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HEADER HYDROLASE 04-FEB-08 3C6B
TITLE REACTION PRODUCT OF PARAOXON AND S-FORMYLGLUTATHIONE
TITLE 2 HYDROLASE W197I MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FGH;
COMPND 5 EC: 3.1.2.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 GENE: YJL068C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET13
KEYWDS CYSTEINE SULFENIC ACID, SERINE HYDROLASE, THIOESTERASE,
KEYWDS 2 FORMALDEHYDE, ORGANOPHOSPHATE, CYTOPLASM, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.LEGLER,C.B.MILLARD
REVDAT 1 12-AUG-08 3C6B 0
JRNL AUTH P.M.LEGLER,D.KUMARAN,S.SWAMINATHAN,F.W.STUDIER,
JRNL AUTH 2 C.B.MILLARD
JRNL TITL STRUCTURAL CHARACTERIZATION AND REVERSAL OF THE
JRNL TITL 2 NATURAL ORGANOPHOSPHATE RESISTANCE OF
JRNL TITL 3 S-FORMYLGLUTATHIONE HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 15361
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 + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 825
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 923
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 44
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2382
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.50000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : 0.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.25000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.270
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.502
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2415 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3264 ; 2.059 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 288 ;13.968 ; 5.069
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;33.433 ;24.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;17.134 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.969 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1872 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1017 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1564 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 101 ; 0.116 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 31 ; 0.214 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.134 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1492 ; 1.072 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2315 ; 1.695 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1084 ; 2.746 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 949 ; 3.838 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3C6B COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046395.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-2007
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : BRUKER FR591
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : MULTILAYER MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16188
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 78.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.050
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 FOR THE DATA SET : 11.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.35
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.320
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: PDB ENTRY ID 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.085M SODIUM ACETATE TRIHYDRATE PH
REMARK 280 4.6, 0.17M AMMONIUM ACETATE, 25.5% W/V PEG 4000, 15% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 28.95100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.95100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.49500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
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 -1.000000 0.000000 0.000000 -54.34619
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -78.91293
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 LYS A 143
REMARK 465 ASN A 144
REMARK 465 GLY A 145
REMARK 465 ASP A 146
REMARK 465 VAL A 147
REMARK 465 GLU A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
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),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 GLU A 117 CD GLU A 117 OE1 0.075
REMARK 500 ASP A 275 CB ASP A 275 CG -0.165
