HEADER LYASE 04-OCT-01 1K3U
TITLE CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-
TITLE 2 [1H-INDOL-3-YL-ACETYL]ASPARTIC 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
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 4 13-JUL-11 1K3U 1 VERSN
REVDAT 3 24-FEB-09 1K3U 1 VERSN
REVDAT 2 01-APR-03 1K3U 1 JRNL
REVDAT 1 03-JUL-02 1K3U 0
JRNL AUTH M.WEYAND,I.SCHLICHTING,A.MARABOTTI,A.MOZZARELLI
JRNL TITL CRYSTAL STRUCTURES OF A NEW CLASS OF ALLOSTERIC EFFECTORS
JRNL TITL 2 COMPLEXED TO TRYPTOPHAN SYNTHASE.
JRNL REF J.BIOL.CHEM. V. 277 10647 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11756456
JRNL DOI 10.1074/JBC.M111285200
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
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 (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 73596
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3938
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.20
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 712
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73000
REMARK 3 B22 (A**2) : 1.21000
REMARK 3 B33 (A**2) : -0.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.910
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.029 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 2.293 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 5.292 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;17.513 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; 0.147 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; 0.235 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; 1.304 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 2.079 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 3.369 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 5.336 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: GLU 11 B EXISTS IN TWO CONFORMATIONS,
REMARK 3 EACH WITH 50% OCCUPANCY. WITH CONFORMATION A, HOH 709 EXISTS.
REMARK 3 WITH CONFORMATION B, HOH 710 EXISTS.
REMARK 4
REMARK 4 1K3U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-01.
REMARK 100 THE RCSB ID CODE IS RCSB014526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.842
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : PREMIRROR, BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77570
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.050
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
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 (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.12300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 1QOP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 7.8, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 91.20450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.85900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.20450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.85900
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 182.40900
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 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 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 939 O HOH B 1239 1565 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 PHE A 82 CE2 PHE A 82 CD2 0.131
REMARK 500 TYR B 52 CE2 TYR B 52 CD2 0.106
REMARK 500 SER B 143 CA SER B 143 CB 0.091
REMARK 500 MET B 152 SD MET B 152 CE -0.407
REMARK 500 ARG B 206 CG ARG B 206 CD 0.164
REMARK 500 GLU B 210 CD GLU B 210 OE2 0.067
REMARK 500 ASP B 291 CB ASP B 291 CG -0.226
REMARK 500 TYR B 298 CE1 TYR B 298 CZ 0.097
REMARK 500 GLU B 364 CD GLU B 364 OE1 -0.069
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 42 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 42 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 PRO A 93 N - CD - CG ANGL. DEV. = -10.6 DEGREES
REMARK 500 ASP A 130 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 159 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 225 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 38 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 131 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 150 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 206 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP B 225 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 275 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 MET B 286 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 ASP B 291 CB - CG - OD1 ANGL. DEV. = -11.7 DEGREES
REMARK 500 ASP B 381 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 394 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 PHE A 212 116.35 98.70
REMARK 500 CYS B 62 73.05 -112.15
REMARK 500 THR B 165 -153.31 -133.35
REMARK 500 ALA B 269 66.05 -118.54
REMARK 500 LEU B 304 40.80 -100.40
REMARK 500 SER B 308 -152.23 -142.35
REMARK 500 ALA B 393 -8.83 -53.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1048 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH B 884 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B 932 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B 953 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B1016 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH B1030 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B1128 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH B1133 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH B1162 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH B1175 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH B1176 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B1219 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1254 DISTANCE = 6.48 ANGSTROMS
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 803 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 308 O
REMARK 620 2 HOH B 828 O 101.5
REMARK 620 3 PHE B 306 O 87.3 164.0
REMARK 620 4 HOH B 870 O 149.0 91.2 74.9
REMARK 620 5 GLY B 232 O 96.6 89.2 103.2 111.9
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 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IAD A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE
REMARK 900 COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]GLYCINE ACID
REMARK 900 RELATED ID: 1K7F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE
REMARK 900 COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]VALINE ACID
DBREF 1K3U A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 1K3U B 2 397 UNP P0A2K1 TRPB_SALTY 1 396
SEQADV 1K3U SER B 34 UNP P0A2K1 ARG 33 CLONING ARTIFACT
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 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 803 1
HET IAD A 801 21
HET PLP B 802 15
HETNAM NA SODIUM ION
HETNAM IAD N-[1H-INDOL-3-YL-ACETYL]ASPARTIC ACID
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 NA NA 1+
FORMUL 4 IAD C14 H14 N2 O5
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *712(H2 O)
HELIX 1 1 GLU A 2 ARG A 14 1 13
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 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 CYS B 62 ALA B 67 1 6
HELIX 18 18 ASP B 79 LEU B 81 5 3
HELIX 19 19 LYS B 87 MET B 101 1 15
HELIX 20 20 GLY B 113 GLY B 127 1 15
HELIX 21 21 ALA B 136 GLN B 142 1 7
HELIX 22 22 GLN B 142 MET B 152 1 11
HELIX 23 23 THR B 165 TYR B 181 1 17
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 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 ALA B 393 1 11
SHEET 1 A 9 ALA A 149 ILE A 151 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 MET A 101 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 GLY B 277 O ALA B 284
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 LEU B 372 N THR B 72
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 ILE B 253 N VAL B 227
SHEET 6 C 6 ASP B 323 THR B 328 1 O VAL B 325 N GLU B 256
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 TYR B 186 1 O HIS B 185 N GLU B 105
LINK NZ LYS B 87 C4A PLP B 802 1555 1555 1.49
LINK NA NA B 803 O SER B 308 1555 1555 2.32
LINK NA NA B 803 O HOH B 828 1555 1555 2.37
LINK NA NA B 803 O PHE B 306 1555 1555 2.49
LINK NA NA B 803 O HOH B 870 1555 1555 2.43
LINK NA NA B 803 O GLY B 232 1555 1555 2.26
CISPEP 1 ASP A 27 PRO A 28 0 0.75
CISPEP 2 ARG B 55 PRO B 56 0 -0.96
CISPEP 3 HIS B 195 PRO B 196 0 8.36
SITE 1 AC1 5 GLY B 232 PHE B 306 SER B 308 HOH B 828
SITE 2 AC1 5 HOH B 870
SITE 1 AC2 16 PHE A 22 ASP A 60 ILE A 64 LEU A 100
SITE 2 AC2 16 TYR A 175 THR A 183 GLY A 184 GLY A 211
SITE 3 AC2 16 PHE A 212 GLY A 213 ILE A 214 ILE A 232
SITE 4 AC2 16 SER A 233 GLY A 234 SER A 235 HOH A 857
SITE 1 AC3 17 ALA B 85 HIS B 86 LYS B 87 THR B 190
SITE 2 AC3 17 CYS B 230 GLY B 232 GLY B 233 GLY B 234
SITE 3 AC3 17 SER B 235 ASN B 236 GLY B 303 GLU B 350
SITE 4 AC3 17 SER B 377 GLY B 378 HOH B 804 HOH B 816
SITE 5 AC3 17 HOH B 848
CRYST1 182.409 59.718 67.177 90.00 94.52 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 0.005482 0.000000 0.000433 0.00000
SCALE2 0.000000 0.016745 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
