HEADER LYASE 28-APR-06 2CLO
TITLE TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX
TITLE 2 WITH (NAPHTHALENE-2'-SULFONYL)-2-AMINO-1-ETHYLPHOSPHATE
TITLE 3 (F19)
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PSTB7;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 10 ORGANISM_TAXID: 602;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: CB149;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PSTB7
KEYWDS LYASE, AROMATIC AMINO ACID BIOSYNTHESIS, CARBON-OXYGEN
KEYWDS 2 LYASE, AMINO-ACID BIOSYNTHESIS, TRYPTOPHAN BIOSYNTHESIS,
KEYWDS 3 ALLOSTERIC ENZYME, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NGO,N.KIMMICH,R.HARRIS,D.NIKS,L.BLUMENSTEIN,V.KULIK,
AUTHOR 2 T.R.BARENDS,I.SCHLICHTING,M.F.DUNN
REVDAT 5 24-FEB-09 2CLO 1 VERSN
REVDAT 4 13-MAY-08 2CLO 1 JRNL REMARK
REVDAT 3 09-OCT-07 2CLO 1 REMARK
REVDAT 2 03-JUL-07 2CLO 1 JRNL
REVDAT 1 12-JUN-07 2CLO 0
JRNL AUTH H.NGO,N.KIMMICH,R.HARRIS,D.NIKS,L.BLUMENSTEIN,
JRNL AUTH 2 V.KULIK,T.R.BARENDS,I.SCHLICHTING,M.F.DUNN
JRNL TITL ALLOSTERIC REGULATION OF SUBSTRATE CHANNELING IN
JRNL TITL 2 TRYPTOPHAN SYNTHASE: MODULATION OF THE L-SERINE
JRNL TITL 3 REACTION IN STAGE I OF THE BETA-REACTION BY ALPHA-
JRNL TITL 4 SITE LIGANDS.
JRNL REF BIOCHEMISTRY V. 46 7740 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17559232
JRNL DOI 10.1021/BI7003872
REMARK 2
REMARK 2 RESOLUTION. 1.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3276122.19
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 112621
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 SET) : 0.232
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5632
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 17479
REMARK 3 BIN R VALUE (WORKING SET) : 0.285
REMARK 3 BIN FREE R VALUE : 0.305
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 920
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4895
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.19
REMARK 3 B22 (A**2) : 6.09
REMARK 3 B33 (A**2) : -3.90
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.40
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.399049
REMARK 3 BSOL : 50.3918
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : TRPS_LIG.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : F19.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TRPS_LIG.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : F19.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2CLO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-06.
REMARK 100 THE PDBE ID CODE IS EBI-28605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-05
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.905
REMARK 200 MONOCHROMATOR : SI 111 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124324
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.45
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.2
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.63
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
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 91.36500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.36500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.07000
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 PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK ALSO PROVIDES INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.5 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 182.73000
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 400
REMARK 400 COMPOUND
REMARK 400 THE ALPHA SUBUNIT OF TRYPTOPHAN SYNTHASE TAKES PART IN ALDOL
REMARK 400 CLEAVAGE OF INDOLEGLYCEROL PHOSPHATE TO INDOLE AND GLYCERALDEHYDE
REMARK 400 3-PHOSPHATE
REMARK 400 THE BETA SUBUNIT OF TRYPTOPHAN SYNTHASE IS RESPONSIBLE FOR
REMARK 400 THE SYNTHESIS OF L-TRYPTOPHAN FROM INDOLE AND L-SERINE.
