HEADER LYASE 18-SEP-00 1FUY
TITLE CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN
TITLE 2 SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.20;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRYPTOPHAN SYNTHASE BETA CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 EC: 4.2.1.20;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 CELL_LINE: CB149;
SOURCE 5 GENE: TRPA/TRPB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSTB7;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 12 ORGANISM_TAXID: 602;
SOURCE 13 CELL_LINE: CB149;
SOURCE 14 GENE: TRPA/TRPB;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PSTB7
KEYWDS LYASE, CARBON-OXYGEN LYASE, TRYPTOPHAN BIOSYNTHESIS, PYRIDOXAL
KEYWDS 2 PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WEYAND,I.SCHLICHTING
REVDAT 3 13-JUL-11 1FUY 1 VERSN
REVDAT 2 24-FEB-09 1FUY 1 VERSN
REVDAT 1 17-JAN-01 1FUY 0
JRNL AUTH M.WEYAND,I.SCHLICHTING
JRNL TITL STRUCTURAL BASIS FOR THE IMPAIRED CHANNELING AND ALLOSTERIC
JRNL TITL 2 INTER-SUBUNIT COMMUNICATION IN THE BETA A169L/BETA C170W
JRNL TITL 3 MUTANT OF TRYPTOPHAN SYNTHASE.
JRNL REF J.BIOL.CHEM. V. 275 41058 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 11034989
JRNL DOI 10.1074/JBC.C000479200
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 0.9
REMARK 3 NUMBER OF REFLECTIONS : 32603
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1634
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4963
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 2.500 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.017 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FUY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-94
REMARK 200 TEMPERATURE (KELVIN) : 275.0
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.15
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34995
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04400
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) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 37.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.19
REMARK 200 R MERGE FOR SHELL (I) : 0.29500
REMARK 200 R SYM FOR SHELL (I) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME SOLUTION: 10 MG/ML TRPS IN
REMARK 280 50 MM BICINE PH 7.8, 1 MM EDTA, 5 MM DITHIOERYTHRITOL, 20 MUM
REMARK 280 PYRIDOXAL-5'-PHOSPHATE RESERVOI SOLUTION: 50 MM BICINE PH 7.8, 5
REMARK 280 MM EDTA, 5 MM DITHIOERYTHRITOL, 0.1 MM PYRIDOXAL-5'-PHOSPHATE, 2
REMARK 280 MM SPERMINE, 8-12 % PEG 8000 CRYSTALLIZATION DROP CONSISTED AN
REMARK 280 INITIAL FIP CONCENTRATION OF 7 MM, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.00000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.35000
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 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSTRUCTED FROM
REMARK 300 CHAIN A AND CHAIN B SYMMETRY PARTNERS ARE GENERATED BY THE TWO-FOLD.
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: TETRAMERIC
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 184.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ARG A 188
REMARK 465 GLY A 189
REMARK 465 ALA A 190
REMARK 465 LEU A 191
REMARK 465 PRO A 192
REMARK 465 ALA A 268
REMARK 465 GLY B 395
REMARK 465 GLU B 396
REMARK 465 ILE B 397
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 ASN A 187 CG OD1
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 ARG A 3 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 GLU A 5 CA - CB - CG ANGL. DEV. = 19.1 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 VAL A 23 N - CA - CB ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 38 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 60 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 PHE A 82 CB - CG - CD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 PHE A 82 CB - CG - CD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 85 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 112 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 PHE A 114 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE A 114 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP A 130 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 GLU A 135 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ASP A 159 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TYR A 175 CB - CG - CD2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 175 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU A 193 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 HIS A 194 CA - CB - CG ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 225 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 256 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 267 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 55 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 CYS B 62 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 TYR B 74 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 100 NH1 - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG B 100 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ILE B 106 CA - CB - CG2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG B 131 CD - NE - CZ ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG B 131 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 148 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 150 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 MET B 152 CA - CB - CG ANGL. DEV. = -10.9 DEGREES
REMARK 500 TYR B 186 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 GLU B 203 OE1 - CD - OE2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG B 206 CD - NE - CZ ANGL. DEV. = 44.4 DEGREES
REMARK 500 ARG B 206 NH1 - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG B 206 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG B 222 CG - CD - NE ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG B 222 CD - NE - CZ ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG B 222 NE - CZ - NH1 ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG B 222 NE - CZ - NH2 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG B 275 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG B 275 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 65 ANGLE DEVIATIONS.
