HEADER TRANSFERASE 30-OCT-17 6BHI
TITLE CRYSTAL STRUCTURE OF SETDB1 WITH A MODIFIED H3 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETDB1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 190-410;
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,
COMPND 7 SET DOMAIN BIFURCATED 1;
COMPND 8 EC: 2.1.1.43;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: HISTONE H3.1;
COMPND 13 CHAIN: B;
COMPND 14 SYNONYM: HISTONE H3/A, HISTONE H3/B, HISTONE H3/C, HISTONE H3/D,
COMPND 15 HISTONE H3/F, HISTONE H3/H, HISTONE H3/I, HISTONE H3/J, HISTONE H3/K,
COMPND 16 HISTONE H3/L;
COMPND 17 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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-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 STRUCTURAL GENOMICS, EPIGENETICS, HISTONE MODIFICATION, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.QIN,W.TEMPEL,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (SGC)
REVDAT 4 15-NOV-23 6BHI 1 REMARK
REVDAT 3 04-OCT-23 6BHI 1 REMARK
REVDAT 2 03-JAN-18 6BHI 1 JRNL
REVDAT 1 06-DEC-17 6BHI 0
JRNL AUTH R.Z.JURKOWSKA,S.QIN,G.KUNGULOVSKI,W.TEMPEL,Y.LIU,
JRNL AUTH 2 P.BASHTRYKOV,J.STIEFELMAIER,T.P.JURKOWSKI,S.KUDITHIPUDI,
JRNL AUTH 3 S.WEIRICH,R.TAMAS,H.WU,L.DOMBROVSKI,P.LOPPNAU,R.REINHARDT,
JRNL AUTH 4 J.MIN,A.JELTSCH
JRNL TITL H3K14AC IS LINKED TO METHYLATION OF H3K9 BY THE TRIPLE TUDOR
JRNL TITL 2 DOMAIN OF SETDB1.
JRNL REF NAT COMMUN V. 8 2057 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29234025
JRNL DOI 10.1038/S41467-017-02259-9
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 50707
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2671
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3757
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.054
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.055
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.253
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1911 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1813 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2605 ; 1.820 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4211 ; 1.014 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 6.875 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;30.164 ;23.026
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 340 ;11.661 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.268 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 289 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2100 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 402 ; 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): 927 ; 2.577 ; 1.587
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 928 ; 2.577 ; 1.589
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1164 ; 2.929 ; 2.376
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): 3724 ; 2.294 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 150 ;22.424 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3779 ; 9.880 ; 5.000
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: COOT WAS USED FOR INTERACTIVE MODEL
REMARK 3 BUILDING. MODEL GEOMETRY WAS EVALUATED WITH MOLPROBITY.
REMARK 3 SIDECHAIN DENSITY FOR SETDB1-M401 IS INCONSISTENT WITH RESIDUE
REMARK 3 TYPE.
REMARK 4
REMARK 4 6BHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230846.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53403
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 41.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.94200
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: PHASER
REMARK 200 STARTING MODEL: EARLIER VERSION OF MODEL FROM PDB ENTRY 6BHD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2 M LITHIUM SULFATE,
REMARK 280 0.1 M HEPES, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.85900
REMARK 290 SMTRY3 2 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: 1430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 MET A 172
REMARK 465 HIS A 173
REMARK 465 HIS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 HIS A 177
REMARK 465 HIS A 178
REMARK 465 SER A 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 ARG A 182
REMARK 465 GLU A 183
REMARK 465 ASN A 184
REMARK 465 LEU A 185
REMARK 465 TYR A 186
REMARK 465 PHE A 187
REMARK 465 GLN A 188
REMARK 465 GLY A 189
REMARK 465 ALA A 255
REMARK 465 SER A 407
REMARK 465 ALA A 408
REMARK 465 LEU A 409
REMARK 465 GLU A 410
REMARK 465 LYS B 4
REMARK 465 GLN B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 ARG B 8
REMARK 465 GLN B 19
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 194 CE NZ
REMARK 470 ARG A 209 NE CZ NH1 NH2
REMARK 470 LYS A 211 CE NZ
REMARK 470 ASN A 236 OD1 ND2
REMARK 470 LYS A 237 CD CE NZ
REMARK 470 LYS A 239 NZ
REMARK 470 ASP A 256 OD1 OD2
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 LYS A 269 NZ
REMARK 470 GLN A 273 CG CD OE1 NE2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 LYS A 290 NZ