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 MET A 1
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 ALA A 190
REMARK 465 LEU A 191
REMARK 465 PRO A 192
REMARK 465 LEU A 193
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 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 ALA A 268 CA C O CB
REMARK 470 GLN B 63 CG CD OE1 NE2
REMARK 470 LYS B 392 CA C O CB CG CD CE NZ
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 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 5.70 -67.37
REMARK 500 ASN A 244 22.50 -142.95
REMARK 500 THR B 165 -163.89 -129.90
REMARK 500 ALA B 269 67.36 -117.95
REMARK 500 SER B 308 -154.67 -137.63
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 0.08 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 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 B1393 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 232 O
REMARK 620 2 SER B 308 O 88.5
REMARK 620 3 PHE B 306 O 105.0 84.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F19 A1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLS B1392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B1393
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A50 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE
REMARK 900 PROPANOL PHOSPHATE
REMARK 900 RELATED ID: 1A5A RELATED DB: PDB
REMARK 900 CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE,
REMARK 900 INDOLE-3-GLYCEROL PHOSPHATE, BOUND TO A
REMARK 900 MUTANT (ALPHAD60N) TRYPTOPHAN SYNTHASE
REMARK 900 ALPHA2BETA2 COMPLEX REVEALS THE CORRECT
REMARK 900 ORIENTATION OF ACTIVE SITE ALPHA GLU 49
REMARK 900 RELATED ID: 1A5B RELATED DB: PDB
REMARK 900 CRYO-CRYSTALLOGRAPHY OF A TRUE SUBSTRATE,
REMARK 900 INDOLE-3-GLYCEROL PHOSPHATE, BOUND TO A
REMARK 900 MUTANT (ALPHA D60N) TRYPTOPHAN SYNTHASE ALPHA
REMARK 900 =2=BETA=2= COMPLEX REVEALS THE CORRECT
REMARK 900 ORIENTATION OF ACTIVE SITE ALPHA GLU 49
REMARK 900 RELATED ID: 1A5S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE
REMARK 900 PROPANOL PHOSPHATE AND L-SER BOUND AS
REMARK 900 AMINO ACRYLATE TO THE BETA SITE
REMARK 900 RELATED ID: 1BEU RELATED DB: PDB
REMARK 900 TRP SYNTHASE (D60N-IPP-SER) WITH K+
REMARK 900 RELATED ID: 1BKS RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM
REMARK 900 RELATED ID: 1C29 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 900 BACTERIAL TRYPTOPHAN SYNTHASE WITH THE
REMARK 900 TRANSITION STATE ANALOGUE INHIBITOR 4-(2-
REMARK 900 HYDROXYPHENYLTHIO)-1-BUTENYLPHOSPHONIC ACID
REMARK 900 RELATED ID: 1C8V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 900 BACTERIAL TRYPTOPHAN SYNTHASE WITH THE
REMARK 900 TRANSITION STATE ANALOGUE INHIBITOR 4-(2-
REMARK 900 HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACID
REMARK 900 RELATED ID: 1C9D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 900 BACTERIAL TRYPTOPHAN SYNTHASE WITH THE
REMARK 900 TRANSITION STATE ANALOGUE INHIBITOR 4-(2-
REMARK 900 HYDROXY-4-FLUOROPHENYLTHIO)-BUTYLPHOSPHONIC ACID
REMARK 900 RELATED ID: 1CW2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 900 BACTERIAL TRYPTOPHAN SYNTHASE WITH THE
REMARK 900 TRANSITION STATE ANALOGUE INHIBITOR 4-(2-