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 VAL A 30 CB - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 VAL A 30 CG1 - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 275 CB - CG - OD1 ANGL. DEV. = -7.0 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 CYS A 10 -131.72 56.82
REMARK 500 THR A 59 -12.50 78.63
REMARK 500 ALA A 108 40.96 -153.82
REMARK 500 GLN A 124 53.61 -109.05
REMARK 500 ASP A 153 -73.72 -114.50
REMARK 500 LYS A 249 61.96 33.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PV1 RELATED DB: PDB
REMARK 900 S. CEREVISAE S-FORMYLGLUTATHIONE HYDROLASE
DBREF 3C6B A 1 299 UNP P40363 SFGH_YEAST 1 299
SEQADV 3C6B ILE A 197 UNP P40363 TRP 197 ENGINEERED
SEQRES 1 A 299 MET LYS VAL VAL LYS GLU PHE SER VAL CYS GLY GLY ARG
SEQRES 2 A 299 LEU ILE LYS LEU SER HIS ASN SER ASN SER THR LYS THR
SEQRES 3 A 299 SER MET ASN VAL ASN ILE TYR LEU PRO LYS HIS TYR TYR
SEQRES 4 A 299 ALA GLN ASP PHE PRO ARG ASN LYS ARG ILE PRO THR VAL
SEQRES 5 A 299 PHE TYR LEU SER GLY LEU THR CSO THR PRO ASP ASN ALA
SEQRES 6 A 299 SER GLU LYS ALA PHE TRP GLN PHE GLN ALA ASP LYS TYR
SEQRES 7 A 299 GLY PHE ALA ILE VAL PHE PRO ASP THR SER PRO ARG GLY
SEQRES 8 A 299 ASP GLU VAL ALA ASN ASP PRO GLU GLY SER TRP ASP PHE
SEQRES 9 A 299 GLY GLN GLY ALA GLY PHE TYR LEU ASN ALA THR GLN GLU
SEQRES 10 A 299 PRO TYR ALA GLN HIS TYR GLN MET TYR ASP TYR ILE HIS
SEQRES 11 A 299 LYS GLU LEU PRO GLN THR LEU ASP SER HIS PHE ASN LYS
SEQRES 12 A 299 ASN GLY ASP VAL LYS LEU ASP PHE LEU ASP ASN VAL ALA
SEQRES 13 A 299 ILE THR GLY HIS SDP MET GLY GLY TYR GLY ALA ILE CYS
SEQRES 14 A 299 GLY TYR LEU LYS GLY TYR SER GLY LYS ARG TYR LYS SER
SEQRES 15 A 299 CYS SER ALA PHE ALA PRO ILE VAL ASN PRO SER ASN VAL
SEQRES 16 A 299 PRO ILE GLY GLN LYS ALA PHE LYS GLY TYR LEU GLY GLU
SEQRES 17 A 299 GLU LYS ALA GLN TRP GLU ALA TYR ASP PRO CYS LEU LEU
SEQRES 18 A 299 ILE LYS ASN ILE ARG HIS VAL GLY ASP ASP ARG ILE LEU
SEQRES 19 A 299 ILE HIS VAL GLY ASP SER ASP PRO PHE LEU GLU GLU HIS
SEQRES 20 A 299 LEU LYS PRO GLU LEU LEU LEU GLU ALA VAL LYS ALA THR
SEQRES 21 A 299 SER TRP GLN ASP TYR VAL GLU ILE LYS LYS VAL HIS GLY
SEQRES 22 A 299 PHE ASP HIS SER TYR TYR PHE VAL SER THR PHE VAL PRO
SEQRES 23 A 299 GLU HIS ALA GLU PHE HIS ALA ARG ASN LEU GLY LEU ILE
MODRES 3C6B CSO A 60 CYS S-HYDROXYCYSTEINE
MODRES 3C6B SDP A 161 SER
HET CSO A 60 7
HET SDP A 161 14
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM SDP 2-AMINO-3-(DIETHOXY-PHOSPHORYLOXY)-PROPIONIC ACID
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 1 SDP C7 H16 N O6 P
FORMUL 2 HOH *40(H2 O)
HELIX 1 1 PRO A 35 ALA A 40 1 6
HELIX 2 2 PRO A 62 ALA A 69 1 8
HELIX 3 3 PHE A 70 GLY A 79 1 10
HELIX 4 4 PRO A 118 HIS A 122 5 5
HELIX 5 5 GLN A 124 LYS A 131 1 8
HELIX 6 6 LYS A 131 ASN A 142 1 12
HELIX 7 7 SDP A 161 GLY A 174 1 14
HELIX 8 8 ASN A 191 ASN A 194 5 4
HELIX 9 9 VAL A 195 GLY A 207 1 13
HELIX 10 10 TRP A 213 TYR A 216 5 4
HELIX 11 11 ASP A 217 ILE A 222 1 6
HELIX 12 12 LYS A 223 ILE A 225 5 3
HELIX 13 13 PRO A 250 VAL A 257 1 8
HELIX 14 14 TRP A 262 ASP A 264 5 3
HELIX 15 15 SER A 277 LEU A 296 1 20
SHEET 1 A 9 LYS A 2 VAL A 9 0
SHEET 2 A 9 GLY A 12 ASN A 20 -1 O LYS A 16 N LYS A 5
SHEET 3 A 9 SER A 27 LEU A 34 -1 O ILE A 32 N ILE A 15
SHEET 4 A 9 ALA A 81 PHE A 84 -1 O PHE A 84 N ASN A 31
SHEET 5 A 9 ILE A 49 LEU A 55 1 N VAL A 52 O ALA A 81
SHEET 6 A 9 LEU A 149 GLY A 159 1 O ASP A 150 N ILE A 49
SHEET 7 A 9 SER A 182 PHE A 186 1 O PHE A 186 N GLY A 159
SHEET 8 A 9 ILE A 233 GLY A 238 1 O HIS A 236 N ALA A 185
SHEET 9 A 9 VAL A 266 VAL A 271 1 O LYS A 269 N ILE A 235
LINK C THR A 59 N CSO A 60 1555 1555 1.34
LINK C CSO A 60 N THR A 61 1555 1555 1.32
LINK C HIS A 160 N SDP A 161 1555 1555 1.39
LINK C SDP A 161 N MET A 162 1555 1555 1.42
CISPEP 1 GLU A 117 PRO A 118 0 10.30
CRYST1 57.902 68.990 78.993 90.00 92.58 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 0.017271 0.000000 0.000778 0.00000
SCALE2 0.000000 0.014495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012672 0.00000
TER 2343 ILE A 299
MASTER 318 0 2 15 9 0 0 6 2382 1 25 23
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