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HEADER HYDROLASE 23-SEP-02 1MU0
TITLE CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR F1
TITLE 2 COMPLEX WITH PCK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIP, PROLYL AMINOPEPTIDASE, PAP, TRICORN PROTEASE
COMPND 5 INTERACTING FACTOR F1;
COMPND 6 EC: 3.4.11.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 GENE: TA0830;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET6C
KEYWDS ALPHA-BETA HYDROLASE, CAP DOMAIN, CAGED ACTIVE SITE, PROLYL
KEYWDS 2 PEPTIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GOETTIG,M.GROLL,J.-S.KIM,R.HUBER,H.BRANDSTETTER
REVDAT 1 06-NOV-02 1MU0 0
JRNL AUTH P.GOETTIG,M.GROLL,J.-S.KIM,R.HUBER,H.BRANDSTETTER
JRNL TITL STRUCTURES OF THE TRICORN-INTERACTING FACTOR F1
JRNL TITL 2 WITH DIFFERENT LIGANDS EXPLAIN ITS CATALYTIC
JRNL TITL 3 MECHANISM
JRNL REF EMBO J. V. 21 5343 2002
JRNL REFN ASTM EMJODG UK ISSN 0261-4189
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.3
REMARK 3 NUMBER OF REFLECTIONS : 9956
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) : 0.314
REMARK 3 FREE R VALUE : 0.366
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 510
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2357
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.89000
REMARK 3 B22 (A**2) : -9.59000
REMARK 3 B33 (A**2) : -6.30000
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) : 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) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MU0 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
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 : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12507
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1MT3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 100 MM BIS-TRIS-HCL
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 28.78950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.21750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.86050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.21750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.78950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.86050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 14 N - CA - C ANGL. DEV. = 5.9 DEGREES
REMARK 500 PRO A 25 C - N - CA ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 43 N - CA - C ANGL. DEV. = 6.3 DEGREES
REMARK 500 HIS A 181 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 ILE A 207 N - CA - C ANGL. DEV. = 5.7 DEGREES
REMARK 500 VAL A 246 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 THR A 247 N - CA - C ANGL. DEV. = 7.1 DEGREES
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE REACTION OF PHENYLALANYLCHLOROMETHYL KETONE
REMARK 600 (PCK) WITH SER105 RESULTED IN A COVALENTLY BOUND
REMARK 600 HETEROMOLECULE (PHK).
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MT3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR
REMARK 900 SELENOMETHIONINE-F1
