HEADER LYASE 26-OCT-01 1K8Z
TITLE CRYSTAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE BETA-SER178PRO MUTANT
TITLE 2 COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID
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 GENE: TRPA/TRPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CB149;
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 GENE: TRPA/TRPB;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PSTB7
KEYWDS CARBON-OXYGEN LYASE, TRYPTOPHAN BIOSYNTHESIS, PYRIDOXAL PHOSPHATE,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WEYAND,I.SCHLICHTING,A.MARABOTTI,A.MOZZARELLI
REVDAT 6 16-AUG-23 1K8Z 1 REMARK
REVDAT 5 27-OCT-21 1K8Z 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1K8Z 1 VERSN
REVDAT 3 24-FEB-09 1K8Z 1 VERSN
REVDAT 2 01-APR-03 1K8Z 1 JRNL
REVDAT 1 19-JUN-02 1K8Z 0
JRNL AUTH M.WEYAND,I.SCHLICHTING,P.HERDE,A.MARABOTTI,A.MOZZARELLI
JRNL TITL CRYSTAL STRUCTURE OF THE BETA SER178--> PRO MUTANT OF
JRNL TITL 2 TRYPTOPHAN SYNTHASE. A "KNOCK-OUT" ALLOSTERIC ENZYME.
JRNL REF J.BIOL.CHEM. V. 277 10653 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11756454
JRNL DOI 10.1074/JBC.M111031200
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 75314
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 + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4063
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4925
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 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) : 0.086 ; 0.021
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : 0.167 ; 0.500
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.013 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.480 ; 0.200
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) : 0.172 ; 0.500
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) : 3.856 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.766 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.489 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.008 ; 4.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79408
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 2.597
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.35
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.110
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 1QOP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.80
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 92.21000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.51750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.21000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.51750
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 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 184.42000
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 179
REMARK 465 SER A 180
REMARK 465 GLY A 181
REMARK 465 VAL A 182
REMARK 465 THR A 183
REMARK 465 GLY A 184
REMARK 465 ALA A 185
REMARK 465 GLU A 186
REMARK 465 ASN A 187
REMARK 465 ARG A 188
REMARK 465 GLY A 189
REMARK 465 GLU B 396
REMARK 465 ILE B 397
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 O GLY B 54 O HOH B 735 2.06
REMARK 500 O HOH B 627 O HOH B 748 2.12
REMARK 500 O HOH B 702 O HOH B 738 2.13
REMARK 500 NH2 ARG B 222 O HOH B 736 2.13
REMARK 500 O HOH A 623 O HOH B 645 2.15
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 5 N GLU A 5 CA 0.157
REMARK 500 GLU A 5 CD GLU A 5 OE1 0.078
