HEADER BIFUNCTIONAL(ISOMERASE AND SYNTHASE) 21-JUN-91 1PII
TITLE THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME
TITLE 2 PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE
TITLE 3 SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-(5'PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.1.1.48;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS BIFUNCTIONAL(ISOMERASE AND SYNTHASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WILMANNS,J.P.PRIESTLE,J.N.JANSONIUS
REVDAT 5 14-FEB-24 1PII 1 REMARK
REVDAT 4 29-NOV-17 1PII 1 REMARK HELIX
REVDAT 3 24-FEB-09 1PII 1 VERSN
REVDAT 2 01-APR-03 1PII 1 JRNL
REVDAT 1 31-JAN-94 1PII 0
JRNL AUTH M.WILMANNS,J.P.PRIESTLE,T.NIERMANN,J.N.JANSONIUS
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME
JRNL TITL 2 PHOSPHORIBOSYLANTHRANILATE ISOMERASE:
JRNL TITL 3 INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI
JRNL TITL 4 REFINED AT 2.0 A RESOLUTION.
JRNL REF J.MOL.BIOL. V. 223 477 1992
JRNL REFN ISSN 0022-2836
JRNL PMID 1738159
JRNL DOI 10.1016/0022-2836(92)90665-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.WILMANNS,C.C.HYDE,D.R.DAVIES,K.KIRSCHNER,J.N.JANSONIUS
REMARK 1 TITL STRUCTURAL CONSERVATION IN PARALLEL BETA(SLASH)ALPHA-BARREL
REMARK 1 TITL 2 ENZYMES THAT CATALYZE THREE SEQUENTIAL REACTIONS IN THE
REMARK 1 TITL 3 PATHWAY OF TRYPTOPHAN BIOSYNTHESIS
REMARK 1 REF BIOCHEMISTRY V. 30 9161 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.P.PRIESTLE,M.G.GRUETTER,J.L.WHITE,M.G.VINCENT,M.KANIA,
REMARK 1 AUTH 2 E.WILSON,T.S.JARDETZKY,K.KIRSCHNER,J.N.JANSONIUS
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME
REMARK 1 TITL 2 N-(5'-PHOSPHORIBOSYL)ANTHRANILATE
REMARK 1 TITL 3 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE FROM
REMARK 1 TITL 4 ESCHERICHIA COLI
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 84 5690 1987
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.L.WHITE,M.G.GRUETTER,E.WILSON,C.THALLER,G.C.FORD,
REMARK 1 AUTH 2 J.D.G.SMIT,J.N.JANSONIUS,K.KIRSCHNER
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC DATA
REMARK 1 TITL 2 OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYL-ANTHRANILATE
REMARK 1 TITL 3 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE FROM
REMARK 1 TITL 4 ESCHERICHIA COLI
REMARK 1 REF FEBS LETT. V. 148 87 1982
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 44611
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3478
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 628
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.010 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 3.200 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE REFINED CRYSTAL STRUCTURE OF PRAI:IGPS INCLUDES TWO
REMARK 3 PHOSPHATE IONS, ONE BOUND TO EACH ACTIVE SITE OF THIS
REMARK 3 BIFUNCTIONAL ENZYME.
REMARK 4
REMARK 4 1PII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 34.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.00000
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: MONOMERIC
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 400
REMARK 400 COMPOUND
REMARK 400 THE SECONDARY STRUCTURAL ELEMENTS (ALPHA-HELICES,
REMARK 400 BETA-STRANDS, TURNS) WERE DETERMINED WITH THE PROGRAM DSSP
REMARK 400 (KABSCH AND SANDER, 1983).
