HEADER HYDROLASE 18-OCT-02 1J00
TITLE E. COLI THIOESTERASE I/PROTEASE I/LYSOPHOSPHOLIPASE L1 IN COMPLEXED
TITLE 2 WITH DIETHYL PHOSPHONO MOIETY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOESTERASE I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYL-COA THIOESTERASE I, PROTEASE I, LYSOPHOSPHOLIPASE L1;
COMPND 5 EC: 3.1.2.-, 3.1.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: TESA/APEA/PLDC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-20B(+)
KEYWDS HYDROLASE, PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-C.LO,J.-F.SHAW,Y.-C.LIAW
REVDAT 4 25-OCT-23 1J00 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1J00 1 VERSN
REVDAT 2 24-FEB-09 1J00 1 VERSN
REVDAT 1 08-JUL-03 1J00 0
JRNL AUTH Y.-C.LO,S.-C.LIN,J.-F.SHAW,Y.-C.LIAW
JRNL TITL CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOESTERASE
JRNL TITL 2 I/PROTEASE I/LYSOPHOSPHOLIPASE L1: CONSENSUS SEQUENCE BLOCKS
JRNL TITL 3 CONSTITUTE THE CATALYTIC CENTER OF SGNH-HYDROLASES THROUGH A
JRNL TITL 4 CONSERVED HYDROGEN BOND NETWORK
JRNL REF J.MOL.BIOL. V. 330 539 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12842470
JRNL DOI 10.1016/S0022-2836(03)00637-5
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 14582
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) : 0.239
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1486
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2045
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 216
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1416
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.39000
REMARK 3 B22 (A**2) : 9.39000
REMARK 3 B33 (A**2) : -18.78000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.860 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.180 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.290 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 43.35
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000005458.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 133
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL17B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12714
REMARK 200 MONOCHROMATOR : SI111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAC SCIENCE DIP-2030
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XPRESS, DIP2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JRL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-[N-MORPHOLINO]ETHANESULFONIC ACID,
REMARK 280 PEGMME5000, AMMONIUM SULFATE, PH 6.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 -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 85.94900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 24.95350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 24.95350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 128.92350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 24.95350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 24.95350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.97450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 24.95350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 24.95350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 128.92350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 24.95350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 24.95350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.97450
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 85.94900
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0.000000 -1.000000 0.000000 49.90700
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 49.90700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 85.94900
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 GLN A 32
REMARK 465 ASN A 179
REMARK 465 ASP A 181
REMARK 465 SER A 182
REMARK 465 LEU A 183
REMARK 465 GLU A 184
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 HIS A 188
REMARK 465 HIS A 189
REMARK 465 HIS A 190
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 HIS A 180 N CA C O CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1048 O HOH A 1086 8665 2.10
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 ASP A 9 -151.42 -113.98
REMARK 500 LYS A 34 -109.72 -160.11
REMARK 500 ALA A 40 58.47 -98.32
REMARK 500 GLN A 62 57.20 38.80
REMARK 500 TYR A 113 -10.14 -143.44
REMARK 500 ARG A 115 -75.10 -56.86
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 SO4 A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JRL RELATED DB: PDB
REMARK 900 1JRL CONTAINS THE SAME PROTEIN, L109P MUTANT
REMARK 900 RELATED ID: 1IVN RELATED DB: PDB
REMARK 900 1IVN CONTAINS THE SAME PROTEIN, NATIVE TAP STRUCTURE
DBREF 1J00 A 1 182 UNP P29679 TESA_ECOLI 27 208
SEQADV 1J00 SDP A 10 UNP P29679 SER 36 MODIFIED RESIDUE
SEQADV 1J00 LEU A 183 UNP P29679 EXPRESSION TAG
SEQADV 1J00 GLU A 184 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 185 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 186 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 187 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 188 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 189 UNP P29679 EXPRESSION TAG
SEQADV 1J00 HIS A 190 UNP P29679 EXPRESSION TAG
SEQRES 1 A 190 ALA ASP THR LEU LEU ILE LEU GLY ASP SDP LEU SER ALA
SEQRES 2 A 190 GLY TYR ARG MET SER ALA SER ALA ALA TRP PRO ALA LEU
SEQRES 3 A 190 LEU ASN ASP LYS TRP GLN SER LYS THR SER VAL VAL ASN
SEQRES 4 A 190 ALA SER ILE SER GLY ASP THR SER GLN GLN GLY LEU ALA
SEQRES 5 A 190 ARG LEU PRO ALA LEU LEU LYS GLN HIS GLN PRO ARG TRP
SEQRES 6 A 190 VAL LEU VAL GLU LEU GLY GLY ASN ASP GLY LEU ARG GLY
SEQRES 7 A 190 PHE GLN PRO GLN GLN THR GLU GLN THR LEU ARG GLN ILE
SEQRES 8 A 190 LEU GLN ASP VAL LYS ALA ALA ASN ALA GLU PRO LEU LEU
SEQRES 9 A 190 MET GLN ILE ARG LEU PRO ALA ASN TYR GLY ARG ARG TYR
SEQRES 10 A 190 ASN GLU ALA PHE SER ALA ILE TYR PRO LYS LEU ALA LYS
SEQRES 11 A 190 GLU PHE ASP VAL PRO LEU LEU PRO PHE PHE MET GLU GLU
SEQRES 12 A 190 VAL TYR LEU LYS PRO GLN TRP MET GLN ASP ASP GLY ILE
SEQRES 13 A 190 HIS PRO ASN ARG ASP ALA GLN PRO PHE ILE ALA ASP TRP
SEQRES 14 A 190 MET ALA LYS GLN LEU GLN PRO LEU VAL ASN HIS ASP SER
SEQRES 15 A 190 LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 1J00 SDP A 10 SER
HET SDP A 10 14
HET SO4 A 501 5
HETNAM SDP 2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 1 SDP C7 H16 N O6 P
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *91(H2 O)
HELIX 1 1 ASP A 9 GLY A 14 1 6
HELIX 2 2 SER A 18 ALA A 21 5 4
HELIX 3 3 ALA A 22 TRP A 31 1 10
HELIX 4 4 THR A 46 GLN A 62 1 17
HELIX 5 5 GLN A 80 ALA A 98 1 19
HELIX 6 6 ARG A 116 PHE A 132 1 17
HELIX 7 7 PHE A 140 LEU A 146 1 7
HELIX 8 8 LYS A 147 MET A 151 5 5
HELIX 9 9 ASN A 159 ASP A 161 5 3
HELIX 10 10 ALA A 162 GLN A 175 1 14
HELIX 11 11 PRO A 176 VAL A 178 5 3
SHEET 1 A 5 SER A 36 SER A 41 0
SHEET 2 A 5 THR A 3 GLY A 8 1 N LEU A 4 O SER A 36
SHEET 3 A 5 TRP A 65 GLU A 69 1 O LEU A 67 N LEU A 5
SHEET 4 A 5 GLU A 101 MET A 105 1 O LEU A 103 N VAL A 66
SHEET 5 A 5 LEU A 136 LEU A 137 1 O LEU A 137 N LEU A 104
LINK C ASP A 9 N SDP A 10 1555 1555 1.34
LINK C SDP A 10 N LEU A 11 1555 1555 1.33
SITE 1 AC1 7 MET A 17 SER A 18 ALA A 21 ARG A 53
SITE 2 AC1 7 LEU A 57 ARG A 160 HOH A1028
CRYST1 49.907 49.907 171.898 90.00 90.00 90.00 P 43 21 2 8
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 0.020037 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005817 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