REMARK 500 GLU A 5 CD GLU A 5 OE2 0.071
REMARK 500 LEU A 7 CG LEU A 7 CD2 0.267
REMARK 500 PHE A 8 CE2 PHE A 8 CD2 0.154
REMARK 500 GLN A 10 N GLN A 10 CA -0.128
REMARK 500 LEU A 11 CA LEU A 11 CB 0.145
REMARK 500 ASP A 13 CB ASP A 13 CG 0.249
REMARK 500 GLU A 16 CD GLU A 16 OE1 0.083
REMARK 500 GLY A 17 N GLY A 17 CA 0.110
REMARK 500 ALA A 18 CA ALA A 18 C 0.162
REMARK 500 VAL A 20 CB VAL A 20 CG1 0.200
REMARK 500 PRO A 21 CA PRO A 21 CB -0.164
REMARK 500 PHE A 22 CD1 PHE A 22 CE1 0.125
REMARK 500 THR A 24 CA THR A 24 CB 0.217
REMARK 500 GLY A 29 CA GLY A 29 C 0.097
REMARK 500 GLU A 31 CG GLU A 31 CD 0.093
REMARK 500 GLU A 31 CD GLU A 31 OE2 0.113
REMARK 500 ILE A 37 CA ILE A 37 C 0.162
REMARK 500 ASP A 38 N ASP A 38 CA 0.140
REMARK 500 THR A 39 C THR A 39 O 0.128
REMARK 500 GLU A 49 CB GLU A 49 CG -0.118
REMARK 500 GLU A 49 CD GLU A 49 OE1 0.070
REMARK 500 GLY A 51 N GLY A 51 CA 0.119
REMARK 500 VAL A 52 CB VAL A 52 CG1 0.221
REMARK 500 VAL A 52 CA VAL A 52 C 0.201
REMARK 500 PRO A 53 CG PRO A 53 CD 0.207
REMARK 500 PHE A 54 CA PHE A 54 CB -0.160
REMARK 500 PHE A 54 CA PHE A 54 C 0.226
REMARK 500 SER A 55 N SER A 55 CA 0.131
REMARK 500 PRO A 62 CD PRO A 62 N 0.087
REMARK 500 GLN A 65 CG GLN A 65 CD 0.233
REMARK 500 ARG A 70 NE ARG A 70 CZ -0.089
REMARK 500 PHE A 72 CE1 PHE A 72 CZ 0.120
REMARK 500 ALA A 74 CA ALA A 74 CB 0.193
REMARK 500 PHE A 82 CD1 PHE A 82 CE1 -0.259
REMARK 500 PHE A 82 CE1 PHE A 82 CZ 0.135
REMARK 500 GLU A 83 CG GLU A 83 CD 0.123
REMARK 500 MET A 84 C MET A 84 O 0.151
REMARK 500 LEU A 85 CA LEU A 85 CB -0.139
REMARK 500 ALA A 86 CA ALA A 86 CB 0.146
REMARK 500 LEU A 87 CG LEU A 87 CD1 0.230
REMARK 500 HIS A 92 C HIS A 92 O 0.118
REMARK 500 THR A 94 CA THR A 94 CB 0.218
REMARK 500 ILE A 95 C ILE A 95 O 0.139
REMARK 500 PRO A 96 CA PRO A 96 CB -0.162
REMARK 500 ILE A 97 N ILE A 97 CA 0.193
REMARK 500 ILE A 97 C GLY A 98 N 0.183
REMARK 500 GLY A 98 CA GLY A 98 C 0.177
REMARK 500 MET A 101 CB MET A 101 CG 0.247
REMARK 500
REMARK 500 THIS ENTRY HAS 672 BOND DEVIATIONS.
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 ARG A 3 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR A 4 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 TYR A 4 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR A 4 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR A 4 CD1 - CE1 - CZ ANGL. DEV. = -7.5 DEGREES
REMARK 500 LEU A 7 CB - CG - CD1 ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU A 7 CB - CG - CD2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 LEU A 11 CA - CB - CG ANGL. DEV. = -18.0 DEGREES
REMARK 500 LEU A 11 CB - CG - CD2 ANGL. DEV. = 18.2 DEGREES
REMARK 500 ASP A 13 CB - CG - OD1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ALA A 18 N - CA - CB ANGL. DEV. = -9.7 DEGREES
REMARK 500 VAL A 20 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 VAL A 23 N - CA - CB ANGL. DEV. = 14.2 DEGREES
REMARK 500 THR A 24 CA - CB - CG2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ILE A 37 CG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ILE A 41 CG1 - CB - CG2 ANGL. DEV. = -17.6 DEGREES
REMARK 500 ASP A 46 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ALA A 47 N - CA - CB ANGL. DEV. = 15.2 DEGREES
REMARK 500 ALA A 47 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 LEU A 48 CA - C - O ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU A 48 CA - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU A 50 C - N - CA ANGL. DEV. = -16.2 DEGREES
