HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 11-NOV-15 5EPL
TITLE CRYSTAL STRUCTURE OF CHROMODOMAIN OF CBX4 IN COMPLEX WITH INHIBITOR
TITLE 2 UNC3866
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 SUMO-PROTEIN LIGASE CBX4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CHROMOBOX PROTEIN HOMOLOG 4,POLYCOMB 2 HOMOLOG,HPC2;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UNC3866;
COMPND 9 CHAIN: C, D;
COMPND 10 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: CBX4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 OTHER_DETAILS: SYNTHETIC
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,W.TEMPEL,J.R.WALKER,J.I.STUCKEY,B.M.DICKSON,L.I.JAMES,S.V.FRYE,
AUTHOR 2 C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 5 27-NOV-19 5EPL 1 REMARK HETNAM HETSYN ATOM
REVDAT 4 24-FEB-16 5EPL 1 JRNL
REVDAT 3 17-FEB-16 5EPL 1 JRNL
REVDAT 2 13-JAN-16 5EPL 1 AUTHOR
REVDAT 1 23-DEC-15 5EPL 0
JRNL AUTH J.I.STUCKEY,B.M.DICKSON,N.CHENG,Y.LIU,J.L.NORRIS,
JRNL AUTH 2 S.H.CHOLENSKY,W.TEMPEL,S.QIN,K.G.HUBER,C.SAGUM,K.BLACK,F.LI,
JRNL AUTH 3 X.P.HUANG,B.L.ROTH,B.M.BAUGHMAN,G.SENISTERRA,S.G.PATTENDEN,
JRNL AUTH 4 M.VEDADI,P.J.BROWN,M.T.BEDFORD,J.MIN,C.H.ARROWSMITH,
JRNL AUTH 5 L.I.JAMES,S.V.FRYE
JRNL TITL A CELLULAR CHEMICAL PROBE TARGETING THE CHROMODOMAINS OF
JRNL TITL 2 POLYCOMB REPRESSIVE COMPLEX 1.
JRNL REF NAT.CHEM.BIOL. V. 12 180 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 26807715
JRNL DOI 10.1038/NCHEMBIO.2007
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 14370
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1566
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) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1142
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1970
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1040
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.53000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -1.71000
REMARK 3 B12 (A**2) : 0.26000
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): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.790
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1102 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1071 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1499 ; 1.753 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2449 ; 1.037 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 119 ; 6.698 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;26.329 ;22.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 182 ;11.826 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;11.552 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 150 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1209 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 268 ; 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): 500 ; 1.692 ; 1.777
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 493 ; 1.671 ; 1.757
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 622 ; 2.428 ; 2.645
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 59
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6140 44.3827 5.4479
REMARK 3 T TENSOR
REMARK 3 T11: 0.0269 T22: 0.0091
REMARK 3 T33: 0.0259 T12: -0.0039
REMARK 3 T13: 0.0022 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.2446 L22: 1.1528
REMARK 3 L33: 3.5625 L12: 0.3394
REMARK 3 L13: -0.2863 L23: 0.8125
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: 0.0351 S13: -0.0757
REMARK 3 S21: -0.1153 S22: 0.0238 S23: -0.1379
REMARK 3 S31: -0.0956 S32: 0.1602 S33: -0.0422
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7264 33.6792 8.9303
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.0546
REMARK 3 T33: 0.0251 T12: -0.0081
REMARK 3 T13: 0.0090 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 3.9104 L22: 5.0650
REMARK 3 L33: 2.4453 L12: 2.4020
REMARK 3 L13: -0.6834 L23: -0.4104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.2141 S13: -0.2270
REMARK 3 S21: 0.2322 S22: -0.1629 S23: -0.0305
REMARK 3 S31: 0.1298 S32: -0.1698 S33: 0.1451
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: THE STRUCTURE WAS SOLVED BY MOLECULAR
REMARK 3 REPLACEMENT WITH AN ISOMORPHOUS CRYSTAL, FOLLOWED BY PHASE
REMARK 3 IMPROVEMENT AND AUTOMATED MODEL BUILDING WITH ARP/WARP.
