Header
HEADER LYASE 01-FEB-07 2OR2
TITLE STRUCTURE OF THE W47A/W242A MUTANT OF BACTERIAL
TITLE 2 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-PHOSPHATIDYLINOSITOL PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHATIDYLINOSITOL DIACYLGLYCEROL-LYASE,
COMPND 5 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C, PI-PLC;
COMPND 6 EC: 4.6.1.13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THURINGIENSIS;
SOURCE 3 ORGANISM_TAXID: 1428;
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_VECTOR_TYPE: PLASMID
KEYWDS PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C, PI-PLC,
KEYWDS 2 DIMER, INTERFACIALLY IMPAIRED, MEMBRANE BINDING, TIM BARREL,
KEYWDS 3 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SHAO,X.SHI,H.WEHBI,C.ZAMBONELLI,J.F.HEAD,B.A.SEATON,
AUTHOR 2 M.F.ROBERTS
REVDAT 3 24-FEB-09 2OR2 1 VERSN
REVDAT 2 29-MAY-07 2OR2 1 JRNL
REVDAT 1 13-FEB-07 2OR2 0
JRNL AUTH C.SHAO,X.SHI,H.WEHBI,C.ZAMBONELLI,J.F.HEAD,
JRNL AUTH 2 B.A.SEATON,M.F.ROBERTS
JRNL TITL DIMER STRUCTURE OF AN INTERFACIALLY IMPAIRED
JRNL TITL 2 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C.
JRNL REF J.BIOL.CHEM. V. 282 9228 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17213187
JRNL DOI 10.1074/JBC.M610918200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.84 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 58605
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 4788
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 576
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.30600
REMARK 3 B22 (A**2) : 0.73200
REMARK 3 B33 (A**2) : 7.57300
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) : 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) : 1.323 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.093 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.937 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.884 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 42.41
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OR2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60615
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.15800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% 2-METHYL-2,4-PENTANEDIOL, 16%
REMARK 280 PEG400, PH 5.4, VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 32.21200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.06900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.01400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.06900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.21200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.01400
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE TWO MONOMERS
