HEADER TRANSCRIPTION 28-JUN-11 3SMR
TITLE CRYSTAL STRUCTURE OF HUMAN WD REPEAT DOMAIN 5 WITH COMPOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD REPEAT-CONTAINING PROTEIN 5;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BMP2-INDUCED 3-KB GENE PROTEIN;
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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: E.COLI BL21(DE3) V2RPRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS WDR5, SGC, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, WD
KEYWDS 2 REPEAT DOMAIN 5, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,L.DOMBROVSKI,G.A.WASNEY,W.TEMPEL,G.SENISTERRA,Y.BOLSHAN,
AUTHOR 2 D.SMIL,K.T.NGUYEN,T.HAJIAN,G.PODA,R.AL-AWAR,C.BOUNTRA,J.WEIGELT,
AUTHOR 3 A.M.EDWARDS,P.J.BROWN,M.SCHAPIRA,C.H.ARROWSMITH,M.VEDADI,H.WU,
AUTHOR 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 13-SEP-23 3SMR 1 REMARK SEQADV
REVDAT 2 16-MAY-18 3SMR 1 JRNL
REVDAT 1 31-AUG-11 3SMR 0
JRNL AUTH G.SENISTERRA,H.WU,A.ALLALI-HASSANI,G.A.WASNEY,
JRNL AUTH 2 D.BARSYTE-LOVEJOY,L.DOMBROVSKI,A.DONG,K.T.NGUYEN,D.SMIL,
JRNL AUTH 3 Y.BOLSHAN,T.HAJIAN,H.HE,A.SEITOVA,I.CHAU,F.LI,G.PODA,
JRNL AUTH 4 J.F.COUTURE,P.J.BROWN,R.AL-AWAR,M.SCHAPIRA,C.H.ARROWSMITH,
JRNL AUTH 5 M.VEDADI
JRNL TITL SMALL-MOLECULE INHIBITION OF MLL ACTIVITY BY DISRUPTION OF
JRNL TITL 2 ITS INTERACTION WITH WDR5.
JRNL REF BIOCHEM. J. V. 449 151 2013
JRNL REFN ESSN 1470-8728
JRNL PMID 22989411
JRNL DOI 10.1042/BJ20121280
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 103163
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1043
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7383
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9233
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 228
REMARK 3 SOLVENT ATOMS : 822
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.20000
REMARK 3 B22 (A**2) : -0.98000
REMARK 3 B33 (A**2) : -0.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.578
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9776 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13280 ; 1.134 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1233 ; 6.844 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 369 ;30.519 ;25.122
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1555 ;13.264 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;23.264 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1490 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7286 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 6101 ; 0.350 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9849 ; 0.645 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3675 ; 0.988 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3431 ; 1.567 ; 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 : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 31 A 334
REMARK 3 RESIDUE RANGE : A 1000 A 1000
REMARK 3 RESIDUE RANGE : A 500 A 692
REMARK 3 ORIGIN FOR THE GROUP (A): 123.5767 47.3645 33.0886
REMARK 3 T TENSOR
REMARK 3 T11: 0.0278 T22: 0.0465