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 NZ LYS A 78 O HOH A 536 2.04
REMARK 500 OG SER A 237 O2 PO4 A 453 2.11
REMARK 500 O HOH A 598 O HOH A 744 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 17 CD GLU A 17 OE2 0.081
REMARK 500 ARG A 197 CD ARG A 197 NE -0.148
REMARK 500 ARG A 197 CZ ARG A 197 NH2 0.119
REMARK 500 GLU A 347 CD GLU A 347 OE1 0.071
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 11 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 67 C - N - CA ANGL. DEV. = 22.9 DEGREES
REMARK 500 ASP A 67 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 PHE A 68 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 ARG A 127 CD - NE - CZ ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP A 132 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 142 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 143 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ALA A 173 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 187 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP A 187 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 197 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 197 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 199 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 250 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 267 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 273 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 273 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 289 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 289 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 289 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLN A 295 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP A 315 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP A 315 CB - CG - OD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ASP A 318 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 318 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLU A 363 N - CA - CB ANGL. DEV. = 11.6 DEGREES
REMARK 500 LEU A 365 CB - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 GLN A 371 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 ASP A 379 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASN A 380 N - CA - C ANGL. DEV. = -21.7 DEGREES
REMARK 500 GLY A 384 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 SER A 385 N - CA - C ANGL. DEV. = -20.6 DEGREES
REMARK 500 GLN A 387 C - N - CA ANGL. DEV. = 21.2 DEGREES
REMARK 500 GLN A 387 N - CA - C ANGL. DEV. = 23.3 DEGREES
REMARK 500 ARG A 388 C - N - CA ANGL. DEV. = 17.6 DEGREES
REMARK 500 ARG A 388 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 388 N - CA - C ANGL. DEV. = 24.7 DEGREES
REMARK 500 ASP A 390 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 390 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 411 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 411 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 440 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 440 NE - CZ - NH2 ANGL. DEV. = -3.5 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 GLN A 23 70.61 -154.77
REMARK 500 PHE A 28 -9.99 -146.57
REMARK 500 ASP A 67 40.27 -50.47
REMARK 500 GLN A 130 6.21 86.49
REMARK 500 SER A 215 139.86 77.09
REMARK 500 ALA A 285 -38.35 -39.88
REMARK 500 PRO A 304 48.22 -78.39
REMARK 500 ARG A 388 141.55 33.35
REMARK 500 ASN A 427 -99.12 -139.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 197 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 713
REMARK 615 HOH A 748
REMARK 615 HOH A 782
REMARK 615 HOH A 856
REMARK 615 HOH A 857
REMARK 615 HOH A 951
REMARK 615 HOH A 1011
REMARK 615 HOH A 1024
REMARK 700
REMARK 700 SHEET
REMARK 700 PRAI:IGPS CONSISTS OF TWO BETA/ALPHA-BARRELS, WHICH CAN BE
REMARK 700 SUPERIMPOSED ON EACH OTHER. IGPS HAS AN N-TERMINAL
REMARK 700 EXTENSION OUTSIDE OF THE BETA/ALPHA-BARREL, COMPRISING
REMARK 700 RESIDUES 1-48.
REMARK 700 THE SHEET PRESENTED AS *I* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST
REMARK 700 AND LAST STRANDS ARE IDENTICAL.
REMARK 700 THE SHEET PRESENTED AS *P* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST
REMARK 700 AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ASS
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE OF IGPS
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASI
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE OF PRAI
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 454
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 329 IS IDENTIFIED AS VAL IN PIR ENTRY GWEC.
REMARK 999 RECENT RESEQUENCING CONFIRMED THAT RESIDUE 329 IS ALA. IT
REMARK 999 IS PRESENTED AS ALA IN THIS ENTRY.
