HEADER TRANSCRIPTION 19-JUL-10 2XL3
TITLE WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD REPEAT-CONTAINING PROTEIN 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: WDR5, BMP2-INDUCED 3-KB GENE PROTEIN, WD REPEAT-CONTAINING
COMPND 5 PROTEIN BIG-3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RETINOBLASTOMA-BINDING PROTEIN 5;
COMPND 9 CHAIN: C, E;
COMPND 10 FRAGMENT: RESIDUES 369-381;
COMPND 11 SYNONYM: RBBP5, RBBP-5;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: HISTONE H3.1;
COMPND 15 CHAIN: D, F;
COMPND 16 FRAGMENT: AMINO TERMINAL TAIL, RESIDUES 2-9;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: POPINJ;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_COMMON: MOUSE;
SOURCE 18 ORGANISM_TAXID: 10090
KEYWDS TRANSCRIPTION, MLL COMPLEX, H3K4 METHYLATION, WD-40 BETA-PROPELLER
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ODHO,S.M.SOUTHALL,J.R.WILSON
REVDAT 5 20-DEC-23 2XL3 1 REMARK
REVDAT 4 29-JUN-11 2XL3 1 HETSYN
REVDAT 3 27-OCT-10 2XL3 1 JRNL
REVDAT 2 01-SEP-10 2XL3 1 JRNL
REVDAT 1 04-AUG-10 2XL3 0
JRNL AUTH Z.ODHO,S.M.SOUTHALL,J.R.WILSON
JRNL TITL CHARACTERISATION OF A NOVEL WDR5 BINDING SITE THAT RECRUITS
JRNL TITL 2 RBBP5 THROUGH A CONSERVED MOTIF AND ENHANCES METHYLATION OF
JRNL TITL 3 H3K4 BY MLL1.
JRNL REF J.BIOL.CHEM. V. 285 32967 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20716525
JRNL DOI 10.1074/JBC.M110.159921
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 16657
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.6928 - 4.9040 0.96 2796 159 0.1793 0.2092
REMARK 3 2 4.9040 - 3.8934 0.98 2777 154 0.1339 0.1991
REMARK 3 3 3.8934 - 3.4015 0.96 2768 117 0.1619 0.2183
REMARK 3 4 3.4015 - 3.0906 0.92 2627 138 0.1767 0.2963
REMARK 3 5 3.0906 - 2.8691 0.88 2511 124 0.1999 0.2562
REMARK 3 6 2.8691 - 2.7000 0.84 2346 140 0.2131 0.2945
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 25.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 31.17020
REMARK 3 B22 (A**2) : -23.27760
REMARK 3 B33 (A**2) : -7.89260
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.01830
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 5027
REMARK 3 ANGLE : 1.100 6822
REMARK 3 CHIRALITY : 0.073 777
REMARK 3 PLANARITY : 0.003 850
REMARK 3 DIHEDRAL : 16.071 1748
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 32:334 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 32:334 )
REMARK 3 ATOM PAIRS NUMBER : 2326
REMARK 3 RMSD : 0.036
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2XL3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1290044672.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16657
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 86.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2H13
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M K2SO4 20 % PEG 3350, PH 8.0