REMARK 3 PHENIX.ELBOW/MOGUL WAS USED TO GENERATE GEOMETRY RESTRAINTS FOR
REMARK 3 INHIBITOR BUILDING BLOCKS. LIGAND WAS USED FOR PREPARATION OF
REMARK 3 LINK RESTRAINTS. LINK RESTRAINTS WERE MANUALLY MODIFIED, FOR
REMARK 3 EXAMPLE TO ESTABLISH PLANAR GEOMETRY OF METHYL ESTER TERMINUS OF
REMARK 3 INHIBITOR. COOT WAS USED FOR INTERACTIVE MODEL BUILDING. MODEL
REMARK 3 GEOMETRY WAS EVALUATED WITH MOLPROBITY.ELECTRON DENSITY DID NOT
REMARK 3 FULLY RESOLVE THE LIGAND'S C-TERMINAL SERINE ESTER MOIETY
REMARK 4
REMARK 4 5EPL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 0.9786036
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16048
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 44.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 20.40
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 19.60
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2M SODIUM CHLORIDE, 0.1
REMARK 280 M SODIUM CACODYLATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.35233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 88.70467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 66.52850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 110.88083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.17617
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.35233
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 88.70467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 110.88083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 66.52850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 22.17617
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: AUTHORS HAVE NOT INDICATED THE BIOLOGICAL UNIT
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE UNC3866 IS OLIGOPEPTIDE, A MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: UNC3866
REMARK 400 CHAIN: C, D
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 ARG A 60
REMARK 465 GLU A 61
REMARK 465 ARG A 62
REMARK 465 GLN A 63
REMARK 465 GLU A 64
REMARK 465 GLN A 65
REMARK 465 GLU B 64
REMARK 465 GLN B 65
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 18 CE NZ
REMARK 470 LYS A 23 CE NZ
REMARK 470 ASN A 59 C O CB CG OD1 ND2
REMARK 470 LYS B 18 CE NZ
REMARK 470 LYS B 23 CD CE NZ
REMARK 470 LYS B 38 NZ
REMARK 470 GLN B 58 CD OE1 NE2
REMARK 470 ARG B 60 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 62 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 63 C O CB CG CD OE1 NE2
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 C 207 DISTANCE = 6.17 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for UNC3866 chain C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for UNC3866 chain D
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EQ0 RELATED DB: PDB
REMARK 900 RELATED ID: 5EPJ RELATED DB: PDB
REMARK 900 RELATED ID: 5EPK RELATED DB: PDB
DBREF 5EPL A 8 65 UNP O00257 CBX4_HUMAN 8 65
DBREF 5EPL B 8 65 UNP O00257 CBX4_HUMAN 8 65
DBREF 5EPL C 0 5 PDB 5EPL 5EPL 0 5
DBREF 5EPL D 0 5 PDB 5EPL 5EPL 0 5
SEQADV 5EPL GLY A 6 UNP O00257 EXPRESSION TAG
SEQADV 5EPL SER A 7 UNP O00257 EXPRESSION TAG
SEQADV 5EPL GLY B 6 UNP O00257 EXPRESSION TAG
SEQADV 5EPL SER B 7 UNP O00257 EXPRESSION TAG
