HEADER TRANSCRIPTION 01-DEC-14 4X3K
TITLE CRYSTAL STRUCTURE OF CHROMOBOX HOMOLOG 7 (CBX7) CHROMODOMAIN WITH
TITLE 2 H3K27ME3 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHROMOBOX PROTEIN HOMOLOG 7;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: H3K27ME3 PEPTIDE;
COMPND 7 CHAIN: C, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CBX7, D15ERTD417E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS CBX7, CHROMODOMAIN, H3K27ME3
EXPDTA X-RAY DIFFRACTION
AUTHOR C.REN,M.M.ZHOU
REVDAT 1 04-MAR-15 4X3K 0
JRNL AUTH C.REN,K.MOROHASHI,A.N.PLOTNIKOV,J.JAKONCIC,S.G.SMITH,J.LI,
JRNL AUTH 2 L.ZENG,Y.RODRIGUEZ,V.STOJANOFF,M.WALSH,M.M.ZHOU
JRNL TITL SMALL-MOLECULE MODULATORS OF METHYL-LYSINE BINDING FOR THE
JRNL TITL 2 CBX7 CHROMODOMAIN.
JRNL REF CHEM.BIOL. V. 22 161 2015
JRNL REFN ISSN 1074-5521
JRNL PMID 25660273
JRNL DOI 10.1016/J.CHEMBIOL.2014.11.021
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 23418
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1258
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1686
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 97
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1194
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 167
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.255
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1240 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1234 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1662 ; 2.346 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2848 ; 0.935 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 142 ; 6.599 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ;26.937 ;21.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 240 ;14.282 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.782 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 162 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1322 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 286 ; 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): 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
REMARK 4
REMARK 4 4X3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24687
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG MME550, 0.1 M MES PH6.5, 0.01
REMARK 280 M ZINC SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 16.61500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C ALA A 66 O HOH A 203 1.41
REMARK 500 O HOH D 105 O HOH D 107 1.78
REMARK 500 OE1 GLU B 58 K K B 102 1.86
REMARK 500 OE2 GLU B 62 K K B 102 1.96
REMARK 500 OE1 GLU B 61 K K B 102 1.98
REMARK 500 O HOH D 105 O HOH D 108 2.00
REMARK 500 NH1 ARG A 22 O HOH A 201 2.04
REMARK 500 NZ LYS B 19 K K B 102 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE MET B 6 O HOH A 230 2646 2.01
REMARK 500 NH1 ARG A 22 O ASP A 64 2646 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 8 CD GLU A 8 OE2 -0.069
REMARK 500 TYR A 39 CE1 TYR A 39 CZ -0.095
REMARK 500 GLU A 45 CD GLU A 45 OE2 0.069
REMARK 500 GLU B 46 CD GLU B 46 OE1 0.101
REMARK 500 GLU B 59 CD GLU B 59 OE2 -0.095
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 22 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 50 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 17 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU B 46 CG - CD - OE1 ANGL. DEV. = 13.3 DEGREES
REMARK 500 ASP B 50 CB - CG - OD2 ANGL. DEV. = -8.0 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 LYS A 23 44.68 39.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 101 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 5 ND1
REMARK 620 2 GLU A 8 OE1 109.5
REMARK 620 3 HIS A 47 NE2 101.9 104.9
REMARK 620 4 GLU B 59 OE2 162.6 85.4 64.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 101 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 5 ND1
REMARK 620 2 GLU B 8 OE1 107.0
REMARK 620 3 HIS B 47 NE2 106.9 105.6
REMARK 620 4 GLU A 59 OE2 168.1 63.4 70.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 102 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 58 OE2