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 GLU A 2 41.87 -160.36
REMARK 500 ARG A 15 74.80 38.43
REMARK 500 PHE A 212 114.33 91.94
REMARK 500 ASN A 244 32.95 -97.51
REMARK 500 GLN B 142 44.88 -105.54
REMARK 500 SER B 308 -157.17 -136.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN B 317 -10.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE B 65 22.7 L L OUTSIDE RANGE
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 NA B 400 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 306 O
REMARK 620 2 HOH B 419 O 77.2
REMARK 620 3 SER B 308 O 87.5 152.1
REMARK 620 4 HOH B 405 O 162.1 89.8 99.2
REMARK 620 5 GLY B 232 O 107.5 108.3 98.4 88.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FIP A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QOP RELATED DB: PDB
REMARK 900 1QOP CONTAINS THE WILD-TYPE PROTEIN COMPLEXED WITH INDOLE-
REMARK 900 PROPANOL PHOSPHATE
REMARK 900 RELATED ID: 1A50 RELATED DB: PDB
REMARK 900 1A50 CONTAINS THE WILD-TYPE PROTEIN COMPLEXED WITH 5-FLUORO
REMARK 900 -INDOLE-PROPANOL PHOSPHATE
DBREF 1FUY A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 1FUY B 2 397 UNP P0A2K1 TRPB_SALTY 1 396
SEQADV 1FUY SER B 34 UNP P0A2K1 ARG 33 CLONING ARTIFACT
SEQADV 1FUY LEU B 169 UNP P0A2K1 ALA 168 ENGINEERED
SEQADV 1FUY TRP B 170 UNP P0A2K1 CYS 169 ENGINEERED
SEQRES 1 A 268 MET GLU ARG TYR GLU ASN LEU PHE ALA GLN LEU ASN ASP
SEQRES 2 A 268 ARG ARG GLU GLY ALA PHE VAL PRO PHE VAL THR LEU GLY
SEQRES 3 A 268 ASP PRO GLY ILE GLU GLN SER LEU LYS ILE ILE ASP THR
SEQRES 4 A 268 LEU ILE ASP ALA GLY ALA ASP ALA LEU GLU LEU GLY VAL
SEQRES 5 A 268 PRO PHE SER ASP PRO LEU ALA ASP GLY PRO THR ILE GLN
SEQRES 6 A 268 ASN ALA ASN LEU ARG ALA PHE ALA ALA GLY VAL THR PRO
SEQRES 7 A 268 ALA GLN CYS PHE GLU MET LEU ALA LEU ILE ARG GLU LYS
SEQRES 8 A 268 HIS PRO THR ILE PRO ILE GLY LEU LEU MET TYR ALA ASN
SEQRES 9 A 268 LEU VAL PHE ASN ASN GLY ILE ASP ALA PHE TYR ALA ARG
SEQRES 10 A 268 CYS GLU GLN VAL GLY VAL ASP SER VAL LEU VAL ALA ASP
SEQRES 11 A 268 VAL PRO VAL GLU GLU SER ALA PRO PHE ARG GLN ALA ALA
SEQRES 12 A 268 LEU ARG HIS ASN ILE ALA PRO ILE PHE ILE CYS PRO PRO
SEQRES 13 A 268 ASN ALA ASP ASP ASP LEU LEU ARG GLN VAL ALA SER TYR
SEQRES 14 A 268 GLY ARG GLY TYR THR TYR LEU LEU SER ARG SER GLY VAL
SEQRES 15 A 268 THR GLY ALA GLU ASN ARG GLY ALA LEU PRO LEU HIS HIS
SEQRES 16 A 268 LEU ILE GLU LYS LEU LYS GLU TYR HIS ALA ALA PRO ALA
SEQRES 17 A 268 LEU GLN GLY PHE GLY ILE SER SER PRO GLU GLN VAL SER
SEQRES 18 A 268 ALA ALA VAL ARG ALA GLY ALA ALA GLY ALA ILE SER GLY
SEQRES 19 A 268 SER ALA ILE VAL LYS ILE ILE GLU LYS ASN LEU ALA SER
SEQRES 20 A 268 PRO LYS GLN MET LEU ALA GLU LEU ARG SER PHE VAL SER
SEQRES 21 A 268 ALA MET LYS ALA ALA SER ARG ALA
SEQRES 1 B 396 THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY GLY
SEQRES 2 B 396 MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN GLN
SEQRES 3 B 396 LEU GLU GLU ALA PHE VAL SER ALA GLN LYS ASP PRO GLU
