HEADER DNA BINDING PROTEIN 14-OCT-15 5E8G
TITLE CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF HUMAN TRANSCRIPTION
TITLE 2 FACTOR FLI1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRIEND LEUKEMIA INTEGRATION 1 TRANSCRIPTION FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 276-399;
COMPND 5 SYNONYM: PROTO-ONCOGENE FLI-1,TRANSCRIPTION FACTOR ERGB;
COMPND 6 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: FLI1;
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
KEYWDS TRANSCRIPTION, DNA BINDING, EWING SARCOMA, WINGED HELIX, ETS FAMILY,
KEYWDS 2 DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HOU,O.V.TSODIKOV
REVDAT 5 27-SEP-23 5E8G 1 LINK
REVDAT 4 20-NOV-19 5E8G 1 JRNL REMARK LINK
REVDAT 3 30-DEC-15 5E8G 1 JRNL
REVDAT 2 16-DEC-15 5E8G 1 JRNL
REVDAT 1 09-DEC-15 5E8G 0
JRNL AUTH C.HOU,O.V.TSODIKOV
JRNL TITL STRUCTURAL BASIS FOR DIMERIZATION AND DNA BINDING OF
JRNL TITL 2 TRANSCRIPTION FACTOR FLI1.
JRNL REF BIOCHEMISTRY V. 54 7365 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 26618620
JRNL DOI 10.1021/ACS.BIOCHEM.5B01121
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16370
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 869
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3088
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.42000
REMARK 3 B12 (A**2) : -0.13000
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): 0.479
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.223
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.739
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3176 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2932 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4264 ; 1.233 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6728 ; 0.748 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 368 ; 5.236 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 168 ;36.536 ;23.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 564 ;17.787 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;18.319 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 420 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3596 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 812 ; 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): 1484 ; 3.734 ; 6.678
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1483 ; 3.713 ; 6.676
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1848 ; 5.858 ; 9.998
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1849 ; 5.857 ;10.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1692 ; 3.814 ; 7.142
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1693 ; 3.813 ; 7.143
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2417 ; 6.344 ;10.540
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3731 ; 8.995 ;53.648
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3732 ; 8.994 ;53.659
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 : 1.20
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 5E8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17449
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.67000
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: MOLREP
REMARK 200 STARTING MODEL: 4IRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 5.5, 0.1 M