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 40.66000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F
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 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 GLU A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 PRO A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 ARG A 14
REMARK 465 ALA A 15
REMARK 465 GLN A 16
REMARK 465 PRO A 17
REMARK 465 THR A 18
REMARK 465 PRO A 19
REMARK 465 SER A 20
REMARK 465 SER A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 THR A 24
REMARK 465 GLN A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 PRO A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
REMARK 465 VAL A 31
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 GLU B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 PRO B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 ARG B 14
REMARK 465 ALA B 15
REMARK 465 GLN B 16
REMARK 465 PRO B 17
REMARK 465 THR B 18
REMARK 465 PRO B 19
REMARK 465 SER B 20
REMARK 465 SER B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 THR B 24
REMARK 465 GLN B 25
REMARK 465 SER B 26
REMARK 465 LYS B 27
REMARK 465 PRO B 28
REMARK 465 THR B 29
REMARK 465 PRO B 30
REMARK 465 TYR C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 GLU C 4
REMARK 465 THR D 6
REMARK 465 ALA D 7
REMARK 465 ARG D 8
REMARK 465 TYR D 9
REMARK 465 TYR E 1
REMARK 465 ALA E 2
REMARK 465 ALA E 3
REMARK 465 GLU E 4
REMARK 465 ASP E 5
REMARK 465 GLN F 5
REMARK 465 THR F 6
REMARK 465 ALA F 7
REMARK 465 ARG F 8
REMARK 465 TYR F 9
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 159 CG CD CE NZ
REMARK 470 LYS A 245 CG CD CE NZ
REMARK 470 LYS A 259 CG CD CE NZ
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 LYS B 259 CG CD CE NZ
REMARK 470 LYS F 4 CG CD CE NZ
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 GLU A 80 -75.63 -111.37
REMARK 500 ASN A 136 149.78 -175.43
REMARK 500 GLU A 151 16.87 80.33
REMARK 500 ARG A 181 -33.63 -36.63
REMARK 500 TYR A 191 -8.43 -59.25
REMARK 500 ASP A 211 -142.13 -88.21
REMARK 500 LEU A 234 36.41 -68.24
REMARK 500 SER A 244 -73.69 -63.83
REMARK 500 LEU A 249 -64.99 -97.98
REMARK 500 LYS A 259 -37.13 -132.72
REMARK 500 ASN A 281 -0.96 76.38
REMARK 500 ASP A 324 -61.95 -123.44
REMARK 500 SER B 54 150.00 -48.70
REMARK 500 GLU B 80 -75.00 -111.39
REMARK 500 ASP B 150 3.73 -68.54
REMARK 500 ARG B 181 -33.41 -37.15
REMARK 500 ASP B 211 -141.26 -86.22
REMARK 500 LEU B 234 37.81 -70.23
REMARK 500 SER B 244 -73.41 -64.74
REMARK 500 LEU B 249 -64.97 -97.33
REMARK 500 LYS B 259 -37.16 -131.84
REMARK 500 VAL B 268 11.33 -141.53
REMARK 500 VAL B 303 126.03 -39.47
REMARK 500 ASP B 324 -62.22 -122.95
REMARK 500 GLU C 6 146.60 72.49
REMARK 500 VAL C 13 56.81 -106.48
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 GOL B 1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1336