REMARK 500 VAL A 52 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ASP A 56 CB - CG - OD2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 THR A 63 OG1 - CB - CG2 ANGL. DEV. = -15.4 DEGREES
REMARK 500 THR A 63 CA - CB - CG2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 VAL A 76 CA - CB - CG2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 GLN A 80 O - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 LYS A 91 CD - CE - NZ ANGL. DEV. = -15.5 DEGREES
REMARK 500 HIS A 92 O - C - N ANGL. DEV. = -11.9 DEGREES
REMARK 500 PRO A 93 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 PRO A 93 C - N - CD ANGL. DEV. = -15.4 DEGREES
REMARK 500 PRO A 93 N - CD - CG ANGL. DEV. = -10.3 DEGREES
REMARK 500 PRO A 96 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 96 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO A 96 O - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 ILE A 97 CA - C - O ANGL. DEV. = 13.2 DEGREES
REMARK 500 ILE A 97 O - C - N ANGL. DEV. = -15.7 DEGREES
REMARK 500 GLY A 98 O - C - N ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU A 100 CB - CG - CD1 ANGL. DEV. = -14.7 DEGREES
REMARK 500 LEU A 100 CB - CG - CD2 ANGL. DEV. = 20.0 DEGREES
REMARK 500 LEU A 100 O - C - N ANGL. DEV. = 11.7 DEGREES
REMARK 500 LEU A 105 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 PHE A 107 CB - CG - CD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 PHE A 107 CB - CG - CD1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 PHE A 107 CG - CD1 - CE1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 PHE A 107 CE1 - CZ - CE2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 PHE A 107 CZ - CE2 - CD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 PHE A 114 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 PHE A 114 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 553 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 LEU A 58 0.97 -60.87
REMARK 500 LEU A 191 101.91 88.21
REMARK 500 PHE A 212 118.02 82.61
REMARK 500 CYS B 62 67.40 -108.66
REMARK 500 VAL B 139 -71.02 -47.32
REMARK 500 THR B 165 -146.65 -119.31
REMARK 500 ALA B 191 49.82 -89.17
REMARK 500 SER B 308 -159.80 -134.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 267 ALA A 268 143.78
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 GLY B 54 -12.80
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 503 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 PHE B 306 O 115.0
REMARK 620 3 SER B 308 O 98.5 86.8
REMARK 620 4 HOH B 511 O 96.2 145.1 104.5
REMARK 620 5 HOH B 623 O 105.3 73.9 154.0 83.5
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 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IAG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K7X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN
REMARK 900 SYNTHASE
REMARK 900 RELATED ID: 1K8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE BETA-SER178PRO MUTANT
REMARK 900 COMPLEXED WITH D,L-ALPHA-GLYCEROL-3-PHOSPHATE
DBREF 1K8Z A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 1K8Z B 2 397 UNP P0A2K1 TRPB_SALTY 1 396
SEQADV 1K8Z SER B 34 UNP P0A2K1 ARG 33 CLONING ARTIFACT
SEQADV 1K8Z PRO B 178 UNP P0A2K1 SER 177 ENGINEERED MUTATION
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 ALA CYS
SEQRES 14 B 396 ASN GLU ALA LEU ARG ASP TRP PRO 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 IAG A 501 17
