HEADER NUCLEOTIDE-BINDING PROTEIN 11-DEC-97 1FHI
TITLE SUBSTRATE ANALOG (IB2) COMPLEX WITH THE FRAGILE HISTIDINE
TITLE 2 TRIAD PROTEIN, FHIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRAGILE HISTIDINE TRIAD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FHIT;
COMPND 5 EC: 3.6.1.29;
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: FHIT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109/DE3/LACIQ;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSGA02
KEYWDS NUCLEOTIDE-BINDING PROTEIN, CANCER, DIADENOSINE
KEYWDS 2 TRIPHOSPHATE HYDROLASE, HISTIDINE TRIAD, TUMOR SUPPRESSOR
EXPDTA X-RAY DIFFRACTION
AUTHOR H.C.PACE,P.N.GARRISON,L.D.BARNES,A.DRAGANESCU,A.ROSLER,
AUTHOR 2 G.M.BLACKBURN,Z.SIPRASHVILI,C.M.CROCE,K.HUEBNER,C.BRENNER
REVDAT 2 24-FEB-09 1FHI 1 VERSN
REVDAT 1 17-JUN-98 1FHI 0
JRNL AUTH H.C.PACE,P.N.GARRISON,A.K.ROBINSON,L.D.BARNES,
JRNL AUTH 2 A.DRAGANESCU,A.ROSLER,G.M.BLACKBURN,Z.SIPRASHVILI,
JRNL AUTH 3 C.M.CROCE,K.HUEBNER,C.BRENNER
JRNL TITL GENETIC, BIOCHEMICAL, AND CRYSTALLOGRAPHIC
JRNL TITL 2 CHARACTERIZATION OF FHIT-SUBSTRATE COMPLEXES AS
JRNL TITL 3 THE ACTIVE SIGNALING FORM OF FHIT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 95 5484 1998
JRNL REFN ISSN 0027-8424
JRNL PMID 9576908
JRNL DOI 10.1073/PNAS.95.10.5484
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.BRENNER,H.C.PACE,P.N.GARRISON,A.K.ROBINSON,
REMARK 1 AUTH 2 A.ROSLER,X.H.LIU,G.M.BLACKBURN,C.M.CROCE,K.HUEBNER,
REMARK 1 AUTH 3 L.D.BARNES
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF COMPLEXES
REMARK 1 TITL 2 MODELING THE ACTIVE STATE OF THE FRAGILE HISTIDINE
REMARK 1 TITL 3 TRIAD PROTEIN
REMARK 1 REF PROTEIN ENG. V. 10 1461 1998
REMARK 1 REFN ISSN 0269-2139
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 61.0
REMARK 3 NUMBER OF REFLECTIONS : 2535
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) : 0.241
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 125
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.028
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 33.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 157
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.5160
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 11
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.156
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1210
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 3
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.56
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : IB2.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.PEP
REMARK 3 TOPOLOGY FILE 3 : WATER2.TOPH
REMARK 3 TOPOLOGY FILE 4 : IB2.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FHI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-97
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 2965
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 43.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 68.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 39.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: REFINEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 1FIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: FHIT PROTEIN (13.4 MG/ML) WAS
REMARK 280 COCRYSTALLIZED WITH 2.5 MOLAR EQUIVALENTS OF IB2 BY MIXING
REMARK 280 WITH AN EQUAL VOLUME (2.5 - 4 MICROLITERS) OF 2 M AMMONIUM
REMARK 280 SULFATE, 4% PEG 400 0.1 M NA HEPES PH 7.5 ON A SILICONIZED
REMARK 280 COVERSLIP WHICH WAS SEALED OVER A 0.8 ML VOLUME OF THE SAME
REMARK 280 SOLUTION FOR 1 - 4 WEEKS AT ROOM TEMPERATURE., VAPOR DIFFUSION
REMARK 280 - HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 89.50433
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 179.00867
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 134.25650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 223.76083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.75217
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 89.50433
