HEADER HYDROLASE 20-APR-10 3MMJ
TITLE STRUCTURE OF THE PTP-LIKE PHYTASE FROM SELENOMONAS RUMINANTIUM IN
TITLE 2 COMPLEX WITH MYO-INOSITOL HEXAKISPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYO-INOSITOL HEXAPHOSPHATE PHOSPHOHYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SELENOMONAS RUMINANTIUM;
SOURCE 3 ORGANISM_TAXID: 971;
SOURCE 4 STRAIN: JY35;
SOURCE 5 GENE: PHYA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PHYTASE, PROTEIN TYROSINE PHOSPHATASE, INOSITOL PHOSPHATE, INOSITOL
KEYWDS 2 PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,L.B.SELINGER,S.C.MOSIMANN
REVDAT 5 06-SEP-23 3MMJ 1 REMARK
REVDAT 4 06-OCT-21 3MMJ 1 SEQADV
REVDAT 3 14-OCT-20 3MMJ 1 REMARK HETSYN
REVDAT 2 17-APR-13 3MMJ 1 JRNL VERSN
REVDAT 1 15-JUN-11 3MMJ 0
JRNL AUTH R.J.GRUNINGER,S.DOBING,A.D.SMITH,L.M.BRUDER,L.B.SELINGER,
JRNL AUTH 2 H.J.WIEDEN,S.C.MOSIMANN
JRNL TITL SUBSTRATE BINDING IN PROTEIN-TYROSINE PHOSPHATASE-LIKE
JRNL TITL 2 INOSITOL POLYPHOSPHATASES.
JRNL REF J.BIOL.CHEM. V. 287 9722 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22139834
JRNL DOI 10.1074/JBC.M111.309872
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
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) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 120565
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) : 0.177
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 6015
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 : 5103
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 129
REMARK 3 SOLVENT ATOMS : 885
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.29800
REMARK 3 B22 (A**2) : -2.74300
REMARK 3 B33 (A**2) : 4.04200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.46100
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 : ISOTROPIC
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 3MMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : KHOZU DOUBLE FLAT CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120565
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 51.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.76100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: 2B4U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-10% PEG8000, 200-300 NACL, 50 MM
REMARK 280 SODIUM ACETATE, PH 4.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 68.47500
REMARK 290 SMTRY3 2 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: 5970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
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 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 B 33
