HEADER GENE REGULATION 31-MAY-06 2H6N
TITLE HISTONE H3 RECOGNITION AND PRESENTATION BY THE WDR5 MODULE OF THE MLL1
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD-REPEAT PROTEIN 5;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 23-334;
COMPND 5 SYNONYM: BMP2-INDUCED 3-KB GENE PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H3 K4-ME2 9-RESIDUE PEPTIDE;
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: WDR5, BIG3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED USING SOLID
SOURCE 14 PHASE SYNTHESIS
KEYWDS WD40 WD-REPEAT HISTONE MODIFICATION MLL SET CHROMATIN, GENE
KEYWDS 2 REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.RUTHENBURG,W.-K.WANG,D.M.GRAYBOSCH,H.LI,C.D.ALLIS,D.J.PATEL,
AUTHOR 2 G.L.VERDINE
REVDAT 5 30-AUG-23 2H6N 1 LINK
REVDAT 4 13-JUL-11 2H6N 1 VERSN
REVDAT 3 24-FEB-09 2H6N 1 VERSN
REVDAT 2 15-AUG-06 2H6N 1 JRNL
REVDAT 1 04-JUL-06 2H6N 0
JRNL AUTH A.J.RUTHENBURG,W.-K.WANG,D.M.GRAYBOSCH,H.LI,C.D.ALLIS,
JRNL AUTH 2 D.J.PATEL,G.L.VERDINE
JRNL TITL HISTONE H3 RECOGNITION AND PRESENTATION BY THE WDR5 MODULE
JRNL TITL 2 OF THE MLL1 COMPLEX.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 13 704 2006
JRNL REFN ISSN 1545-9993
JRNL PMID 16829959
JRNL DOI 10.1038/NSMB1119
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 90444
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 5610
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5779
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 376
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4853
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 632
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 23.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : 0.34000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.444
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4966 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6733 ; 1.292 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 621 ; 7.017 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;32.246 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 856 ;11.848 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.046 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 763 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3640 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2176 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3423 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 474 ; 0.105 ; 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): 47 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 45 ; 0.092 ; 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): 3175 ; 0.730 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5014 ; 1.165 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2082 ; 1.914 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1719 ; 2.955 ; 4.500
