HEADER TRANSFERASE 24-OCT-06 2J8A
TITLE X-RAY STRUCTURE OF THE N-TERMINUS RRM DOMAIN OF SET1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4
COMPND 3 SPECIFIC;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: N-TERMINUS RRM DOMAIN, RESIDUES 247-375;
COMPND 6 SYNONYM: COMPASS COMPONENT SET1, SET DOMAIN-CONTAINING
COMPND 7 PROTEIN 1, SET1 HISTONE METHYLTRANSFERASE;
COMPND 8 EC: 2.1.1.43;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: S228C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GOLD;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-9
KEYWDS HISTONE METHYLTRANSFERASE, RRM FOLD, TELOMERE, TRANSFERASE,
KEYWDS 2 NUCLEAR PROTEIN, METHYLTRANSFERASE, CHROMOSOMAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,I.VARLET,
AUTHOR 2 P.SALAH,M.PAMBLANCO,P.LUCIANO,S.QUEVILLON-CHERUEL,
AUTHOR 3 J.SOLLIER,N.LEULLIOT,J.COUPRIE,V.TORDERA,S.ZINN-JUSTIN,
AUTHOR 4 S.CHAVEZ,H.VAN TILBEURGH,V.GELI
REVDAT 3 24-FEB-09 2J8A 1 VERSN
REVDAT 2 03-APR-07 2J8A 1 REMARK
REVDAT 1 20-MAR-07 2J8A 0
JRNL AUTH L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,
JRNL AUTH 2 I.VARLET,P.SALAH,M.PAMBLANCO,P.LUCIANO,
JRNL AUTH 3 S.QUEVILLON-CHERUEL,J.SOLLIER,N.LEULLIOT,J.COUPRIE,
JRNL AUTH 4 V.TORDERA,S.ZINN-JUSTIN,S.CHAVEZ,H.VAN TILBEURGH,
JRNL AUTH 5 V.GELI
JRNL TITL X-RAY STRUCTURE OF THE N-TERMINUS RRM DOMAIN OF
JRNL TITL 2 SET1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.TRESAUGUES,P.M.DEHE,R.GUEROIS,A.RODRIGUEZ-GIL,
REMARK 1 AUTH 2 I.VARLET,P.SALAH,M.PAMBLANCO,P.LUCIANO,
REMARK 1 AUTH 3 S.QUEVILLON-CHERUEL,J.SOLLIER,N.LEULLIOT,J.COUPRIE,
REMARK 1 AUTH 4 V.TORDERA,S.ZINN-JUSTIN,S.CHAVEZ,H.VAN TILBEURGH,
REMARK 1 AUTH 5 V.GELI
REMARK 1 TITL STRUCTURAL CHARACTERIZATION OF SET1 RNA
REMARK 1 TITL 2 RECOGNITION MOTIFS AND THEIR ROLE IN HISTONE H3
REMARK 1 TITL 3 LYSINE 4 METHYLATION.
REMARK 1 REF J.MOL.BIOL. V. 359 1170 2006
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 16787775
REMARK 1 DOI 10.1016/J.JMB.2006.04.050
REMARK 2
REMARK 2 RESOLUTION. 3.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 6381
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 321
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 443
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.4300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 915
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS :
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.435
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.234
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 933 ; 0.054 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1255 ; 4.097 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 112 ;12.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 43 ;31.879 ;25.581
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 173 ;25.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ; 6.192 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 141 ; 0.335 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 685 ; 0.016 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 520 ; 0.348 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 651 ; 0.392 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 50 ; 0.232 ; 0.200
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): 44 ; 0.297 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.096 ; 0.200
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): 586 ; 2.273 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 919 ; 3.563 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 403 ; 5.078 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 336 ; 7.741 ; 4.500
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
REMARK 3 RIDING POSITIONS. RESIDUES 302-306 AND 367-CTERMINUS ARE
REMARK 3 DISORDERED
REMARK 4
REMARK 4 2J8A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-06.
