HEADER TRANSCRIPTION 04-OCT-06 2J6W
TITLE R164N MUTANT OF THE RUNX1 RUNT DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUNT-RELATED TRANSCRIPTION FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RUNT DOMAIN, RESIDUES 46-185;
COMPND 5 SYNONYM: CORE-BINDING FACTOR ALPHA 2 SUBUNIT, CBF-ALPHA 2, ACUTE
COMPND 6 MYELOID LEUKEMIA 1 PROTEIN, ONCOGENE AML-1, POLYOMAVIRUS ENHANCER-
COMPND 7 BINDING PROTEIN 2 ALPHA B SUBUNIT, PEBP2-ALPHA B, PEA2-ALPHA B, SL3-3
COMPND 8 ENHANCER FACTOR 1 ALPHA B SUBUNIT, SL3/AKV CORE-BINDING FACTOR ALPHA
COMPND 9 B SUBUNIT, R164N MUTANT OF THE RUNX1 RUNT DOMAIN;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: 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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3C
KEYWDS TRANSCRIPTION FACTOR, TRANSCRIPTION/DNA, CHLORIDE BINDING, ACUTE
KEYWDS 2 MYELOID LEUKEMIA, TRANSCRIPTION REGULATION, TRANSCRIPTION, NUCLEAR
KEYWDS 3 PROTEIN, PHOSPHORYLATION, AML, RUNX1, IG FOLD, RUNT DOMAIN, DNA-
KEYWDS 4 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GREMBECKA,L.ZHE,S.M.LUKASIK,Y.LIU,I.BIELNICKA,J.H.BUSHWELLER,
AUTHOR 2 N.A.SPECK
REVDAT 5 13-DEC-23 2J6W 1 REMARK
REVDAT 4 10-AUG-11 2J6W 1 JRNL REMARK
REVDAT 3 13-JUL-11 2J6W 1 VERSN
REVDAT 2 24-FEB-09 2J6W 1 VERSN
REVDAT 1 09-OCT-07 2J6W 0
JRNL AUTH Z.LI,S.M.LUKASIK,Y.LIU,J.GREMBECKA,I.BIELNICKA,
JRNL AUTH 2 J.H.BUSHWELLER,N.A.SPECK
JRNL TITL A MUTATION IN THE S-SWITCH REGION OF THE RUNT DOMAIN ALTERS
JRNL TITL 2 THE DYNAMICS OF AN ALLOSTERIC NETWORK RESPONSIBLE FOR
JRNL TITL 3 CBFBETA REGULATION.
JRNL REF J.MOL.BIOL. V. 364 1073 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 17059830
JRNL DOI 10.1016/J.JMB.2006.10.002
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 7186
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700
REMARK 3 FREE R VALUE TEST SET COUNT : 776
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 384
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1894
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.71000
REMARK 3 B22 (A**2) : -1.95000
REMARK 3 B33 (A**2) : 1.22000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.01000
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): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.272
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.087
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1934 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1774 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2638 ; 2.238 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4114 ; 1.774 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 2.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;27.479 ;23.659
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 304 ;10.071 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ; 9.051 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 312 ; 0.045 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2156 ; 0.001 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 384 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 259 ; 0.118 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1512 ; 0.094 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 871 ; 0.125 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1062 ; 0.060 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 64 ; 0.068 ; 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): 10 ; 0.041 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 64 ; 0.081 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.058 ; 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): 1595 ; 0.081 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2016 ; 0.095 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 797 ; 0.130 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 622 ; 0.215 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 50 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9450 17.2180 15.5250
REMARK 3 T TENSOR
REMARK 3 T11: -0.2292 T22: 0.1109
REMARK 3 T33: -0.3347 T12: -0.0538