HET NA B 503 1
HET PLP B 502 15
HETNAM IAG N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID
HETNAM NA SODIUM ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 IAG C12 H12 N2 O3
FORMUL 4 NA NA 1+
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *377(H2 O)
HELIX 1 1 MET A 1 ARG A 14 1 14
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 PRO A 192 TYR A 203 1 12
HELIX 11 11 SER A 216 ALA A 226 1 11
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 MET B 101 1 15
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 TRP B 177 1 13
HELIX 23 23 PRO B 178 SER B 180 5 3
HELIX 24 24 PRO B 196 PHE B 204 1 9
HELIX 25 25 ARG B 206 GLY B 221 1 16
HELIX 26 26 GLY B 234 ALA B 242 1 9
HELIX 27 27 ASP B 243 ILE B 245 5 3
HELIX 28 28 GLY B 261 GLY B 265 5 5
HELIX 29 29 ALA B 269 GLY B 274 1 6
HELIX 30 30 SER B 301 ASP B 305 5 5
HELIX 31 31 GLY B 310 ILE B 319 1 10
HELIX 32 32 ASP B 329 GLY B 344 1 16
HELIX 33 33 ALA B 348 GLN B 365 1 18
HELIX 34 34 GLY B 380 LYS B 382 5 3
HELIX 35 35 ASP B 383 GLY B 395 1 13
SHEET 1 A 9 ALA A 149 PRO A 150 0
SHEET 2 A 9 SER A 125 VAL A 128 1 N VAL A 126 O ALA A 149
SHEET 3 A 9 ILE A 97 MET A 101 1 N LEU A 99 O LEU A 127
SHEET 4 A 9 LEU A 48 GLY A 51 1 N LEU A 50 O GLY A 98
SHEET 5 A 9 ALA A 18 THR A 24 1 N VAL A 23 O GLY A 51
SHEET 6 A 9 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20
SHEET 7 A 9 ALA A 208 GLY A 211 1 N GLN A 210 O ILE A 232
SHEET 8 A 9 THR A 174 LEU A 177 1 N LEU A 176 O LEU A 209
SHEET 9 A 9 ILE A 153 CYS A 154 1 N CYS A 154 O TYR A 175
SHEET 1 B 4 TYR B 8 PHE B 9 0
SHEET 2 B 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9
SHEET 3 B 4 GLY B 281 MET B 286 -1 O LYS B 283 N GLY B 13
SHEET 4 B 4 ARG B 275 TYR B 279 -1 N ARG B 275 O MET B 286
SHEET 1 C 6 LEU B 59 LYS B 61 0
SHEET 2 C 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 C 6 GLN B 370 LEU B 376 1 O VAL B 374 N LYS B 76
SHEET 4 C 6 ALA B 226 CYS B 230 1 N ILE B 228 O VAL B 373
SHEET 5 C 6 GLY B 251 GLY B 259 1 O VAL B 255 N ALA B 229
SHEET 6 C 6 ASP B 323 THR B 328 1 O VAL B 325 N GLY B 254
SHEET 1 D 4 GLU B 155 VAL B 159 0
SHEET 2 D 4 LYS B 129 GLY B 135 1 N ILE B 132 O ILE B 157
SHEET 3 D 4 GLU B 105 THR B 110 1 N ALA B 108 O TYR B 133
SHEET 4 D 4 ALA B 184 MET B 187 1 O MET B 187 N ILE B 107
LINK NZ LYS B 87 C4A PLP B 502 1555 1555 1.58
LINK O GLY B 232 NA NA B 503 1555 1555 2.18
LINK O PHE B 306 NA NA B 503 1555 1555 2.56
LINK O SER B 308 NA NA B 503 1555 1555 2.29
LINK NA NA B 503 O HOH B 511 1555 1555 2.48
LINK NA NA B 503 O HOH B 623 1555 1555 2.29
CISPEP 1 ASP A 27 PRO A 28 0 1.97
CISPEP 2 ARG B 55 PRO B 56 0 -7.29
CISPEP 3 HIS B 195 PRO B 196 0 20.41
SITE 1 AC1 5 GLY B 232 PHE B 306 SER B 308 HOH B 511
SITE 2 AC1 5 HOH B 623
SITE 1 AC2 10 PHE A 22 GLU A 49 ASP A 60 ILE A 64
SITE 2 AC2 10 LEU A 100 TYR A 175 PHE A 212 GLY A 234
SITE 3 AC2 10 SER A 235 HOH A 545
SITE 1 AC3 16 HIS B 86 LYS B 87 GLN B 114 THR B 190
SITE 2 AC3 16 CYS B 230 GLY B 232 GLY B 233 GLY B 234
SITE 3 AC3 16 SER B 235 ASN B 236 GLY B 303 GLU B 350
SITE 4 AC3 16 SER B 377 GLY B 378 HOH B 520 HOH B 680
CRYST1 184.420 61.035 67.534 90.00 94.69 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 0.005422 0.000000 0.000445 0.00000
SCALE2 0.000000 0.016384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014857 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
