HEADER CARBON-OXYGEN LYASE 11-OCT-95 1TTP
TITLE TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF CESIUM, ROOM
TITLE 2 TEMPERATURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPTOPHAN SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.20;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: STRUCTURE IN THE PRESENCE OF CESIUM;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRYPTOPHAN SYNTHASE;
COMPND 9 CHAIN: B;
COMPND 10 EC: 4.2.1.20;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: STRUCTURE IN THE PRESENCE OF CESIUM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 STRAIN: TB2211;
SOURCE 5 GENE: TRPA/TRPB/TRPC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PSTH8;
SOURCE 9 EXPRESSION_SYSTEM_GENE: TRPA/TRPB/TRPC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 12 ORGANISM_TAXID: 602;
SOURCE 13 STRAIN: TB2211;
SOURCE 14 GENE: TRPA/TRPB/TRPC;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PSTH8;
SOURCE 18 EXPRESSION_SYSTEM_GENE: TRPA/TRPB/TRPC
KEYWDS CARBON-OXYGEN LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RHEE,K.PARRIS,S.AHMED,E.W.MILES,D.R.DAVIES
REVDAT 3 13-JUL-11 1TTP 1 VERSN
REVDAT 2 24-FEB-09 1TTP 1 VERSN
REVDAT 1 08-MAR-96 1TTP 0
JRNL AUTH S.RHEE,K.D.PARRIS,S.A.AHMED,E.W.MILES,D.R.DAVIES
JRNL TITL EXCHANGE OF K+ OR CS+ FOR NA+ INDUCES LOCAL AND LONG-RANGE
JRNL TITL 2 CHANGES IN THE THREE-DIMENSIONAL STRUCTURE OF THE TRYPTOPHAN
JRNL TITL 3 SYNTHASE ALPHA2BETA2 COMPLEX.
JRNL REF BIOCHEMISTRY V. 35 4211 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8672457
JRNL DOI 10.1021/BI952506D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.C.HYDE,E.W.MILES
REMARK 1 TITL THE TRYPTOPHAN SYNTHASE MULTIENZYME COMPLEX: EXPLORING
REMARK 1 TITL 2 STRUCTURE-FUNCTION RELATIONSHIPS WITH X-RAY CRYSTALLOGRAPHY
REMARK 1 TITL 3 AND MUTAGENESIS
REMARK 1 REF BIO/TECHNOLOGY V. 8 27 1990
REMARK 1 REFN ISSN 0733-222X
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.C.HYDE,S.A.AHMED,E.A.PADLAN,E.W.MILES,D.R.DAVIES
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE
REMARK 1 TITL 2 ALPHA2BETA2 MULTIENZYME COMPLEX FROM SALMONELLA TYPHIMURIUM
REMARK 1 REF J.BIOL.CHEM. V. 263 17857 1988
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.A.AHMED,E.W.MILES,D.R.DAVIES
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC DATA
REMARK 1 TITL 2 OF THE TRYPTOPHAN SYNTHASE ALPHA2BETA2 COMPLEX FROM
REMARK 1 TITL 3 SALMONELLA TYPHIMURIUM
REMARK 1 REF J.BIOL.CHEM. V. 260 3716 1985
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 67.2
REMARK 3 NUMBER OF REFLECTIONS : 22351
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.700
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4887
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 2.86
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.58
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TTP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-DEC-94
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25385
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.2
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.09900
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 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 92.65000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.65000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.65000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.65000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -243.0 KCAL/MOL