REMARK 280 CO2+ SULFATE HEPTAHYDRATE, 24% PEG 4000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.27550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.57358
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.38000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 70.27550
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 40.57358
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.38000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 70.27550
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 40.57358
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.38000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.14716
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 56.76000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 81.14716
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 56.76000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 81.14716
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 56.76000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 272
REMARK 465 PRO A 273
REMARK 465 HIS A 274
REMARK 465 MET A 275
REMARK 465 PRO A 276
REMARK 465 GLY A 277
REMARK 465 SER A 278
REMARK 465 HIS A 372
REMARK 465 PRO A 373
REMARK 465 THR A 374
REMARK 465 GLU A 375
REMARK 465 SER A 376
REMARK 465 SER A 377
REMARK 465 MET A 378
REMARK 465 TYR A 379
REMARK 465 LYS A 380
REMARK 465 TYR A 381
REMARK 465 PRO A 382
REMARK 465 SER A 383
REMARK 465 ASP A 384
REMARK 465 ILE A 385
REMARK 465 SER A 386
REMARK 465 TYR A 387
REMARK 465 MET A 388
REMARK 465 PRO A 389
REMARK 465 SER A 390
REMARK 465 TYR A 391
REMARK 465 HIS A 392
REMARK 465 ALA A 393
REMARK 465 HIS A 394
REMARK 465 GLN A 395
REMARK 465 GLN A 396
REMARK 465 LYS A 397
REMARK 465 VAL A 398
REMARK 465 ASN A 399
REMARK 465 GLY B 272
REMARK 465 PRO B 273
REMARK 465 HIS B 274
REMARK 465 MET B 275
REMARK 465 PRO B 276
REMARK 465 GLY B 277
REMARK 465 SER B 278
REMARK 465 HIS B 372
REMARK 465 PRO B 373
REMARK 465 THR B 374
REMARK 465 GLU B 375
REMARK 465 SER B 376
REMARK 465 SER B 377
REMARK 465 MET B 378
REMARK 465 TYR B 379
REMARK 465 LYS B 380
REMARK 465 TYR B 381
REMARK 465 PRO B 382
REMARK 465 SER B 383
REMARK 465 ASP B 384
REMARK 465 ILE B 385
REMARK 465 SER B 386
REMARK 465 TYR B 387
REMARK 465 MET B 388
REMARK 465 PRO B 389
REMARK 465 SER B 390
REMARK 465 TYR B 391
REMARK 465 HIS B 392
REMARK 465 ALA B 393
REMARK 465 HIS B 394
REMARK 465 GLN B 395
REMARK 465 GLN B 396
REMARK 465 LYS B 397
REMARK 465 VAL B 398
REMARK 465 ASN B 399
REMARK 465 GLY C 272
REMARK 465 PRO C 273
REMARK 465 HIS C 274
REMARK 465 MET C 275
REMARK 465 PRO C 276
REMARK 465 GLY C 277
REMARK 465 SER C 278
REMARK 465 HIS C 372
REMARK 465 PRO C 373
REMARK 465 THR C 374
REMARK 465 GLU C 375
REMARK 465 SER C 376
REMARK 465 SER C 377
REMARK 465 MET C 378
REMARK 465 TYR C 379
REMARK 465 LYS C 380
REMARK 465 TYR C 381
REMARK 465 PRO C 382
REMARK 465 SER C 383
REMARK 465 ASP C 384
REMARK 465 ILE C 385
REMARK 465 SER C 386
REMARK 465 TYR C 387
REMARK 465 MET C 388
REMARK 465 PRO C 389
REMARK 465 SER C 390
REMARK 465 TYR C 391
REMARK 465 HIS C 392
REMARK 465 ALA C 393
REMARK 465 HIS C 394
REMARK 465 GLN C 395
REMARK 465 GLN C 396
REMARK 465 LYS C 397
REMARK 465 VAL C 398
REMARK 465 ASN C 399
REMARK 465 GLY D 272
REMARK 465 PRO D 273
REMARK 465 HIS D 274
REMARK 465 MET D 275
REMARK 465 PRO D 276