REMARK 300 IN THE ASYMMETRIC UNIT. THE TWO MONOMERS FOLLOW A PSEUDO 2-FOLD
REMARK 300 SYMMETRY
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 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 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 LYS A 12 29.76 -140.96
REMARK 500 TYR A 136 -55.76 -129.08
REMARK 500 GLU A 146 -138.22 -128.76
REMARK 500 ILE A 149 126.08 -39.43
REMARK 500 VAL A 188 -61.61 -99.19
REMARK 500 LYS A 201 48.38 -140.33
REMARK 500 ASN A 243 76.03 -66.09
REMARK 500 TYR A 275 72.64 45.34
REMARK 500 SER B 2 41.41 -149.41
REMARK 500 LYS B 12 31.38 -143.19
REMARK 500 PRO B 106 -7.87 -59.50
REMARK 500 TYR B 136 -55.67 -123.89
REMARK 500 GLU B 146 -134.84 -129.97
REMARK 500 VAL B 188 -71.27 -116.70
REMARK 500 SER B 237 111.99 -26.12
REMARK 500 TYR B 275 72.60 44.63
REMARK 500 ASN B 277 -166.65 -161.46
REMARK 500 ALA B 291 0.12 -69.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2OR2 A 1 296 UNP P08954 PLC_BACTU 32 327
DBREF 2OR2 B 1 296 UNP P08954 PLC_BACTU 32 327
SEQADV 2OR2 ALA A 47 UNP P08954 TRP 78 ENGINEERED
SEQADV 2OR2 ALA A 242 UNP P08954 TRP 273 ENGINEERED
SEQADV 2OR2 ALA B 47 UNP P08954 TRP 78 ENGINEERED
SEQADV 2OR2 ALA B 242 UNP P08954 TRP 273 ENGINEERED
SEQRES 1 A 296 ALA SER SER VAL ASN GLU LEU GLU ASN TRP SER LYS TRP
SEQRES 2 A 296 MET GLN PRO ILE PRO ASP ASN ILE PRO LEU ALA ARG ILE
SEQRES 3 A 296 SER ILE PRO GLY THR HIS ASP SER GLY THR PHE LYS LEU
SEQRES 4 A 296 GLN ASN PRO ILE LYS GLN VAL ALA GLY MET THR GLN GLU
SEQRES 5 A 296 TYR ASP PHE ARG TYR GLN MET ASP HIS GLY ALA ARG ILE
SEQRES 6 A 296 PHE ASP ILE ARG GLY ARG LEU THR ASP ASP ASN THR ILE
SEQRES 7 A 296 VAL LEU HIS HIS GLY PRO LEU TYR LEU TYR VAL THR LEU
SEQRES 8 A 296 HIS GLU PHE ILE ASN GLU ALA LYS GLN PHE LEU LYS ASP
SEQRES 9 A 296 ASN PRO SER GLU THR ILE ILE MET SER LEU LYS LYS GLU
SEQRES 10 A 296 TYR GLU ASP MET LYS GLY ALA GLU GLY SER PHE SER SER
SEQRES 11 A 296 THR PHE GLU LYS ASN TYR PHE VAL ASP PRO ILE PHE LEU
SEQRES 12 A 296 LYS THR GLU GLY ASN ILE LYS LEU GLY ASP ALA ARG GLY
SEQRES 13 A 296 LYS ILE VAL LEU LEU LYS ARG TYR SER GLY SER ASN GLU
SEQRES 14 A 296 SER GLY GLY TYR ASN ASN PHE TYR TRP PRO ASP ASN GLU
SEQRES 15 A 296 THR PHE THR THR THR VAL ASN GLN ASN VAL ASN VAL THR
SEQRES 16 A 296 VAL GLN ASP LYS TYR LYS VAL ASN TYR ASP GLU LYS VAL
SEQRES 17 A 296 LYS SER ILE LYS ASP THR MET ASP GLU THR MET ASN ASN
SEQRES 18 A 296 SER GLU ASP LEU ASN HIS LEU TYR ILE ASN PHE THR SER
SEQRES 19 A 296 LEU SER SER GLY GLY THR ALA ALA ASN SER PRO TYR TYR
SEQRES 20 A 296 TYR ALA SER TYR ILE ASN PRO GLU ILE ALA ASN ASP ILE
SEQRES 21 A 296 LYS GLN LYS ASN PRO THR ARG VAL GLY TRP VAL ILE GLN