REMARK 999
REMARK 999 SEQUENCE ADVISORY NOTICE:
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME:TRPC_ECOLI
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 ARG 94 GLN 94
REMARK 999 SER 319 VAL 319
REMARK 999 VAL 329 ALA 329
REMARK 999 THR 398 SER 398
DBREF 1PII A 1 452 UNP P00909 TRPC_ECOLI 2 453
SEQRES 1 A 452 MET GLN THR VAL LEU ALA LYS ILE VAL ALA ASP LYS ALA
SEQRES 2 A 452 ILE TRP VAL GLU ALA ARG LYS GLN GLN GLN PRO LEU ALA
SEQRES 3 A 452 SER PHE GLN ASN GLU VAL GLN PRO SER THR ARG HIS PHE
SEQRES 4 A 452 TYR ASP ALA LEU GLN GLY ALA ARG THR ALA PHE ILE LEU
SEQRES 5 A 452 GLU CYS LYS LYS ALA SER PRO SER LYS GLY VAL ILE ARG
SEQRES 6 A 452 ASP ASP PHE ASP PRO ALA ARG ILE ALA ALA ILE TYR LYS
SEQRES 7 A 452 HIS TYR ALA SER ALA ILE SER VAL LEU THR ASP GLU LYS
SEQRES 8 A 452 TYR PHE GLN GLY SER PHE ASN PHE LEU PRO ILE VAL SER
SEQRES 9 A 452 GLN ILE ALA PRO GLN PRO ILE LEU CYS LYS ASP PHE ILE
SEQRES 10 A 452 ILE ASP PRO TYR GLN ILE TYR LEU ALA ARG TYR TYR GLN
SEQRES 11 A 452 ALA ASP ALA CYS LEU LEU MET LEU SER VAL LEU ASP ASP
SEQRES 12 A 452 ASP GLN TYR ARG GLN LEU ALA ALA VAL ALA HIS SER LEU
SEQRES 13 A 452 GLU MET GLY VAL LEU THR GLU VAL SER ASN GLU GLU GLU
SEQRES 14 A 452 GLN GLU ARG ALA ILE ALA LEU GLY ALA LYS VAL VAL GLY
SEQRES 15 A 452 ILE ASN ASN ARG ASP LEU ARG ASP LEU SER ILE ASP LEU
SEQRES 16 A 452 ASN ARG THR ARG GLU LEU ALA PRO LYS LEU GLY HIS ASN
SEQRES 17 A 452 VAL THR VAL ILE SER GLU SER GLY ILE ASN THR TYR ALA
SEQRES 18 A 452 GLN VAL ARG GLU LEU SER HIS PHE ALA ASN GLY PHE LEU
SEQRES 19 A 452 ILE GLY SER ALA LEU MET ALA HIS ASP ASP LEU HIS ALA
SEQRES 20 A 452 ALA VAL ARG ARG VAL LEU LEU GLY GLU ASN LYS VAL CYS
SEQRES 21 A 452 GLY LEU THR ARG GLY GLN ASP ALA LYS ALA ALA TYR ASP
SEQRES 22 A 452 ALA GLY ALA ILE TYR GLY GLY LEU ILE PHE VAL ALA THR
SEQRES 23 A 452 SER PRO ARG CYS VAL ASN VAL GLU GLN ALA GLN GLU VAL
SEQRES 24 A 452 MET ALA ALA ALA PRO LEU GLN TYR VAL GLY VAL PHE ARG
SEQRES 25 A 452 ASN HIS ASP ILE ALA ASP VAL VAL ASP LYS ALA LYS VAL
SEQRES 26 A 452 LEU SER LEU ALA ALA VAL GLN LEU HIS GLY ASN GLU GLU
SEQRES 27 A 452 GLN LEU TYR ILE ASP THR LEU ARG GLU ALA LEU PRO ALA
SEQRES 28 A 452 HIS VAL ALA ILE TRP LYS ALA LEU SER VAL GLY GLU THR
SEQRES 29 A 452 LEU PRO ALA ARG GLU PHE GLN HIS VAL ASP LYS TYR VAL
SEQRES 30 A 452 LEU ASP ASN GLY GLN GLY GLY SER GLY GLN ARG PHE ASP
SEQRES 31 A 452 TRP SER LEU LEU ASN GLY GLN SER LEU GLY ASN VAL LEU
SEQRES 32 A 452 LEU ALA GLY GLY LEU GLY ALA ASP ASN CYS VAL GLU ALA
SEQRES 33 A 452 ALA GLN THR GLY CYS ALA GLY LEU ASP PHE ASN SER ALA
SEQRES 34 A 452 VAL GLU SER GLN PRO GLY ILE LYS ASP ALA ARG LEU LEU
SEQRES 35 A 452 ALA SER VAL PHE GLN THR LEU ARG ALA TYR
HET PO4 A 453 5
HET PO4 A 454 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 HOH *628(H2 O)