REMARK 465 GLY D 277
REMARK 465 SER D 278
REMARK 465 HIS D 372
REMARK 465 PRO D 373
REMARK 465 THR D 374
REMARK 465 GLU D 375
REMARK 465 SER D 376
REMARK 465 SER D 377
REMARK 465 MET D 378
REMARK 465 TYR D 379
REMARK 465 LYS D 380
REMARK 465 TYR D 381
REMARK 465 PRO D 382
REMARK 465 SER D 383
REMARK 465 ASP D 384
REMARK 465 ILE D 385
REMARK 465 SER D 386
REMARK 465 TYR D 387
REMARK 465 MET D 388
REMARK 465 PRO D 389
REMARK 465 SER D 390
REMARK 465 TYR D 391
REMARK 465 HIS D 392
REMARK 465 ALA D 393
REMARK 465 HIS D 394
REMARK 465 GLN D 395
REMARK 465 GLN D 396
REMARK 465 LYS D 397
REMARK 465 VAL D 398
REMARK 465 ASN D 399
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 CO CO A 401 O HOH A 504 1.66
REMARK 500 OD2 ASP A 361 O HOH A 501 1.92
REMARK 500 OD2 ASP C 361 O HOH C 501 1.97
REMARK 500 OD2 ASP D 313 O HOH D 501 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 361 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 361 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP D 361 CB - CG - OD2 ANGL. DEV. = 7.0 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 326 59.26 25.70
REMARK 500 TYR A 356 9.19 56.64
REMARK 500 SER B 326 63.19 36.89
REMARK 500 TYR B 356 13.89 57.21
REMARK 500 SER C 326 45.60 39.64
REMARK 500 TYR C 356 13.11 57.71
REMARK 500 GLN D 280 50.63 -99.60
REMARK 500 TYR D 341 -55.80 -29.38
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 CO A 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 361 OD1
REMARK 620 2 ASP A 361 OD2 59.1
REMARK 620 3 HIS A 363 ND1 153.3 96.2
REMARK 620 4 HOH A 501 O 81.7 60.6 95.1
REMARK 620 5 HOH A 503 O 82.6 84.3 85.2 144.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO C 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 502 O
REMARK 620 2 ASP C 361 OD1 112.3
REMARK 620 3 ASP C 361 OD2 160.6 59.2
REMARK 620 4 HIS C 363 ND1 96.2 151.5 93.7
REMARK 620 5 HOH C 501 O 97.5 95.5 67.8 80.5
REMARK 620 6 HOH C 503 O 99.5 74.5 94.9 101.4 162.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 361 OD1
REMARK 620 2 ASP B 361 OD2 60.8
REMARK 620 3 HIS B 363 ND1 152.1 95.2
REMARK 620 4 HOH B 501 O 108.3 84.7 81.1
REMARK 620 5 HOH B 502 O 64.4 86.9 103.1 170.9
REMARK 620 6 HOH C 502 O 108.4 160.1 98.6 83.4 103.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO D 401 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 361 OD1
REMARK 620 2 ASP D 361 OD2 59.5
REMARK 620 3 HIS D 363 ND1 145.0 88.7
REMARK 620 4 HOH D 501 O 118.0 168.3 96.1
REMARK 620 5 HOH D 502 O 60.5 79.1 102.1 110.2
REMARK 620 6 HOH D 503 O 96.4 86.3 95.6 82.6 156.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E8I RELATED DB: PDB
DBREF 5E8G A 276 399 UNP Q01543 FLI1_HUMAN 276 399
DBREF 5E8G B 276 399 UNP Q01543 FLI1_HUMAN 276 399
DBREF 5E8G C 276 399 UNP Q01543 FLI1_HUMAN 276 399
DBREF 5E8G D 276 399 UNP Q01543 FLI1_HUMAN 276 399