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 185.30000
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 SER A 178
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 MET B 1
REMARK 465 THR B 2
REMARK 465 LYS B 392
REMARK 465 ALA B 393
REMARK 465 ARG B 394
REMARK 465 GLY B 395
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 CA LEU A 176 N LEU A 177 1.79
REMARK 500
REMARK 500 REMARK: NULL
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 CS CS B 401 CS CS B 401 2655 1.88
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 LEU A 177 N LEU A 177 CA 0.578
REMARK 500 LEU A 177 CA LEU A 177 CB 0.592
REMARK 500 LEU A 177 CB LEU A 177 CG -0.280
REMARK 500 LEU A 177 CG LEU A 177 CD2 0.789
REMARK 500 LEU A 177 C LEU A 177 O -0.130
REMARK 500 ALA A 190 N ALA A 190 CA 1.217
REMARK 500 ALA A 190 CA ALA A 190 CB 0.306
REMARK 500 ALA A 190 C ALA A 190 O 0.815
REMARK 500 ALA A 190 C LEU A 191 N 0.290
REMARK 500 HIS B 86 NE2 HIS B 86 CD2 -0.069
REMARK 500 LYS B 87 CB LYS B 87 CG 0.180
REMARK 500 HIS B 185 NE2 HIS B 185 CD2 -0.078
REMARK 500 HIS B 313 NE2 HIS B 313 CD2 -0.068
REMARK 500 HIS B 342 NE2 HIS B 342 CD2 -0.075
REMARK 500 HIS B 357 NE2 HIS B 357 CD2 -0.067
REMARK 500 HIS B 388 NE2 HIS B 388 CD2 -0.068
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. = 3.9 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 TYR A 169 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LEU A 177 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 LEU A 177 CA - CB - CG ANGL. DEV. = -43.5 DEGREES
REMARK 500 LEU A 177 CD1 - CG - CD2 ANGL. DEV. = -50.1 DEGREES
REMARK 500 LEU A 177 CB - CG - CD1 ANGL. DEV. = -13.9 DEGREES
REMARK 500 LEU A 177 CB - CG - CD2 ANGL. DEV. = 37.7 DEGREES
REMARK 500 LEU A 177 CA - C - O ANGL. DEV. = -21.9 DEGREES
REMARK 500 LEU A 176 CA - C - N ANGL. DEV. = -36.4 DEGREES
REMARK 500 LEU A 176 O - C - N ANGL. DEV. = 31.0 DEGREES
REMARK 500 LEU A 177 C - N - CA ANGL. DEV. = -46.4 DEGREES
REMARK 500 ALA A 190 CB - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ALA A 190 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 ALA A 190 N - CA - C ANGL. DEV. = 29.3 DEGREES
REMARK 500 ALA A 190 CA - C - O ANGL. DEV. = -22.5 DEGREES
REMARK 500 ALA A 190 CA - C - N ANGL. DEV. = 23.8 DEGREES
REMARK 500 ALA A 190 O - C - N ANGL. DEV. = -17.9 DEGREES
REMARK 500 LEU A 191 C - N - CA ANGL. DEV. = 19.2 DEGREES
REMARK 500 LEU A 245 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 THR B 3 CA - CB - CG2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 34 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 LEU B 80 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 VAL B 91 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG B 150 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TRP B 177 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TRP B 177 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 222 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 222 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR B 279 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR B 279 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TYR B 315 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 379 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 379 NE - CZ - NH2 ANGL. DEV. = -4.2 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 SER A 55 -87.71 -52.04
REMARK 500 ASN A 157 39.18 -77.87
REMARK 500 LEU A 191 109.78 81.74