SEQRES 22 A 296 ASP TYR ILE ASN GLU LYS TRP SER PRO LEU LEU TYR GLN
SEQRES 23 A 296 GLU VAL ILE ARG ALA ASN LYS SER LEU ILE
SEQRES 1 B 296 ALA SER SER VAL ASN GLU LEU GLU ASN TRP SER LYS TRP
SEQRES 2 B 296 MET GLN PRO ILE PRO ASP ASN ILE PRO LEU ALA ARG ILE
SEQRES 3 B 296 SER ILE PRO GLY THR HIS ASP SER GLY THR PHE LYS LEU
SEQRES 4 B 296 GLN ASN PRO ILE LYS GLN VAL ALA GLY MET THR GLN GLU
SEQRES 5 B 296 TYR ASP PHE ARG TYR GLN MET ASP HIS GLY ALA ARG ILE
SEQRES 6 B 296 PHE ASP ILE ARG GLY ARG LEU THR ASP ASP ASN THR ILE
SEQRES 7 B 296 VAL LEU HIS HIS GLY PRO LEU TYR LEU TYR VAL THR LEU
SEQRES 8 B 296 HIS GLU PHE ILE ASN GLU ALA LYS GLN PHE LEU LYS ASP
SEQRES 9 B 296 ASN PRO SER GLU THR ILE ILE MET SER LEU LYS LYS GLU
SEQRES 10 B 296 TYR GLU ASP MET LYS GLY ALA GLU GLY SER PHE SER SER
SEQRES 11 B 296 THR PHE GLU LYS ASN TYR PHE VAL ASP PRO ILE PHE LEU
SEQRES 12 B 296 LYS THR GLU GLY ASN ILE LYS LEU GLY ASP ALA ARG GLY
SEQRES 13 B 296 LYS ILE VAL LEU LEU LYS ARG TYR SER GLY SER ASN GLU
SEQRES 14 B 296 SER GLY GLY TYR ASN ASN PHE TYR TRP PRO ASP ASN GLU
SEQRES 15 B 296 THR PHE THR THR THR VAL ASN GLN ASN VAL ASN VAL THR
SEQRES 16 B 296 VAL GLN ASP LYS TYR LYS VAL ASN TYR ASP GLU LYS VAL
SEQRES 17 B 296 LYS SER ILE LYS ASP THR MET ASP GLU THR MET ASN ASN
SEQRES 18 B 296 SER GLU ASP LEU ASN HIS LEU TYR ILE ASN PHE THR SER
SEQRES 19 B 296 LEU SER SER GLY GLY THR ALA ALA ASN SER PRO TYR TYR
SEQRES 20 B 296 TYR ALA SER TYR ILE ASN PRO GLU ILE ALA ASN ASP ILE
SEQRES 21 B 296 LYS GLN LYS ASN PRO THR ARG VAL GLY TRP VAL ILE GLN
SEQRES 22 B 296 ASP TYR ILE ASN GLU LYS TRP SER PRO LEU LEU TYR GLN
SEQRES 23 B 296 GLU VAL ILE ARG ALA ASN LYS SER LEU ILE
FORMUL 3 HOH *576(H2 O)
HELIX 1 1 SER A 3 ASN A 9 5 7
HELIX 2 2 ASP A 33 GLY A 35 5 3
HELIX 3 3 THR A 36 ASN A 41 1 6
HELIX 4 4 PRO A 42 GLN A 45 5 4
HELIX 5 5 ASP A 54 HIS A 61 1 8
HELIX 6 6 LEU A 91 ASN A 105 1 15
HELIX 7 7 SER A 127 TYR A 136 1 10
HELIX 8 8 LYS A 150 ARG A 155 1 6
HELIX 9 9 ASN A 203 ASN A 221 1 19
HELIX 10 10 SER A 244 ASN A 264 1 21
HELIX 11 11 LEU A 283 ALA A 291 1 9
HELIX 12 12 ASN A 292 ILE A 296 5 5
HELIX 13 13 SER B 3 ASN B 9 5 7
HELIX 14 14 PRO B 22 ILE B 26 5 5
HELIX 15 15 ASP B 33 LEU B 39 5 7
HELIX 16 16 ASN B 41 GLN B 45 5 5
HELIX 17 17 ASP B 54 HIS B 61 1 8
HELIX 18 18 LEU B 91 ASN B 105 1 15
HELIX 19 19 SER B 127 TYR B 136 1 10
HELIX 20 20 LYS B 150 ARG B 155 1 6
HELIX 21 21 ASN B 203 ASN B 221 1 19
HELIX 22 22 SER B 244 ASN B 264 1 21
HELIX 23 23 LEU B 283 ALA B 291 1 9
HELIX 24 24 ASN B 292 ILE B 296 5 5
SHEET 1 A 5 LEU A 85 THR A 90 0
SHEET 2 A 5 ILE A 78 HIS A 82 -1 N LEU A 80 O VAL A 89