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 GLN A 33 CG CD OE1 NE2
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 PHE A 54 -6.79 -142.45
REMARK 500 HIS A 224 -5.72 76.39
REMARK 500 SER A 252 -144.91 -135.03
REMARK 500 VAL A 256 -84.72 -114.65
REMARK 500 PHE B 54 -6.07 -143.33
REMARK 500 HIS B 224 -6.75 79.25
REMARK 500 SER B 252 -141.87 -135.57
REMARK 500 VAL B 256 -83.89 -114.04
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 IHP A 1900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IHP B 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B4U RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C252S MUTANT OF SELENOMONAS RUMINANTIUM PTP-LIKE
REMARK 900 PHYTASE
DBREF 3MMJ A 33 346 UNP Q7WUJ1 Q7WUJ1_SELRU 33 346
DBREF 3MMJ B 33 346 UNP Q7WUJ1 Q7WUJ1_SELRU 33 346
SEQADV 3MMJ SER A 252 UNP Q7WUJ1 CYS 252 ENGINEERED MUTATION
SEQADV 3MMJ SER B 252 UNP Q7WUJ1 CYS 252 ENGINEERED MUTATION
SEQRES 1 A 314 GLN THR VAL THR GLU PRO VAL GLY SER TYR ALA ARG ALA
SEQRES 2 A 314 GLU ARG PRO GLN ASP PHE GLU GLY PHE VAL TRP ARG LEU
SEQRES 3 A 314 ASP ASN ASP GLY LYS GLU ALA LEU PRO ARG ASN PHE ARG
SEQRES 4 A 314 THR SER ALA ASP ALA LEU ARG ALA PRO GLU LYS LYS PHE
SEQRES 5 A 314 HIS LEU ASP ALA ALA TYR VAL PRO SER ARG GLU GLY MET
SEQRES 6 A 314 ASP ALA LEU HIS ILE SER GLY SER SER ALA PHE THR PRO
SEQRES 7 A 314 ALA GLN LEU LYS ASN VAL ALA ALA LYS LEU ARG GLU LYS
SEQRES 8 A 314 THR ALA GLY PRO ILE TYR ASP VAL ASP LEU ARG GLN GLU
SEQRES 9 A 314 SER HIS GLY TYR LEU ASP GLY ILE PRO VAL SER TRP TYR
SEQRES 10 A 314 GLY GLU ARG ASP TRP ALA ASN LEU GLY LYS SER GLN HIS
SEQRES 11 A 314 GLU ALA LEU ALA ASP GLU ARG HIS ARG LEU HIS ALA ALA
SEQRES 12 A 314 LEU HIS LYS THR VAL TYR ILE ALA PRO LEU GLY LYS HIS
SEQRES 13 A 314 LYS LEU PRO GLU GLY GLY GLU VAL ARG ARG VAL GLN LYS
SEQRES 14 A 314 VAL GLN THR GLU GLN GLU VAL ALA GLU ALA ALA GLY MET
SEQRES 15 A 314 ARG TYR PHE ARG ILE ALA ALA THR ASP HIS VAL TRP PRO
SEQRES 16 A 314 THR PRO GLU ASN ILE ASP ARG PHE LEU ALA PHE TYR ARG
SEQRES 17 A 314 THR LEU PRO GLN ASP ALA TRP LEU HIS PHE HIS SER GLU
SEQRES 18 A 314 ALA GLY VAL GLY ARG THR THR ALA PHE MET VAL MET THR
SEQRES 19 A 314 ASP MET LEU LYS ASN PRO SER VAL SER LEU LYS ASP ILE
SEQRES 20 A 314 LEU TYR ARG GLN HIS GLU ILE GLY GLY PHE TYR TYR GLY
SEQRES 21 A 314 GLU PHE PRO ILE LYS THR LYS ASP LYS ASP SER TRP LYS
SEQRES 22 A 314 THR LYS TYR TYR ARG GLU LYS ILE VAL MET ILE GLU GLN
SEQRES 23 A 314 PHE TYR ARG TYR VAL GLN GLU ASN ARG ALA ASP GLY TYR
SEQRES 24 A 314 GLN THR PRO TRP SER VAL TRP LEU LYS SER HIS PRO ALA
