HEADER TRANSCRIPTION ACTIVATOR 13-APR-00 1ETV
TITLE THE CRYSTAL STRUCTURE OF E. COLI FIS MUTANT G72A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FACTOR FOR INVERSION STIMULATION;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FIS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (-FIS);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS TRANSCRIPTIONAL ACTIVATION REGION, DNA-BINDING PROTEIN, TRANSCRIPTION
KEYWDS 2 ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.S.CHENG,W.Z.YANG,R.C.JOHNSON,H.S.YUAN
REVDAT 5 07-FEB-24 1ETV 1 REMARK
REVDAT 4 03-NOV-21 1ETV 1 SEQADV
REVDAT 3 24-FEB-09 1ETV 1 VERSN
REVDAT 2 01-APR-03 1ETV 1 JRNL
REVDAT 1 11-OCT-00 1ETV 0
JRNL AUTH Y.S.CHENG,W.Z.YANG,R.C.JOHNSON,H.S.YUAN
JRNL TITL STRUCTURAL ANALYSIS OF THE TRANSCRIPTIONAL ACTIVATION ON
JRNL TITL 2 FIS: CRYSTAL STRUCTURES OF SIX FIS MUTANTS WITH DIFFERENT
JRNL TITL 3 ACTIVATION PROPERTIES.
JRNL REF J.MOL.BIOL. V. 302 1139 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11183780
JRNL DOI 10.1006/JMBI.2000.4123
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 12664
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 SET) : 0.223
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1007
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1841
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1249
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 96
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : -3.20000
REMARK 3 B33 (A**2) : 2.70000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.003
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.980 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 56.52
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ETV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.710
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.57
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43600
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: THE WILD-TYPE FIS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML PROTEIN, 0.5 M SODIUM
REMARK 280 CHLORIDE, 0.05 M NA-HEPES (PH 7.5), 15% PEG4000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.14500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.63000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.63000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.14500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.18500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAINS THAT GIVE ONE BIOLOGICAL
REMARK 300 DIMER MOLECULE.
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: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MUTATION AT BC TURN AT THE TRANSCRIPTIONAL ACTIVATION REGION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PHE A 2
REMARK 465 GLU A 3
REMARK 465 GLN A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 SER A 14
REMARK 465 THR A 15
REMARK 465 VAL A 16
REMARK 465 ASN A 17
REMARK 465 SER A 18
REMARK 465 GLN A 19
REMARK 465 ASP A 20
REMARK 465 GLN A 21
REMARK 465 VAL A 22
REMARK 465 THR A 23
REMARK 465 GLN A 24
REMARK 465 ASN A 43
REMARK 465 GLY A 44
REMARK 465 GLN A 45