REMARK 3 T33: 0.0118 T12: -0.0044
REMARK 3 T13: 0.0001 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.5264 L22: 2.1687
REMARK 3 L33: 1.3033 L12: -0.5685
REMARK 3 L13: -0.3842 L23: 0.3180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: -0.0475 S13: -0.0363
REMARK 3 S21: 0.1235 S22: -0.0117 S23: 0.0495
REMARK 3 S31: 0.0917 S32: -0.0456 S33: 0.0677
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 31 B 334
REMARK 3 RESIDUE RANGE : B 1000 B 1000
REMARK 3 RESIDUE RANGE : B 500 B 731
REMARK 3 ORIGIN FOR THE GROUP (A): 120.6379 0.4969 32.5156
REMARK 3 T TENSOR
REMARK 3 T11: 0.0235 T22: 0.0394
REMARK 3 T33: 0.0160 T12: -0.0234
REMARK 3 T13: 0.0039 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.0961 L22: 1.3668
REMARK 3 L33: 1.1315 L12: 0.0105
REMARK 3 L13: -0.4827 L23: -0.1383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0182 S12: -0.0330 S13: 0.0078
REMARK 3 S21: 0.0208 S22: -0.0375 S23: -0.0561
REMARK 3 S31: 0.0651 S32: -0.0048 S33: 0.0557
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 31 C 334
REMARK 3 RESIDUE RANGE : C 1000 C 1000
REMARK 3 RESIDUE RANGE : C 500 C 709
REMARK 3 ORIGIN FOR THE GROUP (A): 104.0711 23.6719 59.1255
REMARK 3 T TENSOR
REMARK 3 T11: 0.0902 T22: 0.0396
REMARK 3 T33: 0.0349 T12: -0.0227
REMARK 3 T13: 0.0410 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.2884 L22: 1.9663
REMARK 3 L33: 0.8338 L12: 0.0839
REMARK 3 L13: 0.3340 L23: -0.2903
REMARK 3 S TENSOR
REMARK 3 S11: 0.1092 S12: 0.0732 S13: 0.1580
REMARK 3 S21: 0.1971 S22: -0.1237 S23: 0.1487
REMARK 3 S31: -0.1250 S32: 0.0771 S33: 0.0145
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 31 D 334
REMARK 3 RESIDUE RANGE : D 1000 D 1000
REMARK 3 RESIDUE RANGE : D 500 D 724
REMARK 3 ORIGIN FOR THE GROUP (A): 104.0960 69.8570 59.7434
REMARK 3 T TENSOR
REMARK 3 T11: 0.0605 T22: 0.0566
REMARK 3 T33: 0.0368 T12: -0.0294
REMARK 3 T13: 0.0335 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.9792 L22: 1.5245
REMARK 3 L33: 0.8770 L12: -0.0317
REMARK 3 L13: 0.3095 L23: -0.1241
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: 0.1152 S13: -0.0099
REMARK 3 S21: 0.1226 S22: -0.0350 S23: 0.0966
REMARK 3 S31: -0.0768 S32: 0.1108 S33: 0.0388
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 3SMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-11
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VERIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104206
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.80700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.120
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: 2O9K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350,9.2M NH4 ACETATE, 0.1 BIS
REMARK 280 TRIS PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
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 102.08550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.73350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 102.08550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.73350