SEQRES 25 A 314 LYS ALA
SEQRES 1 B 314 GLN THR VAL THR GLU PRO VAL GLY SER TYR ALA ARG ALA
SEQRES 2 B 314 GLU ARG PRO GLN ASP PHE GLU GLY PHE VAL TRP ARG LEU
SEQRES 3 B 314 ASP ASN ASP GLY LYS GLU ALA LEU PRO ARG ASN PHE ARG
SEQRES 4 B 314 THR SER ALA ASP ALA LEU ARG ALA PRO GLU LYS LYS PHE
SEQRES 5 B 314 HIS LEU ASP ALA ALA TYR VAL PRO SER ARG GLU GLY MET
SEQRES 6 B 314 ASP ALA LEU HIS ILE SER GLY SER SER ALA PHE THR PRO
SEQRES 7 B 314 ALA GLN LEU LYS ASN VAL ALA ALA LYS LEU ARG GLU LYS
SEQRES 8 B 314 THR ALA GLY PRO ILE TYR ASP VAL ASP LEU ARG GLN GLU
SEQRES 9 B 314 SER HIS GLY TYR LEU ASP GLY ILE PRO VAL SER TRP TYR
SEQRES 10 B 314 GLY GLU ARG ASP TRP ALA ASN LEU GLY LYS SER GLN HIS
SEQRES 11 B 314 GLU ALA LEU ALA ASP GLU ARG HIS ARG LEU HIS ALA ALA
SEQRES 12 B 314 LEU HIS LYS THR VAL TYR ILE ALA PRO LEU GLY LYS HIS
SEQRES 13 B 314 LYS LEU PRO GLU GLY GLY GLU VAL ARG ARG VAL GLN LYS
SEQRES 14 B 314 VAL GLN THR GLU GLN GLU VAL ALA GLU ALA ALA GLY MET
SEQRES 15 B 314 ARG TYR PHE ARG ILE ALA ALA THR ASP HIS VAL TRP PRO
SEQRES 16 B 314 THR PRO GLU ASN ILE ASP ARG PHE LEU ALA PHE TYR ARG
SEQRES 17 B 314 THR LEU PRO GLN ASP ALA TRP LEU HIS PHE HIS SER GLU
SEQRES 18 B 314 ALA GLY VAL GLY ARG THR THR ALA PHE MET VAL MET THR
SEQRES 19 B 314 ASP MET LEU LYS ASN PRO SER VAL SER LEU LYS ASP ILE
SEQRES 20 B 314 LEU TYR ARG GLN HIS GLU ILE GLY GLY PHE TYR TYR GLY
SEQRES 21 B 314 GLU PHE PRO ILE LYS THR LYS ASP LYS ASP SER TRP LYS
SEQRES 22 B 314 THR LYS TYR TYR ARG GLU LYS ILE VAL MET ILE GLU GLN
SEQRES 23 B 314 PHE TYR ARG TYR VAL GLN GLU ASN ARG ALA ASP GLY TYR
SEQRES 24 B 314 GLN THR PRO TRP SER VAL TRP LEU LYS SER HIS PRO ALA
SEQRES 25 B 314 LYS ALA
HET IHP A1900 36
HET PO4 A 1 5
HET ACT A1501 4
HET ACT A1503 4
HET GOL A 400 6
HET GOL A 401 6
HET IHP B1901 36
HET PO4 B 2 5
HET ACT B1500 4
HET ACT B1502 4
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET CL B2000 1
HETNAM IHP INOSITOL HEXAKISPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN IHP MYO-INOSITOL HEXAKISPHOSPHATE; INOSITOL 1,2,3,4,5,6-
HETSYN 2 IHP HEXAKISPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 IHP 2(C6 H18 O24 P6)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 ACT 4(C2 H3 O2 1-)
FORMUL 7 GOL 5(C3 H8 O3)
FORMUL 16 CL CL 1-
FORMUL 17 HOH *885(H2 O)
HELIX 1 1 SER A 41 GLU A 46 5 6
HELIX 2 2 ARG A 47 PHE A 51 5 5
HELIX 3 3 GLU A 81 HIS A 85 5 5
HELIX 4 4 GLY A 96 HIS A 101 1 6
HELIX 5 5 THR A 109 GLU A 122 1 14
HELIX 6 6 ARG A 152 TRP A 154 5 3
HELIX 7 7 SER A 160 LEU A 176 1 17
HELIX 8 8 GLY A 186 LEU A 190 5 5
HELIX 9 9 THR A 204 ALA A 212 1 9