SHEET 3 A 5 ILE A 65 LEU A 72 -1 N ARG A 69 O HIS A 81
SHEET 4 A 5 ILE A 110 LYS A 116 1 O LYS A 115 N GLY A 70
SHEET 5 A 5 ILE A 158 ARG A 163 1 O VAL A 159 N ILE A 110
SHEET 1 B 8 LEU A 85 THR A 90 0
SHEET 2 B 8 ILE A 78 HIS A 82 -1 N LEU A 80 O VAL A 89
SHEET 3 B 8 ILE A 65 LEU A 72 -1 N ARG A 69 O HIS A 81
SHEET 4 B 8 ILE A 28 THR A 31 1 N THR A 31 O ILE A 65
SHEET 5 B 8 TRP A 270 GLN A 273 1 O GLN A 273 N GLY A 30
SHEET 6 B 8 HIS A 227 PHE A 232 1 N TYR A 229 O TRP A 270
SHEET 7 B 8 VAL A 192 GLN A 197 1 N ASN A 193 O LEU A 228
SHEET 8 B 8 THR A 183 ASN A 189 -1 N THR A 186 O VAL A 194
SHEET 1 C 5 LEU B 85 THR B 90 0
SHEET 2 C 5 ILE B 78 HIS B 82 -1 N LEU B 80 O VAL B 89
SHEET 3 C 5 ILE B 65 LEU B 72 -1 N ARG B 69 O HIS B 81
SHEET 4 C 5 ILE B 110 LYS B 116 1 O SER B 113 N PHE B 66
SHEET 5 C 5 ILE B 158 ARG B 163 1 O VAL B 159 N ILE B 110
SHEET 1 D 8 LEU B 85 THR B 90 0
SHEET 2 D 8 ILE B 78 HIS B 82 -1 N LEU B 80 O VAL B 89
SHEET 3 D 8 ILE B 65 LEU B 72 -1 N ARG B 69 O HIS B 81
SHEET 4 D 8 ILE B 28 THR B 31 1 N THR B 31 O ILE B 65
SHEET 5 D 8 TRP B 270 GLN B 273 1 O GLN B 273 N GLY B 30
SHEET 6 D 8 HIS B 227 PHE B 232 1 N ASN B 231 O TRP B 270
SHEET 7 D 8 VAL B 192 GLN B 197 1 N ASN B 193 O LEU B 228
SHEET 8 D 8 THR B 183 ASN B 189 -1 N THR B 186 O VAL B 194
CISPEP 1 SER A 281 PRO A 282 0 -0.18
CISPEP 2 SER B 281 PRO B 282 0 -0.25
CRYST1 64.424 70.028 154.138 90.00 90.00 90.00 P 21 21 21 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 0.015522 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006488 0.00000
TITLE STRUCTURE OF THE W47A/W242A MUTANT OF BACTERIAL
TITLE 2 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1-PHOSPHATIDYLINOSITOL PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHATIDYLINOSITOL DIACYLGLYCEROL-LYASE,
COMPND 5 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C, PI-PLC;
COMPND 6 EC: 4.6.1.13;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THURINGIENSIS;
SOURCE 3 ORGANISM_TAXID: 1428;
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_VECTOR_TYPE: PLASMID
KEYWDS PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C, PI-PLC,
KEYWDS 2 DIMER, INTERFACIALLY IMPAIRED, MEMBRANE BINDING, TIM BARREL,
KEYWDS 3 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SHAO,X.SHI,H.WEHBI,C.ZAMBONELLI,J.F.HEAD,B.A.SEATON,
AUTHOR 2 M.F.ROBERTS
REVDAT 3 24-FEB-09 2OR2 1 VERSN
REVDAT 2 29-MAY-07 2OR2 1 JRNL
REVDAT 1 13-FEB-07 2OR2 0
JRNL AUTH C.SHAO,X.SHI,H.WEHBI,C.ZAMBONELLI,J.F.HEAD,
JRNL AUTH 2 B.A.SEATON,M.F.ROBERTS
JRNL TITL DIMER STRUCTURE OF AN INTERFACIALLY IMPAIRED
JRNL TITL 2 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C.