REMARK 900 RELATED ID: 1MTZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRICORN INTERACTING FACTOR F1
DBREF 1MU0 A 1 293 SWS P96084 PIP_THEAC 1 293
SEQRES 1 A 293 MET ASP GLN GLU CYS ILE GLU ASN TYR ALA LYS VAL ASN
SEQRES 2 A 293 GLY ILE TYR ILE TYR TYR LYS LEU CYS LYS ALA PRO GLU
SEQRES 3 A 293 GLU LYS ALA LYS LEU MET THR MET HIS GLY GLY PRO GLY
SEQRES 4 A 293 MET SER HIS ASP TYR LEU LEU SER LEU ARG ASP MET THR
SEQRES 5 A 293 LYS GLU GLY ILE THR VAL LEU PHE TYR ASP GLN PHE GLY
SEQRES 6 A 293 CYS GLY ARG SER GLU GLU PRO ASP GLN SER LYS PHE THR
SEQRES 7 A 293 ILE ASP TYR GLY VAL GLU GLU ALA GLU ALA LEU ARG SER
SEQRES 8 A 293 LYS LEU PHE GLY ASN GLU LYS VAL PHE LEU MET GLY SER
SEQRES 9 A 293 SER TYR GLY GLY ALA LEU ALA LEU ALA TYR ALA VAL LYS
SEQRES 10 A 293 TYR GLN ASP HIS LEU LYS GLY LEU ILE VAL SER GLY GLY
SEQRES 11 A 293 LEU SER SER VAL PRO LEU THR VAL LYS GLU MET ASN ARG
SEQRES 12 A 293 LEU ILE ASP GLU LEU PRO ALA LYS TYR ARG ASP ALA ILE
SEQRES 13 A 293 LYS LYS TYR GLY SER SER GLY SER TYR GLU ASN PRO GLU
SEQRES 14 A 293 TYR GLN GLU ALA VAL ASN TYR PHE TYR HIS GLN HIS LEU
SEQRES 15 A 293 LEU ARG SER GLU ASP TRP PRO PRO GLU VAL LEU LYS SER
SEQRES 16 A 293 LEU GLU TYR ALA GLU ARG ARG ASN VAL TYR ARG ILE MET
SEQRES 17 A 293 ASN GLY PRO ASN GLU PHE THR ILE THR GLY THR ILE LYS
SEQRES 18 A 293 ASP TRP ASP ILE THR ASP LYS ILE SER ALA ILE LYS ILE
SEQRES 19 A 293 PRO THR LEU ILE THR VAL GLY GLU TYR ASP GLU VAL THR
SEQRES 20 A 293 PRO ASN VAL ALA ARG VAL ILE HIS GLU LYS ILE ALA GLY
SEQRES 21 A 293 SER GLU LEU HIS VAL PHE ARG ASP CYS SER HIS LEU THR
SEQRES 22 A 293 MET TRP GLU ASP ARG GLU GLY TYR ASN LYS LEU LEU SER
SEQRES 23 A 293 ASP PHE ILE LEU LYS HIS LEU
HET PHK A 300 13
HETNAM PHK 3-AMINO-1-CHLORO-4-PHENYL-BUTANOL-2-YL
FORMUL 2 PHK C10 H13 N1 O1 CL1
FORMUL 3 HOH *37(H2 O1)
HELIX 1 1 SER A 41 GLU A 54 5 14
HELIX 2 2 ASP A 73 PHE A 77 5 5
HELIX 3 3 THR A 78 GLY A 95 1 18
HELIX 4 4 SER A 105 GLN A 119 1 15
HELIX 5 5 SER A 133 LEU A 148 1 16
HELIX 6 6 PRO A 149 TYR A 159 1 11
HELIX 7 7 ASN A 167 LEU A 182 1 16
HELIX 8 8 PRO A 189 ARG A 202 1 14
HELIX 9 9 ASN A 203 ASN A 209 1 7
HELIX 10 10 LYS A 228 ILE A 232 5 5
HELIX 11 11 THR A 247 ILE A 258 1 12
HELIX 12 12 LEU A 272 ASP A 277 1 6
HELIX 13 13 ASP A 277 HIS A 292 1 16
SHEET 1 A 8 ILE A 6 LYS A 11 0
SHEET 2 A 8 TYR A 16 CYS A 22 -1 O LEU A 21 N ILE A 6
SHEET 3 A 8 ILE A 56 ASP A 62 -1 O PHE A 60 N LYS A 20
SHEET 4 A 8 ALA A 29 MET A 34 1 N LEU A 31 O LEU A 59
SHEET 5 A 8 VAL A 99 SER A 104 1 O PHE A 100 N MET A 32
SHEET 6 A 8 LEU A 122 SER A 128 1 O ILE A 126 N GLY A 103
SHEET 7 A 8 THR A 236 GLY A 241 1 O LEU A 237 N LEU A 125
SHEET 8 A 8 GLU A 262 PHE A 266 1 O HIS A 264 N ILE A 238
SSBOND 1 CYS A 5 CYS A 22
LINK C PHK A 300 OG SER A 105
CISPEP 1 ALA A 24 PRO A 25 0 0.09
CISPEP 2 GLY A 37 PRO A 38 0 -0.02
CRYST1 57.579 61.721 80.435 90.00 90.00 90.00 P 21 21 21 4
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 0.017367 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012432 0.00000
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