SEQRES 1 A 60 GLY SER GLU HIS VAL PHE ALA VAL GLU SER ILE GLU LYS
SEQRES 2 A 60 LYS ARG ILE ARG LYS GLY ARG VAL GLU TYR LEU VAL LYS
SEQRES 3 A 60 TRP ARG GLY TRP SER PRO LYS TYR ASN THR TRP GLU PRO
SEQRES 4 A 60 GLU GLU ASN ILE LEU ASP PRO ARG LEU LEU ILE ALA PHE
SEQRES 5 A 60 GLN ASN ARG GLU ARG GLN GLU GLN
SEQRES 1 B 60 GLY SER GLU HIS VAL PHE ALA VAL GLU SER ILE GLU LYS
SEQRES 2 B 60 LYS ARG ILE ARG LYS GLY ARG VAL GLU TYR LEU VAL LYS
SEQRES 3 B 60 TRP ARG GLY TRP SER PRO LYS TYR ASN THR TRP GLU PRO
SEQRES 4 B 60 GLU GLU ASN ILE LEU ASP PRO ARG LEU LEU ILE ALA PHE
SEQRES 5 B 60 GLN ASN ARG GLU ARG GLN GLU GLN
SEQRES 1 C 6 5R0 PHE ALA LEU ELY 5R5
SEQRES 1 D 6 5R0 PHE ALA LEU ELY 5R5
HET 5R0 C 0 12
HET ELY C 4 13
HET 5R5 C 5 16
HET 5R0 D 0 12
HET ELY D 4 13
HET 5R5 D 5 12
HET UNX A 101 1
HET UNX A 102 1
HET UNX A 103 1
HET UNX B 101 1
HET UNX B 102 1
HET UNX B 103 1
HET UNX B 104 1
HET UNX B 105 1
HETNAM 5R0 4-~{TERT}-BUTYLBENZOIC ACID
HETNAM ELY N~6~,N~6~-DIETHYL-L-LYSINE
HETNAM 5R5 METHYL L-SERINATE
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN ELY (2S)-2-AZANYL-6-(DIETHYLAMINO)HEXANOIC ACID
HETSYN 5R5 METHYL (2~{S})-2-AZANYL-3-OXIDANYL-PROPANOATE
FORMUL 3 5R0 2(C11 H14 O2)
FORMUL 3 ELY 2(C10 H22 N2 O2)
FORMUL 3 5R5 2(C4 H9 N O3)
FORMUL 5 UNX 8(X)
FORMUL 13 HOH *117(H2 O)
HELIX 1 AA1 SER A 36 ASN A 40 5 5
HELIX 2 AA2 GLU A 46 ILE A 48 5 3
HELIX 3 AA3 ASP A 50 GLN A 58 5 9
HELIX 4 AA4 GLY B 6 GLU B 8 5 3
HELIX 5 AA5 SER B 36 ASN B 40 5 5
HELIX 6 AA6 GLU B 46 ILE B 48 5 3
HELIX 7 AA7 PRO B 51 GLU B 61 1 11
SHEET 1 AA1 2 VAL A 10 PHE A 11 0
SHEET 2 AA1 2 ALA C 2 LEU C 3 -1 O ALA C 2 N PHE A 11
SHEET 1 AA2 3 VAL A 13 ARG A 22 0
SHEET 2 AA2 3 ARG A 25 TRP A 32 -1 O LEU A 29 N GLU A 17
SHEET 3 AA2 3 THR A 41 PRO A 44 -1 O THR A 41 N VAL A 30
SHEET 1 AA3 2 VAL B 10 PHE B 11 0
SHEET 2 AA3 2 ALA D 2 LEU D 3 -1 O ALA D 2 N PHE B 11
SHEET 1 AA4 3 VAL B 13 ARG B 22 0
SHEET 2 AA4 3 ARG B 25 TRP B 32 -1 O LEU B 29 N GLU B 17
SHEET 3 AA4 3 THR B 41 PRO B 44 -1 O GLU B 43 N TYR B 28
LINK C1 5R0 C 0 N PHE C 1 1555 1555 1.36
LINK C LEU C 3 N ELY C 4 1555 1555 1.33
LINK C ELY C 4 N A5R5 C 5 1555 1555 1.36
LINK C ELY C 4 N B5R5 C 5 1555 1555 1.36
LINK C1 5R0 D 0 N PHE D 1 1555 1555 1.34
LINK C LEU D 3 N ELY D 4 1555 1555 1.32
LINK C ELY D 4 N 5R5 D 5 1555 1555 1.33
SITE 1 AC1 19 HIS A 9 VAL A 10 PHE A 11 ALA A 12
SITE 2 AC1 19 VAL A 13 TRP A 32 TRP A 35 GLU A 43
SITE 3 AC1 19 ASN A 47 LEU A 49 ASP A 50 ARG A 52
SITE 4 AC1 19 LEU A 53 HOH A 212 HOH A 216 ALA B 12
SITE 5 AC1 19 HOH C 201 HOH C 202 HOH C 203
SITE 1 AC2 22 GLU A 8 HIS A 9 LEU A 49 PRO A 51
SITE 2 AC2 22 HIS B 9 VAL B 10 PHE B 11 ALA B 12
SITE 3 AC2 22 VAL B 13 TRP B 32 TRP B 35 TYR B 39
SITE 4 AC2 22 GLU B 43 ASN B 47 LEU B 49 ASP B 50
SITE 5 AC2 22 ARG B 52 LEU B 53 HOH B 212 HOH B 231
SITE 6 AC2 22 HOH D 201 HOH D 202
CRYST1 65.178 65.178 133.057 90.00 90.00 120.00 P 61 2 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 0.015343 0.008858 0.000000 0.00000
SCALE2 0.000000 0.017716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007516 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
