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PDBsum entry 1a5a

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1a5a
Jmol
Contents
Protein chains
255 a.a. *
389 a.a. *
Ligands
PLP
Metals
__K
Waters ×394
* Residue conservation analysis
HEADER    LYASE                                   12-FEB-98   1A5A
TITLE     CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL PHOSPHATE,
TITLE    2 BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE ALPHA2BETA2 COMPLEX
TITLE    3 REVEALS THE CORRECT ORIENTATION OF ACTIVE SITE ALPHA GLU 49
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 MUTATION: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: TRYPTOPHAN SYNTHASE (BETA CHAIN);
COMPND   9 CHAIN: B;
COMPND  10 EC: 4.2.1.20;
COMPND  11 ENGINEERED: 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_CELL_LINE: CB149;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PSTB7;
SOURCE  10 EXPRESSION_SYSTEM_GENE: TRPA/TRPB;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE  13 ORGANISM_TAXID: 602;
SOURCE  14 CELL_LINE: CB149;
SOURCE  15 GENE: TRPA/TRPB;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: CB149;
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PSTB7;
SOURCE  20 EXPRESSION_SYSTEM_GENE: TRPA/TRPB
KEYWDS    CARBON-OXYGEN LYASE, MUTATION AT POSITION 60 (ASP --> ASN) IN THE A-
KEYWDS   2 SUBUNIT, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.RHEE,E.W.MILES,D.R.DAVIES
REVDAT   3   13-JUL-11 1A5A    1       VERSN
REVDAT   2   24-FEB-09 1A5A    1       VERSN
REVDAT   1   27-MAY-98 1A5A    0
JRNL        AUTH   S.RHEE,E.W.MILES,D.R.DAVIES
JRNL        TITL   CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE, INDOLE-3-GLYCEROL
JRNL        TITL 2 PHOSPHATE, BOUND TO A MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE
JRNL        TITL 3 ALPHA2BETA2 COMPLEX REVEALS THE CORRECT ORIENTATION OF
JRNL        TITL 4 ACTIVE SITE ALPHAGLU49.
JRNL        REF    J.BIOL.CHEM.                  V. 273  8553 1998
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   9535826
JRNL        DOI    10.1074/JBC.273.15.8553
REMARK   2
REMARK   2 RESOLUTION.    1.90 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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 77.7
REMARK   3   NUMBER OF REFLECTIONS             : 43791
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION  : X-PLOR SCRIPT
REMARK   3   R VALUE            (WORKING SET) : 0.238
REMARK   3   FREE R VALUE                     : 0.298
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2650
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320
REMARK   3   BIN FREE R VALUE                    : 0.3880
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.00
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            : 4879
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 394
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.60
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.61
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.42
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  : PARAMCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1A5A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : FEB-96
REMARK 200  TEMPERATURE           (KELVIN) : 95
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRROR
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          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49520
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05900
REMARK 200   FOR THE DATA SET  : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.27000
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS
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   (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM NABICINE (PH 7.8), 1MM NA-EDTA,
REMARK 280  0.8-1.5MM SPERMINE, 12% PEG8000
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       91.75000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.70000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       91.75000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.70000
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      183.50000
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     LEU A   177
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     LEU 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   K      K B   500     O    HOH B   770              0.00
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    LYS B  87   CB    LYS B  87   CG      0.166
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      -59.37    -19.39
REMARK 500    PRO A  57       84.72    -56.28
REMARK 500    ASN A 157       33.15    -95.12
REMARK 500    GLN B 142       41.70   -108.33
REMARK 500    ALA B 242      -57.51    -29.87
REMARK 500    SER B 299      146.72   -171.60
REMARK 500    ASP B 305       51.92    -94.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR B 298         0.06    SIDE CHAIN
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 B 739        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH B 767        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH B 802        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH B 819        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH B 830        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH B 843        DISTANCE =  5.28 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                               K B 500   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 306   O
