HEADER HYDROLASE 14-JUL-08 3DT8
TITLE CRYSTAL STRUCTURE OF BOVIN BRAIN PLATELET ACTIVATING FACTOR
TITLE 2 ACETYLHYDROLASE COVALENTLY INHIBITED BY SARIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT
COMPND 3 ALPHA;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PAF ACETYLHYDROLASE 29 KDA SUBUNIT, PAF-AH 29 KDA SUBUNIT,
COMPND 6 PAF-AH SUBUNIT ALPHA, PAFAH SUBUNIT ALPHA;
COMPND 7 EC: 3.1.1.47;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 GENE: PAFAH1B3, PAFAHG;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PLATELET ACTIVATING FACTOR ACETYLHYDROLASE, PAF-AH IB, ALPHA-1
KEYWDS 2 SUBUNIT, LIS1, GROUP VIII PHOSPHOLIPASE A2, 26 KDA, SARIN,
KEYWDS 3 CYTOPLASM, HYDROLASE, LIPID DEGRADATION, PLATELET FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.EPSTEIN,U.SAMANTA,B.J.BAHNSON
REVDAT 5 30-AUG-23 3DT8 1 REMARK
REVDAT 4 20-OCT-21 3DT8 1 SEQADV
REVDAT 3 24-JUL-19 3DT8 1 REMARK LINK
REVDAT 2 25-OCT-17 3DT8 1 REMARK
REVDAT 1 12-MAY-09 3DT8 0
JRNL AUTH T.M.EPSTEIN,U.SAMANTA,S.D.KIRBY,D.M.CERASOLI,B.J.BAHNSON
JRNL TITL CRYSTAL STRUCTURES OF BRAIN GROUP-VIII PHOSPHOLIPASE A2 IN
JRNL TITL 2 NONAGED COMPLEXES WITH THE ORGANOPHOSPHORUS NERVE AGENTS
JRNL TITL 3 SOMAN AND SARIN.
JRNL REF BIOCHEMISTRY V. 48 3425 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19271773
JRNL DOI 10.1021/BI8023527
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.S.HO,L.SWENSON,U.DEREWENDA,L.SERRE,Y.WEI,Z.DAUTER,
REMARK 1 AUTH 2 M.HATTORI,T.ADACHI,J.AOKI,H.ARAI,K.INOUE,Z.S.DEREWENDA
REMARK 1 TITL BRAIN ACETYLHYDROLASE THAT INACTIVATES PLATELET-ACTIVATING
REMARK 1 TITL 2 FACTOR IS A G-PROTEIN-LIKE TRIMER
REMARK 1 REF NATURE V. 385 89 1997
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC OF CCP4I FOR FINAL REFINEMENT
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 21079
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1157
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1409
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1696
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.34000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.51000
REMARK 3 B12 (A**2) : -0.17000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.141
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.656
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1742 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2371 ; 1.443 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 211 ; 5.597 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;34.270 ;22.989
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 281 ;15.988 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.858 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 258 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1350 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 840 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1166 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 105 ; 0.114 ; 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): 25 ; 0.147 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.088 ; 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): 1088 ; 1.484 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1707 ; 1.778 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 730 ; 2.621 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 664 ; 4.191 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048458.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23181
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 70.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.57700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS, REFMAC OF CCP4I FOR FINAL REFINEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 1WAB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 24.26133