REMARK 900 HYDROXYPHENYLSULFINYL)-BUTYLPHOSPHONIC ACID
REMARK 900 RELATED ID: 1CX9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK 900 BACTERIAL TRYPTOPHAN SYNTHASE WITH THE
REMARK 900 TRANSITION STATE ANALOGUE INHIBITOR 4-(2-
REMARK 900 AMINOPHENYLTHIO)-BUTYLPHOSPHONIC ACID
REMARK 900 RELATED ID: 1FUY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETAA169L/BETAC170W
REMARK 900 DOUBLE MUTANT OFTRYPTOPHAN SYNTHASE COMPLEXED
REMARK 900 WITH 5-FLUORO-INDOLE-PROPANOLPHOSPHATE
REMARK 900 RELATED ID: 1K3U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASECOMPLEXED WITH N-[1H-INDOL-3-YL-
REMARK 900 ACETYL]ASPARTIC ACID
REMARK 900 RELATED ID: 1K7E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASECOMPLEXED WITH N-[1H-INDOL-3-YL-
REMARK 900 ACETYL]GLYCINE ACID
REMARK 900 RELATED ID: 1K7F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASECOMPLEXED WITH N-[1H-INDOL-3-YL-
REMARK 900 ACETYL]VALINE ACID
REMARK 900 RELATED ID: 1K7X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BETA-SER178PRO
REMARK 900 MUTANT OFTRYPTOPHAN SYNTHASE
REMARK 900 RELATED ID: 1K8X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF
REMARK 900 TRYPTOPHANSYNTHASE FROM SALMONELLA TYPHIMURIUM
REMARK 900 RELATED ID: 1K8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE
REMARK 900 BETA-SER178PROMUTANT COMPLEXED WITH D,L-
REMARK 900 ALPHA-GLYCEROL-3-PHOSPHATE
REMARK 900 RELATED ID: 1K8Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE
REMARK 900 BETA-SER178PROMUTANT COMPLEXED WITH N-[1H-
REMARK 900 INDOL-3-YL-ACETYL]GLYCINE ACID
REMARK 900 RELATED ID: 1KFB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF
REMARK 900 TRYPTOPHANSYNTHASE FROM SALMONELLA TYPHIMURIUM
REMARK 900 WITH INDOLE GLYCEROLPHOSPHATE
REMARK 900 RELATED ID: 1KFC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF
REMARK 900 TRYPTOPHANSYNTHASE FROM SALMONELLA TYPHIMURIUM
REMARK 900 WITH INDOLE PROPANOLPHOSPHATE
REMARK 900 RELATED ID: 1KFE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF
REMARK 900 TRYPTOPHANSYNTHASE FROM SALMONELLA TYPHIMURIUM
REMARK 900 WITH L-SER BOUND TOTHE BETA SITE
REMARK 900 RELATED ID: 1KFJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASECOMPLEXED WITH L-SERINE
REMARK 900 RELATED ID: 1KFK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPTOPHAN SYNTHASE FROM
REMARK 900 SALMONELLATYPHIMURIUM
REMARK 900 RELATED ID: 1QOP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASE COMPLEXED WITH INDOLE PROPANOL
REMARK 900 PHOSPHATE
REMARK 900 RELATED ID: 1QOQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASE COMPLEXED WITH INDOLE GLYCEROL
REMARK 900 PHOSPHATE
REMARK 900 RELATED ID: 1TJP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASECOMPLEXED WITH 1-[(2-HYDROXYLPHENYL)
REMARK 900 AMINO]3-GLYCEROLPHOSPHATE
REMARK 900 RELATED ID: 1TTP RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN THE PRESENCE OF
REMARK 900 CESIUM, ROOM TEMPERATURE
REMARK 900 RELATED ID: 1TTQ RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN THE PRESENCE OF
REMARK 900 POTASSIUM AT ROOM TEMPERATURE
REMARK 900 RELATED ID: 1UBS RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE WITH A MUTATION OF LYS