REMARK 100 THE PDBE ID CODE IS EBI-30296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7192
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 39.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.01000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 0.31000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.15M AMMONIUM SULFATE,50MM
REMARK 280 NACITRATE PH4.6,4% POLYPROPYLENE-GLYCOL 400,3% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 61.89500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.89500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.89500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.89500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.89500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.89500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 61.89500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.89500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.89500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.89500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.89500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.89500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 61.89500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.89500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.89500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.89500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.89500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.89500
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 30.94750
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 92.84250
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 30.94750
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 30.94750
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 30.94750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 92.84250
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 30.94750
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 92.84250
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 30.94750
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 92.84250
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 30.94750
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 92.84250
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 92.84250
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 30.94750
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 92.84250
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 30.94750
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 30.94750
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 30.94750
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 92.84250
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 30.94750
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 30.94750
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 92.84250
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 92.84250
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 92.84250
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 30.94750
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 92.84250
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 30.94750
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 92.84250
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 30.94750
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 30.94750
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 30.94750
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 GENERATING THE BIOMOLECULE
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: PQS
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 246
REMARK 465 SER A 302
REMARK 465 SER A 303
REMARK 465 ASP A 304
REMARK 465 GLY A 305
REMARK 465 LYS A 306
REMARK 465 ILE A 307
REMARK 465 LYS A 367
REMARK 465 ALA A 368
REMARK 465 LYS A 369
REMARK 465 GLU A 370
REMARK 465 LYS A 371
REMARK 465 GLU A 372
REMARK 465 ALA A 373
REMARK 465 GLU A 374
REMARK 465 ASN A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
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 CYS A 248 CB CYS A 248 SG -0.130
REMARK 500 GLU A 249 CB GLU A 249 CG -0.175
REMARK 500 TYR A 253 CD2 TYR A 253 CE2 0.117
REMARK 500 THR A 260 CA THR A 260 CB 0.173
REMARK 500 TYR A 271 CB TYR A 271 CG -0.110
REMARK 500 TYR A 271 CD2 TYR A 271 CE2 0.106
REMARK 500 PHE A 281 CE2 PHE A 281 CZ 0.116
REMARK 500 GLU A 282 CB GLU A 282 CG -0.154
REMARK 500 PHE A 284 CE2 PHE A 284 CZ 0.127
REMARK 500 VAL A 295 C VAL A 295 O 0.118
REMARK 500 ALA A 301 CA ALA A 301 CB 0.153
REMARK 500 SER A 323 CA SER A 323 CB 0.113