REMARK 3 T13: 0.0534 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 3.0934 L22: 5.9979
REMARK 3 L33: 6.2781 L12: 0.2526
REMARK 3 L13: -0.2408 L23: 1.9086
REMARK 3 S TENSOR
REMARK 3 S11: 0.0708 S12: -0.0495 S13: 0.0443
REMARK 3 S21: 0.0567 S22: -0.1605 S23: 0.0784
REMARK 3 S31: -0.0006 S32: -0.0806 S33: 0.0897
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 50 B 173
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8480 -17.0970 18.7470
REMARK 3 T TENSOR
REMARK 3 T11: -0.2214 T22: 0.1137
REMARK 3 T33: -0.2583 T12: -0.0376
REMARK 3 T13: 0.0697 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 2.2660 L22: 2.8049
REMARK 3 L33: 6.0319 L12: 1.2688
REMARK 3 L13: -0.2082 L23: 0.1894
REMARK 3 S TENSOR
REMARK 3 S11: -0.0423 S12: -0.0344 S13: 0.0615
REMARK 3 S21: -0.0495 S22: 0.0402 S23: 0.1474
REMARK 3 S31: -0.1839 S32: 0.0539 S33: 0.0021
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2J6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1290030143.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97940
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BUILT IN ANL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7962
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EAO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 8000, 0.1M SODIUM CACODYLATE
REMARK 280 PH=6.5, 0.2M AMMONIUM SULFATE, PH 6.5
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 45.97400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.24850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.97400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.24850
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 72 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 81 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 164 TO ASN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 72 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 81 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ARG 164 TO ASN
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 SER A 46
REMARK 465 GLY A 47
REMARK 465 ASP A 48
REMARK 465 ARG A 49
REMARK 465 ARG A 174
REMARK 465 GLU A 175
REMARK 465 PRO A 176
REMARK 465 ARG A 177
REMARK 465 ARG A 178
REMARK 465 HIS A 179
REMARK 465 ARG A 180
REMARK 465 GLN A 181
REMARK 465 LYS A 182
REMARK 465 LEU A 183
REMARK 465 ASP A 184
REMARK 465 ASP A 185
REMARK 465 SER B 46
REMARK 465 GLY B 47
REMARK 465 ASP B 48
REMARK 465 ARG B 49
REMARK 465 ARG B 174
REMARK 465 GLU B 175
REMARK 465 PRO B 176
REMARK 465 ARG B 177
REMARK 465 ARG B 178
REMARK 465 HIS B 179
REMARK 465 ARG B 180
REMARK 465 GLN B 181
REMARK 465 LYS B 182
REMARK 465 LEU B 183
REMARK 465 ASP B 184
REMARK 465 ASP B 185
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 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 133 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 64 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ASN A 112 89.69 -161.52
REMARK 500 ASP A 133 65.79 -154.27
REMARK 500 ASN B 132 -70.65 -46.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1175
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EAN RELATED DB: PDB
REMARK 900 AN "S-SWITCH" AND CHLORIDE IONS MODULATE THE DNA-BINDING ABILITY OF
REMARK 900 RUNX/AML1
REMARK 900 RELATED ID: 1EAO RELATED DB: PDB
REMARK 900 AN "S-SWITCH" AND CHLORIDE IONS MODULATE THE DNA-BINDING ABILITY OF
REMARK 900 RUNX/AML1
REMARK 900 RELATED ID: 1EAQ RELATED DB: PDB
REMARK 900 AN "S-SWITCH" AND CHLORIDE IONS MODULATE THE DNA-BINDING ABILITY OF
REMARK 900 RUNX/AML1
REMARK 900 RELATED ID: 1HJB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN AND C/EBPBETA
REMARK 900 BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER
REMARK 900 RELATED ID: 1HJC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND TO A
REMARK 900 DNA FRAGMENT FROM THE CSF-1R PROMOTER
REMARK 900 RELATED ID: 1IO4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-CBFBETA CORE
REMARK 900 DOMAIN HETERODIMER AND C/EBPBETA BZIPHOMODIMER BOUND TO A DNA
REMARK 900 FRAGMENT FROM THE CSF-1R PROMOTER