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U35 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NUCLEOSOME CORE PARTICLECONTAINING THE
REMARK 900 HISTONE DOMAIN OF MACROH2A
REMARK 900 RELATED ID: 2WP1 RELATED DB: PDB
REMARK 900 STRUCTURE OF BRDT BROMODOMAIN 2 BOUND TO AN ACETYLATED HISTONE H3
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1GUW RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHROMODOMAIN FROM MOUSE HP1BETA IN COMPLEX WITH
REMARK 900 THE LYSINE 9- METHYL HISTONE H3 N-TERMINAL PEPTIDE, NMR, 25
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 2XL2 RELATED DB: PDB
REMARK 900 WDR5 IN COMPLEX WITH RBBP5 PEPTIDE RECRUITED TO NOVEL SITE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NON NATIVE CARBOXY TERMINAL TYROSINE
REMARK 999 NON NATIVE TYROSINE AT AMINO TERMINAL
DBREF 2XL3 A 1 334 UNP P61965 WDR5_MOUSE 1 334
DBREF 2XL3 B 1 334 UNP P61965 WDR5_MOUSE 1 334
DBREF 2XL3 C 2 14 UNP Q8BX09 RBBP5_MOUSE 369 381
DBREF 2XL3 D 1 8 UNP P68433 H31_MOUSE 2 9
DBREF 2XL3 E 2 14 UNP Q8BX09 RBBP5_MOUSE 369 381
DBREF 2XL3 F 1 8 UNP P68433 H31_MOUSE 2 9
SEQADV 2XL3 TYR C 1 UNP Q8BX09 EXPRESSION TAG
SEQADV 2XL3 TYR D 9 UNP P68433 EXPRESSION TAG
SEQADV 2XL3 TYR E 1 UNP Q8BX09 EXPRESSION TAG
SEQADV 2XL3 TYR F 9 UNP P68433 EXPRESSION TAG
SEQRES 1 A 334 MET ALA THR GLU GLU LYS LYS PRO GLU THR GLU ALA ALA
SEQRES 2 A 334 ARG ALA GLN PRO THR PRO SER SER SER ALA THR GLN SER
SEQRES 3 A 334 LYS PRO THR PRO VAL LYS PRO ASN TYR ALA LEU LYS PHE
SEQRES 4 A 334 THR LEU ALA GLY HIS THR LYS ALA VAL SER SER VAL LYS
SEQRES 5 A 334 PHE SER PRO ASN GLY GLU TRP LEU ALA SER SER SER ALA
SEQRES 6 A 334 ASP LYS LEU ILE LYS ILE TRP GLY ALA TYR ASP GLY LYS
SEQRES 7 A 334 PHE GLU LYS THR ILE SER GLY HIS LYS LEU GLY ILE SER
SEQRES 8 A 334 ASP VAL ALA TRP SER SER ASP SER ASN LEU LEU VAL SER
SEQRES 9 A 334 ALA SER ASP ASP LYS THR LEU LYS ILE TRP ASP VAL SER
SEQRES 10 A 334 SER GLY LYS CYS LEU LYS THR LEU LYS GLY HIS SER ASN
SEQRES 11 A 334 TYR VAL PHE CYS CYS ASN PHE ASN PRO GLN SER ASN LEU
SEQRES 12 A 334 ILE VAL SER GLY SER PHE ASP GLU SER VAL ARG ILE TRP
SEQRES 13 A 334 ASP VAL LYS THR GLY LYS CYS LEU LYS THR LEU PRO ALA
SEQRES 14 A 334 HIS SER ASP PRO VAL SER ALA VAL HIS PHE ASN ARG ASP
SEQRES 15 A 334 GLY SER LEU ILE VAL SER SER SER TYR ASP GLY LEU CYS
SEQRES 16 A 334 ARG ILE TRP ASP THR ALA SER GLY GLN CYS LEU LYS THR
SEQRES 17 A 334 LEU ILE ASP ASP ASP ASN PRO PRO VAL SER PHE VAL LYS
SEQRES 18 A 334 PHE SER PRO ASN GLY LYS TYR ILE LEU ALA ALA THR LEU
SEQRES 19 A 334 ASP ASN THR LEU LYS LEU TRP ASP TYR SER LYS GLY LYS
SEQRES 20 A 334 CYS LEU LYS THR TYR THR GLY HIS LYS ASN GLU LYS TYR
SEQRES 21 A 334 CYS ILE PHE ALA ASN PHE SER VAL THR GLY GLY LYS TRP
SEQRES 22 A 334 ILE VAL SER GLY SER GLU ASP ASN LEU VAL TYR ILE TRP
SEQRES 23 A 334 ASN LEU GLN THR LYS GLU ILE VAL GLN LYS LEU GLN GLY
SEQRES 24 A 334 HIS THR ASP VAL VAL ILE SER THR ALA CYS HIS PRO THR
