HEADER STRUCTURAL GENOMICS, GENE REGULATION 10-JUN-06 2H9L
TITLE WDR5DELTA23
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD-REPEAT PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BMP2-INDUCED 3-KB GENE PROTEIN, WDR5;
COMPND 5 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
KEYWDS WDR5, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, GENE
KEYWDS 2 REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.MIN,A.SCHUETZ,A.ALLALI-HASSANI,F.MARTIN,P.LOPPNAU,M.VEDADI,
AUTHOR 2 J.WEIGELT,M.SUNDSTROM,A.M.EDWARDS,C.H.ARROWSMITH,A.BOCHKAREV,
AUTHOR 3 A.N.PLOTNIKOV,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 14-FEB-24 2H9L 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2H9L 1 VERSN
REVDAT 3 03-OCT-06 2H9L 1 JRNL
REVDAT 2 12-SEP-06 2H9L 1 JRNL
REVDAT 1 01-AUG-06 2H9L 0
JRNL AUTH A.SCHUETZ,A.ALLALI-HASSANI,P.LOPPNAU,M.VEDADI,A.BOCHKAREV,
JRNL AUTH 2 A.N.PLOTNIKOV,C.H.ARROWSMITH,J.MIN
JRNL TITL STRUCTURAL BASIS FOR MOLECULAR RECOGNITION AND PRESENTATION
JRNL TITL 2 OF HISTONE H3 BY WDR5.
JRNL REF EMBO J. V. 25 4245 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16946699
JRNL DOI 10.1038/SJ.EMBOJ.7601316
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 32047
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1689
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1589
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2487
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 423
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -0.73000
REMARK 3 B12 (A**2) : 0.00000
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): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.932
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2607 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3547 ; 1.339 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 332 ; 7.652 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;30.950 ;25.248
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 448 ;13.405 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;22.985 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 393 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1940 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1242 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1757 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 345 ; 0.120 ; 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): 66 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 37 ; 0.140 ; 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): 1666 ; 0.754 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2643 ; 1.217 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1098 ; 2.025 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 904 ; 3.139 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2H9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU), DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33771
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 62.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 5000 MME, 0.1M BIS-TRIS 6.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K, PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 25.04700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.96700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.76750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.96700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.04700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.76750
REMARK 290 SMTRY3 4 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: MONOMERIC
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 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 SER A 13
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 ASP A 212 CB CG OD1 OD2
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 567 O HOH A 881 2.12
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 OD1 ASN A 214 O HOH A 818 3545 1.83
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 GLU A 151 5.21 80.59
REMARK 500 ASP A 212 -66.58 132.30
REMARK 500 ASN A 214 79.38 10.71
REMARK 500 LEU A 321 -166.18 -76.16
REMARK 500 LEU A 321 -169.17 -76.16
REMARK 500 ASP A 324 -62.97 -126.73
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GNQ RELATED DB: PDB
REMARK 900 RELATED ID: 2H92 RELATED DB: PDB