REMARK 900 87 ->THR IN THE B SUBUNIT AND IN THE
REMARK 900 PRESENCE OF LIGAND L-SERINE
REMARK 900 RELATED ID: 1WBJ RELATED DB: PDB
REMARK 900 WILDTYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH
REMARK 900 GLYCEROL PHOSPHATE
REMARK 900 RELATED ID: 2CLE RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN COMPLEX WITH N-(4'-
REMARK 900 TRIFLUOROMETHOXYBENZOYL)-2-AMINO-1-
REMARK 900 ETHYLPHOSPHATE (F6) - LOWF6 COMPLEX
REMARK 900 RELATED ID: 2CLF RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN COMPLEX WITH N-(4'-
REMARK 900 TRIFLUOROMETHOXYBENZOYL)-2-AMINO-1-
REMARK 900 ETHYLPHOSPHATE (F6) - HIGHF6 COMPLEX
REMARK 900 RELATED ID: 2CLI RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN COMPLEX WITH N-(4'-
REMARK 900 TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
REMARK 900 ETHYLPHOSPHATE (F9)
REMARK 900 RELATED ID: 2CLK RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE IN COMPLEX WITH D-
REMARK 900 GLYCERALDEHYDE 3-PHOSPHATE (G3P)
REMARK 900 RELATED ID: 2CLL RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE)
REMARK 900 IN COMPLEX WITH N-(4'-
REMARK 900 TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-
REMARK 900 ETHYLPHOSPHATE (F9)
REMARK 900 RELATED ID: 2CLM RELATED DB: PDB
REMARK 900 TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE)
REMARK 900 IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZOYL
REMARK 900 )-2-AMINO-1-ETHYLPHOSPHATE (F6)
REMARK 900 RELATED ID: 2TRS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF MUTANT (BETAK87T)
REMARK 900 TRYPTOPHAN SYNTHASE ALPHA=2 BETA=2= COMPLEX
REMARK 900 WITH LIGANDS BOUND TO THE ACTIVE SITES
REMARK 900 OF THE ALPHA AND BETA SUBUNITS REVEAL
REMARK 900 LIGAND-INDUCED CONFORMATIONAL CHANGES
REMARK 900 RELATED ID: 2TSY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF MUTANT (BETAK87T)
REMARK 900 TRYPTOPHAN SYNTHASE ALPHA=2 BETA=2= COMPLEX
REMARK 900 WITH LIGANDS BOUND TO THE ACTIVE SITES
REMARK 900 OF THE ALPHA AND BETA SUBUNITS REVEAL
REMARK 900 LIGAND-INDUCED CONFORMATIONAL CHANGES
REMARK 900 RELATED ID: 2TYS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF MUTANT (BETAK87T)
REMARK 900 TRYPTOPHAN SYNTHASE ALPHA=2 BETA=2= COMPLEX
REMARK 900 WITH LIGANDS BOUND TO THE ACTIVE SITES
REMARK 900 OF THE ALPHA AND BETA SUBUNITS REVEAL
REMARK 900 LIGAND-INDUCED CONFORMATIONAL CHANGES
REMARK 900 RELATED ID: 2WSY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN
REMARK 900 SYNTHASE
DBREF 2CLO A 1 268 UNP P00929 TRPA_SALTY 1 268
DBREF 2CLO B 2 397 UNP P0A2K1 TRPB_SALTY 1 396
SEQADV 2CLO ARG B 34 UNP P0A2K1 SER 33 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 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 ARG 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 F19 A1268 21
HET PLS B1392 22
HET NA B1393 1
HETNAM PLS [3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM 2 PLS PYRIDIN-4-YLMETHYL]-SERINE
HETNAM F19 2-[(2-NAPHTHYLSULFONYL)AMINO]ETHYL
HETNAM 2 F19 DIHYDROGEN PHOSPHATE
HETNAM NA SODIUM ION
HETSYN PLS PYRIDOXYL-SERINE-5-MONOPHOSPHATE
FORMUL 3 PLS C11 H17 N2 O8 P
FORMUL 4 F19 C12 H14 N O6 P S
FORMUL 5 NA NA 1+