SEQADV 5E8G GLY A 272 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G PRO A 273 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G HIS A 274 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G MET A 275 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G GLY B 272 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G PRO B 273 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G HIS B 274 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G MET B 275 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G GLY C 272 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G PRO C 273 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G HIS C 274 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G MET C 275 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G GLY D 272 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G PRO D 273 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G HIS D 274 UNP Q01543 EXPRESSION TAG
SEQADV 5E8G MET D 275 UNP Q01543 EXPRESSION TAG
SEQRES 1 A 128 GLY PRO HIS MET PRO GLY SER GLY GLN ILE GLN LEU TRP
SEQRES 2 A 128 GLN PHE LEU LEU GLU LEU LEU SER ASP SER ALA ASN ALA
SEQRES 3 A 128 SER CYS ILE THR TRP GLU GLY THR ASN GLY GLU PHE LYS
SEQRES 4 A 128 MET THR ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY GLU
SEQRES 5 A 128 ARG LYS SER LYS PRO ASN MET ASN TYR ASP LYS LEU SER
SEQRES 6 A 128 ARG ALA LEU ARG TYR TYR TYR ASP LYS ASN ILE MET THR
SEQRES 7 A 128 LYS VAL HIS GLY LYS ARG TYR ALA TYR LYS PHE ASP PHE
SEQRES 8 A 128 HIS GLY ILE ALA GLN ALA LEU GLN PRO HIS PRO THR GLU
SEQRES 9 A 128 SER SER MET TYR LYS TYR PRO SER ASP ILE SER TYR MET
SEQRES 10 A 128 PRO SER TYR HIS ALA HIS GLN GLN LYS VAL ASN
SEQRES 1 B 128 GLY PRO HIS MET PRO GLY SER GLY GLN ILE GLN LEU TRP
SEQRES 2 B 128 GLN PHE LEU LEU GLU LEU LEU SER ASP SER ALA ASN ALA
SEQRES 3 B 128 SER CYS ILE THR TRP GLU GLY THR ASN GLY GLU PHE LYS
SEQRES 4 B 128 MET THR ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY GLU
SEQRES 5 B 128 ARG LYS SER LYS PRO ASN MET ASN TYR ASP LYS LEU SER
SEQRES 6 B 128 ARG ALA LEU ARG TYR TYR TYR ASP LYS ASN ILE MET THR
SEQRES 7 B 128 LYS VAL HIS GLY LYS ARG TYR ALA TYR LYS PHE ASP PHE
SEQRES 8 B 128 HIS GLY ILE ALA GLN ALA LEU GLN PRO HIS PRO THR GLU
SEQRES 9 B 128 SER SER MET TYR LYS TYR PRO SER ASP ILE SER TYR MET
SEQRES 10 B 128 PRO SER TYR HIS ALA HIS GLN GLN LYS VAL ASN
SEQRES 1 C 128 GLY PRO HIS MET PRO GLY SER GLY GLN ILE GLN LEU TRP
SEQRES 2 C 128 GLN PHE LEU LEU GLU LEU LEU SER ASP SER ALA ASN ALA
SEQRES 3 C 128 SER CYS ILE THR TRP GLU GLY THR ASN GLY GLU PHE LYS
SEQRES 4 C 128 MET THR ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY GLU
SEQRES 5 C 128 ARG LYS SER LYS PRO ASN MET ASN TYR ASP LYS LEU SER
SEQRES 6 C 128 ARG ALA LEU ARG TYR TYR TYR ASP LYS ASN ILE MET THR
SEQRES 7 C 128 LYS VAL HIS GLY LYS ARG TYR ALA TYR LYS PHE ASP PHE
SEQRES 8 C 128 HIS GLY ILE ALA GLN ALA LEU GLN PRO HIS PRO THR GLU
SEQRES 9 C 128 SER SER MET TYR LYS TYR PRO SER ASP ILE SER TYR MET
SEQRES 10 C 128 PRO SER TYR HIS ALA HIS GLN GLN LYS VAL ASN
SEQRES 1 D 128 GLY PRO HIS MET PRO GLY SER GLY GLN ILE GLN LEU TRP
SEQRES 2 D 128 GLN PHE LEU LEU GLU LEU LEU SER ASP SER ALA ASN ALA
SEQRES 3 D 128 SER CYS ILE THR TRP GLU GLY THR ASN GLY GLU PHE LYS
SEQRES 4 D 128 MET THR ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY GLU
SEQRES 5 D 128 ARG LYS SER LYS PRO ASN MET ASN TYR ASP LYS LEU SER
SEQRES 6 D 128 ARG ALA LEU ARG TYR TYR TYR ASP LYS ASN ILE MET THR
SEQRES 7 D 128 LYS VAL HIS GLY LYS ARG TYR ALA TYR LYS PHE ASP PHE
SEQRES 8 D 128 HIS GLY ILE ALA GLN ALA LEU GLN PRO HIS PRO THR GLU
SEQRES 9 D 128 SER SER MET TYR LYS TYR PRO SER ASP ILE SER TYR MET
SEQRES 10 D 128 PRO SER TYR HIS ALA HIS GLN GLN LYS VAL ASN
HET CO A 401 1
HET CO B 401 1
