENSITY. AMPLITUDES AND UNMERGED
REMARK 3 INTENSITIES ARE INCLUDED WITH THIS DEPOSITION. DIFFRACTION
REMARK 3 IMAGES WILL BE DEPOSITED IN A PUBLIC REPOSITORY. GEOMETRY
REMARK 3 RESTRAINTS FOR THE FRAGMENT CANDIDATE WERE PREPARED WITH GRADE.
REMARK 3 SOME OCCUPANCIES WERE REFINED WITH PHENIX SOFTWARE. AMBIGUOUS
REMARK 3 DIFFERENCE DENSITY SUGGESTS MORE THAN ONE MAIN CHAIN
REMARK 3 CONFORMATION FOR RESIDUES 235..239.
REMARK 4
REMARK 4 5KCO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222007.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.26
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43355
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 1.44500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: 3DLM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-3350, 0.2M LITHIUM SULFATE,
REMARK 280 0.1M BIS-TRIS. TRYPSIN HAD BEEN ADDED TO THE PROTEIN STOCK
REMARK 280 SOLUTION., PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
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 27.88600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.26100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.88050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.26100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.88600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.88050
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 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 179
REMARK 465 HIS A 180
REMARK 465 HIS A 181
REMARK 465 HIS A 182
REMARK 465 HIS A 183
REMARK 465 HIS A 184
REMARK 465 HIS A 185
REMARK 465 SER A 186
REMARK 465 SER A 187
REMARK 465 GLY A 188
REMARK 465 ARG A 189
REMARK 465 LYS A 402
REMARK 465 THR A 403
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 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 NZ
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 LYS A 267 CD CE NZ
REMARK 470 LYS A 269 CD CE NZ
REMARK 470 LYS A 288 CE NZ
REMARK 470 LYS A 355 CE NZ
REMARK 470 ASP A 381 CG OD1 OD2
REMARK 470 MET A 401 C O CB CG SD CE
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 GLU A 283 CD GLU A 283 OE1 0.067
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 ARG A 315 NE - CZ - NH1 ANGL. DEV. = 3.2 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 -8.81 90.33
REMARK 500 SER A 201 -10.98 92.66
REMARK 500 ASN A 236 51.31 -116.12
REMARK 500 LYS A 237 -171.44 -175.48
REMARK 500 ASP A 250 51.83 -95.22
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 6RO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 553
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KCH RELATED DB: PDB
DBREF 5KCO A 196 403 UNP Q15047 SETB1_HUMAN 196 403
SEQADV 5KCO MET A 179 UNP Q15047 INITIATING METHIONINE
SEQADV 5KCO HIS A 180 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO HIS A 181 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO HIS A 182 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO HIS A 183 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO HIS A 184 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO HIS A 185 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO SER A 186 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO SER A 187 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO GLY A 188 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO ARG A 189 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO GLU A 190 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO ASN A 191 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO LEU A 192 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO TYR A 193 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO PHE A 194 UNP Q15047 EXPRESSION TAG