SEQRES 4 B 396 PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR ALA
SEQRES 5 B 396 GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE THR
SEQRES 6 B 396 ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU ASP
SEQRES 7 B 396 LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL LEU
SEQRES 8 B 396 GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER GLU
SEQRES 9 B 396 ILE ILE ALA GLU THR GLY ALA GLY GLN HIS GLY VAL ALA
SEQRES 10 B 396 SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS ARG
SEQRES 11 B 396 ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER PRO
SEQRES 12 B 396 ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL ILE
SEQRES 13 B 396 PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP LEU TRP
SEQRES 14 B 396 ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU THR
SEQRES 15 B 396 ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS PRO
SEQRES 16 B 396 TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE GLY
SEQRES 17 B 396 GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY ARG
SEQRES 18 B 396 LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY SER
SEQRES 19 B 396 ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP THR
SEQRES 20 B 396 SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS GLY
SEQRES 21 B 396 ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS GLY
SEQRES 22 B 396 ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET MET
SEQRES 23 B 396 GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER ILE
SEQRES 24 B 396 SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN HIS
SEQRES 25 B 396 ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL SER
SEQRES 26 B 396 ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR LEU
SEQRES 27 B 396 CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER SER
SEQRES 28 B 396 HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU GLN
SEQRES 29 B 396 PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER GLY
SEQRES 30 B 396 ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE LEU
SEQRES 31 B 396 LYS ALA ARG GLY GLU ILE
HET NA B 400 1
HET FIP A 269 18
HET PLP B 401 15
HETNAM NA SODIUM ION
HETNAM FIP 5-FLUOROINDOLE PROPANOL PHOSPHATE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 NA NA 1+
FORMUL 4 FIP C11 H13 F N O4 P
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *190(H2 O)
HELIX 1 1 GLU A 2 ASP A 13 1 12
HELIX 2 2 GLY A 29 ALA A 43 1 15
HELIX 3 3 GLY A 61 ALA A 74 1 14
HELIX 4 4 THR A 77 HIS A 92 1 16
HELIX 5 5 TYR A 102 ASN A 108 1 7
HELIX 6 6 GLY A 110 GLY A 122 1 13
HELIX 7 7 PRO A 132 GLU A 135 5 4
HELIX 8 8 SER A 136 HIS A 146 1 11
HELIX 9 9 ASP A 159 GLY A 170 1 12
HELIX 10 10 LEU A 193 TYR A 203 1 11
HELIX 11 11 SER A 216 GLY A 227 1 12
HELIX 12 12 GLY A 234 ASN A 244 1 11
HELIX 13 13 SER A 247 ALA A 265 1 19
HELIX 14 14 PRO B 18 ILE B 20 5 3
HELIX 15 15 LEU B 21 LYS B 37 1 17
HELIX 16 16 ASP B 38 TYR B 52 1 15