REMARK 620 2 GLU B 61 OE2 120.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG C 4 and M3L C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L C 5 and SER C 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG D 4 and M3L D 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L D 5 and SER D 6
DBREF 4X3K A 7 66 UNP Q8VDS3 CBX7_MOUSE 7 66
DBREF 4X3K B 7 66 UNP Q8VDS3 CBX7_MOUSE 7 66
DBREF 4X3K C 1 7 PDB 4X3K 4X3K 1 7
DBREF 4X3K D 1 7 PDB 4X3K 4X3K 1 7
SEQADV 4X3K GLY A 3 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K SER A 4 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K HIS A 5 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K MET A 6 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K GLY B 3 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K SER B 4 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K HIS B 5 UNP Q8VDS3 EXPRESSION TAG
SEQADV 4X3K MET B 6 UNP Q8VDS3 EXPRESSION TAG
SEQRES 1 A 64 GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER
SEQRES 2 A 64 ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR
SEQRES 3 A 64 LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR
SEQRES 4 A 64 TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL
SEQRES 5 A 64 MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA
SEQRES 1 B 64 GLY SER HIS MET GLY GLU GLN VAL PHE ALA VAL GLU SER
SEQRES 2 B 64 ILE ARG LYS LYS ARG VAL ARG LYS GLY LYS VAL GLU TYR
SEQRES 3 B 64 LEU VAL LYS TRP LYS GLY TRP PRO PRO LYS TYR SER THR
SEQRES 4 B 64 TRP GLU PRO GLU GLU HIS ILE LEU ASP PRO ARG LEU VAL
SEQRES 5 B 64 MET ALA TYR GLU GLU LYS GLU GLU ARG ASP ARG ALA
SEQRES 1 C 7 LYS ALA ALA ARG M3L SER ALA
SEQRES 1 D 7 LYS ALA ALA ARG M3L SER ALA
HET M3L C 5 12
HET M3L D 5 12
HET NI A 101 1
HET NI B 101 1
HET K B 102 1
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM NI NICKEL (II) ION
HETNAM K POTASSIUM ION
FORMUL 3 M3L 2(C9 H21 N2 O2 1+)
FORMUL 5 NI 2(NI 2+)
FORMUL 7 K K 1+
FORMUL 8 HOH *167(H2 O)
HELIX 1 AA1 PRO A 36 SER A 40 5 5
HELIX 2 AA2 GLU A 46 ILE A 48 5 3
HELIX 3 AA3 ASP A 50 ALA A 66 1 17
HELIX 4 AA4 PRO B 36 SER B 40 5 5
HELIX 5 AA5 GLU B 46 ILE B 48 5 3
HELIX 6 AA6 ASP B 50 ARG B 65 1 16
SHEET 1 AA1 4 THR A 41 PRO A 44 0
SHEET 2 AA1 4 LYS A 25 TRP A 32 -1 N VAL A 30 O THR A 41
SHEET 3 AA1 4 VAL A 10 ARG A 22 -1 N ARG A 17 O LEU A 29
SHEET 4 AA1 4 ALA C 2 ARG C 4 -1 O ALA C 3 N PHE A 11
SHEET 1 AA2 4 THR B 41 PRO B 44 0
SHEET 2 AA2 4 LYS B 25 TRP B 32 -1 N VAL B 30 O THR B 41
SHEET 3 AA2 4 VAL B 10 ARG B 22 -1 N ARG B 17 O LEU B 29
SHEET 4 AA2 4 ALA D 2 ARG D 4 -1 O ALA D 3 N PHE B 11
LINK ND1 HIS A 5 NI NI A 101 1555 1555 2.07
LINK OE1 GLU A 8 NI NI A 101 1555 1555 1.98
LINK NE2 HIS A 47 NI NI A 101 1555 1555 2.06
LINK ND1 HIS B 5 NI NI B 101 1555 1555 2.14
LINK OE1 GLU B 8 NI NI B 101 1555 1555 1.77
LINK NE2 HIS B 47 NI NI B 101 1555 1555 2.05
LINK OE2 GLU B 58 K K B 102 1555 1555 2.82
LINK OE2 GLU B 61 K K B 102 1555 1555 3.12
LINK C ARG C 4 N M3L C 5 1555 1555 1.34
LINK C M3L C 5 N SER C 6 1555 1555 1.31
LINK C ARG D 4 N M3L D 5 1555 1555 1.33
LINK C M3L D 5 N SER D 6 1555 1555 1.32
LINK OE2 GLU A 59 NI NI B 101 1555 2656 1.96
LINK OE2 GLU B 59 NI NI A 101 1555 2556 1.88
SITE 1 AC1 3 HIS A 5 GLU A 8 HIS A 47
SITE 1 AC2 3 HIS B 5 GLU B 8 HIS B 47
SITE 1 AC3 4 LYS B 19 GLU B 58 GLU B 61 GLU B 62
SITE 1 AC4 12 HIS A 5 GLU A 8 GLN A 9 PHE A 11
SITE 2 AC4 12 TRP A 32 TRP A 35 GLU A 43 HIS A 47
SITE 3 AC4 12 HOH A 211 ALA C 3 SER C 6 HOH C 108
SITE 1 AC5 11 GLN A 9 PHE A 11 TRP A 32 TRP A 35
SITE 2 AC5 11 GLU A 43 HIS A 47 HOH A 211 ARG C 4
SITE 3 AC5 11 ALA C 7 HOH C 101 HOH C 105
SITE 1 AC6 13 PRO A 51 HIS B 5 GLU B 8 GLN B 9
SITE 2 AC6 13 TRP B 32 TRP B 35 GLU B 43 HIS B 47
SITE 3 AC6 13 HOH B 265 ALA D 3 SER D 6 ALA D 7
SITE 4 AC6 13 HOH D 102
SITE 1 AC7 9 GLN B 9 TRP B 32 TRP B 35 GLU B 43
SITE 2 AC7 9 HIS B 47 ALA D 3 ARG D 4 ALA D 7
SITE 3 AC7 9 HOH D 102
CRYST1 45.460 33.230 46.160 90.00 95.80 90.00 P 1 21 1 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 0.021997 0.000000 0.002234 0.00000
SCALE2 0.000000 0.030093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END