SEQRES 25 A 334 GLU ASN ILE ILE ALA SER ALA ALA LEU GLU ASN ASP LYS
SEQRES 26 A 334 THR ILE LYS LEU TRP LYS SER ASP CYS
SEQRES 1 B 334 MET ALA THR GLU GLU LYS LYS PRO GLU THR GLU ALA ALA
SEQRES 2 B 334 ARG ALA GLN PRO THR PRO SER SER SER ALA THR GLN SER
SEQRES 3 B 334 LYS PRO THR PRO VAL LYS PRO ASN TYR ALA LEU LYS PHE
SEQRES 4 B 334 THR LEU ALA GLY HIS THR LYS ALA VAL SER SER VAL LYS
SEQRES 5 B 334 PHE SER PRO ASN GLY GLU TRP LEU ALA SER SER SER ALA
SEQRES 6 B 334 ASP LYS LEU ILE LYS ILE TRP GLY ALA TYR ASP GLY LYS
SEQRES 7 B 334 PHE GLU LYS THR ILE SER GLY HIS LYS LEU GLY ILE SER
SEQRES 8 B 334 ASP VAL ALA TRP SER SER ASP SER ASN LEU LEU VAL SER
SEQRES 9 B 334 ALA SER ASP ASP LYS THR LEU LYS ILE TRP ASP VAL SER
SEQRES 10 B 334 SER GLY LYS CYS LEU LYS THR LEU LYS GLY HIS SER ASN
SEQRES 11 B 334 TYR VAL PHE CYS CYS ASN PHE ASN PRO GLN SER ASN LEU
SEQRES 12 B 334 ILE VAL SER GLY SER PHE ASP GLU SER VAL ARG ILE TRP
SEQRES 13 B 334 ASP VAL LYS THR GLY LYS CYS LEU LYS THR LEU PRO ALA
SEQRES 14 B 334 HIS SER ASP PRO VAL SER ALA VAL HIS PHE ASN ARG ASP
SEQRES 15 B 334 GLY SER LEU ILE VAL SER SER SER TYR ASP GLY LEU CYS
SEQRES 16 B 334 ARG ILE TRP ASP THR ALA SER GLY GLN CYS LEU LYS THR
SEQRES 17 B 334 LEU ILE ASP ASP ASP ASN PRO PRO VAL SER PHE VAL LYS
SEQRES 18 B 334 PHE SER PRO ASN GLY LYS TYR ILE LEU ALA ALA THR LEU
SEQRES 19 B 334 ASP ASN THR LEU LYS LEU TRP ASP TYR SER LYS GLY LYS
SEQRES 20 B 334 CYS LEU LYS THR TYR THR GLY HIS LYS ASN GLU LYS TYR
SEQRES 21 B 334 CYS ILE PHE ALA ASN PHE SER VAL THR GLY GLY LYS TRP
SEQRES 22 B 334 ILE VAL SER GLY SER GLU ASP ASN LEU VAL TYR ILE TRP
SEQRES 23 B 334 ASN LEU GLN THR LYS GLU ILE VAL GLN LYS LEU GLN GLY
SEQRES 24 B 334 HIS THR ASP VAL VAL ILE SER THR ALA CYS HIS PRO THR
SEQRES 25 B 334 GLU ASN ILE ILE ALA SER ALA ALA LEU GLU ASN ASP LYS
SEQRES 26 B 334 THR ILE LYS LEU TRP LYS SER ASP CYS
SEQRES 1 C 14 TYR ALA ALA GLU ASP GLU GLU VAL ASP VAL THR SER VAL
SEQRES 2 C 14 ASP
SEQRES 1 D 9 ALA ARG THR LYS GLN THR ALA ARG TYR
SEQRES 1 E 14 TYR ALA ALA GLU ASP GLU GLU VAL ASP VAL THR SER VAL
SEQRES 2 E 14 ASP
SEQRES 1 F 9 ALA ARG THR LYS GLN THR ALA ARG TYR
HET GOL A1335 6
HET GOL A1336 6
HET GOL B1335 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 HOH *107(H2 O)
SHEET 1 AA 4 ALA A 36 LEU A 41 0
SHEET 2 AA 4 ILE A 327 LYS A 331 -1 O ILE A 327 N LEU A 41
SHEET 3 AA 4 ILE A 315 ALA A 320 -1 O ILE A 316 N TRP A 330
SHEET 4 AA 4 VAL A 304 CYS A 309 -1 N ILE A 305 O ALA A 319
SHEET 1 AB 4 VAL A 48 PHE A 53 0
SHEET 2 AB 4 TRP A 59 SER A 64 -1 O ALA A 61 N LYS A 52
SHEET 3 AB 4 ILE A 69 GLY A 73 -1 O LYS A 70 N SER A 62
SHEET 4 AB 4 PHE A 79 ILE A 83 -1 N GLU A 80 O ILE A 71
SHEET 1 AC 4 ILE A 90 TRP A 95 0
SHEET 2 AC 4 LEU A 101 SER A 106 -1 O VAL A 103 N ALA A 94
SHEET 3 AC 4 THR A 110 ASP A 115 -1 O THR A 110 N SER A 106
SHEET 4 AC 4 CYS A 121 LYS A 126 -1 N LEU A 122 O ILE A 113