REMARK 900 RELATED ID: 2H93 RELATED DB: PDB
REMARK 900 RELATED ID: 2H94 RELATED DB: PDB
REMARK 900 RELATED ID: 2H95 RELATED DB: PDB
DBREF 2H9L A 24 334 UNP P61964 WDR5_HUMAN 24 334
SEQADV 2H9L MET A 6 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 7 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 8 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 9 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 10 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 11 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L HIS A 12 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L SER A 13 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L SER A 14 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L GLY A 15 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L ARG A 16 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L GLU A 17 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L ASN A 18 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L LEU A 19 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L TYR A 20 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L PHE A 21 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L GLN A 22 UNP P61964 CLONING ARTIFACT
SEQADV 2H9L GLY A 23 UNP P61964 CLONING ARTIFACT
SEQRES 1 A 329 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 329 LEU TYR PHE GLN GLY THR GLN SER LYS PRO THR PRO VAL
SEQRES 3 A 329 LYS PRO ASN TYR ALA LEU LYS PHE THR LEU ALA GLY HIS
SEQRES 4 A 329 THR LYS ALA VAL SER SER VAL LYS PHE SER PRO ASN GLY
SEQRES 5 A 329 GLU TRP LEU ALA SER SER SER ALA ASP LYS LEU ILE LYS
SEQRES 6 A 329 ILE TRP GLY ALA TYR ASP GLY LYS PHE GLU LYS THR ILE
SEQRES 7 A 329 SER GLY HIS LYS LEU GLY ILE SER ASP VAL ALA TRP SER
SEQRES 8 A 329 SER ASP SER ASN LEU LEU VAL SER ALA SER ASP ASP LYS
SEQRES 9 A 329 THR LEU LYS ILE TRP ASP VAL SER SER GLY LYS CYS LEU
SEQRES 10 A 329 LYS THR LEU LYS GLY HIS SER ASN TYR VAL PHE CYS CYS
SEQRES 11 A 329 ASN PHE ASN PRO GLN SER ASN LEU ILE VAL SER GLY SER
SEQRES 12 A 329 PHE ASP GLU SER VAL ARG ILE TRP ASP VAL LYS THR GLY
SEQRES 13 A 329 LYS CYS LEU LYS THR LEU PRO ALA HIS SER ASP PRO VAL
SEQRES 14 A 329 SER ALA VAL HIS PHE ASN ARG ASP GLY SER LEU ILE VAL
SEQRES 15 A 329 SER SER SER TYR ASP GLY LEU CYS ARG ILE TRP ASP THR
SEQRES 16 A 329 ALA SER GLY GLN CYS LEU LYS THR LEU ILE ASP ASP ASP
SEQRES 17 A 329 ASN PRO PRO VAL SER PHE VAL LYS PHE SER PRO ASN GLY
SEQRES 18 A 329 LYS TYR ILE LEU ALA ALA THR LEU ASP ASN THR LEU LYS
SEQRES 19 A 329 LEU TRP ASP TYR SER LYS GLY LYS CYS LEU LYS THR TYR
SEQRES 20 A 329 THR GLY HIS LYS ASN GLU LYS TYR CYS ILE PHE ALA ASN
SEQRES 21 A 329 PHE SER VAL THR GLY GLY LYS TRP ILE VAL SER GLY SER
SEQRES 22 A 329 GLU ASP ASN LEU VAL TYR ILE TRP ASN LEU GLN THR LYS
SEQRES 23 A 329 GLU ILE VAL GLN LYS LEU GLN GLY HIS THR ASP VAL VAL
SEQRES 24 A 329 ILE SER THR ALA CYS HIS PRO THR GLU ASN ILE ILE ALA
SEQRES 25 A 329 SER ALA ALA LEU GLU ASN ASP LYS THR ILE LYS LEU TRP
SEQRES 26 A 329 LYS SER ASP CYS
HET SO4 A 501 5
HET SO4 A 502 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 HOH *423(H2 O)
HELIX 1 1 SER A 14 LEU A 19 5 6
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 SER A 318 O LYS A 328
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 LYS A 70 N SER A 62
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 LEU A 111 ASP A 115 -1 O TRP A 114 N LEU A 102
SHEET 4 C 4 CYS A 121 LEU A 125 -1 O LEU A 125 N LEU A 111
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 LEU A 194 ASP A 199 -1 O TRP A 198 N ILE A 186
SHEET 4 E 4 CYS A 205 ILE A 210 -1 O LYS A 207 N ILE A 197
SHEET 1 F 4 VAL A 217 PHE A 222 0
SHEET 2 F 4 TYR A 228 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 TRP A 273 N SER A 267
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
SITE 1 AC1 10 LYS A 272 ASN A 287 LEU A 288 GLN A 289
SITE 2 AC1 10 HOH A 519 HOH A 572 HOH A 601 HOH A 610
SITE 3 AC1 10 HOH A 621 HOH A 848
SITE 1 AC2 8 LYS A 221 ASN A 265 PHE A 266 HOH A 510
SITE 2 AC2 8 HOH A 574 HOH A 620 HOH A 630 HOH A 737
CRYST1 50.094 55.535 123.934 90.00 90.00 90.00 P 21 21 21 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 0.019962 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008069 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