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 48.52267
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 48.52267
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 24.26133
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 THR A 217
REMARK 465 GLN A 218
REMARK 465 ASP A 219
REMARK 465 GLN A 220
REMARK 465 GLY A 221
REMARK 465 GLN A 222
REMARK 465 GLY A 223
REMARK 465 GLY A 224
REMARK 465 ALA A 225
REMARK 465 PRO A 226
REMARK 465 LEU A 227
REMARK 465 PRO A 228
REMARK 465 GLU A 229
REMARK 465 PRO A 230
REMARK 465 SER A 231
REMARK 465 PRO A 232
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 -116.95 -35.90
REMARK 500 HIS A 66 67.73 69.57
REMARK 500 HIS A 166 96.81 -161.93
REMARK 500 LEU A 194 -57.97 -146.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 54 SER A 55 -144.47
REMARK 500 SER A 55 GLU A 56 -37.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WAB RELATED DB: PDB
REMARK 900 SAME WILD TYPE PROTEIN
REMARK 900 RELATED ID: 3DT6 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH PARAOXON
REMARK 900 RELATED ID: 3DT9 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH SOMAN
DBREF 3DT8 A 1 232 UNP Q29460 PA1B3_BOVIN 1 232
SEQADV 3DT8 SER A 55 UNP Q29460 CYS 55 ENGINEERED MUTATION
SEQRES 1 A 232 MET SER GLY ASP GLU ASN PRO ALA SER LYS PRO THR PRO
SEQRES 2 A 232 VAL GLN ASP VAL GLN GLY ASP GLY ARG TRP MET SER LEU
SEQRES 3 A 232 HIS HIS ARG PHE VAL ALA ASP SER LYS ASP LYS GLU PRO
SEQRES 4 A 232 GLU VAL VAL PHE ILE GLY ASP SGB LEU VAL GLN LEU MET
SEQRES 5 A 232 HIS GLN SER GLU ILE TRP ARG GLU LEU PHE SER PRO LEU
SEQRES 6 A 232 HIS ALA LEU ASN PHE GLY ILE GLY GLY ASP SER THR GLN
SEQRES 7 A 232 HIS VAL LEU TRP ARG LEU GLU ASN GLY GLU LEU GLU HIS
SEQRES 8 A 232 ILE ARG PRO LYS ILE VAL VAL VAL TRP VAL GLY THR ASN
SEQRES 9 A 232 ASN HIS GLY HIS THR ALA GLU GLN VAL THR GLY GLY ILE
SEQRES 10 A 232 LYS ALA ILE VAL GLN LEU VAL ASN GLU ARG GLN PRO GLN
SEQRES 11 A 232 ALA ARG VAL VAL VAL LEU GLY LEU LEU PRO ARG GLY GLN
SEQRES 12 A 232 HIS PRO ASN PRO LEU ARG GLU LYS ASN ARG ARG VAL ASN
SEQRES 13 A 232 GLU LEU VAL ARG ALA ALA LEU ALA GLY HIS PRO ARG ALA
SEQRES 14 A 232 HIS PHE LEU ASP ALA ASP PRO GLY PHE VAL HIS SER ASP
SEQRES 15 A 232 GLY THR ILE SER HIS HIS ASP MET TYR ASP TYR LEU HIS
SEQRES 16 A 232 LEU SER ARG LEU GLY TYR THR PRO VAL CYS ARG ALA LEU
SEQRES 17 A 232 HIS SER LEU LEU LEU ARG LEU LEU THR GLN ASP GLN GLY
SEQRES 18 A 232 GLN GLY GLY ALA PRO LEU PRO GLU PRO SER PRO
MODRES 3DT8 SGB A 47 SER
HET SGB A 47 13
HETNAM SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE
FORMUL 1 SGB C7 H16 N O5 P
FORMUL 2 HOH *91(H2 O)
HELIX 1 1 ASN A 6 LYS A 10 5 5
HELIX 2 2 GLY A 21 LYS A 37 1 17
HELIX 3 3 ASP A 46 LEU A 51 1 6
HELIX 4 4 ILE A 57 PHE A 62 1 6
HELIX 5 5 SER A 63 LEU A 65 5 3
HELIX 6 6 SER A 76 ASN A 86 1 11
HELIX 7 7 THR A 109 GLN A 128 1 20
HELIX 8 8 ASN A 146 GLY A 165 1 20
HELIX 9 9 SER A 197 LEU A 216 1 20
SHEET 1 A 5 ALA A 67 GLY A 71 0
SHEET 2 A 5 VAL A 41 GLY A 45 1 N PHE A 43 O PHE A 70
SHEET 3 A 5 ILE A 96 TRP A 100 1 O VAL A 98 N VAL A 42
SHEET 4 A 5 ARG A 132 LEU A 136 1 O VAL A 134 N VAL A 99
SHEET 5 A 5 ALA A 169 LEU A 172 1 O HIS A 170 N VAL A 133
LINK C ASP A 46 N SGB A 47 1555 1555 1.33
LINK C SGB A 47 N LEU A 48 1555 1555 1.39
CRYST1 81.322 81.322 72.784 90.00 90.00 120.00 P 31 2 1 6
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 0.012297 0.007100 0.000000 0.00000
SCALE2 0.000000 0.014199 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013739 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
