HEADER TRANSCRIPTION/DNA 27-JUN-13 4LG0
TITLE STRUCTURE OF A TERNARY FOXO1-ETS1 DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORKHEAD BOX PROTEIN O1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN, UNP RESIDUES 143-270;
COMPND 5 SYNONYM: FORKHEAD BOX PROTEIN O1A, FORKHEAD IN RHABDOMYOSARCOMA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN C-ETS-1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: DNA BINDING DOMAIN, UNP RESIDUES 331-440;
COMPND 11 SYNONYM: P54;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-
COMPND 15 D(*DTP*DTP*DCP*DAP*DCP*DGP*DGP*DTP*DTP*DTP*DCP*DCP*DTP*DGP*DTP*DTP*DA
COMPND 16 P*DTP*DTP*DGP*DT)-3');
COMPND 17 CHAIN: C;
COMPND 18 FRAGMENT: FOX-ETS SITE FROM VE-CADHERIN;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: DNA (5'-
COMPND 22 D(*DAP*DAP*DAP*DCP*DAP*DAP*DTP*DAP*DAP*DCP*DAP*DGP*DGP*DAP*DAP*DAP*DC
COMPND 23 P*DCP*DGP*DTP*DG)-3');
COMPND 24 CHAIN: D;
COMPND 25 FRAGMENT: FOX-ETS SITE FROM VE-CADHERIN;
COMPND 26 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: FKHR, FOXO1, FOXO1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-50B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: C-ETS-1, ETS1, EWSR2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-19;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.;
SOURCE 24 MOL_ID: 4;
SOURCE 25 SYNTHETIC: YES;
SOURCE 26 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS DEOXYRIBONUCLEIC ACID, COMPLEX (DNA-BINDING PROTEIN-DNA),
KEYWDS 2 PHOSPHOPROTEIN, PROTO-ONCOGENE, TRANSCRIPTION-DNA COMPLEX, WINGED
KEYWDS 3 HELIX, FORKHEAD DOMAIN, ETS BINDING DOMAIN, HELIX-TURN-HELIX,
KEYWDS 4 TRANSCRIPTION, TRANSCRIPTION REGULATION, DNA-BINDING,
KEYWDS 5 PHOSPHORYLATION, NUCLEUS
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BIRRANE,W.C.CHOY,D.DATTA,C.A.GEIGER,M.A.GRANT
REVDAT 2 28-FEB-24 4LG0 1 REMARK SEQADV LINK
REVDAT 1 02-JUL-14 4LG0 0
JRNL AUTH G.BIRRANE,W.C.CHOY,D.DATTA,C.A.GEIGER,M.A.GRANT
JRNL TITL STRUCTURE OF A TERNARY FOXO1-ETS1 DNA COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0047
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 25814
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1460
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1609
REMARK 3 NUCLEIC ACID ATOMS : 855
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.69000
REMARK 3 B22 (A**2) : -3.85000
REMARK 3 B33 (A**2) : 5.54000
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): 0.181
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.355
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2695 ; 0.013 ; 0.016
REMARK 3 BOND LENGTHS OTHERS (A): 2106 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3812 ; 1.584 ; 1.646
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4891 ; 1.079 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 6.502 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;36.702 ;23.415
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 311 ;14.535 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.152 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 358 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2432 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 623 ; 0.001 ; 0.020
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): 819 ; 4.628 ; 5.282
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 818 ; 4.626 ; 5.273
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1022 ; 6.732 ; 7.874
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1023 ; 6.729 ; 7.886
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1876 ; 4.414 ; 4.988
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1876 ; 4.414 ; 4.987
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2791 ; 6.589 ; 7.376
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3337 ;10.127 ;40.935
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3338 ;10.125 ;40.954
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 156 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7640 23.2270 18.2970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2107 T22: 0.6493
REMARK 3 T33: 0.1093 T12: 0.0395
REMARK 3 T13: 0.0383 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 2.2999 L22: 0.3195
REMARK 3 L33: 3.9836 L12: 0.1010
REMARK 3 L13: -0.0206 L23: -0.9490
REMARK 3 S TENSOR