REMARK 500 HIS A 204 32.22 75.20
REMARK 500 PRO A 207 107.79 -27.15
REMARK 500 SER A 215 -9.65 -146.95
REMARK 500 LEU A 245 -56.41 -21.11
REMARK 500 ALA A 265 17.86 -69.17
REMARK 500 ARG A 267 45.67 -91.31
REMARK 500 TYR B 16 73.94 -104.23
REMARK 500 ALA B 85 122.25 176.75
REMARK 500 HIS B 86 -17.52 -42.80
REMARK 500 HIS B 160 59.48 -173.05
REMARK 500 TYR B 181 -8.44 -55.77
REMARK 500 ALA B 229 128.52 179.30
REMARK 500 ALA B 242 -53.87 -24.13
REMARK 500 GLU B 263 5.06 -65.44
REMARK 500 ALA B 269 51.28 -119.38
REMARK 500 SER B 297 -145.65 -80.44
REMARK 500 TYR B 298 146.59 -177.81
REMARK 500 SER B 308 -158.47 -155.12
REMARK 500 PRO B 311 -49.76 -21.01
REMARK 500 PRO B 366 -17.20 -48.05
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 SER A 247 PRO A 248 -149.96
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 MET A 1 -13.21
REMARK 500 ALA A 190 44.02
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 CS B 400 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 306 O
REMARK 620 2 SER B 308 O 66.9
REMARK 620 3 VAL B 231 O 148.8 116.2
REMARK 620 4 GLY B 268 O 101.2 132.5 97.4
REMARK 620 5 GLY B 232 O 95.3 74.5 59.0 152.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS B 401 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 56 O
REMARK 620 2 GLY B 54 O 60.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: COF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 402
DBREF 1TTP A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 1TTP B 2 397 UNP P00933 TRPB_SALTY 1 396
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 397 MET THR THR LEU LEU ASN PRO TYR PHE GLY GLU PHE GLY
SEQRES 2 B 397 GLY MET TYR VAL PRO GLN ILE LEU MET PRO ALA LEU ASN
SEQRES 3 B 397 GLN LEU GLU GLU ALA PHE VAL ARG ALA GLN LYS ASP PRO
SEQRES 4 B 397 GLU PHE GLN ALA GLN PHE ALA ASP LEU LEU LYS ASN TYR
SEQRES 5 B 397 ALA GLY ARG PRO THR ALA LEU THR LYS CYS GLN ASN ILE
SEQRES 6 B 397 THR ALA GLY THR ARG THR THR LEU TYR LEU LYS ARG GLU
SEQRES 7 B 397 ASP LEU LEU HIS GLY GLY ALA HIS LYS THR ASN GLN VAL
SEQRES 8 B 397 LEU GLY GLN ALA LEU LEU ALA LYS ARG MET GLY LYS SER
SEQRES 9 B 397 GLU ILE ILE ALA GLU THR GLY ALA GLY GLN HIS GLY VAL
SEQRES 10 B 397 ALA SER ALA LEU ALA SER ALA LEU LEU GLY LEU LYS CYS
SEQRES 11 B 397 ARG ILE TYR MET GLY ALA LYS ASP VAL GLU ARG GLN SER
SEQRES 12 B 397 PRO ASN VAL PHE ARG MET ARG LEU MET GLY ALA GLU VAL
SEQRES 13 B 397 ILE PRO VAL HIS SER GLY SER ALA THR LEU LYS ASP ALA
SEQRES 14 B 397 CYS ASN GLU ALA LEU ARG ASP TRP SER GLY SER TYR GLU
SEQRES 15 B 397 THR ALA HIS TYR MET LEU GLY THR ALA ALA GLY PRO HIS
SEQRES 16 B 397 PRO TYR PRO THR ILE VAL ARG GLU PHE GLN ARG MET ILE
SEQRES 17 B 397 GLY GLU GLU THR LYS ALA GLN ILE LEU ASP LYS GLU GLY
SEQRES 18 B 397 ARG LEU PRO ASP ALA VAL ILE ALA CYS VAL GLY GLY GLY
SEQRES 19 B 397 SER ASN ALA ILE GLY MET PHE ALA ASP PHE ILE ASN ASP
SEQRES 20 B 397 THR SER VAL GLY LEU ILE GLY VAL GLU PRO GLY GLY HIS
SEQRES 21 B 397 GLY ILE GLU THR GLY GLU HIS GLY ALA PRO LEU LYS HIS
SEQRES 22 B 397 GLY ARG VAL GLY ILE TYR PHE GLY MET LYS ALA PRO MET
SEQRES 23 B 397 MET GLN THR ALA ASP GLY GLN ILE GLU GLU SER TYR SER
SEQRES 24 B 397 ILE SER ALA GLY LEU ASP PHE PRO SER VAL GLY PRO GLN
SEQRES 25 B 397 HIS ALA TYR LEU ASN SER ILE GLY ARG ALA ASP TYR VAL
SEQRES 26 B 397 SER ILE THR ASP ASP GLU ALA LEU GLU ALA PHE LYS THR
SEQRES 27 B 397 LEU CYS ARG HIS GLU GLY ILE ILE PRO ALA LEU GLU SER
SEQRES 28 B 397 SER HIS ALA LEU ALA HIS ALA LEU LYS MET MET ARG GLU
