HEADER LYASE 10-JUN-01 1JCM
TITLE TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE AND
TITLE 2 IN COMPLEX WITH A CDRP-RELATED SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE;
COMPND 3 CHAIN: P;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (1-259 AA) OF THE BIFUNCTIONAL ENZYME
COMPND 5 ANTHRANILATE ISOMERASE, IGPS:PRAI;
COMPND 6 SYNONYM: IGPS; TRYPTOPHAN BIOSYNTHESIS PROTEIN TRPCF;
COMPND 7 EC: 4.1.1.48;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET21A(+)-ECTRPC
KEYWDS BETA-ALPHA-BARREL, DISULPHIDE BRIDGE, STABILITY MUTANT, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.IVENS,O.MAYANS,H.SZADKOWSKI,M.WILMANNS,K.KIRSCHNER
REVDAT 5 27-OCT-21 1JCM 1 REMARK SEQADV
REVDAT 4 16-NOV-11 1JCM 1 HETATM
REVDAT 3 13-JUL-11 1JCM 1 VERSN
REVDAT 2 24-FEB-09 1JCM 1 VERSN
REVDAT 1 10-JUN-02 1JCM 0
JRNL AUTH A.IVENS,O.MAYANS,H.SZADKOWSKI,C.JURGENS,M.WILMANNS,
JRNL AUTH 2 K.KIRSCHNER
JRNL TITL STABILIZATION OF A (BETAALPHA)8-BARREL PROTEIN BY AN
JRNL TITL 2 ENGINEERED DISULFIDE BRIDGE.
JRNL REF EUR.J.BIOCHEM. V. 269 1145 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11856350
JRNL DOI 10.1046/J.1432-1033.2002.02745.X
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16944
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.319
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1099
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4400
REMARK 3 BIN FREE R VALUE : 0.4900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 93
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 : 2033
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 135
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.70000
REMARK 3 B22 (A**2) : -2.70000
REMARK 3 B33 (A**2) : 5.50000
REMARK 3 B12 (A**2) : -6.40000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1JCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 0.911
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17306
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM POTASSIUM PHOSPHATE PH 5.0, 1.2
REMARK 280 M AMMONIUM SULPHATE, 5 MM EDTA, PH 5.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP AT 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.37250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 78.37250
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.37250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 78.37250
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 78.37250
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 78.37250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P
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 -0.500000 -0.866025 0.000000 81.63800
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 40.81900
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 70.70058
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 P PO4 P 705 LIES ON A SPECIAL POSITION.
REMARK 375 O1 PO4 P 705 LIES ON A SPECIAL POSITION.
REMARK 375 P PO4 P 702 LIES ON A SPECIAL POSITION.
REMARK 375 P PO4 P 703 LIES ON A SPECIAL POSITION.
REMARK 375 O3 PO4 P 703 LIES ON A SPECIAL POSITION.
REMARK 375 P PO4 P 704 LIES ON A SPECIAL POSITION.
REMARK 375 HOH P 708 LIES ON A SPECIAL POSITION.
REMARK 375 HOH P 800 LIES ON A SPECIAL POSITION.
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 GLN P 23 77.86 -112.85
REMARK 500 PHE P 28 -17.96 -171.29
REMARK 500 GLN P 29 -92.60 -30.86
REMARK 500 ASN P 30 27.52 -59.22
REMARK 500 PRO P 34 170.21 -50.56
REMARK 500 THR P 36 36.12 -92.41
REMARK 500 ASP P 69 86.82 -174.73
REMARK 500 TYR P 77 -19.51 -49.36
REMARK 500 TYR P 80 -40.96 -132.82
REMARK 500 SER P 104 -18.94 -48.47
REMARK 500 GLN P 130 15.48 83.66
REMARK 500 LEU P 188 0.63 -65.17
REMARK 500 LEU P 205 -8.65 -48.24
REMARK 500 HIS P 207 -175.67 -67.18
REMARK 500 ASN P 208 16.74 55.70
REMARK 500 SER P 215 141.32 78.64
REMARK 500 GLU P 256 -156.81 -89.97