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, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY 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 ASP A 211
REMARK 465 ASP A 212
REMARK 465 GLY 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 ASP B 212
REMARK 465 GLY C 23
REMARK 465 THR C 24
REMARK 465 GLN C 25
REMARK 465 SER C 26
REMARK 465 LYS C 27
REMARK 465 PRO C 28
REMARK 465 THR C 29
REMARK 465 PRO C 30
REMARK 465 ASP C 211
REMARK 465 GLY D 23
REMARK 465 THR D 24
REMARK 465 GLN D 25
REMARK 465 SER D 26
REMARK 465 LYS D 27
REMARK 465 PRO D 28
REMARK 465 THR D 29
REMARK 465 PRO D 30
REMARK 465 ASP D 211
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 VAL A 31 CG1 CG2
REMARK 470 LYS A 32 CG CD CE NZ
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 87 CE NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 LYS A 207 CE NZ
REMARK 470 ILE A 210 CG1 CG2 CD1
REMARK 470 LYS A 227 CD CE NZ
REMARK 470 LYS A 245 CD CE NZ
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 LYS A 256 CD CE NZ
REMARK 470 LYS A 331 CG CD CE NZ
REMARK 470 LYS B 78 CD CE NZ
REMARK 470 LYS B 87 CE NZ
REMARK 470 LYS B 120 CD CE NZ
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 162 CG CD CE NZ
REMARK 470 ARG B 181 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 207 CD CE NZ
REMARK 470 ASN B 214 CG OD1 ND2
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 LYS B 245 CD CE NZ
REMARK 470 LYS B 247 CG CD CE NZ
REMARK 470 LYS B 256 CD CE NZ
REMARK 470 LYS B 259 CE NZ
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 LYS C 32 CE NZ
REMARK 470 LYS C 87 CE NZ
REMARK 470 LYS C 120 CD CE NZ
REMARK 470 LYS C 159 CG CD CE NZ
REMARK 470 LYS C 162 CG CD CE NZ
REMARK 470 ASP C 212 CG OD1 OD2
REMARK 470 LYS C 227 CG CD CE NZ
REMARK 470 LYS C 239 NZ
REMARK 470 SER C 244 OG
REMARK 470 LYS C 245 CE NZ
REMARK 470 LYS C 247 CG CD CE NZ
REMARK 470 VAL D 31 CG1 CG2
REMARK 470 LYS D 32 CG CD CE NZ
REMARK 470 LYS D 87 CE NZ
REMARK 470 LYS D 120 CD CE NZ
REMARK 470 LYS D 159 CD CE NZ
REMARK 470 LYS D 162 CD CE NZ
REMARK 470 ILE D 210 CG1 CG2 CD1
REMARK 470 LYS D 227 CG CD CE NZ
REMARK 470 SER D 244 OG
REMARK 470 LYS D 245 CE NZ
REMARK 470 LYS D 247 CD CE NZ
REMARK 470 LYS D 256 CD CE NZ
REMARK 470 GLU D 322 CD OE1 OE2
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 ASP A 150 4.20 -68.47
REMARK 500 ASN A 214 61.78 37.62
REMARK 500 ASN A 214 68.57 -118.32
REMARK 500 LEU A 234 35.60 -83.92
REMARK 500 LYS A 259 -50.34 -127.08
REMARK 500 LYS A 291 -1.40 75.80
REMARK 500 LEU A 321 -164.41 -79.04
REMARK 500 LEU A 321 -163.17 -79.04
REMARK 500 ASP A 324 -64.69 -120.31
REMARK 500 LEU B 234 34.02 -74.30
REMARK 500 ASN B 257 87.12 -153.25
REMARK 500 LYS B 259 -50.16 -122.51
REMARK 500 LYS B 291 -1.89 76.80
REMARK 500 LEU B 321 -158.44 -84.01
REMARK 500 ASP B 324 -64.29 -126.62
REMARK 500 LYS C 67 1.78 80.31
REMARK 500 ASP C 150 1.73 -67.23
REMARK 500 LEU C 234 32.52 -76.51
REMARK 500 ASN C 257 88.60 -159.12
REMARK 500 LYS C 259 -50.42 -128.41
REMARK 500 LEU C 321 -167.50 -77.01
REMARK 500 ASP D 150 3.78 -67.50