JRNL REF J.BIOL.CHEM. V. 282 9228 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17213187
JRNL DOI 10.1074/JBC.M610918200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.84 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 58605
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 4788
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 576
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.30600
REMARK 3 B22 (A**2) : 0.73200
REMARK 3 B33 (A**2) : 7.57300
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) : 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) : 1.323 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.093 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.937 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.884 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 42.41
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OR2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60615
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.15800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% 2-METHYL-2,4-PENTANEDIOL, 16%
REMARK 280 PEG400, PH 5.4, VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 32.21200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.06900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.01400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.06900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.21200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.01400
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE TWO MONOMERS
REMARK 300 IN THE ASYMMETRIC UNIT. THE TWO MONOMERS FOLLOW A PSEUDO 2-FOLD
REMARK 300 SYMMETRY
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 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 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 LYS A 12 29.76 -140.96
REMARK 500 TYR A 136 -55.76 -129.08
REMARK 500 GLU A 146 -138.22 -128.76
REMARK 500 ILE A 149 126.08 -39.43
REMARK 500 VAL A 188 -61.61 -99.19
REMARK 500 LYS A 201 48.38 -140.33
REMARK 500 ASN A 243 76.03 -66.09
REMARK 500 TYR A 275 72.64 45.34
REMARK 500 SER B 2 41.41 -149.41
REMARK 500 LYS B 12 31.38 -143.19
REMARK 500 PRO B 106 -7.87 -59.50
REMARK 500 TYR B 136 -55.67 -123.89
REMARK 500 GLU B 146 -134.84 -129.97
REMARK 500 VAL B 188 -71.27 -116.70
REMARK 500 SER B 237 111.99 -26.12
REMARK 500 TYR B 275 72.60 44.63
REMARK 500 ASN B 277 -166.65 -161.46
REMARK 500 ALA B 291 0.12 -69.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2OR2 A 1 296 UNP P08954 PLC_BACTU 32 327
DBREF 2OR2 B 1 296 UNP P08954 PLC_BACTU 32 327
SEQADV 2OR2 ALA A 47 UNP P08954 TRP 78 ENGINEERED
SEQADV 2OR2 ALA A 242 UNP P08954 TRP 273 ENGINEERED
SEQADV 2OR2 ALA B 47 UNP P08954 TRP 78 ENGINEERED
SEQADV 2OR2 ALA B 242 UNP P08954 TRP 273 ENGINEERED