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 : 4
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 31 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1363 .9431 33.6061
REMARK 3 T TENSOR
REMARK 3 T11: -.0043 T22: -.0279
REMARK 3 T33: -.0087 T12: .0165
REMARK 3 T13: -.0212 T23: -.0209
REMARK 3 L TENSOR
REMARK 3 L11: .4390 L22: .4096
REMARK 3 L33: .2579 L12: -.1557
REMARK 3 L13: -.2615 L23: -.0317
REMARK 3 S TENSOR
REMARK 3 S11: .0203 S12: .0227 S13: -.0544
REMARK 3 S21: -.0515 S22: -.0729 S23: .0365
REMARK 3 S31: -.0154 S32: -.0237 S33: .0527
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 30 B 334
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0543 23.1737 16.2718
REMARK 3 T TENSOR
REMARK 3 T11: -.0046 T22: -.0357
REMARK 3 T33: -.0122 T12: .0030
REMARK 3 T13: -.0255 T23: .0074
REMARK 3 L TENSOR
REMARK 3 L11: .4705 L22: .3183
REMARK 3 L33: .3922 L12: -.0523
REMARK 3 L13: -.1882 L23: .1866
REMARK 3 S TENSOR
REMARK 3 S11: -.0229 S12: .0092 S13: -.0164
REMARK 3 S21: .0416 S22: -.0115 S23: -.0358
REMARK 3 S31: -.0037 S32: -.0133 S33: .0344
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 8
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3526 4.7938 43.8165
REMARK 3 T TENSOR
REMARK 3 T11: -.0049 T22: -.0225
REMARK 3 T33: -.0284 T12: -.0034
REMARK 3 T13: -.0009 T23: .0024
REMARK 3 L TENSOR
REMARK 3 L11: .4603 L22: 4.1673
REMARK 3 L33: 1.9511 L12: -.3924
REMARK 3 L13: .1471 L23: 1.4111
REMARK 3 S TENSOR
REMARK 3 S11: -.0696 S12: -.2018 S13: .1038
REMARK 3 S21: .1783 S22: .0280 S23: -.0501
REMARK 3 S31: .0074 S32: -.0554 S33: .0416
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 8
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6863 27.1601 6.4209
REMARK 3 T TENSOR
REMARK 3 T11: -.0048 T22: .0151
REMARK 3 T33: -.0428 T12: .0197
REMARK 3 T13: .0078 T23: -.0075
REMARK 3 L TENSOR
REMARK 3 L11: .5678 L22: 4.3353
REMARK 3 L33: 1.5904 L12: .6706
REMARK 3 L13: .7312 L23: -.6526
REMARK 3 S TENSOR
REMARK 3 S11: -.1658 S12: .1519 S13: .0839
REMARK 3 S21: -.1441 S22: .0397 S23: .0396
REMARK 3 S31: -.0308 S32: -.0559 S33: .1261
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2H6N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000037995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98710
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90444
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 43.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.46400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ERJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY HANGING DROP
REMARK 280 VAPOUR EQUILIBRATION IN NEXTAL PLATES AS FOLLOWS: 1 UL OF 10 15
REMARK 280 MG ML-1 PROTEIN SOLUTION (10 MM TRIS HCL (PH 7.4), 50 MM NACL,
REMARK 280 AND 10 MM 2-MERCAPTOETHANOL) WERE MIXED WITH 1 UL OF WELL