REMARK 620 2 GLY B 232   O   119.8
REMARK 620 3 HOH B 670   O   153.9  85.5
REMARK 620 4 SER B 308   O    77.3  85.3 100.7
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PLP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: COENZYME PLP BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 501
DBREF  1A5A A    1   268  UNP    P00929   TRPA_SALTY       1    268
DBREF  1A5A B    2   397  UNP    P0A2K1   TRPB_SALTY       1    396
SEQADV 1A5A ASN A   60  UNP  P00929    ASP    60 ENGINEERED
SEQADV 1A5A LEU B  396  UNP  P0A2K1    GLU   395 CONFLICT
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 ASN 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 LEU ILE
HET      K  B 500       1
HET    PLP  B 501      15
HETNAM       K POTASSIUM ION
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN     PLP VITAMIN B6 PHOSPHATE
FORMUL   3    K    K 1+
FORMUL   4  PLP    C8 H10 N O6 P
FORMUL   5  HOH   *394(H2 O)
HELIX    1   1 GLU A    2  ASP A   13  1                                  12
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  PHE A  107  1                                   5
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  GLU A  202  1                                  10
HELIX   11  11 PRO A  217  ALA A  226  1                                  10
HELIX   12  12 SER A  235  ALA A  246  1                                  12
HELIX   13  13 PRO A  248  SER A  266  1                                  19
HELIX   14  14 GLN B   19  LYS B   37  1                                  19
HELIX   15  15 PRO B   39  ASN B   51  1                                  13
HELIX   16  16 GLN B   63  THR B   66  1                                   4
HELIX   17  17 GLU B   78  LEU B   80  5                                   3
HELIX   18  18 ASN B   89  ARG B  100  1                                  12
HELIX   19  19 GLN B  114  LEU B  125  1                                  12
HELIX   20  20 ALA B  136  VAL B  139  1                                   4
HELIX   21  21 SER B  143  LEU B  151  1                                   9
HELIX   22  22 LEU B  166  SER B  180  1                                  15
HELIX   23  23 TYR B  197  GLU B  203  1                                   7
HELIX   24  24 MET B  207  LYS B  219  1                                  13
HELIX   25  25 SER B  235  PHE B  244  1                                  10
HELIX   26  26 ILE B  262  THR B  264  5                                   3
HELIX   27  27 PRO B  270  HIS B  273  1                                   4
HELIX   28  28 ALA B  302  LEU B  304  5                                   3
HELIX   29  29 PRO B  311  SER B  318  1                                   8
HELIX   30  30 ASP B  329  GLU B  343  1                                  15
HELIX   31  31 SER B  351  ARG B  363  1                                  13
HELIX   32  32 ASP B  381  ASP B  383  5                                   3
HELIX   33  33 THR B  386  ASP B  389  1                                   4
SHEET    1   A 5 GLY A 230  SER A 233  0
SHEET    2   A 5 ALA A  18  THR A  24  1  N  ALA A  18   O  ALA A 231
SHEET    3   A 5 ALA A  47  GLY A  51  1  N  ALA A  47   O  PRO A  21
SHEET    4   A 5 PRO A  96  MET A 101  1  N  PRO A  96   O  LEU A  48
SHEET    5   A 5 SER A 125  VAL A 128  1  N  SER A 125   O  LEU A  99
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 6 LEU B  59  LYS B  61  0
SHEET    2   C 6 THR B  71  ARG B  77 -1  N  LEU B  75   O  THR B  60
SHEET    3   C 6 GLN B 370  LEU B 376  1  N  GLN B 370   O  THR B  72
SHEET    4   C 6 ALA B 226  CYS B 230  1  N  ALA B 226   O  VAL B 373
SHEET    5   C 6 GLY B 251  GLY B 259  1  N  GLY B 251   O  VAL B 227
SHEET    6   C 6 ALA B 322  THR B 328  1  N  ASP B 323   O  LEU B 252
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 2 ARG B 275  TYR B 279  0
SHEET    2   E 2 MET B 282  MET B 286 -1  N  MET B 286   O  ARG B 275
LINK         C4A PLP B 501                 NZ  LYS B  87     1555   1555  1.34
LINK         K     K B 500                 O   PHE B 306     1555   1555  2.65
LINK         K     K B 500                 O   GLY B 232     1555   1555  2.51
LINK         K     K B 500                 O   HOH B 670     1555   1555  2.66
LINK         K     K B 500                 O   SER B 308     1555   1555  2.71
CISPEP   1 ASP A   27    PRO A   28          0         1.33
CISPEP   2 ARG B   55    PRO B   56          0         0.04
CISPEP   3 HIS B  195    PRO B  196          0         1.62
SITE     1 PLP  1 PLP B 501
SITE     1 AC1  4 GLY B 232  PHE B 306  SER B 308  HOH B 670
SITE     1 AC2 16 HIS B  86  LYS B  87  GLN B 114  THR B 190
SITE     2 AC2 16 CYS B 230  GLY B 232  GLY B 233  GLY B 234
SITE     3 AC2 16 SER B 235  ASN B 236  GLY B 303  GLU B 350
SITE     4 AC2 16 SER B 377  GLY B 378  HOH B 598  HOH B 833
CRYST1  183.500   59.400   67.300  90.00  94.60  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      0.005450  0.000000  0.000438        0.00000
SCALE2      0.000000  0.016835  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014907        0.00000
      
PROCHECK
Go to PROCHECK summary
 References