SEQRES 1 A 296 ALA SER SER VAL ASN GLU LEU GLU ASN TRP SER LYS TRP
SEQRES 2 A 296 MET GLN PRO ILE PRO ASP ASN ILE PRO LEU ALA ARG ILE
SEQRES 3 A 296 SER ILE PRO GLY THR HIS ASP SER GLY THR PHE LYS LEU
SEQRES 4 A 296 GLN ASN PRO ILE LYS GLN VAL ALA GLY MET THR GLN GLU
SEQRES 5 A 296 TYR ASP PHE ARG TYR GLN MET ASP HIS GLY ALA ARG ILE
SEQRES 6 A 296 PHE ASP ILE ARG GLY ARG LEU THR ASP ASP ASN THR ILE
SEQRES 7 A 296 VAL LEU HIS HIS GLY PRO LEU TYR LEU TYR VAL THR LEU
SEQRES 8 A 296 HIS GLU PHE ILE ASN GLU ALA LYS GLN PHE LEU LYS ASP
SEQRES 9 A 296 ASN PRO SER GLU THR ILE ILE MET SER LEU LYS LYS GLU
SEQRES 10 A 296 TYR GLU ASP MET LYS GLY ALA GLU GLY SER PHE SER SER
SEQRES 11 A 296 THR PHE GLU LYS ASN TYR PHE VAL ASP PRO ILE PHE LEU
SEQRES 12 A 296 LYS THR GLU GLY ASN ILE LYS LEU GLY ASP ALA ARG GLY
SEQRES 13 A 296 LYS ILE VAL LEU LEU LYS ARG TYR SER GLY SER ASN GLU
SEQRES 14 A 296 SER GLY GLY TYR ASN ASN PHE TYR TRP PRO ASP ASN GLU
SEQRES 15 A 296 THR PHE THR THR THR VAL ASN GLN ASN VAL ASN VAL THR
SEQRES 16 A 296 VAL GLN ASP LYS TYR LYS VAL ASN TYR ASP GLU LYS VAL
SEQRES 17 A 296 LYS SER ILE LYS ASP THR MET ASP GLU THR MET ASN ASN
SEQRES 18 A 296 SER GLU ASP LEU ASN HIS LEU TYR ILE ASN PHE THR SER
SEQRES 19 A 296 LEU SER SER GLY GLY THR ALA ALA ASN SER PRO TYR TYR
SEQRES 20 A 296 TYR ALA SER TYR ILE ASN PRO GLU ILE ALA ASN ASP ILE
SEQRES 21 A 296 LYS GLN LYS ASN PRO THR ARG VAL GLY TRP VAL ILE GLN
SEQRES 22 A 296 ASP TYR ILE ASN GLU LYS TRP SER PRO LEU LEU TYR GLN
SEQRES 23 A 296 GLU VAL ILE ARG ALA ASN LYS SER LEU ILE
SEQRES 1 B 296 ALA SER SER VAL ASN GLU LEU GLU ASN TRP SER LYS TRP
SEQRES 2 B 296 MET GLN PRO ILE PRO ASP ASN ILE PRO LEU ALA ARG ILE
SEQRES 3 B 296 SER ILE PRO GLY THR HIS ASP SER GLY THR PHE LYS LEU
SEQRES 4 B 296 GLN ASN PRO ILE LYS GLN VAL ALA GLY MET THR GLN GLU
SEQRES 5 B 296 TYR ASP PHE ARG TYR GLN MET ASP HIS GLY ALA ARG ILE
SEQRES 6 B 296 PHE ASP ILE ARG GLY ARG LEU THR ASP ASP ASN THR ILE
SEQRES 7 B 296 VAL LEU HIS HIS GLY PRO LEU TYR LEU TYR VAL THR LEU
SEQRES 8 B 296 HIS GLU PHE ILE ASN GLU ALA LYS GLN PHE LEU LYS ASP
SEQRES 9 B 296 ASN PRO SER GLU THR ILE ILE MET SER LEU LYS LYS GLU
SEQRES 10 B 296 TYR GLU ASP MET LYS GLY ALA GLU GLY SER PHE SER SER
SEQRES 11 B 296 THR PHE GLU LYS ASN TYR PHE VAL ASP PRO ILE PHE LEU
SEQRES 12 B 296 LYS THR GLU GLY ASN ILE LYS LEU GLY ASP ALA ARG GLY
SEQRES 13 B 296 LYS ILE VAL LEU LEU LYS ARG TYR SER GLY SER ASN GLU
SEQRES 14 B 296 SER GLY GLY TYR ASN ASN PHE TYR TRP PRO ASP ASN GLU
SEQRES 15 B 296 THR PHE THR THR THR VAL ASN GLN ASN VAL ASN VAL THR
SEQRES 16 B 296 VAL GLN ASP LYS TYR LYS VAL ASN TYR ASP GLU LYS VAL
SEQRES 17 B 296 LYS SER ILE LYS ASP THR MET ASP GLU THR MET ASN ASN
SEQRES 18 B 296 SER GLU ASP LEU ASN HIS LEU TYR ILE ASN PHE THR SER
SEQRES 19 B 296 LEU SER SER GLY GLY THR ALA ALA ASN SER PRO TYR TYR