REMARK 280 SOLUTION COMPOSED OF 50 MM HEPES (PH 7.5), 100 MM POTASSIUM
REMARK 280 FORMATE, AND 10-20% (W/V) POLYETHYLENE GLYCOL 3350 AND
REMARK 280 EQUILIBRATED AT ROOM TEMPERATURE OVERNIGHT AGAINST 1 ML OF WELL
REMARK 280 SOLUTION.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.37250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.06550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.37250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.06550
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 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 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 LYS C 9
REMARK 465 LYS D 9
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 O HOH A 534 O HOH A 544 2.10
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 LEU A 238 CA - CB - CG ANGL. DEV. = 15.1 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 LEU A 234 41.24 -81.75
REMARK 500 GLU B 151 6.84 82.62
REMARK 500 LEU B 234 43.00 -83.17
REMARK 500 ASP B 324 -67.43 -122.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CO0 RELATED DB: PDB
REMARK 900 WDR5 WITH UNMODIFIED HISTONE H3
REMARK 900 RELATED ID: 2CNX RELATED DB: PDB
REMARK 900 WDR5 WITH HISTONE H3 DIMETHYLATED AT K4, COMPLEX II
REMARK 900 RELATED ID: 2H68 RELATED DB: PDB
REMARK 900 APO-WDR5
REMARK 900 RELATED ID: 2H6K RELATED DB: PDB
REMARK 900 WDR5 WITH HISTONE H3 MONOMETHYLATED AT K4
REMARK 900 RELATED ID: 2H6Q RELATED DB: PDB
DBREF 2H6N A 23 334 UNP P61964 WDR5_HUMAN 23 334
DBREF 2H6N B 23 334 UNP P61964 WDR5_HUMAN 23 334
DBREF 2H6N C 1 9 PDB 2H6N 2H6N 1 9
DBREF 2H6N D 1 9 PDB 2H6N 2H6N 1 9
SEQRES 1 A 312 ALA THR GLN SER LYS PRO THR PRO VAL LYS PRO ASN TYR
SEQRES 2 A 312 ALA LEU LYS PHE THR LEU ALA GLY HIS THR LYS ALA VAL
SEQRES 3 A 312 SER SER VAL LYS PHE SER PRO ASN GLY GLU TRP LEU ALA
SEQRES 4 A 312 SER SER SER ALA ASP LYS LEU ILE LYS ILE TRP GLY ALA
SEQRES 5 A 312 TYR ASP GLY LYS PHE GLU LYS THR ILE SER GLY HIS LYS
SEQRES 6 A 312 LEU GLY ILE SER ASP VAL ALA TRP SER SER ASP SER ASN
SEQRES 7 A 312 LEU LEU VAL SER ALA SER ASP ASP LYS THR LEU LYS ILE
SEQRES 8 A 312 TRP ASP VAL SER SER GLY LYS CYS LEU LYS THR LEU LYS
SEQRES 9 A 312 GLY HIS SER ASN TYR VAL PHE CYS CYS ASN PHE ASN PRO
SEQRES 10 A 312 GLN SER ASN LEU ILE VAL SER GLY SER PHE ASP GLU SER
SEQRES 11 A 312 VAL ARG ILE TRP ASP VAL LYS THR GLY LYS CYS LEU LYS
SEQRES 12 A 312 THR LEU PRO ALA HIS SER ASP PRO VAL SER ALA VAL HIS
SEQRES 13 A 312 PHE ASN ARG ASP GLY SER LEU ILE VAL SER SER SER TYR
SEQRES 14 A 312 ASP GLY LEU CYS ARG ILE TRP ASP THR ALA SER GLY GLN
SEQRES 15 A 312 CYS LEU LYS THR LEU ILE ASP ASP ASP ASN PRO PRO VAL
SEQRES 16 A 312 SER PHE VAL LYS PHE SER PRO ASN GLY LYS TYR ILE LEU
SEQRES 17 A 312 ALA ALA THR LEU ASP ASN THR LEU LYS LEU TRP ASP TYR
SEQRES 18 A 312 SER LYS GLY LYS CYS LEU LYS THR TYR THR GLY HIS LYS