REMARK 3 S11: -0.1278 S12: -0.3204 S13: -0.0605
REMARK 3 S21: -0.1677 S22: 0.2017 S23: -0.0166
REMARK 3 S31: 0.1658 S32: -0.7185 S33: -0.0739
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 333 B 438
REMARK 3 ORIGIN FOR THE GROUP (A): 69.5700 24.9600 12.2310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.5005
REMARK 3 T33: 0.2764 T12: 0.0932
REMARK 3 T13: 0.0463 T23: 0.1063
REMARK 3 L TENSOR
REMARK 3 L11: 2.5332 L22: 1.8094
REMARK 3 L33: 0.7639 L12: 1.1574
REMARK 3 L13: 0.0727 L23: 0.0951
REMARK 3 S TENSOR
REMARK 3 S11: -0.1239 S12: 0.0255 S13: -0.0808
REMARK 3 S21: -0.0554 S22: -0.1045 S23: -0.2970
REMARK 3 S31: 0.0958 S32: 0.2765 S33: 0.2284
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 21
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1430 16.7580 15.3440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0896 T22: 0.3447
REMARK 3 T33: 0.3176 T12: 0.1468
REMARK 3 T13: 0.0652 T23: 0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 1.6654 L22: 1.0365
REMARK 3 L33: 0.8819 L12: -1.0166
REMARK 3 L13: 0.2531 L23: 0.4166
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: 0.1004 S13: -0.0525
REMARK 3 S21: 0.0398 S22: -0.1233 S23: -0.0047
REMARK 3 S31: 0.1366 S32: -0.0261 S33: 0.0778
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 21
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9450 21.5580 15.2030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2513 T22: 0.4834
REMARK 3 T33: 0.3056 T12: 0.0389
REMARK 3 T13: 0.0566 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 2.1521 L22: 0.0626
REMARK 3 L33: 1.4295 L12: -0.0486
REMARK 3 L13: -1.3257 L23: -0.1043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.1913 S13: -0.1835
REMARK 3 S21: 0.0515 S22: -0.1657 S23: 0.0626
REMARK 3 S31: -0.1744 S32: 0.2840 S33: 0.2123
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 4LG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080582.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075,0.9793,0.979
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27722
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 12.00
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.05M 2-AMINO-2
REMARK 280 -HYDROXYMETHYL-PROPANE-1,3-DIOL, 0.1M POTASSIUM CHLORIDE, 0.01M
REMARK 280 MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 68.16250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.16250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.32900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 57.47200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.32900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 57.47200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.16250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.32900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 57.47200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.16250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.32900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 57.47200
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 138
REMARK 465 PRO A 139
REMARK 465 GLY A 140
REMARK 465 TYR A 141
REMARK 465 PRO A 142
REMARK 465 GLY A 143
REMARK 465 PRO A 144
REMARK 465 LEU A 145
REMARK 465 ALA A 146
REMARK 465 GLY A 147
REMARK 465 GLN A 148
REMARK 465 PRO A 149
REMARK 465 ARG A 150
REMARK 465 LYS A 151
REMARK 465 SER A 152
REMARK 465 SER A 153
REMARK 465 SER A 154
REMARK 465 SER A 155
REMARK 465 LYS A 245
REMARK 465 SER A 246
REMARK 465 GLY A 247
REMARK 465 LYS A 248
REMARK 465 SER A 249
REMARK 465 PRO A 250
REMARK 465 ARG A 251
REMARK 465 ARG A 252
REMARK 465 ARG A 253
REMARK 465 ALA A 254
REMARK 465 ALA A 255
REMARK 465 SER A 256
REMARK 465 MET A 257
REMARK 465 ASP A 258
REMARK 465 ASN A 259
REMARK 465 ASN A 260
REMARK 465 SER A 261
REMARK 465 LYS A 262
REMARK 465 PHE A 263
REMARK 465 ALA A 264
REMARK 465 LYS A 265
REMARK 465 SER A 266
REMARK 465 ARG A 267
REMARK 465 SER A 268
REMARK 465 ARG A 269
REMARK 465 ALA A 270
REMARK 465 MET B 329
REMARK 465 GLY B 330
REMARK 465 GLY B 331
REMARK 465 SER B 332
REMARK 465 ALA B 439
REMARK 465 ASP B 440
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 DT C 19 O5' - P - OP2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 DT D 7 C1' - O4' - C4' ANGL. DEV. = -7.3 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 SER A 203 121.00 -27.23