REMARK 500 SER A 324 CA SER A 324 CB 0.102
REMARK 500 PHE A 327 CA PHE A 327 CB -0.137
REMARK 500 PHE A 327 CB PHE A 327 CG -0.121
REMARK 500 PHE A 331 CD2 PHE A 331 CE2 0.128
REMARK 500 PHE A 331 CE1 PHE A 331 CZ 0.117
REMARK 500 LEU A 343 C LEU A 343 O 0.123
REMARK 500 SER A 348 C SER A 348 O 0.131
REMARK 500 LYS A 349 CD LYS A 349 CE 0.210
REMARK 500 LYS A 349 CE LYS A 349 NZ 0.228
REMARK 500 VAL A 351 CA VAL A 351 CB -0.134
REMARK 500 GLU A 352 CG GLU A 352 CD 0.132
REMARK 500 ILE A 353 CA ILE A 353 CB -0.161
REMARK 500 ASN A 354 N ASN A 354 CA -0.120
REMARK 500 LYS A 356 CE LYS A 356 NZ 0.183
REMARK 500 LYS A 366 CD LYS A 366 CE 0.190
REMARK 500 LYS A 366 CE LYS A 366 NZ 0.172
REMARK 500 LYS A 366 CG LYS A 366 CD 0.235
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 CYS A 248 CA - CB - SG ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP A 257 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 257 CB - CG - OD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 THR A 259 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LYS A 269 CD - CE - NZ ANGL. DEV. = -20.5 DEGREES
REMARK 500 LYS A 273 CD - CE - NZ ANGL. DEV. = 14.4 DEGREES
REMARK 500 GLU A 277 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 LEU A 293 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 HIS A 321 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 MET A 329 CG - SD - CE ANGL. DEV. = 10.6 DEGREES
REMARK 500 VAL A 335 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 LEU A 343 CB - CG - CD1 ANGL. DEV. = -16.1 DEGREES
REMARK 500 GLU A 352 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 GLU A 352 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU A 365 CA - CB - CG ANGL. DEV. = 18.7 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 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 CYS A 248 -34.34 -136.32
REMARK 500 ASP A 257 -74.04 -28.35
REMARK 500 ASN A 262 35.93 -146.20
REMARK 500 ASP A 265 -72.62 -43.49
REMARK 500 ILE A 266 -74.82 -16.52
REMARK 500 SER A 267 -28.10 -27.56
REMARK 500 ASN A 270 -83.95 -33.51
REMARK 500 TYR A 271 -49.21 -28.05
REMARK 500 LYS A 273 -41.87 -25.73
REMARK 500 LYS A 274 39.53 -63.80
REMARK 500 HIS A 280 132.75 171.35
REMARK 500 ALA A 290 -2.83 63.55
REMARK 500 HIS A 294 53.66 71.69
REMARK 500 ALA A 310 -75.15 -47.46
REMARK 500 ALA A 311 -35.88 -32.71
REMARK 500 ALA A 313 -78.71 -39.79
REMARK 500 ALA A 314 -62.07 -26.14
REMARK 500 SER A 323 -86.47 -35.85
REMARK 500 ASN A 364 -36.23 -31.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 247 CYS A 248 -139.77
REMARK 500 THR A 260 THR A 261 147.48
REMARK 500 TYR A 300 ALA A 301 144.58
REMARK 500 ASP A 309 ALA A 310 138.33
REMARK 500 GLU A 363 ASN A 364 146.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 THR A 259 5.2 L D EXPECTING SP3
REMARK 500 GLN A 264 19.1 L L OUTSIDE RANGE
REMARK 500 PHE A 272 22.4 L L OUTSIDE RANGE
REMARK 500 GLU A 277 46.7 L L OUTSIDE RANGE
REMARK 500 HIS A 321 12.0 L L OUTSIDE RANGE
REMARK 500 GLU A 363 23.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2J8A A 246 246 PDB 2J8A 2J8A 246 246
DBREF 2J8A A 247 375 UNP P38827 SET1_YEAST 247 375
DBREF 2J8A A 376 381 PDB 2J8A 2J8A 376 381
SEQRES 1 A 136 MET SER CYS GLU ILE VAL VAL TYR PRO ALA GLN ASP SER
SEQRES 2 A 136 THR THR THR ASN ILE GLN ASP ILE SER ILE LYS ASN TYR
SEQRES 3 A 136 PHE LYS LYS TYR GLY GLU ILE SER HIS PHE GLU ALA PHE
SEQRES 4 A 136 ASN ASP PRO ASN SER ALA LEU PRO LEU HIS VAL TYR LEU
SEQRES 5 A 136 ILE LYS TYR ALA SER SER ASP GLY LYS ILE ASN ASP ALA
SEQRES 6 A 136 ALA LYS ALA ALA PHE SER ALA VAL ARG LYS HIS GLU SER
SEQRES 7 A 136 SER GLY CYS PHE ILE MET GLY PHE LYS PHE GLU VAL ILE
SEQRES 8 A 136 LEU ASN LYS HIS SER ILE LEU ASN ASN ILE ILE SER LYS
SEQRES 9 A 136 PHE VAL GLU ILE ASN VAL LYS LYS LEU GLN LYS LEU GLN
SEQRES 10 A 136 GLU ASN LEU LYS LYS ALA LYS GLU LYS GLU ALA GLU ASN
SEQRES 11 A 136 HIS HIS HIS HIS HIS HIS
HELIX 1 1 GLN A 264 LYS A 274 1 11
HELIX 2 2 ASP A 309 HIS A 321 1 13
HELIX 3 3 SER A 341 LEU A 365 1 25
SHEET 1 AA 5 HIS A 280 ASN A 285 0
SHEET 2 AA 5 PRO A 292 LYS A 299 -1 N LEU A 293 O PHE A 284
SHEET 3 AA 5 GLU A 249 PRO A 254 -1 O ILE A 250 N ILE A 298
SHEET 4 AA 5 PHE A 331 LEU A 337 -1 O GLU A 334 N TYR A 253
SHEET 5 AA 5 CYS A 326 ILE A 328 -1 O CYS A 326 N PHE A 333
CRYST1 123.790 123.790 123.790 90.00 90.00 90.00 P 43 3 2 24
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 0.008078 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008078 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008078 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