REMARK 500 GLU D 151 1.71 80.20
REMARK 500 LEU D 234 37.33 -81.70
REMARK 500 ASN D 257 88.58 -154.90
REMARK 500 ASN D 257 89.07 -154.90
REMARK 500 LYS D 259 -52.31 -134.63
REMARK 500 LYS D 259 -52.31 -126.09
REMARK 500 LEU D 321 -168.45 -78.49
REMARK 500 ASP D 324 -62.56 -120.13
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 NP7 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2018
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2020
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NP7 B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2022
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NP7 C 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2017
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2021
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NP7 D 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2012
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2016
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2019
DBREF 3SMR A 24 334 UNP P61964 WDR5_HUMAN 24 334
DBREF 3SMR B 24 334 UNP P61964 WDR5_HUMAN 24 334
DBREF 3SMR C 24 334 UNP P61964 WDR5_HUMAN 24 334
DBREF 3SMR D 24 334 UNP P61964 WDR5_HUMAN 24 334
SEQADV 3SMR GLY A 23 UNP P61964 EXPRESSION TAG
SEQADV 3SMR GLY B 23 UNP P61964 EXPRESSION TAG
SEQADV 3SMR GLY C 23 UNP P61964 EXPRESSION TAG
SEQADV 3SMR GLY D 23 UNP P61964 EXPRESSION TAG
SEQRES 1 A 312 GLY 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 GLY 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 312 GLY THR GLN SER LYS PRO THR PRO VAL LYS PRO ASN TYR
SEQRES 2 C 312 ALA LEU LYS PHE THR LEU ALA GLY HIS THR LYS ALA VAL
SEQRES 3 C 312 SER SER VAL LYS PHE SER PRO ASN GLY GLU TRP LEU ALA
SEQRES 4 C 312 SER SER SER ALA ASP LYS LEU ILE LYS ILE TRP GLY ALA
SEQRES 5 C 312 TYR ASP GLY LYS PHE GLU LYS THR ILE SER GLY HIS LYS
SEQRES 6 C 312 LEU GLY ILE SER ASP VAL ALA TRP SER SER ASP SER ASN
SEQRES 7 C 312 LEU LEU VAL SER ALA SER ASP ASP LYS THR LEU LYS ILE
SEQRES 8 C 312 TRP ASP VAL SER SER GLY LYS CYS LEU LYS THR LEU LYS
SEQRES 9 C 312 GLY HIS SER ASN TYR VAL PHE CYS CYS ASN PHE ASN PRO
SEQRES 10 C 312 GLN SER ASN LEU ILE VAL SER GLY SER PHE ASP GLU SER
SEQRES 11 C 312 VAL ARG ILE TRP ASP VAL LYS THR GLY LYS CYS LEU LYS
SEQRES 12 C 312 THR LEU PRO ALA HIS SER ASP PRO VAL SER ALA VAL HIS
SEQRES 13 C 312 PHE ASN ARG ASP GLY SER LEU ILE VAL SER SER SER TYR
SEQRES 14 C 312 ASP GLY LEU CYS ARG ILE TRP ASP THR ALA SER GLY GLN
SEQRES 15 C 312 CYS LEU LYS THR LEU ILE ASP ASP ASP ASN PRO PRO VAL
SEQRES 16 C 312 SER PHE VAL LYS PHE SER PRO ASN GLY LYS TYR ILE LEU
SEQRES 17 C 312 ALA ALA THR LEU ASP ASN THR LEU LYS LEU TRP ASP TYR
SEQRES 18 C 312 SER LYS GLY LYS CYS LEU LYS THR TYR THR GLY HIS LYS
SEQRES 19 C 312 ASN GLU LYS TYR CYS ILE PHE ALA ASN PHE SER VAL THR
SEQRES 20 C 312 GLY GLY LYS TRP ILE VAL SER GLY SER GLU ASP ASN LEU
SEQRES 21 C 312 VAL TYR ILE TRP ASN LEU GLN THR LYS GLU ILE VAL GLN
SEQRES 22 C 312 LYS LEU GLN GLY HIS THR ASP VAL VAL ILE SER THR ALA
SEQRES 23 C 312 CYS HIS PRO THR GLU ASN ILE ILE ALA SER ALA ALA LEU