SEQADV 5KCO GLN A 195 UNP Q15047 EXPRESSION TAG
SEQRES 1 A 225 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 225 LEU TYR PHE GLN GLY ASP LEU ILE VAL SER MET ARG ILE
SEQRES 3 A 225 LEU GLY LYS LYS ARG THR LYS THR TRP HIS LYS GLY THR
SEQRES 4 A 225 LEU ILE ALA ILE GLN THR VAL GLY PRO GLY LYS LYS TYR
SEQRES 5 A 225 LYS VAL LYS PHE ASP ASN LYS GLY LYS SER LEU LEU SER
SEQRES 6 A 225 GLY ASN HIS ILE ALA TYR ASP TYR HIS PRO PRO ALA ASP
SEQRES 7 A 225 LYS LEU TYR VAL GLY SER ARG VAL VAL ALA LYS TYR LYS
SEQRES 8 A 225 ASP GLY ASN GLN VAL TRP LEU TYR ALA GLY ILE VAL ALA
SEQRES 9 A 225 GLU THR PRO ASN VAL LYS ASN LYS LEU ARG PHE LEU ILE
SEQRES 10 A 225 PHE PHE ASP ASP GLY TYR ALA SER TYR VAL THR GLN SER
SEQRES 11 A 225 GLU LEU TYR PRO ILE CYS ARG PRO LEU LYS LYS THR TRP
SEQRES 12 A 225 GLU ASP ILE GLU ASP ILE SER CYS ARG ASP PHE ILE GLU
SEQRES 13 A 225 GLU TYR VAL THR ALA TYR PRO ASN ARG PRO MET VAL LEU
SEQRES 14 A 225 LEU LYS SER GLY GLN LEU ILE LYS THR GLU TRP GLU GLY
SEQRES 15 A 225 THR TRP TRP LYS SER ARG VAL GLU GLU VAL ASP GLY SER
SEQRES 16 A 225 LEU VAL ARG ILE LEU PHE LEU ASP ASP LYS ARG CYS GLU
SEQRES 17 A 225 TRP ILE TYR ARG GLY SER THR ARG LEU GLU PRO MET PHE
SEQRES 18 A 225 SER MET LYS THR
HET SO4 A 501 5
HET SO4 A 502 5
HET 6RO A 503 12
HET UNX A 504 1
HET UNX A 505 1
HET UNX A 506 1
HET UNX A 507 1
HET UNX A 508 1
HET UNX A 509 1
HET UNX A 510 1
HET UNX A 511 1
HET UNX A 512 1
HET UNX A 513 1
HET UNX A 514 1
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
HET UNX A 528 1
HET UNX A 529 1
HET UNX A 530 1
HET UNX A 531 1
HET UNX A 532 1
HET UNX A 533 1
HET UNX A 534 1
HET UNX A 535 1
HET UNX A 536 1
HET UNX A 537 1
HET UNX A 538 1
HET UNX A 539 1
HET UNX A 540 1
HET UNX A 541 1
HET UNX A 542 1
HET UNX A 543 1
HET UNX A 544 1
HET UNX A 545 1
HET UNX A 546 1
HET UNX A 547 1
HET UNX A 548 1
HET UNX A 549 1
HET UNX A 550 1
HET DMS A 551 4
HET DMS A 552 4
HET DMS A 553 4
HETNAM SO4 SULFATE ION
HETNAM 6RO ~{N}-(4-CHLOROPHENYL)METHANESULFONAMIDE
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 6RO C7 H8 CL N O2 S
FORMUL 5 UNX 47(X)
FORMUL 52 DMS 3(C2 H6 O S)
FORMUL 55 HOH *143(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 MET A 401 1 7
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 GLN A 273 GLU A 283 -1 N ALA A 282 O LEU A 294
SHEET 4 AA4 5 ARG A 263 ASP A 270 -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 THR A 361 N TRP A 358
SHEET 3 AA5 4 LEU A 374 PHE A 379 -1 O ARG A 376 N GLU A 368
SHEET 4 AA5 4 ARG A 384 TYR A 389 -1 O ILE A 388 N VAL A 375
CISPEP 1 TYR A 340 PRO A 341 0 13.20
SITE 1 AC1 5 HIS A 214 LYS A 215 HOH A 612 HOH A 634
SITE 2 AC1 5 HOH A 639
SITE 1 AC2 5 ARG A 209 TRP A 363 LYS A 364 ASP A 381
SITE 2 AC2 5 HOH A 614
SITE 1 AC3 8 PHE A 296 GLY A 300 ALA A 302 SER A 328
SITE 2 AC3 8 PHE A 332 TYR A 389 SER A 392 HOH A 655
SITE 1 AC4 4 LYS A 207 LYS A 208 LYS A 211 HOH A 652
SITE 1 AC5 7 TRP A 358 TRP A 363 PHE A 379 ASP A 382
SITE 2 AC5 7 ARG A 384 HOH A 609 HOH A 672
SITE 1 AC6 3 GLU A 190 ASN A 191 THR A 223
CRYST1 55.772 63.761 70.522 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 0.017930 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014180 0.00000
(ATOM LINES ARE NOT SHOWN.)
END