REMARK 500 ASN P 257 22.60 46.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 137 P 400
DBREF 1JCM P 1 259 GB 775124 AAB60033 1 259
SEQADV 1JCM CYS P 3 GB 775124 THR 3 ENGINEERED MUTATION
SEQADV 1JCM CYS P 189 GB 775124 ARG 189 ENGINEERED MUTATION
SEQRES 1 P 259 MET GLN CYS VAL LEU ALA LYS ILE VAL ALA ASP LYS ALA
SEQRES 2 P 259 ILE TRP VAL GLU ALA ARG LYS GLN GLN GLN PRO LEU ALA
SEQRES 3 P 259 SER PHE GLN ASN GLU VAL GLN PRO SER THR ARG HIS PHE
SEQRES 4 P 259 TYR ASP ALA LEU GLN GLY ALA ARG THR ALA PHE ILE LEU
SEQRES 5 P 259 GLU CYS LYS LYS ALA SER PRO SER LYS GLY VAL ILE ARG
SEQRES 6 P 259 ASP ASP PHE ASP PRO ALA ARG ILE ALA ALA ILE TYR LYS
SEQRES 7 P 259 HIS TYR ALA SER ALA ILE SER VAL LEU THR ASP GLU LYS
SEQRES 8 P 259 TYR PHE GLN GLY SER PHE ASN PHE LEU PRO ILE VAL SER
SEQRES 9 P 259 GLN ILE ALA PRO GLN PRO ILE LEU CYS LYS ASP PHE ILE
SEQRES 10 P 259 ILE ASP PRO TYR GLN ILE TYR LEU ALA ARG TYR TYR GLN
SEQRES 11 P 259 ALA ASP ALA CYS LEU LEU MET LEU SER VAL LEU ASP ASP
SEQRES 12 P 259 ASP GLN TYR ARG GLN LEU ALA ALA VAL ALA HIS SER LEU
SEQRES 13 P 259 GLU MET GLY VAL LEU THR GLU VAL SER ASN GLU GLU GLU
SEQRES 14 P 259 GLN GLU ARG ALA ILE ALA LEU GLY ALA LYS VAL VAL GLY
SEQRES 15 P 259 ILE ASN ASN ARG ASP LEU CYS ASP LEU SER ILE ASP LEU
SEQRES 16 P 259 ASN ARG THR ARG GLU LEU ALA PRO LYS LEU GLY HIS ASN
SEQRES 17 P 259 VAL THR VAL ILE SER GLU SER GLY ILE ASN THR TYR ALA
SEQRES 18 P 259 GLN VAL ARG GLU LEU SER HIS PHE ALA ASN GLY PHE LEU
SEQRES 19 P 259 ILE GLY SER ALA LEU MET ALA HIS ASP ASP LEU HIS ALA
SEQRES 20 P 259 ALA VAL ARG ARG VAL LEU LEU GLY GLU ASN LYS VAL
HET PO4 P 701 5
HET PO4 P 705 5
HET PO4 P 706 5
HET PO4 P 702 5
HET PO4 P 703 5
HET PO4 P 704 5
HET 137 P 400 23
HETNAM PO4 PHOSPHATE ION
HETNAM 137 1-(O-CARBOXY-PHENYLAMINO)-1-DEOXY-D-RIBULOSE-5-
HETNAM 2 137 PHOSPHATE
FORMUL 2 PO4 6(O4 P 3-)
FORMUL 8 137 C12 H18 N O9 P
FORMUL 9 HOH *135(H2 O)
HELIX 1 1 CYS P 3 GLN P 21 1 19
HELIX 2 2 PRO P 24 PHE P 28 5 5
HELIX 3 3 PHE P 28 VAL P 32 5 5
HELIX 4 4 HIS P 38 LEU P 43 1 6
HELIX 5 5 ASP P 69 LYS P 78 1 10
HELIX 6 6 ASP P 89 GLN P 94 1 6
HELIX 7 7 ASN P 98 ALA P 107 1 10
HELIX 8 8 ASP P 119 TYR P 129 1 11
HELIX 9 9 ASP P 142 HIS P 154 1 13
HELIX 10 10 ASN P 166 LEU P 176 1 11
HELIX 11 11 LEU P 195 ALA P 202 1 8
HELIX 12 12 PRO P 203 GLY P 206 5 4
HELIX 13 13 THR P 219 SER P 227 1 9
HELIX 14 14 GLY P 236 ALA P 241 1 6
HELIX 15 15 ASP P 244 LEU P 253 1 10
SHEET 1 A 9 ALA P 49 CYS P 54 0
SHEET 2 A 9 ALA P 83 LEU P 87 1 N ALA P 83 O PHE P 50
SHEET 3 A 9 ILE P 111 LYS P 114 1 N LEU P 112 O ILE P 84
SHEET 4 A 9 ALA P 133 MET P 137 1 O ALA P 133 N CYS P 113
SHEET 5 A 9 GLY P 159 VAL P 164 1 O GLY P 159 N CYS P 134
SHEET 6 A 9 VAL P 180 ASN P 184 1 O VAL P 180 N THR P 162
SHEET 7 A 9 THR P 210 GLU P 214 1 O THR P 210 N VAL P 181
SHEET 8 A 9 GLY P 232 ILE P 235 1 O GLY P 232 N SER P 213
SHEET 9 A 9 ALA P 49 CYS P 54 1 O ALA P 49 N PHE P 233
SHEET 1 B 2 ALA P 57 SER P 58 0
SHEET 2 B 2 GLY P 62 VAL P 63 -1 N GLY P 62 O SER P 58
SHEET 1 C 2 ARG P 186 ASP P 187 0
SHEET 2 C 2 SER P 192 ILE P 193 -1 O SER P 192 N ASP P 187
SSBOND 1 CYS P 3 CYS P 189 1555 1555 1.92
SITE 1 AC1 3 LYS P 61 ARG P 186 ASN P 218
SITE 1 AC2 1 ILE P 14
SITE 1 AC3 4 GLU P 90 SER P 96 PHE P 97 ASN P 98
SITE 1 AC4 3 ARG P 224 HIS P 228 PO4 P 703
SITE 1 AC5 4 ARG P 224 PO4 P 702 PO4 P 704 HOH P 808
SITE 1 AC6 1 PO4 P 703
SITE 1 AC7 19 GLU P 53 LYS P 55 SER P 58 PRO P 59
SITE 2 AC7 19 SER P 60 PHE P 93 LYS P 114 ARG P 186
SITE 3 AC7 19 LEU P 188 LEU P 191 GLU P 214 SER P 215
SITE 4 AC7 19 GLY P 216 LEU P 234 ILE P 235 GLY P 236
SITE 5 AC7 19 SER P 237 HOH P 716 HOH P 745
CRYST1 81.638 81.638 156.745 90.00 90.00 120.00 P 63 2 2 12
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 0.012249 0.007072 -0.000001 0.00000
SCALE2 0.000000 0.014144 -0.000001 0.00000
SCALE3 0.000000 0.000000 0.006380 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