SEQRES 24 C 312 GLU ASN ASP LYS THR ILE LYS LEU TRP LYS SER ASP CYS
SEQRES 1 D 312 GLY THR GLN SER LYS PRO THR PRO VAL LYS PRO ASN TYR
SEQRES 2 D 312 ALA LEU LYS PHE THR LEU ALA GLY HIS THR LYS ALA VAL
SEQRES 3 D 312 SER SER VAL LYS PHE SER PRO ASN GLY GLU TRP LEU ALA
SEQRES 4 D 312 SER SER SER ALA ASP LYS LEU ILE LYS ILE TRP GLY ALA
SEQRES 5 D 312 TYR ASP GLY LYS PHE GLU LYS THR ILE SER GLY HIS LYS
SEQRES 6 D 312 LEU GLY ILE SER ASP VAL ALA TRP SER SER ASP SER ASN
SEQRES 7 D 312 LEU LEU VAL SER ALA SER ASP ASP LYS THR LEU LYS ILE
SEQRES 8 D 312 TRP ASP VAL SER SER GLY LYS CYS LEU LYS THR LEU LYS
SEQRES 9 D 312 GLY HIS SER ASN TYR VAL PHE CYS CYS ASN PHE ASN PRO
SEQRES 10 D 312 GLN SER ASN LEU ILE VAL SER GLY SER PHE ASP GLU SER
SEQRES 11 D 312 VAL ARG ILE TRP ASP VAL LYS THR GLY LYS CYS LEU LYS
SEQRES 12 D 312 THR LEU PRO ALA HIS SER ASP PRO VAL SER ALA VAL HIS
SEQRES 13 D 312 PHE ASN ARG ASP GLY SER LEU ILE VAL SER SER SER TYR
SEQRES 14 D 312 ASP GLY LEU CYS ARG ILE TRP ASP THR ALA SER GLY GLN
SEQRES 15 D 312 CYS LEU LYS THR LEU ILE ASP ASP ASP ASN PRO PRO VAL
SEQRES 16 D 312 SER PHE VAL LYS PHE SER PRO ASN GLY LYS TYR ILE LEU
SEQRES 17 D 312 ALA ALA THR LEU ASP ASN THR LEU LYS LEU TRP ASP TYR
SEQRES 18 D 312 SER LYS GLY LYS CYS LEU LYS THR TYR THR GLY HIS LYS
SEQRES 19 D 312 ASN GLU LYS TYR CYS ILE PHE ALA ASN PHE SER VAL THR
SEQRES 20 D 312 GLY GLY LYS TRP ILE VAL SER GLY SER GLU ASP ASN LEU
SEQRES 21 D 312 VAL TYR ILE TRP ASN LEU GLN THR LYS GLU ILE VAL GLN
SEQRES 22 D 312 LYS LEU GLN GLY HIS THR ASP VAL VAL ILE SER THR ALA
SEQRES 23 D 312 CYS HIS PRO THR GLU ASN ILE ILE ALA SER ALA ALA LEU
SEQRES 24 D 312 GLU ASN ASP LYS THR ILE LYS LEU TRP LYS SER ASP CYS
HET NP7 A1000 26
HET EDO A2002 4
HET EDO A2003 4
HET EDO A2004 4
HET EDO A2013 4
HET EDO A2014 4
HET EDO A2015 4
HET EDO A2018 4
HET EDO A2020 4
HET UNX A 400 1
HET UNX A 401 1
HET UNX A 402 1
HET UNX A 403 1
HET UNX A 404 1
HET UNX A 405 1
HET UNX A 406 1
HET NP7 B1000 26
HET EDO B2000 4
HET EDO B2001 4
HET EDO B2005 4
HET EDO B2006 4
HET EDO B2007 4
HET EDO B2022 4
HET UNX B 400 1
HET UNX B 401 1
HET UNX B 402 1
HET UNX B 403 1
HET UNX B 404 1
HET UNX B 405 1
HET UNX B 406 1
HET UNX B 407 1
HET UNX B 408 1
HET UNX B 409 1
HET NP7 C1000 26
HET EDO C2008 4
HET EDO C2009 4
HET EDO C2010 4
HET EDO C2017 4
HET EDO C2021 4
HET UNX C 400 1
HET UNX C 401 1
HET UNX C 402 1
HET UNX C 403 1
HET UNX C 404 1
HET UNX C 405 1
HET NP7 D1000 26
HET EDO D2011 4
HET EDO D2012 4
HET EDO D2016 4
HET EDO D2019 4
HET UNX D 400 1
HET UNX D 401 1
HET UNX D 402 1
HET UNX D 403 1
HET UNX D 404 1
HET UNX D 405 1
HET UNX D 406 1
HET UNX D 407 1
HET UNX D 408 1
HETNAM NP7 2-CHLORO-N-[2-(4-METHYLPIPERAZIN-1-YL)-5-
HETNAM 2 NP7 NITROPHENYL]BENZAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NP7 4(C18 H19 CL N4 O3)
FORMUL 6 EDO 23(C2 H6 O2)
FORMUL 14 UNX 32(X)
FORMUL 64 HOH *822(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 ALA A 61 N LYS A 52