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 R164N
DBREF 2J6W A 46 185 UNP Q03347 RUNX1_MOUSE 46 185
DBREF 2J6W B 46 185 UNP Q03347 RUNX1_MOUSE 46 185
SEQADV 2J6W SER A 72 UNP Q03347 CYS 72 ENGINEERED MUTATION
SEQADV 2J6W SER A 81 UNP Q03347 CYS 81 ENGINEERED MUTATION
SEQADV 2J6W ASN A 164 UNP Q03347 ARG 164 ENGINEERED MUTATION
SEQADV 2J6W SER B 72 UNP Q03347 CYS 72 ENGINEERED MUTATION
SEQADV 2J6W SER B 81 UNP Q03347 CYS 81 ENGINEERED MUTATION
SEQADV 2J6W ASN B 164 UNP Q03347 ARG 164 ENGINEERED MUTATION
SEQRES 1 A 140 SER GLY ASP ARG SER MET VAL GLU VAL LEU ALA ASP HIS
SEQRES 2 A 140 PRO GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU
SEQRES 3 A 140 SER SER VAL LEU PRO THR HIS TRP ARG SER ASN LYS THR
SEQRES 4 A 140 LEU PRO ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL
SEQRES 5 A 140 PRO ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP
SEQRES 6 A 140 GLU ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA
SEQRES 7 A 140 MET LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE
SEQRES 8 A 140 VAL GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR
SEQRES 9 A 140 ILE THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR
SEQRES 10 A 140 HIS ASN ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU
SEQRES 11 A 140 PRO ARG ARG HIS ARG GLN LYS LEU ASP ASP
SEQRES 1 B 140 SER GLY ASP ARG SER MET VAL GLU VAL LEU ALA ASP HIS
SEQRES 2 B 140 PRO GLY GLU LEU VAL ARG THR ASP SER PRO ASN PHE LEU
SEQRES 3 B 140 SER SER VAL LEU PRO THR HIS TRP ARG SER ASN LYS THR
SEQRES 4 B 140 LEU PRO ILE ALA PHE LYS VAL VAL ALA LEU GLY ASP VAL
SEQRES 5 B 140 PRO ASP GLY THR LEU VAL THR VAL MET ALA GLY ASN ASP
SEQRES 6 B 140 GLU ASN TYR SER ALA GLU LEU ARG ASN ALA THR ALA ALA
SEQRES 7 B 140 MET LYS ASN GLN VAL ALA ARG PHE ASN ASP LEU ARG PHE
SEQRES 8 B 140 VAL GLY ARG SER GLY ARG GLY LYS SER PHE THR LEU THR
SEQRES 9 B 140 ILE THR VAL PHE THR ASN PRO PRO GLN VAL ALA THR TYR
SEQRES 10 B 140 HIS ASN ALA ILE LYS ILE THR VAL ASP GLY PRO ARG GLU
SEQRES 11 B 140 PRO ARG ARG HIS ARG GLN LYS LEU ASP ASP
HET CL A1174 1
HET CL A1175 1
HET CL B1174 1
HET CL B1175 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 4(CL 1-)
FORMUL 7 HOH *49(H2 O)
HELIX 1 1 SER A 50 HIS A 58 1 9
HELIX 2 2 SER B 50 HIS B 58 1 9
SHEET 1 AA 4 VAL A 63 ARG A 64 0
SHEET 2 AA 4 PHE A 70 SER A 72 -1 O SER A 72 N VAL A 63
SHEET 3 AA 4 LYS A 90 ALA A 93 -1 O VAL A 92 N LEU A 71
SHEET 4 AA 4 VAL A 128 ARG A 130 -1 O ALA A 129 N VAL A 91
SHEET 1 AB 2 HIS A 78 ARG A 80 0
SHEET 2 AB 2 LYS A 167 THR A 169 1 O LYS A 167 N TRP A 79
SHEET 1 AC 3 ASN A 112 ALA A 115 0
SHEET 2 AC 3 LEU A 102 ASN A 109 -1 O ALA A 107 N ALA A 115
SHEET 3 AC 3 THR A 121 ALA A 123 -1 O ALA A 122 N VAL A 103
SHEET 1 AD 4 ASN A 112 ALA A 115 0
SHEET 2 AD 4 LEU A 102 ASN A 109 -1 O ALA A 107 N ALA A 115
SHEET 3 AD 4 THR A 147 VAL A 152 -1 O THR A 147 N GLY A 108
SHEET 4 AD 4 GLN A 158 THR A 161 -1 O GLN A 158 N VAL A 152
SHEET 1 AE 2 LEU A 117 ARG A 118 0
SHEET 2 AE 2 ARG A 135 PHE A 136 -1 O ARG A 135 N ARG A 118
SHEET 1 BA 9 LEU B 62 ARG B 64 0
SHEET 2 BA 9 PHE B 70 SER B 73 -1 O SER B 72 N VAL B 63
SHEET 3 BA 9 LYS B 90 ALA B 93 -1 O LYS B 90 N SER B 73
SHEET 4 BA 9 VAL B 128 ARG B 130 -1 O ALA B 129 N VAL B 91
SHEET 5 BA 9 THR B 121 LYS B 125 -1 O ALA B 123 N ARG B 130
SHEET 6 BA 9 LEU B 102 GLY B 108 -1 O VAL B 103 N ALA B 122
SHEET 7 BA 9 PHE B 146 VAL B 152 -1 O THR B 147 N GLY B 108
SHEET 8 BA 9 GLN B 158 THR B 169 -1 O GLN B 158 N VAL B 152
SHEET 9 BA 9 HIS B 78 ARG B 80 1 O TRP B 79 N THR B 169
SHEET 1 BB 2 LEU B 117 ARG B 118 0
SHEET 2 BB 2 ARG B 135 PHE B 136 -1 O ARG B 135 N ARG B 118
CISPEP 1 ASN A 155 PRO A 156 0 -1.46
CISPEP 2 ASN B 155 PRO B 156 0 1.28
SITE 1 AC1 3 ASN A 112 GLU A 116 GLY A 138
SITE 1 AC2 1 VAL B 170
SITE 1 AC3 2 ASN B 112 GLU B 116
CRYST1 91.948 46.497 63.552 90.00 90.66 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 0.010876 0.000000 0.000125 0.00000
SCALE2 0.000000 0.021507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