SEQRES 19 A 312 ASN GLU LYS TYR CYS ILE PHE ALA ASN PHE SER VAL THR
SEQRES 20 A 312 GLY GLY LYS TRP ILE VAL SER GLY SER GLU ASP ASN LEU
SEQRES 21 A 312 VAL TYR ILE TRP ASN LEU GLN THR LYS GLU ILE VAL GLN
SEQRES 22 A 312 LYS LEU GLN GLY HIS THR ASP VAL VAL ILE SER THR ALA
SEQRES 23 A 312 CYS HIS PRO THR GLU ASN ILE ILE ALA SER ALA ALA LEU
SEQRES 24 A 312 GLU ASN ASP LYS THR ILE LYS LEU TRP LYS SER ASP CYS
SEQRES 1 B 312 ALA THR GLN SER LYS PRO THR PRO VAL LYS PRO ASN TYR
SEQRES 2 B 312 ALA LEU LYS PHE THR LEU ALA GLY HIS THR LYS ALA VAL
SEQRES 3 B 312 SER SER VAL LYS PHE SER PRO ASN GLY GLU TRP LEU ALA
SEQRES 4 B 312 SER SER SER ALA ASP LYS LEU ILE LYS ILE TRP GLY ALA
SEQRES 5 B 312 TYR ASP GLY LYS PHE GLU LYS THR ILE SER GLY HIS LYS
SEQRES 6 B 312 LEU GLY ILE SER ASP VAL ALA TRP SER SER ASP SER ASN
SEQRES 7 B 312 LEU LEU VAL SER ALA SER ASP ASP LYS THR LEU LYS ILE
SEQRES 8 B 312 TRP ASP VAL SER SER GLY LYS CYS LEU LYS THR LEU LYS
SEQRES 9 B 312 GLY HIS SER ASN TYR VAL PHE CYS CYS ASN PHE ASN PRO
SEQRES 10 B 312 GLN SER ASN LEU ILE VAL SER GLY SER PHE ASP GLU SER
SEQRES 11 B 312 VAL ARG ILE TRP ASP VAL LYS THR GLY LYS CYS LEU LYS
SEQRES 12 B 312 THR LEU PRO ALA HIS SER ASP PRO VAL SER ALA VAL HIS
SEQRES 13 B 312 PHE ASN ARG ASP GLY SER LEU ILE VAL SER SER SER TYR
SEQRES 14 B 312 ASP GLY LEU CYS ARG ILE TRP ASP THR ALA SER GLY GLN
SEQRES 15 B 312 CYS LEU LYS THR LEU ILE ASP ASP ASP ASN PRO PRO VAL
SEQRES 16 B 312 SER PHE VAL LYS PHE SER PRO ASN GLY LYS TYR ILE LEU
SEQRES 17 B 312 ALA ALA THR LEU ASP ASN THR LEU LYS LEU TRP ASP TYR
SEQRES 18 B 312 SER LYS GLY LYS CYS LEU LYS THR TYR THR GLY HIS LYS
SEQRES 19 B 312 ASN GLU LYS TYR CYS ILE PHE ALA ASN PHE SER VAL THR
SEQRES 20 B 312 GLY GLY LYS TRP ILE VAL SER GLY SER GLU ASP ASN LEU
SEQRES 21 B 312 VAL TYR ILE TRP ASN LEU GLN THR LYS GLU ILE VAL GLN
SEQRES 22 B 312 LYS LEU GLN GLY HIS THR ASP VAL VAL ILE SER THR ALA
SEQRES 23 B 312 CYS HIS PRO THR GLU ASN ILE ILE ALA SER ALA ALA LEU
SEQRES 24 B 312 GLU ASN ASP LYS THR ILE LYS LEU TRP LYS SER ASP CYS
SEQRES 1 C 9 ALA ARG THR MLY GLN THR ALA ARG LYS
SEQRES 1 D 9 ALA ARG THR MLY GLN THR ALA ARG LYS
MODRES 2H6N MLY C 4 LYS N-DIMETHYL-LYSINE
MODRES 2H6N MLY D 4 LYS N-DIMETHYL-LYSINE
HET MLY C 4 11
HET MLY D 4 11
HETNAM MLY N-DIMETHYL-LYSINE
FORMUL 3 MLY 2(C8 H18 N2 O2)
FORMUL 5 HOH *632(H2 O)
SHEET 1 A 4 ALA A 36 LEU A 41 0
SHEET 2 A 4 ILE A 327 LYS A 331 -1 O ILE A 327 N LEU A 41
SHEET 3 A 4 ILE A 315 ALA A 320 -1 N ILE A 316 O TRP A 330
SHEET 4 A 4 VAL A 304 CYS A 309 -1 N ALA A 308 O ALA A 317
SHEET 1 B 4 VAL A 48 PHE A 53 0
SHEET 2 B 4 TRP A 59 SER A 64 -1 O SER A 63 N SER A 49
SHEET 3 B 4 ILE A 69 GLY A 73 -1 O TRP A 72 N LEU A 60
SHEET 4 B 4 PHE A 79 ILE A 83 -1 O ILE A 83 N ILE A 69
SHEET 1 C 4 ILE A 90 TRP A 95 0
SHEET 2 C 4 LEU A 101 SER A 106 -1 O ALA A 105 N SER A 91
SHEET 3 C 4 THR A 110 ASP A 115 -1 O TRP A 114 N LEU A 102