HELIX 1 I0 VAL A 4 GLN A 22 1 19
HELIX 2 I1 PRO A 70 TYR A 77 1 8
HELIX 3 I2 PHE A 97 ALA A 107 1RESIDUES 97-100: 3/10-HELIX 11
HELIX 4 I3 PRO A 120 TYR A 128 1 9
HELIX 5 I4 ASP A 143 HIS A 154 1 12
HELIX 6 I5 GLU A 167 ALA A 175 1 9
HELIX 7 I6 ASN A 196 LEU A 201 1 6
HELIX 8 I7 TYR A 220 LEU A 226 1 7
HELIX 9 I8' SER A 237 MET A 240 1 4
HELIX 10 I8 LEU A 245 LEU A 253 1 9
HELIX 11 P1 GLY A 265 ALA A 274 1 10
HELIX 12 P2 VAL A 293 MET A 300 1 8
HELIX 13 P3 ILE A 316 LEU A 326 1 11
HELIX 14 P4 GLN A 339 ALA A 348 1 10
HELIX 15 P6 TRP A 391 LEU A 394 5 4
HELIX 16 P7 CYS A 413 ALA A 417 1 5
HELIX 17 P8' SER A 428 VAL A 430 5 3
HELIX 18 P8 ALA A 439 ARG A 450 1 12
SHEET 1 I 9 ALA A 49 CYS A 54 0
SHEET 2 I 9 ALA A 83 LEU A 87 -1 N ALA A 83 O PHE A 50
SHEET 3 I 9 PRO A 110 LYS A 114 -1 O PRO A 110 N ILE A 84
SHEET 4 I 9 ALA A 133 MET A 137 -1 N ALA A 133 O ILE A 111
SHEET 5 I 9 GLY A 159 VAL A 164 -1 O GLY A 159 N CYS A 134
SHEET 6 I 9 VAL A 180 ASN A 184 -1 O VAL A 180 N THR A 162
SHEET 7 I 9 THR A 210 GLU A 214 -1 O THR A 210 N VAL A 181
SHEET 8 I 9 GLY A 232 ILE A 235 -1 N GLY A 232 O VAL A 211
SHEET 9 I 9 ALA A 49 CYS A 54 -1 N ILE A 51 O PHE A 233
SHEET 1 P 9 ASN A 257 CYS A 260 0
SHEET 2 P 9 TYR A 278 ILE A 282 -1 N TYR A 278 O ASN A 257
SHEET 3 P 9 GLN A 306 PHE A 311 -1 O GLN A 306 N GLY A 279
SHEET 4 P 9 ALA A 330 LEU A 333 -1 N ALA A 330 O TYR A 307
SHEET 5 P 9 ALA A 354 SER A 360 -1 O ALA A 354 N VAL A 331
SHEET 6 P 9 LYS A 375 ASP A 379 -1 O LYS A 375 N LYS A 357
SHEET 7 P 9 VAL A 402 LEU A 404 -1 N LEU A 403 O TYR A 376
SHEET 8 P 9 GLY A 423 PHE A 426 -1 O GLY A 423 N LEU A 404
SHEET 9 P 9 ASN A 257 CYS A 260 -1 N LYS A 258 O LEU A 424
SITE 1 ASS 24 VAL A 4 LEU A 5 ILE A 8 GLU A 53
SITE 2 ASS 24 LYS A 55 SER A 58 PRO A 59 SER A 60
SITE 3 ASS 24 LYS A 61 TYR A 92 PHE A 93 LYS A 114
SITE 4 ASS 24 PHE A 116 GLU A 163 ASN A 184 ARG A 186
SITE 5 ASS 24 LEU A 188 LEU A 191 GLU A 214 SER A 215
SITE 6 ASS 24 LEU A 234 GLY A 236 SER A 237 ALA A 238
SITE 1 ASI 19 LYS A 258 CYS A 260 ILE A 282 ARG A 289
SITE 2 ASI 19 VAL A 291 VAL A 310 GLN A 332 HIS A 334
SITE 3 ASI 19 ASP A 379 SER A 385 ALA A 405 GLY A 406
SITE 4 ASI 19 GLY A 407 ASP A 425 ASN A 427 SER A 428
SITE 5 ASI 19 ALA A 429 VAL A 430 GLU A 431
SITE 1 AC1 9 LYS A 55 SER A 215 GLY A 216 ILE A 235
SITE 2 AC1 9 GLY A 236 SER A 237 HOH A 455 HOH A 515
SITE 3 AC1 9 HOH A 531
SITE 1 AC2 9 GLY A 383 GLY A 386 GLY A 407 ASN A 427
SITE 2 AC2 9 SER A 428 HOH A 483 HOH A 502 HOH A 706
SITE 3 AC2 9 HOH A 948
CRYST1 104.700 104.700 68.000 90.00 90.00 90.00 P 41 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 0.009551 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014706 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