SHEET 1 AD 4 VAL A 132 PHE A 137 0
SHEET 2 AD 4 LEU A 143 SER A 148 -1 O VAL A 145 N ASN A 136
SHEET 3 AD 4 VAL A 153 ASP A 157 -1 O ARG A 154 N SER A 146
SHEET 4 AD 4 CYS A 163 LEU A 167 -1 N LEU A 164 O ILE A 155
SHEET 1 AE 4 VAL A 174 PHE A 179 0
SHEET 2 AE 4 LEU A 185 SER A 190 -1 O VAL A 187 N HIS A 178
SHEET 3 AE 4 CYS A 195 ASP A 199 -1 O ARG A 196 N SER A 188
SHEET 4 AE 4 CYS A 205 LEU A 209 -1 N LEU A 206 O ILE A 197
SHEET 1 AF 4 VAL A 217 PHE A 222 0
SHEET 2 AF 4 TYR A 228 THR A 233 -1 O LEU A 230 N LYS A 221
SHEET 3 AF 4 THR A 237 ASP A 242 -1 O THR A 237 N THR A 233
SHEET 4 AF 4 LYS A 247 TYR A 252 -1 O LYS A 247 N ASP A 242
SHEET 1 AG 4 ALA A 264 SER A 267 0
SHEET 2 AG 4 TRP A 273 SER A 276 -1 O TRP A 273 N SER A 267
SHEET 3 AG 4 VAL A 283 ASN A 287 -1 O TYR A 284 N SER A 276
SHEET 4 AG 4 ILE A 293 LEU A 297 -1 N VAL A 294 O ILE A 285
SHEET 1 BA 4 ALA B 36 LEU B 41 0
SHEET 2 BA 4 ILE B 327 LYS B 331 -1 O ILE B 327 N LEU B 41
SHEET 3 BA 4 ILE B 315 ALA B 320 -1 O ILE B 316 N TRP B 330
SHEET 4 BA 4 VAL B 304 CYS B 309 -1 N ILE B 305 O ALA B 319
SHEET 1 BB 4 VAL B 48 PHE B 53 0
SHEET 2 BB 4 TRP B 59 SER B 64 -1 O ALA B 61 N LYS B 52
SHEET 3 BB 4 ILE B 69 GLY B 73 -1 O LYS B 70 N SER B 62
SHEET 4 BB 4 PHE B 79 ILE B 83 -1 N GLU B 80 O ILE B 71
SHEET 1 BC 4 ILE B 90 TRP B 95 0
SHEET 2 BC 4 LEU B 101 SER B 106 -1 O VAL B 103 N ALA B 94
SHEET 3 BC 4 LEU B 111 ASP B 115 -1 O LYS B 112 N SER B 104
SHEET 4 BC 4 CYS B 121 LEU B 125 -1 N LEU B 122 O ILE B 113
SHEET 1 BD 4 VAL B 132 PHE B 137 0
SHEET 2 BD 4 LEU B 143 SER B 148 -1 O VAL B 145 N ASN B 136
SHEET 3 BD 4 VAL B 153 ASP B 157 -1 O ARG B 154 N SER B 146
SHEET 4 BD 4 CYS B 163 LEU B 167 -1 N LEU B 164 O ILE B 155
SHEET 1 BE 4 VAL B 174 PHE B 179 0
SHEET 2 BE 4 LEU B 185 SER B 190 -1 O VAL B 187 N HIS B 178
SHEET 3 BE 4 CYS B 195 ASP B 199 -1 O ARG B 196 N SER B 188
SHEET 4 BE 4 CYS B 205 LEU B 209 -1 N LEU B 206 O ILE B 197
SHEET 1 BF 4 VAL B 217 PHE B 222 0
SHEET 2 BF 4 TYR B 228 THR B 233 -1 O LEU B 230 N LYS B 221
SHEET 3 BF 4 THR B 237 ASP B 242 -1 O THR B 237 N THR B 233
SHEET 4 BF 4 LYS B 247 TYR B 252 -1 O LYS B 247 N ASP B 242
SHEET 1 BG 4 ALA B 264 SER B 267 0
SHEET 2 BG 4 TRP B 273 SER B 276 -1 O TRP B 273 N SER B 267
SHEET 3 BG 4 VAL B 283 ASN B 287 -1 O TYR B 284 N SER B 276
SHEET 4 BG 4 ILE B 293 LEU B 297 -1 N VAL B 294 O ILE B 285
SITE 1 AC1 2 TRP B 59 SER B 117
SITE 1 AC2 4 TRP A 59 GLU A 80 LYS A 81 SER A 117
SITE 1 AC3 3 SER A 129 ASP A 150 GLU A 151
CRYST1 47.100 81.320 86.350 90.00 91.13 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 0.021231 0.000000 0.000419 0.00000
SCALE2 0.000000 0.012297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011583 0.00000
MTRIX1 1 0.998316 -0.000389 0.058006 -1.51768 1
MTRIX2 1 -0.000425 -1.000000 0.000610 15.44420 1
MTRIX3 1 0.058006 -0.000634 -0.998316 41.69840 1
(ATOM LINES ARE NOT SHOWN.)
END