SEQRES 20 B 296 TYR ALA SER TYR ILE ASN PRO GLU ILE ALA ASN ASP ILE
SEQRES 21 B 296 LYS GLN LYS ASN PRO THR ARG VAL GLY TRP VAL ILE GLN
SEQRES 22 B 296 ASP TYR ILE ASN GLU LYS TRP SER PRO LEU LEU TYR GLN
SEQRES 23 B 296 GLU VAL ILE ARG ALA ASN LYS SER LEU ILE
FORMUL 3 HOH *576(H2 O)
HELIX 1 1 SER A 3 ASN A 9 5 7
HELIX 2 2 ASP A 33 GLY A 35 5 3
HELIX 3 3 THR A 36 ASN A 41 1 6
HELIX 4 4 PRO A 42 GLN A 45 5 4
HELIX 5 5 ASP A 54 HIS A 61 1 8
HELIX 6 6 LEU A 91 ASN A 105 1 15
HELIX 7 7 SER A 127 TYR A 136 1 10
HELIX 8 8 LYS A 150 ARG A 155 1 6
HELIX 9 9 ASN A 203 ASN A 221 1 19
HELIX 10 10 SER A 244 ASN A 264 1 21
HELIX 11 11 LEU A 283 ALA A 291 1 9
HELIX 12 12 ASN A 292 ILE A 296 5 5
HELIX 13 13 SER B 3 ASN B 9 5 7
HELIX 14 14 PRO B 22 ILE B 26 5 5
HELIX 15 15 ASP B 33 LEU B 39 5 7
HELIX 16 16 ASN B 41 GLN B 45 5 5
HELIX 17 17 ASP B 54 HIS B 61 1 8
HELIX 18 18 LEU B 91 ASN B 105 1 15
HELIX 19 19 SER B 127 TYR B 136 1 10
HELIX 20 20 LYS B 150 ARG B 155 1 6
HELIX 21 21 ASN B 203 ASN B 221 1 19
HELIX 22 22 SER B 244 ASN B 264 1 21
HELIX 23 23 LEU B 283 ALA B 291 1 9
HELIX 24 24 ASN B 292 ILE B 296 5 5
SHEET 1 A 5 LEU A 85 THR A 90 0
SHEET 2 A 5 ILE A 78 HIS A 82 -1 N LEU A 80 O VAL A 89
SHEET 3 A 5 ILE A 65 LEU A 72 -1 N ARG A 69 O HIS A 81
SHEET 4 A 5 ILE A 110 LYS A 116 1 O LYS A 115 N GLY A 70
SHEET 5 A 5 ILE A 158 ARG A 163 1 O VAL A 159 N ILE A 110
SHEET 1 B 8 LEU A 85 THR A 90 0
SHEET 2 B 8 ILE A 78 HIS A 82 -1 N LEU A 80 O VAL A 89
SHEET 3 B 8 ILE A 65 LEU A 72 -1 N ARG A 69 O HIS A 81
SHEET 4 B 8 ILE A 28 THR A 31 1 N THR A 31 O ILE A 65
SHEET 5 B 8 TRP A 270 GLN A 273 1 O GLN A 273 N GLY A 30
SHEET 6 B 8 HIS A 227 PHE A 232 1 N TYR A 229 O TRP A 270
SHEET 7 B 8 VAL A 192 GLN A 197 1 N ASN A 193 O LEU A 228
SHEET 8 B 8 THR A 183 ASN A 189 -1 N THR A 186 O VAL A 194
SHEET 1 C 5 LEU B 85 THR B 90 0
SHEET 2 C 5 ILE B 78 HIS B 82 -1 N LEU B 80 O VAL B 89
SHEET 3 C 5 ILE B 65 LEU B 72 -1 N ARG B 69 O HIS B 81
SHEET 4 C 5 ILE B 110 LYS B 116 1 O SER B 113 N PHE B 66
SHEET 5 C 5 ILE B 158 ARG B 163 1 O VAL B 159 N ILE B 110
SHEET 1 D 8 LEU B 85 THR B 90 0
SHEET 2 D 8 ILE B 78 HIS B 82 -1 N LEU B 80 O VAL B 89
SHEET 3 D 8 ILE B 65 LEU B 72 -1 N ARG B 69 O HIS B 81
SHEET 4 D 8 ILE B 28 THR B 31 1 N THR B 31 O ILE B 65
SHEET 5 D 8 TRP B 270 GLN B 273 1 O GLN B 273 N GLY B 30
SHEET 6 D 8 HIS B 227 PHE B 232 1 N ASN B 231 O TRP B 270
SHEET 7 D 8 VAL B 192 GLN B 197 1 N ASN B 193 O LEU B 228
SHEET 8 D 8 THR B 183 ASN B 189 -1 N THR B 186 O VAL B 194
CISPEP 1 SER A 281 PRO A 282 0 -0.18
CISPEP 2 SER B 281 PRO B 282 0 -0.25
CRYST1 64.424 70.028 154.138 90.00 90.00 90.00 P 21 21 21 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 0.015522 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006488 0.00000