HELIX 17 17 ASP B 79 LEU B 81 5 3
HELIX 18 18 LYS B 87 GLY B 102 1 16
HELIX 19 19 GLY B 113 GLY B 127 1 15
HELIX 20 20 ALA B 136 GLN B 142 1 7
HELIX 21 21 GLN B 142 MET B 152 1 11
HELIX 22 22 THR B 165 TYR B 181 1 17
HELIX 23 23 PRO B 196 PHE B 204 1 9
HELIX 24 24 ARG B 206 GLY B 221 1 16
HELIX 25 25 GLY B 234 ALA B 242 1 9
HELIX 26 26 ASP B 243 ILE B 245 5 3
HELIX 27 27 GLY B 261 GLY B 265 5 5
HELIX 28 28 ALA B 269 GLY B 274 1 6
HELIX 29 29 SER B 301 ASP B 305 5 5
HELIX 30 30 GLY B 310 ILE B 319 1 10
HELIX 31 31 ASP B 329 GLY B 344 1 16
HELIX 32 32 ALA B 348 GLN B 365 1 18
HELIX 33 33 GLY B 380 LYS B 382 5 3
HELIX 34 34 ASP B 383 ARG B 394 1 12
SHEET 1 A 6 ALA A 149 PRO A 150 0
SHEET 2 A 6 SER A 125 VAL A 128 1 N VAL A 126 O ALA A 149
SHEET 3 A 6 ILE A 97 MET A 101 1 O ILE A 97 N SER A 125
SHEET 4 A 6 LEU A 48 GLY A 51 1 O LEU A 48 N GLY A 98
SHEET 5 A 6 ALA A 18 THR A 24 1 O PRO A 21 N GLU A 49
SHEET 6 A 6 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20
SHEET 1 B 3 ILE A 153 CYS A 154 0
SHEET 2 B 3 THR A 174 LEU A 177 1 O TYR A 175 N CYS A 154
SHEET 3 B 3 ALA A 208 GLY A 211 1 O LEU A 209 N LEU A 176
SHEET 1 C 2 TYR B 8 PHE B 9 0
SHEET 2 C 2 PHE B 12 GLY B 13 -1 O PHE B 12 N PHE B 9
SHEET 1 D 6 LEU B 59 LYS B 61 0
SHEET 2 D 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 D 6 GLN B 370 LEU B 376 1 O GLN B 370 N THR B 72
SHEET 4 D 6 ALA B 226 CYS B 230 1 O ALA B 226 N VAL B 373
SHEET 5 D 6 GLY B 251 GLY B 259 1 O GLY B 251 N VAL B 227
SHEET 6 D 6 ASP B 323 THR B 328 1 N ASP B 323 O LEU B 252
SHEET 1 E 4 GLU B 155 VAL B 159 0
SHEET 2 E 4 LYS B 129 GLY B 135 1 O CYS B 130 N GLU B 155
SHEET 3 E 4 GLU B 105 GLU B 109 1 N ILE B 106 O LYS B 129
SHEET 4 E 4 ALA B 184 TYR B 186 1 O HIS B 185 N ILE B 107
SHEET 1 F 2 ARG B 275 TYR B 279 0
SHEET 2 F 2 MET B 282 MET B 286 -1 N MET B 282 O TYR B 279
LINK NZ LYS B 87 C4A PLP B 401 1555 1555 1.46
LINK NA NA B 400 O PHE B 306 1555 1555 2.51
LINK NA NA B 400 O HOH B 419 1555 1555 2.51
LINK NA NA B 400 O SER B 308 1555 1555 2.52
LINK NA NA B 400 O HOH B 405 1555 1555 2.57
LINK NA NA B 400 O GLY B 232 1555 1555 2.45
CISPEP 1 ASP A 27 PRO A 28 0 -0.97
CISPEP 2 ARG B 55 PRO B 56 0 -3.09
CISPEP 3 HIS B 195 PRO B 196 0 5.93
SITE 1 AC1 5 GLY B 232 PHE B 306 SER B 308 HOH B 405
SITE 2 AC1 5 HOH B 419
SITE 1 AC2 11 PHE A 22 ASP A 60 ILE A 153 TYR A 175
SITE 2 AC2 11 THR A 183 GLY A 184 PHE A 212 GLY A 213
SITE 3 AC2 11 GLY A 234 SER A 235 HOH A 297
SITE 1 AC3 15 ALA B 85 HIS B 86 LYS B 87 GLN B 114
SITE 2 AC3 15 THR B 190 CYS B 230 GLY B 232 GLY B 233
SITE 3 AC3 15 GLY B 234 SER B 235 ASN B 236 GLY B 303
SITE 4 AC3 15 GLU B 350 SER B 377 GLY B 378
CRYST1 184.000 60.700 67.400 90.00 95.75 90.00 C 1 2 1 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 0.005435 0.000000 0.000547 0.00000
SCALE2 0.000000 0.016474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014912 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