REMARK 465 ASP A 46
REMARK 465 MET B 1
REMARK 465 PHE B 2
REMARK 465 GLU B 3
REMARK 465 GLN B 4
REMARK 465 SER B 14
REMARK 465 THR B 15
REMARK 465 VAL B 16
REMARK 465 ASN B 17
REMARK 465 SER B 18
REMARK 465 GLN B 19
REMARK 465 ASP B 20
REMARK 465 GLN B 21
REMARK 465 VAL B 22
REMARK 465 THR B 23
REMARK 465 GLN B 24
REMARK 465 LEU B 42
REMARK 465 ASN B 43
REMARK 465 GLY B 44
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 48 15.56 -142.47
REMARK 500 ALA B 40 -4.91 -54.32
REMARK 500 ASN B 48 15.50 -145.38
REMARK 500 ASP B 49 29.97 -145.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FIS RELATED DB: PDB
REMARK 900 3FIS CONTAINS THE WILD-TYPE FIS
REMARK 900 RELATED ID: 1FIP RELATED DB: PDB
REMARK 900 1FIP CONTAINS THE FIS MUTANT P61A
REMARK 900 RELATED ID: 1F36 RELATED DB: PDB
REMARK 900 1F36 CONTAINS THE FIS MUTANT K36E
REMARK 900 RELATED ID: 1ETK RELATED DB: PDB
REMARK 900 1ETK CONTAINS THE FIS MUTANT Q68A
REMARK 900 RELATED ID: 1ETO RELATED DB: PDB
REMARK 900 1ETO CONTAINS THE FIS MUTANT R71L
REMARK 900 RELATED ID: 1ETQ RELATED DB: PDB
REMARK 900 1ETQ CONTAINS THE FIS MUTANT R71Y
REMARK 900 RELATED ID: 1ETW RELATED DB: PDB
REMARK 900 1ETW CONTAINS THE FIS MUTANT G72D
REMARK 900 RELATED ID: 1ETX RELATED DB: PDB
REMARK 900 1ETX CONTAINS THE FIS MUTANT Q74A
REMARK 900 RELATED ID: 1ETY RELATED DB: PDB
REMARK 900 1ETY CONTAINS THE FIS WILD TYPE
DBREF 1ETV A 1 98 UNP P0A6R3 FIS_ECOLI 1 98
DBREF 1ETV B 1 98 UNP P0A6R3 FIS_ECOLI 1 98
SEQADV 1ETV ALA A 72 UNP P0A6R3 GLY 72 ENGINEERED MUTATION
SEQADV 1ETV ALA B 72 UNP P0A6R3 GLY 72 ENGINEERED MUTATION
SEQRES 1 A 98 MET PHE GLU GLN ARG VAL ASN SER ASP VAL LEU THR VAL
SEQRES 2 A 98 SER THR VAL ASN SER GLN ASP GLN VAL THR GLN LYS PRO
SEQRES 3 A 98 LEU ARG ASP SER VAL LYS GLN ALA LEU LYS ASN TYR PHE
SEQRES 4 A 98 ALA GLN LEU ASN GLY GLN ASP VAL ASN ASP LEU TYR GLU
SEQRES 5 A 98 LEU VAL LEU ALA GLU VAL GLU GLN PRO LEU LEU ASP MET
SEQRES 6 A 98 VAL MET GLN TYR THR ARG ALA ASN GLN THR ARG ALA ALA
SEQRES 7 A 98 LEU MET MET GLY ILE ASN ARG GLY THR LEU ARG LYS LYS
SEQRES 8 A 98 LEU LYS LYS TYR GLY MET ASN
SEQRES 1 B 98 MET PHE GLU GLN ARG VAL ASN SER ASP VAL LEU THR VAL
SEQRES 2 B 98 SER THR VAL ASN SER GLN ASP GLN VAL THR GLN LYS PRO
SEQRES 3 B 98 LEU ARG ASP SER VAL LYS GLN ALA LEU LYS ASN TYR PHE
SEQRES 4 B 98 ALA GLN LEU ASN GLY GLN ASP VAL ASN ASP LEU TYR GLU
SEQRES 5 B 98 LEU VAL LEU ALA GLU VAL GLU GLN PRO LEU LEU ASP MET
SEQRES 6 B 98 VAL MET GLN TYR THR ARG ALA ASN GLN THR ARG ALA ALA
SEQRES 7 B 98 LEU MET MET GLY ILE ASN ARG GLY THR LEU ARG LYS LYS
SEQRES 8 B 98 LEU LYS LYS TYR GLY MET ASN
FORMUL 3 HOH *96(H2 O)
HELIX 1 1 PRO A 26 GLN A 41 1 16
HELIX 2 2 ASP A 49 THR A 70 1 22
HELIX 3 3 ASN A 73 GLY A 82 1 10
HELIX 4 4 ASN A 84 TYR A 95 1 12
HELIX 5 5 PRO B 26 ALA B 40 1 15
HELIX 6 6 ASP B 49 THR B 70 1 22
HELIX 7 7 ASN B 73 GLY B 82 1 10
HELIX 8 8 ASN B 84 TYR B 95 1 12
CRYST1 78.290 50.370 47.260 90.00 90.00 90.00 P 21 21 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 0.012773 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021160 0.00000
(ATOM LINES ARE NOT SHOWN.)
END