HET CO C 401 1
HET CO D 401 1
HETNAM CO COBALT (II) ION
FORMUL 5 CO 4(CO 2+)
FORMUL 9 HOH *12(H2 O)
HELIX 1 AA1 GLN A 282 SER A 292 1 11
HELIX 2 AA2 ASP A 293 ALA A 297 5 5
HELIX 3 AA3 ASP A 313 LYS A 325 1 13
HELIX 4 AA4 ASN A 331 LYS A 345 1 15
HELIX 5 AA5 ASP A 361 LEU A 369 1 9
HELIX 6 AA6 GLN B 282 SER B 292 1 11
HELIX 7 AA7 ASP B 293 ALA B 297 5 5
HELIX 8 AA8 ASP B 313 LYS B 325 1 13
HELIX 9 AA9 ASN B 331 LYS B 345 1 15
HELIX 10 AB1 ASP B 361 LEU B 369 1 9
HELIX 11 AB2 GLN C 282 SER C 292 1 11
HELIX 12 AB3 ASP C 293 ALA C 297 5 5
HELIX 13 AB4 ASP C 313 LYS C 325 1 13
HELIX 14 AB5 ASN C 331 LYS C 345 1 15
HELIX 15 AB6 ASP C 361 LEU C 369 1 9
HELIX 16 AB7 GLN D 282 ASP D 293 1 12
HELIX 17 AB8 SER D 294 ALA D 297 5 4
HELIX 18 AB9 ASP D 313 LYS D 325 1 13
HELIX 19 AC1 ASN D 331 LYS D 345 1 15
HELIX 20 AC2 ASP D 361 LEU D 369 1 9
SHEET 1 AA1 4 THR A 301 TRP A 302 0
SHEET 2 AA1 4 GLU A 308 LYS A 310 -1 O LYS A 310 N THR A 301
SHEET 3 AA1 4 ALA A 357 PHE A 360 -1 O TYR A 358 N PHE A 309
SHEET 4 AA1 4 MET A 348 LYS A 350 -1 N THR A 349 O LYS A 359
SHEET 1 AA2 4 THR B 301 TRP B 302 0
SHEET 2 AA2 4 GLU B 308 LYS B 310 -1 O LYS B 310 N THR B 301
SHEET 3 AA2 4 ALA B 357 PHE B 360 -1 O TYR B 358 N PHE B 309
SHEET 4 AA2 4 MET B 348 LYS B 350 -1 N THR B 349 O LYS B 359
SHEET 1 AA3 4 THR C 301 TRP C 302 0
SHEET 2 AA3 4 GLU C 308 LYS C 310 -1 O LYS C 310 N THR C 301
SHEET 3 AA3 4 ALA C 357 PHE C 360 -1 O TYR C 358 N PHE C 309
SHEET 4 AA3 4 MET C 348 LYS C 350 -1 N THR C 349 O LYS C 359
SHEET 1 AA4 4 THR D 301 TRP D 302 0
SHEET 2 AA4 4 GLU D 308 LYS D 310 -1 O LYS D 310 N THR D 301
SHEET 3 AA4 4 ALA D 357 PHE D 360 -1 O TYR D 358 N PHE D 309
SHEET 4 AA4 4 MET D 348 LYS D 350 -1 N THR D 349 O LYS D 359
LINK OD1 ASP A 361 CO CO A 401 1555 1555 2.47
LINK OD2 ASP A 361 CO CO A 401 1555 1555 1.78
LINK ND1 HIS A 363 CO CO A 401 1555 1555 1.85
LINK CO CO A 401 O HOH A 501 1555 1555 2.01
LINK CO CO A 401 O HOH A 503 1555 1555 2.29
LINK O HOH A 502 CO CO C 401 3675 1555 2.03
LINK OD1 ASP B 361 CO CO B 401 1555 1555 2.41
LINK OD2 ASP B 361 CO CO B 401 1555 1555 1.78
LINK ND1 HIS B 363 CO CO B 401 1555 1555 1.85
LINK CO CO B 401 O HOH B 501 1555 1555 1.82
LINK CO CO B 401 O HOH B 502 1555 1555 2.16
LINK CO CO B 401 O HOH C 502 1555 9664 2.05
LINK OD1 ASP C 361 CO CO C 401 1555 1555 2.47
LINK OD2 ASP C 361 CO CO C 401 1555 1555 1.76
LINK ND1 HIS C 363 CO CO C 401 1555 1555 1.85
LINK CO CO C 401 O HOH C 501 1555 1555 1.78
LINK CO CO C 401 O HOH C 503 1555 1555 2.15
LINK OD1 ASP D 361 CO CO D 401 1555 1555 2.42
LINK OD2 ASP D 361 CO CO D 401 1555 1555 1.79
LINK ND1 HIS D 363 CO CO D 401 1555 1555 1.86
LINK CO CO D 401 O HOH D 501 1555 6675 1.92
LINK CO CO D 401 O HOH D 502 1555 1555 2.21
LINK CO CO D 401 O HOH D 503 1555 1555 2.11
SITE 1 AC1 5 ASP A 361 HIS A 363 HOH A 501 HOH A 503
SITE 2 AC1 5 HOH A 504
SITE 1 AC2 5 ASP B 361 HIS B 363 HOH B 501 HOH B 502
SITE 2 AC2 5 HOH C 502
SITE 1 AC3 5 HOH A 502 ASP C 361 HIS C 363 HOH C 501
SITE 2 AC3 5 HOH C 503
SITE 1 AC4 5 ASP D 361 HIS D 363 HOH D 501 HOH D 502
SITE 2 AC4 5 HOH D 503
CRYST1 140.551 140.551 85.140 90.00 90.00 120.00 H 3 36
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 0.007115 0.004108 0.000000 0.00000
SCALE2 0.000000 0.008216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