FORMUL 6 HOH *569(H2 O1)
HELIX 1 1 GLU A 2 ARG A 14 1 13
HELIX 2 2 GLY A 29 GLY A 44 1 16
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 HIS A 194 TYR A 203 1 10
HELIX 11 11 SER A 216 GLY A 227 1 12
HELIX 12 12 GLY A 234 LYS A 243 1 10
HELIX 13 13 SER A 247 ARG A 267 1 21
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 SER B 178 1 14
HELIX 23 23 PRO B 196 PHE B 204 1 9
HELIX 24 24 ARG B 206 GLY B 221 1 16
HELIX 25 25 GLY B 234 ALA B 242 1 9
HELIX 26 26 ASP B 243 ILE B 245 5 3
HELIX 27 27 GLY B 261 GLY B 265 5 5
HELIX 28 28 ALA B 269 GLY B 274 1 6
HELIX 29 29 SER B 301 ASP B 305 5 5
HELIX 30 30 GLY B 310 ILE B 319 1 10
HELIX 31 31 ASP B 329 GLY B 344 1 16
HELIX 32 32 ALA B 348 GLN B 365 1 18
HELIX 33 33 GLY B 380 LYS B 382 5 3
HELIX 34 34 ASP B 383 LEU B 391 1 9
SHEET 1 AA 9 ALA A 149 PRO A 150 0
SHEET 2 AA 9 SER A 125 VAL A 128 1 N VAL A 126 O ALA A 149
SHEET 3 AA 9 ILE A 97 MET A 101 1 O LEU A 99 N LEU A 127
SHEET 4 AA 9 LEU A 48 GLY A 51 1 O LEU A 48 N GLY A 98
SHEET 5 AA 9 ALA A 18 THR A 24 1 O PRO A 21 N GLU A 49
SHEET 6 AA 9 GLY A 230 SER A 233 1 O ALA A 231 N VAL A 20
SHEET 7 AA 9 ALA A 208 GLY A 211 1 O GLN A 210 N ILE A 232
SHEET 8 AA 9 THR A 174 LEU A 177 1 O THR A 174 N LEU A 209
SHEET 9 AA 9 ILE A 153 CYS A 154 1 O CYS A 154 N LEU A 177
SHEET 1 BA 4 TYR B 8 PHE B 9 0
SHEET 2 BA 4 PHE B 12 TYR B 16 -1 O PHE B 12 N PHE B 9
SHEET 3 BA 4 GLY B 281 MET B 286 -1 O GLY B 281 N TYR B 16
SHEET 4 BA 4 ARG B 275 TYR B 279 -1 O ARG B 275 N MET B 286
SHEET 1 BB 6 LEU B 59 LYS B 61 0
SHEET 2 BB 6 THR B 71 ARG B 77 -1 O LEU B 75 N THR B 60
SHEET 3 BB 6 GLN B 370 LEU B 376 1 O GLN B 370 N THR B 72
SHEET 4 BB 6 ALA B 226 CYS B 230 1 O ALA B 226 N VAL B 373
SHEET 5 BB 6 GLY B 251 GLY B 259 1 O GLY B 251 N VAL B 227
SHEET 6 BB 6 ASP B 323 THR B 328 1 O ASP B 323 N GLY B 254
SHEET 1 BC 4 GLU B 155 VAL B 159 0
SHEET 2 BC 4 LYS B 129 GLY B 135 1 O CYS B 130 N GLU B 155
SHEET 3 BC 4 GLU B 105 THR B 110 1 O ILE B 106 N ARG B 131
SHEET 4 BC 4 ALA B 184 MET B 187 1 O HIS B 185 N ILE B 107
LINK NA NA B1393 O GLY B 232 1555 1555 2.44
LINK NA NA B1393 O SER B 308 1555 1555 2.44
LINK NA NA B1393 O PHE B 306 1555 1555 2.53
CISPEP 1 ASP A 27 PRO A 28 0 -0.09
CISPEP 2 ARG B 55 PRO B 56 0 -1.26
CISPEP 3 HIS B 195 PRO B 196 0 3.24
SITE 1 AC1 16 PHE A 22 GLU A 49 ALA A 59 LEU A 100
SITE 2 AC1 16 LEU A 127 ILE A 153 TYR A 175 THR A 183
SITE 3 AC1 16 GLY A 184 PHE A 212 GLY A 213 GLY A 234
SITE 4 AC1 16 SER A 235 HOH A2057 HOH A2157 HOH A2190
SITE 1 AC2 23 HIS B 86 LYS B 87 THR B 110 GLY B 111
SITE 2 AC2 23 ALA B 112 GLY B 113 GLN B 114 HIS B 115
SITE 3 AC2 23 THR B 190 CYS B 230 GLY B 232 GLY B 233
SITE 4 AC2 23 GLY B 234 SER B 235 ASN B 236 ALA B 302
SITE 5 AC2 23 GLY B 303 ASP B 305 GLU B 350 SER B 377
SITE 6 AC2 23 HOH B2376 HOH B2378 HOH B2379
SITE 1 AC3 5 GLY B 232 PHE B 306 SER B 308 HOH B2263
SITE 2 AC3 5 HOH B2301
CRYST1 182.730 60.140 67.510 90.00 94.61 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 0.005473 0.000000 0.000441 0.00000
SCALE2 0.000000 0.016628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014861 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