REMARK 500 ASN A 204 -94.63 119.33
REMARK 500 GLU A 229 -84.65 -48.85
REMARK 500 LYS A 233 78.88 135.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 217 O
REMARK 620 2 SER A 218 O 79.5
REMARK 620 3 HIS A 220 O 87.2 96.1
REMARK 620 4 PHE A 223 O 100.2 170.4 74.3
REMARK 620 5 HOH C 105 O 90.2 81.0 176.4 108.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3COA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FOXO1 DBD BOUND TO IRE DNA ELEMENT
REMARK 900 RELATED ID: 3CO6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FOXO1 DBD BOUND TO DBE1 DNA
REMARK 900 RELATED ID: 1K79 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ETS1 DBD BOUND TO LOW (GGAG) AND HIGH (GGAA)
REMARK 900 AFFINITY DNA
REMARK 900 RELATED ID: 2STT RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF ETS1 BOUND TO DNA
DBREF 4LG0 A 143 270 UNP Q12778 FOXO1_HUMAN 143 270
DBREF 4LG0 B 331 440 UNP P14921 ETS1_HUMAN 331 440
DBREF 4LG0 C 1 21 PDB 4LG0 4LG0 1 21
DBREF 4LG0 D 1 21 PDB 4LG0 4LG0 1 21
SEQADV 4LG0 GLY A 138 UNP Q12778 EXPRESSION TAG
SEQADV 4LG0 PRO A 139 UNP Q12778 EXPRESSION TAG
SEQADV 4LG0 GLY A 140 UNP Q12778 EXPRESSION TAG
SEQADV 4LG0 TYR A 141 UNP Q12778 EXPRESSION TAG
SEQADV 4LG0 PRO A 142 UNP Q12778 EXPRESSION TAG
SEQADV 4LG0 MET B 329 UNP P14921 EXPRESSION TAG
SEQADV 4LG0 GLY B 330 UNP P14921 EXPRESSION TAG
SEQRES 1 A 133 GLY PRO GLY TYR PRO GLY PRO LEU ALA GLY GLN PRO ARG
SEQRES 2 A 133 LYS SER SER SER SER ARG ARG ASN ALA TRP GLY ASN LEU
SEQRES 3 A 133 SER TYR ALA ASP LEU ILE THR LYS ALA ILE GLU SER SER
SEQRES 4 A 133 ALA GLU LYS ARG LEU THR LEU SER GLN ILE TYR GLU TRP
SEQRES 5 A 133 MET VAL LYS SER VAL PRO TYR PHE LYS ASP LYS GLY ASP
SEQRES 6 A 133 SER ASN SER SER ALA GLY TRP LYS ASN SER ILE ARG HIS
SEQRES 7 A 133 ASN LEU SER LEU HIS SER LYS PHE ILE ARG VAL GLN ASN
SEQRES 8 A 133 GLU GLY THR GLY LYS SER SER TRP TRP MET LEU ASN PRO
SEQRES 9 A 133 GLU GLY GLY LYS SER GLY LYS SER PRO ARG ARG ARG ALA
SEQRES 10 A 133 ALA SER MET ASP ASN ASN SER LYS PHE ALA LYS SER ARG
SEQRES 11 A 133 SER ARG ALA
SEQRES 1 B 112 MET GLY GLY SER GLY PRO ILE GLN LEU TRP GLN PHE LEU
SEQRES 2 B 112 LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE ILE
SEQRES 3 B 112 SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER ASP
SEQRES 4 B 112 PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS ASN
SEQRES 5 B 112 LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY LEU
SEQRES 6 B 112 ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR ALA
SEQRES 7 B 112 GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU GLN
SEQRES 8 B 112 SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA MET
SEQRES 9 B 112 LEU ASP VAL LYS PRO ASP ALA ASP
SEQRES 1 C 21 DT DT DC DA DC DG DG DT DT DT DC DC DT
SEQRES 2 C 21 DG DT DT DA DT DT DG DT
SEQRES 1 D 21 DA DA DA DC DA DA DT DA DA DC DA DG DG
SEQRES 2 D 21 DA DA DA DC DC DG DT DG
HET CA A 301 1
HET PG4 B 501 13
HETNAM CA CALCIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 5 CA CA 2+
FORMUL 6 PG4 C8 H18 O5
FORMUL 7 HOH *70(H2 O)
HELIX 1 1 SER A 164 SER A 175 1 12
HELIX 2 2 THR A 182 VAL A 194 1 13
HELIX 3 3 PRO A 195 LYS A 200 5 6
HELIX 4 4 ALA A 207 HIS A 220 1 14
HELIX 5 5 GLN B 336 THR B 346 1 11
HELIX 6 6 ASP B 347 GLN B 351 5 5
HELIX 7 7 ASP B 367 ASN B 380 1 14
HELIX 8 8 ASN B 385 TYR B 396 1 12
HELIX 9 9 ASP B 417 GLY B 423 1 7
HELIX 10 10 THR B 425 LEU B 433 1 9
SHEET 1 A 2 PHE A 223 VAL A 226 0
SHEET 2 A 2 TRP A 236 LEU A 239 -1 O TRP A 236 N VAL A 226
SHEET 1 B 4 SER B 355 TRP B 356 0
SHEET 2 B 4 GLU B 362 LYS B 364 -1 O LYS B 364 N SER B 355
SHEET 3 B 4 VAL B 411 PHE B 414 -1 O TYR B 412 N PHE B 363
SHEET 4 B 4 ILE B 402 LYS B 404 -1 N HIS B 403 O ARG B 413
LINK O LEU A 217 CA CA A 301 1555 1555 2.74
LINK O SER A 218 CA CA A 301 1555 1555 3.13
LINK O HIS A 220 CA CA A 301 1555 1555 2.72
LINK O PHE A 223 CA CA A 301 1555 1555 2.70
LINK CA CA A 301 O HOH C 105 1555 1555 2.87
CISPEP 1 GLY A 232 LYS A 233 0 12.99
SITE 1 AC1 6 LEU A 217 SER A 218 HIS A 220 PHE A 223
SITE 2 AC1 6 HOH A 408 HOH C 105
SITE 1 AC2 4 TRP B 338 VAL B 415 CYS B 416 ASP B 417
CRYST1 68.658 114.944 136.325 90.00 90.00 90.00 C 2 2 21 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 0.014565 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008700 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