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 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 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 206 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 TYR A 252 -1 O TYR A 252 N LEU A 238
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
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 SER B 318 O LYS B 328
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 LEU B 68 GLY B 73 -1 O TRP B 72 N LEU B 60
SHEET 4 I 4 PHE B 79 SER B 84 -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 206 N ILE B 197
SHEET 1 M 4 VAL B 217 PHE B 222 0
SHEET 2 M 4 TYR B 228 THR B 233 -1 O LEU B 230 N LYS B 221
SHEET 3 M 4 THR B 237 ASP B 242 -1 O LYS B 239 N ALA B 231
SHEET 4 M 4 LYS B 247 TYR B 252 -1 O TYR B 252 N LEU B 238
SHEET 1 N 4 ALA B 264 SER B 267 0
SHEET 2 N 4 TRP B 273 SER B 276 -1 O VAL B 275 N ASN B 265
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
SHEET 1 O 4 ALA C 36 LEU C 41 0
SHEET 2 O 4 ILE C 327 LYS C 331 -1 O ILE C 327 N LEU C 41
SHEET 3 O 4 ILE C 315 ALA C 320 -1 N ILE C 316 O TRP C 330
SHEET 4 O 4 VAL C 304 CYS C 309 -1 N ALA C 308 O ALA C 317
SHEET 1 P 4 VAL C 48 PHE C 53 0
SHEET 2 P 4 TRP C 59 SER C 64 -1 O ALA C 61 N LYS C 52
SHEET 3 P 4 ILE C 69 GLY C 73 -1 O TRP C 72 N LEU C 60
SHEET 4 P 4 PHE C 79 ILE C 83 -1 O GLU C 80 N ILE C 71
SHEET 1 Q 4 ILE C 90 TRP C 95 0
SHEET 2 Q 4 LEU C 101 SER C 106 -1 O VAL C 103 N ALA C 94
SHEET 3 Q 4 THR C 110 ASP C 115 -1 O TRP C 114 N LEU C 102
SHEET 4 Q 4 CYS C 121 LYS C 126 -1 O LEU C 125 N LEU C 111
SHEET 1 R 4 VAL C 132 PHE C 137 0
SHEET 2 R 4 LEU C 143 SER C 148 -1 O VAL C 145 N ASN C 136
SHEET 3 R 4 VAL C 153 ASP C 157 -1 O TRP C 156 N ILE C 144
SHEET 4 R 4 CYS C 163 LEU C 167 -1 O LEU C 167 N VAL C 153
SHEET 1 S 4 VAL C 174 PHE C 179 0
SHEET 2 S 4 LEU C 185 SER C 190 -1 O VAL C 187 N HIS C 178
SHEET 3 S 4 CYS C 195 ASP C 199 -1 O TRP C 198 N ILE C 186
SHEET 4 S 4 CYS C 205 LEU C 209 -1 O LEU C 206 N ILE C 197
SHEET 1 T 4 VAL C 217 PHE C 222 0
SHEET 2 T 4 TYR C 228 THR C 233 -1 O LEU C 230 N LYS C 221
SHEET 3 T 4 THR C 237 ASP C 242 -1 O TRP C 241 N ILE C 229
SHEET 4 T 4 LYS C 247 TYR C 252 -1 O TYR C 252 N LEU C 238
SHEET 1 U 4 ALA C 264 SER C 267 0
SHEET 2 U 4 TRP C 273 GLY C 277 -1 O VAL C 275 N ASN C 265
SHEET 3 U 4 VAL C 283 ASN C 287 -1 O TYR C 284 N SER C 276
SHEET 4 U 4 ILE C 293 LEU C 297 -1 O VAL C 294 N ILE C 285
SHEET 1 V 4 ALA D 36 LEU D 41 0
SHEET 2 V 4 ILE D 327 LYS D 331 -1 O ILE D 327 N LEU D 41
SHEET 3 V 4 ILE D 315 ALA D 320 -1 N SER D 318 O LYS D 328
SHEET 4 V 4 VAL D 304 CYS D 309 -1 N ALA D 308 O ALA D 317
SHEET 1 W 4 VAL D 48 PHE D 53 0
SHEET 2 W 4 TRP D 59 SER D 64 -1 O ALA D 61 N LYS D 52
SHEET 3 W 4 ILE D 69 GLY D 73 -1 O TRP D 72 N LEU D 60
SHEET 4 W 4 PHE D 79 ILE D 83 -1 O ILE D 83 N ILE D 69
SHEET 1 X 4 ILE D 90 TRP D 95 0
SHEET 2 X 4 LEU D 101 SER D 106 -1 O ALA D 105 N SER D 91
SHEET 3 X 4 THR D 110 ASP D 115 -1 O TRP D 114 N LEU D 102
SHEET 4 X 4 CYS D 121 LYS D 126 -1 O LEU D 122 N ILE D 113
SHEET 1 Y 4 VAL D 132 PHE D 137 0
SHEET 2 Y 4 LEU D 143 SER D 148 -1 O VAL D 145 N ASN D 136