SEQRES 29 B 397 GLN PRO GLU LYS GLU GLN LEU LEU VAL VAL ASN LEU SER
SEQRES 30 B 397 GLY ARG GLY ASP LYS ASP ILE PHE THR VAL HIS ASP ILE
SEQRES 31 B 397 LEU LYS ALA ARG GLY GLU ILE
HET CS B 400 1
HET CS B 401 1
HET PLP B 402 15
HETNAM CS CESIUM ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 CS 2(CS 1+)
FORMUL 5 PLP C8 H10 N O6 P
FORMUL 6 HOH *14(H2 O)
HELIX 1 1 GLU A 2 ARG A 14 5 13
HELIX 2 2 ILE A 30 ALA A 43 1 14
HELIX 3 3 PRO A 62 ALA A 73 1 12
HELIX 4 4 PRO A 78 LYS A 91 1 14
HELIX 5 5 ALA A 103 ASN A 109 1 7
HELIX 6 6 ILE A 111 VAL A 121 1 11
HELIX 7 7 VAL A 133 GLU A 135 5 3
HELIX 8 8 ALA A 137 ARG A 145 1 9
HELIX 9 9 ASP A 160 TYR A 169 1 10
HELIX 10 10 LEU A 193 TYR A 203 1 11
HELIX 11 11 PRO A 217 ALA A 226 1 10
HELIX 12 12 SER A 235 LYS A 243 1 9
HELIX 13 13 PRO A 248 SER A 266 1 19
HELIX 14 14 GLN B 19 LYS B 37 5 19
HELIX 15 15 PRO B 39 ASN B 51 1 13
HELIX 16 16 GLU B 78 LEU B 80 5 3
HELIX 17 17 HIS B 86 MET B 101 5 16
HELIX 18 18 GLN B 114 LEU B 126 1 13
HELIX 19 19 ALA B 136 ARG B 141 1 6
HELIX 20 20 SER B 143 LEU B 151 1 9
HELIX 21 21 LEU B 166 SER B 180 1 15
HELIX 22 22 TYR B 197 GLU B 203 1 7
HELIX 23 23 ARG B 206 LYS B 219 1 14
HELIX 24 24 SER B 235 ASP B 243 1 9
HELIX 25 25 ILE B 262 THR B 264 5 3
HELIX 26 26 PRO B 270 HIS B 273 1 4
HELIX 27 27 ALA B 302 LEU B 304 5 3
HELIX 28 28 PRO B 311 SER B 318 1 8
HELIX 29 29 ASP B 329 GLU B 343 1 15
HELIX 30 30 LEU B 349 GLU B 364 1 16
HELIX 31 31 ASP B 381 ASP B 389 5 9
SHEET 1 A 6 GLY A 230 SER A 233 0
SHEET 2 A 6 ALA A 18 THR A 24 1 N ALA A 18 O ALA A 231
SHEET 3 A 6 ALA A 47 GLY A 51 1 N ALA A 47 O PRO A 21
SHEET 4 A 6 PRO A 96 MET A 101 1 N PRO A 96 O LEU A 48
SHEET 5 A 6 SER A 125 VAL A 128 1 N SER A 125 O LEU A 99
SHEET 6 A 6 ALA A 149 ILE A 151 1 N ALA A 149 O VAL A 126
SHEET 1 B 2 THR A 174 LEU A 176 0
SHEET 2 B 2 ALA A 208 GLN A 210 1 N LEU A 209 O THR A 174
SHEET 1 C 3 LEU B 59 LYS B 61 0
SHEET 2 C 3 THR B 71 ARG B 77 -1 N LEU B 75 O THR B 60
SHEET 3 C 3 GLN B 370 LEU B 376 1 N GLN B 370 O THR B 72
SHEET 1 D 4 ALA B 184 TYR B 186 0
SHEET 2 D 4 GLU B 105 THR B 110 1 N GLU B 105 O HIS B 185
SHEET 3 D 4 LYS B 129 GLY B 135 1 N LYS B 129 O ILE B 106
SHEET 4 D 4 GLU B 155 VAL B 159 1 N GLU B 155 O ILE B 132
SHEET 1 E 3 ALA B 226 CYS B 230 0
SHEET 2 E 3 GLY B 251 GLY B 259 1 N GLY B 251 O VAL B 227
SHEET 3 E 3 ASP B 323 THR B 328 1 N ASP B 323 O GLY B 254
SHEET 1 F 2 VAL B 276 TYR B 279 0
SHEET 2 F 2 MET B 282 PRO B 285 -1 N ALA B 284 O GLY B 277
LINK NZ LYS B 87 C4A PLP B 402 1555 1555 1.38
LINK CS CS B 400 O PHE B 306 1555 1555 3.26
LINK CS CS B 400 O SER B 308 1555 1555 3.44
LINK CS CS B 400 O VAL B 231 1555 1555 3.43
LINK CS CS B 400 O GLY B 268 1555 1555 3.38
LINK CS CS B 400 O GLY B 232 1555 1555 2.87
LINK CS CS B 401 O PRO B 56 1555 1555 3.59
LINK CS CS B 401 O GLY B 54 1555 1555 3.26
CISPEP 1 ASP A 27 PRO A 28 0 -25.85
CISPEP 2 ARG B 55 PRO B 56 0 7.73
CISPEP 3 HIS B 195 PRO B 196 0 13.71
SITE 1 COF 1 LYS B 87
SITE 1 AC1 6 VAL B 231 GLY B 232 GLY B 268 PRO B 270
SITE 2 AC1 6 PHE B 306 SER B 308
SITE 1 AC2 2 GLY B 54 PRO B 56
SITE 1 AC3 11 HIS B 86 LYS B 87 THR B 190 CYS B 230
SITE 2 AC3 11 GLY B 232 GLY B 234 SER B 235 ASN B 236
SITE 3 AC3 11 GLY B 303 SER B 377 GLY B 378
CRYST1 185.300 61.300 68.100 90.00 94.80 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 0.005397 0.000000 0.000453 0.00000
SCALE2 0.000000 0.016313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