SHEET 4 C 4 LYS A 120 LYS A 126 -1 O LEU A 122 N ILE A 113
SHEET 1 D 4 VAL A 132 PHE A 137 0
SHEET 2 D 4 LEU A 143 SER A 148 -1 O VAL A 145 N ASN A 136
SHEET 3 D 4 VAL A 153 ASP A 157 -1 O TRP A 156 N ILE A 144
SHEET 4 D 4 CYS A 163 LEU A 167 -1 O LEU A 167 N VAL A 153
SHEET 1 E 4 VAL A 174 PHE A 179 0
SHEET 2 E 4 LEU A 185 SER A 190 -1 O VAL A 187 N HIS A 178
SHEET 3 E 4 CYS A 195 ASP A 199 -1 O TRP A 198 N ILE A 186
SHEET 4 E 4 CYS A 205 LEU A 209 -1 O LEU A 209 N CYS A 195
SHEET 1 F 4 VAL A 217 PHE A 222 0
SHEET 2 F 4 ILE A 229 THR A 233 -1 O LEU A 230 N LYS A 221
SHEET 3 F 4 THR A 237 ASP A 242 -1 O TRP A 241 N ILE A 229
SHEET 4 F 4 LYS A 247 THR A 253 -1 O LYS A 247 N ASP A 242
SHEET 1 G 4 ALA A 264 SER A 267 0
SHEET 2 G 4 TRP A 273 SER A 276 -1 O VAL A 275 N ASN A 265
SHEET 3 G 4 VAL A 283 ASN A 287 -1 O TYR A 284 N SER A 276
SHEET 4 G 4 ILE A 293 LEU A 297 -1 O VAL A 294 N ILE A 285
SHEET 1 H 4 ALA B 36 LEU B 41 0
SHEET 2 H 4 ILE B 327 LYS B 331 -1 O ILE B 327 N LEU B 41
SHEET 3 H 4 ILE B 315 ALA B 320 -1 N ILE B 316 O TRP B 330
SHEET 4 H 4 VAL B 304 CYS B 309 -1 N ALA B 308 O ALA B 317
SHEET 1 I 4 VAL B 48 PHE B 53 0
SHEET 2 I 4 TRP B 59 SER B 64 -1 O ALA B 61 N LYS B 52
SHEET 3 I 4 ILE B 69 GLY B 73 -1 O LYS B 70 N SER B 62
SHEET 4 I 4 PHE B 79 ILE B 83 -1 O ILE B 83 N ILE B 69
SHEET 1 J 4 ILE B 90 TRP B 95 0
SHEET 2 J 4 LEU B 101 SER B 106 -1 O ALA B 105 N SER B 91
SHEET 3 J 4 THR B 110 ASP B 115 -1 O TRP B 114 N LEU B 102
SHEET 4 J 4 CYS B 121 LYS B 126 -1 O LEU B 125 N LEU B 111
SHEET 1 K 4 VAL B 132 PHE B 137 0
SHEET 2 K 4 LEU B 143 SER B 148 -1 O VAL B 145 N ASN B 136
SHEET 3 K 4 VAL B 153 ASP B 157 -1 O TRP B 156 N ILE B 144
SHEET 4 K 4 CYS B 163 LEU B 167 -1 O LEU B 167 N VAL B 153
SHEET 1 L 4 VAL B 174 PHE B 179 0
SHEET 2 L 4 LEU B 185 SER B 190 -1 O VAL B 187 N HIS B 178
SHEET 3 L 4 CYS B 195 ASP B 199 -1 O TRP B 198 N ILE B 186
SHEET 4 L 4 CYS B 205 LEU B 209 -1 O LEU B 209 N CYS B 195
SHEET 1 M 4 VAL B 217 PHE B 222 0
SHEET 2 M 4 ILE B 229 THR B 233 -1 O LEU B 230 N LYS B 221
SHEET 3 M 4 THR B 237 ASP B 242 -1 O TRP B 241 N ILE B 229
SHEET 4 M 4 LYS B 247 THR B 253 -1 O LYS B 247 N ASP B 242
SHEET 1 N 4 ALA B 264 SER B 267 0
SHEET 2 N 4 TRP B 273 SER B 276 -1 O TRP B 273 N SER B 267
SHEET 3 N 4 VAL B 283 ASN B 287 -1 O TYR B 284 N SER B 276
SHEET 4 N 4 ILE B 293 LEU B 297 -1 O VAL B 294 N ILE B 285
LINK C THR C 3 N MLY C 4 1555 1555 1.34
LINK C MLY C 4 N GLN C 5 1555 1555 1.33
LINK C THR D 3 N MLY D 4 1555 1555 1.33
LINK C MLY D 4 N GLN D 5 1555 1555 1.33
CRYST1 134.745 46.131 112.694 90.00 117.17 90.00 C 1 2 1 8
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 0.007421 0.000000 0.003809 0.00000
SCALE2 0.000000 0.021677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009974 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