SHEET 3 Y 4 VAL D 153 ASP D 157 -1 O TRP D 156 N ILE D 144
SHEET 4 Y 4 CYS D 163 LEU D 167 -1 O LEU D 167 N VAL D 153
SHEET 1 Z 4 VAL D 174 PHE D 179 0
SHEET 2 Z 4 LEU D 185 SER D 190 -1 O VAL D 187 N HIS D 178
SHEET 3 Z 4 CYS D 195 ASP D 199 -1 O TRP D 198 N ILE D 186
SHEET 4 Z 4 CYS D 205 LEU D 209 -1 O LEU D 209 N CYS D 195
SHEET 1 AA 4 VAL D 217 PHE D 222 0
SHEET 2 AA 4 TYR D 228 THR D 233 -1 O LEU D 230 N LYS D 221
SHEET 3 AA 4 THR D 237 ASP D 242 -1 O TRP D 241 N ILE D 229
SHEET 4 AA 4 LYS D 247 TYR D 252 -1 O LYS D 247 N ASP D 242
SHEET 1 AB 4 ALA D 264 SER D 267 0
SHEET 2 AB 4 TRP D 273 GLY D 277 -1 O VAL D 275 N ASN D 265
SHEET 3 AB 4 VAL D 283 ASN D 287 -1 O TYR D 284 N SER D 276
SHEET 4 AB 4 ILE D 293 LEU D 297 -1 O VAL D 294 N ILE D 285
SITE 1 AC1 12 SER A 49 SER A 50 ILE A 90 SER A 91
SITE 2 AC1 12 ASP A 92 PHE A 133 PRO A 173 SER A 175
SITE 3 AC1 12 TYR A 191 CYS A 261 HOH A 576 HOH A 647
SITE 1 AC2 6 PRO A 55 TRP A 95 SER A 96 SER A 97
SITE 2 AC2 6 PHE A 137 EDO A2003
SITE 1 AC3 6 ASN A 136 HIS A 178 LYS A 221 HOH A 522
SITE 2 AC3 6 HOH A 616 EDO A2002
SITE 1 AC4 4 LEU A 164 LYS A 165 THR A 200 ALA A 201
SITE 1 AC5 5 LYS A 165 ALA A 201 SER A 202 HIS B 44
SITE 2 AC5 5 HOH B 560
SITE 1 AC6 2 TRP A 241 HOH A 581
SITE 1 AC7 4 TYR A 260 ASP A 302 LEU A 321 GLU A 322
SITE 1 AC8 7 ASP A 199 SER A 202 LEU A 206 THR B 301
SITE 2 AC8 7 ASP B 324 THR B 326 LYS B 328
SITE 1 AC9 2 LYS A 250 GLN A 289
SITE 1 BC1 15 SER B 49 SER B 50 ILE B 90 SER B 91
SITE 2 BC1 15 ASP B 92 ASP B 107 PHE B 133 SER B 175
SITE 3 BC1 15 TYR B 191 CYS B 261 ILE B 305 HOH B 517
SITE 4 BC1 15 HOH B 540 HOH B 611 HOH B 692
SITE 1 BC2 3 TYR B 228 LYS B 250 GLN B 289
SITE 1 BC3 3 ASP B 98 ASN B 100 LYS C 38
SITE 1 BC4 5 TRP B 95 SER B 97 PHE B 137 ASN B 138
SITE 2 BC4 5 EDO B2022
SITE 1 BC5 3 LYS B 165 THR B 200 ALA B 201
SITE 1 BC6 5 VAL B 31 GLY B 271 LYS B 272 TRP B 273
SITE 2 BC6 5 ASN B 287
SITE 1 BC7 4 SER B 97 HOH B 593 EDO B2005 ASP C 76
SITE 1 BC8 12 SER C 49 SER C 50 ILE C 90 SER C 91
SITE 2 BC8 12 ASP C 92 PHE C 133 PRO C 173 SER C 175
SITE 3 BC8 12 TYR C 191 CYS C 261 ILE C 305 HOH C 660
SITE 1 BC9 4 VAL C 31 GLY C 271 LYS C 272 ASN C 287
SITE 1 CC1 3 TYR C 260 ASP C 302 GLU C 322
SITE 1 CC2 6 THR C 40 THR C 301 ASP C 324 THR C 326
SITE 2 CC2 6 LYS C 328 LEU D 206
SITE 1 CC3 4 PHE C 39 ALA C 74 TYR C 75 LEU C 329
SITE 1 CC4 4 TYR C 228 LYS C 250 GLN C 289 HOH C 595
SITE 1 CC5 13 SER D 49 SER D 50 ILE D 90 SER D 91
SITE 2 CC5 13 ASP D 92 PHE D 133 SER D 175 TYR D 191
SITE 3 CC5 13 CYS D 261 ILE D 305 HOH D 596 HOH D 636
SITE 4 CC5 13 HOH D 680
SITE 1 CC6 3 LYS D 165 THR D 200 ALA D 201
SITE 1 CC7 4 TYR D 228 LYS D 250 GLN D 289 HOH D 602
SITE 1 CC8 5 PHE D 39 ALA D 74 TYR D 75 ILE D 315
SITE 2 CC8 5 LEU D 329
SITE 1 CC9 6 LEU C 206 THR D 40 THR D 301 ASP D 324
SITE 2 CC9 6 THR D 326 LYS D 328
CRYST1 204.171 93.467 64.786 90.00 107.24 90.00 C 1 2 1 16
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 0.004898 0.000000 0.001520 0.00000
SCALE2 0.000000 0.010699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