REMARK 470 GLN A 307 CD OE1 NE2
REMARK 470 LYS A 349 CD CE NZ
REMARK 470 LYS A 364 NZ
REMARK 470 ASP A 382 CG OD1 OD2
REMARK 470 MET A 401 CE
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 THR A 403 OG1 CG2
REMARK 470 SER A 405 OG
REMARK 470 ALA A 406 CA C O CB
REMARK 470 SER B 10 OG
REMARK 470 ARG B 17 CD NE CZ NH1 NH2
REMARK 470 LYS B 18 CA C O CB CG CD CE
REMARK 470 LYS B 18 NZ
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 ASP A 382 N ASP A 382 CA 0.134
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. = 3.1 DEGREES
REMARK 500 MET A 398 CG - SD - CE ANGL. DEV. = -13.5 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 -16.07 104.04
REMARK 500 ASP A 250 55.25 -93.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 811 DISTANCE = 5.95 ANGSTROMS
DBREF 6BHI A 190 410 UNP Q15047 SETB1_HUMAN 190 410
DBREF 6BHI B 4 19 UNP P68431 H31_HUMAN 5 20
SEQADV 6BHI MET A 172 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 173 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 174 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 175 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 176 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 177 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI HIS A 178 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI SER A 179 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI SER A 180 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI GLY A 181 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI ARG A 182 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI GLU A 183 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI ASN A 184 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI LEU A 185 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI TYR A 186 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI PHE A 187 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI GLN A 188 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI GLY A 189 UNP Q15047 EXPRESSION TAG
SEQADV 6BHI ALA A 358 UNP Q15047 TRP 358 ENGINEERED MUTATION
SEQRES 1 A 239 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 239 LEU TYR PHE GLN GLY GLY GLU LEU SER LYS ASP GLY ASP
SEQRES 3 A 239 LEU ILE VAL SER MET ARG ILE LEU GLY LYS LYS ARG THR
SEQRES 4 A 239 LYS THR TRP HIS LYS GLY THR LEU ILE ALA ILE GLN THR
SEQRES 5 A 239 VAL GLY PRO GLY LYS LYS TYR LYS VAL LYS PHE ASP ASN
SEQRES 6 A 239 LYS GLY LYS SER LEU LEU SER GLY ASN HIS ILE ALA TYR
SEQRES 7 A 239 ASP TYR HIS PRO PRO ALA ASP LYS LEU TYR VAL GLY SER
SEQRES 8 A 239 ARG VAL VAL ALA LYS TYR LYS ASP GLY ASN GLN VAL TRP
SEQRES 9 A 239 LEU TYR ALA GLY ILE VAL ALA GLU THR PRO ASN VAL LYS
SEQRES 10 A 239 ASN LYS LEU ARG PHE LEU ILE PHE PHE ASP ASP GLY TYR
SEQRES 11 A 239 ALA SER TYR VAL THR GLN SER GLU LEU TYR PRO ILE CYS
SEQRES 12 A 239 ARG PRO LEU LYS LYS THR TRP GLU ASP ILE GLU ASP ILE
SEQRES 13 A 239 SER CYS ARG ASP PHE ILE GLU GLU TYR VAL THR ALA TYR
SEQRES 14 A 239 PRO ASN ARG PRO MET VAL LEU LEU LYS SER GLY GLN LEU
SEQRES 15 A 239 ILE LYS THR GLU ALA GLU GLY THR TRP TRP LYS SER ARG
SEQRES 16 A 239 VAL GLU GLU VAL ASP GLY SER LEU VAL ARG ILE LEU PHE
SEQRES 17 A 239 LEU ASP ASP LYS ARG CYS GLU TRP ILE TYR ARG GLY SER
SEQRES 18 A 239 THR ARG LEU GLU PRO MET PHE SER MET LYS THR SER SER
SEQRES 19 A 239 ALA SER ALA LEU GLU
SEQRES 1 B 16 LYS GLN THR ALA ARG M3L SER THR GLY GLY ALY ALA PRO
SEQRES 2 B 16 ARG LYS GLN
MODRES 6BHI M3L B 9 LYS MODIFIED RESIDUE
MODRES 6BHI ALY B 14 LYS MODIFIED RESIDUE
HET M3L B 9 12
HET ALY B 14 12
HET UNX A 501 1
HET UNX A 502 1
HET UNX A 503 1
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
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 M3L C9 H21 N2 O2 1+
FORMUL 2 ALY C8 H16 N2 O3
FORMUL 3 UNX 35(X)
FORMUL 38 HOH *224(H2 O)
HELIX 1 AA1 THR A 306 SER A 308 5 3
HELIX 2 AA2 LYS A 319 ILE A 324 5 6
HELIX 3 AA3 ASP A 326 TYR A 340 1 15
HELIX 4 AA4 LEU A 395 SER A 405 1 11
SHEET 1 AA1 4 GLU 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 SER A 243 -1 O SER A 240 N VAL A 232
SHEET 1 AA2 4 GLU 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 TYR A 249 -1 O ALA A 248 N LEU A 205
SHEET 1 AA3 2 LYS A 194 ASP A 195 0
SHEET 2 AA3 2 LEU A 198 ILE A 199 -1 O LEU A 198 N ASP 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 ALA 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 368
SHEET 4 AA5 4 CYS A 385 TYR A 389 -1 O GLU A 386 N ILE A 377
LINK C M3L B 9 N SER B 10 1555 1555 1.31
LINK C GLY B 13 N ALY B 14 1555 1555 1.33
LINK C ALY B 14 N ALA B 15 1555 1555 1.33
CISPEP 1 TYR A 340 PRO A 341 0 13.56
CRYST1 37.849 71.718 52.690 90.00 104.48 90.00 P 1 21 1 2
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 0.026421 0.000000 0.006821 0.00000
SCALE2 0.000000 0.013943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019601 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