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 179.00867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 223.76083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 134.25650
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 44.75217
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: DIMERIC
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 BIOMT1 2 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 44.75217
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 107
REMARK 465 HIS A 108
REMARK 465 ARG A 109
REMARK 465 ASN A 110
REMARK 465 ASP A 111
REMARK 465 SER A 112
REMARK 465 ILE A 113
REMARK 465 TYR A 114
REMARK 465 GLU A 115
REMARK 465 GLU A 116
REMARK 465 LEU A 117
REMARK 465 GLN A 118
REMARK 465 LYS A 119
REMARK 465 HIS A 120
REMARK 465 ASP A 121
REMARK 465 LYS A 122
REMARK 465 GLU A 123
REMARK 465 ASP A 124
REMARK 465 PHE A 125
REMARK 465 PRO A 126
REMARK 465 ALA A 127
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 ASP A 53 CG OD1 OD2
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 GLU A 133 CG CD OE1 OE2
REMARK 470 GLU A 134 CG 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 PHE A 3 104.25 80.16
REMARK 500 PHE A 5 81.93 -161.62
REMARK 500 THR A 19 -168.92 -108.04
REMARK 500 HIS A 48 -0.16 -52.28
REMARK 500 ARG A 51 178.95 -54.66
REMARK 500 GLU A 54 8.91 -62.69
REMARK 500 ARG A 64 -74.52 -60.74
REMARK 500 VAL A 65 -24.30 -33.62
REMARK 500 SER A 77 167.15 165.68
REMARK 500 SER A 81 116.97 -164.38
REMARK 500 HIS A 96 135.66 -178.29
REMARK 500 ALA A 104 160.48 -44.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: HIT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIS 94, HIS 96, HIS 98 THE HISTIDINE TRIAD
REMARK 800 SITE CONTAINS THE MOTIF COMMON TO PROTEINS IN THE HIT
REMARK 800 SUPERFAMILY OF NUCLEOTIDE-BINDING PROTEINS. HIS 96 IS THE
REMARK 800 PRINCIPAL ACTIVE SITE RESIDUE AND SUBSTITUTION WITH ASN
REMARK 800 REDUCES KCAT (10E6)-FOLD WITH LITTLE EFFECT ON KM. HIS 98 IS
REMARK 800 PROPOSED TO H-BOND TO THE SCISSILE BRIDGING OXYGEN OF
REMARK 800 DINUCLEOTIDE SUBSTRATES.
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IB2 A 301
DBREF 1FHI A 1 147 UNP P49789 FHIT_HUMAN 1 147
SEQRES 1 A 147 MET SER PHE ARG PHE GLY GLN HIS LEU ILE LYS PRO SER
SEQRES 2 A 147 VAL VAL PHE LEU LYS THR GLU LEU SER PHE ALA LEU VAL
SEQRES 3 A 147 ASN ARG LYS PRO VAL VAL PRO GLY HIS VAL LEU VAL CYS
SEQRES 4 A 147 PRO LEU ARG PRO VAL GLU ARG PHE HIS ASP LEU ARG PRO
SEQRES 5 A 147 ASP GLU VAL ALA ASP LEU PHE GLN THR THR GLN ARG VAL
SEQRES 6 A 147 GLY THR VAL VAL GLU LYS HIS PHE HIS GLY THR SER LEU
SEQRES 7 A 147 THR PHE SER MET GLN ASP GLY PRO GLU ALA GLY GLN THR
SEQRES 8 A 147 VAL LYS HIS VAL HIS VAL HIS VAL LEU PRO ARG LYS ALA
SEQRES 9 A 147 GLY ASP PHE HIS ARG ASN ASP SER ILE TYR GLU GLU LEU
SEQRES 10 A 147 GLN LYS HIS ASP LYS GLU ASP PHE PRO ALA SER TRP ARG
SEQRES 11 A 147 SER GLU GLU GLU MET ALA ALA GLU ALA ALA ALA LEU ARG
SEQRES 12 A 147 VAL TYR PHE GLN
HET IB2 A 301 49
HETNAM IB2 P1-P2-METHYLENE-P3-THIO-DIADENOSINE TRIPHOSPHATE
HETSYN IB2 ADO-P-CH2-P-PS-ADO
FORMUL 2 IB2 C21 H29 N10 O14 P3 S
FORMUL 3 HOH *3(H2 O)
HELIX 1 1 PRO A 12 VAL A 14 5 3
HELIX 2 2 PHE A 47 ASP A 49 5 3
HELIX 3 3 ASP A 53 THR A 67 1 15
HELIX 4 4 VAL A 69 HIS A 72 1 4
HELIX 5 5 GLU A 132 TYR A 145 1 14
SHEET 1 A 5 SER A 77 MET A 82 0
SHEET 2 A 5 HIS A 96 ARG A 102 -1 N ARG A 102 O SER A 77
SHEET 3 A 5 VAL A 36 PRO A 40 -1 N VAL A 38 O VAL A 97
SHEET 4 A 5 SER A 22 VAL A 26 -1 N LEU A 25 O LEU A 37
SHEET 5 A 5 VAL A 15 LYS A 18 -1 N LEU A 17 O ALA A 24
SITE 1 HIT 3 HIS A 94 HIS A 96 HIS A 98
SITE 1 AC1 13 PHE A 5 ILE A 10 ASN A 27 LEU A 37
SITE 2 AC1 13 THR A 79 SER A 81 GLN A 83 THR A 91
SITE 3 AC1 13 VAL A 92 HIS A 96 HIS A 98 LEU A 100
SITE 4 AC1 13 ARG A 102
CRYST1 50.728 50.728 268.513 90.00 90.00 120.00 P 61 2 2 12
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 0.019713 0.011381 0.000000 0.00000
SCALE2 0.000000 0.022763 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003724 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