HELIX 10 10 THR A 228 THR A 241 1 14
HELIX 11 11 VAL A 256 ASN A 271 1 16
HELIX 12 12 SER A 275 ILE A 286 1 12
HELIX 13 13 LYS A 299 SER A 303 5 5
HELIX 14 14 TRP A 304 ARG A 327 1 24
HELIX 15 15 PRO A 334 HIS A 342 1 9
HELIX 16 16 SER B 41 GLU B 46 5 6
HELIX 17 17 ARG B 47 GLU B 52 5 6
HELIX 18 18 GLU B 81 HIS B 85 5 5
HELIX 19 19 GLY B 96 HIS B 101 1 6
HELIX 20 20 THR B 109 GLU B 122 1 14
HELIX 21 21 GLY B 150 TRP B 154 5 5
HELIX 22 22 SER B 160 LEU B 176 1 17
HELIX 23 23 GLY B 186 LEU B 190 5 5
HELIX 24 24 THR B 204 ALA B 212 1 9
HELIX 25 25 THR B 228 LEU B 242 1 15
HELIX 26 26 VAL B 256 ASN B 271 1 16
HELIX 27 27 SER B 275 ILE B 286 1 12
HELIX 28 28 LYS B 299 TRP B 304 5 6
HELIX 29 29 LYS B 305 ARG B 327 1 23
HELIX 30 30 PRO B 334 HIS B 342 1 9
SHEET 1 A 6 GLU A 195 ARG A 198 0
SHEET 2 A 6 THR A 179 ALA A 183 -1 N VAL A 180 O ARG A 197
SHEET 3 A 6 GLY A 53 LEU A 58 1 N TRP A 56 O ALA A 183
SHEET 4 A 6 ILE A 144 GLY A 150 -1 O SER A 147 N ARG A 57
SHEET 5 A 6 HIS A 138 LEU A 141 -1 N GLY A 139 O VAL A 146
SHEET 6 A 6 VAL A 202 GLN A 203 -1 O GLN A 203 N TYR A 140
SHEET 1 B 5 ARG A 71 THR A 72 0
SHEET 2 B 5 ILE A 102 SER A 105 -1 O GLY A 104 N ARG A 71
SHEET 3 B 5 TRP A 247 HIS A 251 1 O PHE A 250 N SER A 103
SHEET 4 B 5 ILE A 128 ARG A 134 1 N VAL A 131 O HIS A 249
SHEET 5 B 5 ARG A 215 ALA A 221 1 O ARG A 215 N ASP A 130
SHEET 1 C 6 GLU B 195 ARG B 198 0
SHEET 2 C 6 THR B 179 ALA B 183 -1 N VAL B 180 O ARG B 197
SHEET 3 C 6 VAL B 55 LEU B 58 1 N TRP B 56 O ALA B 183
SHEET 4 C 6 ILE B 144 TYR B 149 -1 O SER B 147 N ARG B 57
SHEET 5 C 6 HIS B 138 LEU B 141 -1 N GLY B 139 O VAL B 146
SHEET 6 C 6 VAL B 202 GLN B 203 -1 O GLN B 203 N TYR B 140
SHEET 1 D 5 ARG B 71 THR B 72 0
SHEET 2 D 5 ILE B 102 SER B 105 -1 O GLY B 104 N ARG B 71
SHEET 3 D 5 TRP B 247 HIS B 251 1 O PHE B 250 N SER B 103
SHEET 4 D 5 ILE B 128 ARG B 134 1 N TYR B 129 O TRP B 247
SHEET 5 D 5 ARG B 215 ALA B 221 1 O ILE B 219 N ASP B 132
SITE 1 AC1 27 ARG A 57 ARG A 68 ASP A 153 LYS A 189
SITE 2 AC1 27 ASP A 223 HIS A 224 SER A 252 GLU A 253
SITE 3 AC1 27 ALA A 254 GLY A 255 VAL A 256 GLY A 257
SITE 4 AC1 27 ARG A 258 LYS A 305 TYR A 309 LYS A 312
SITE 5 AC1 27 GOL A 401 ACT A1501 HOH A2038 HOH A2060
SITE 6 AC1 27 HOH A2171 HOH A2254 HOH A2630 HOH A2631
SITE 7 AC1 27 HOH A2633 HOH A2638 HOH A2791
SITE 1 AC2 9 ASP A 223 SER A 252 GLU A 253 ALA A 254
SITE 2 AC2 9 GLY A 255 VAL A 256 GLY A 257 ARG A 258
SITE 3 AC2 9 HOH A2038
SITE 1 AC3 7 HIS A 224 LYS A 305 TYR A 308 TYR A 309
SITE 2 AC3 7 LYS A 312 IHP A1900 HOH A2254
SITE 1 AC4 5 TYR A 42 ARG A 310 GLU A 311 ALA A 346
SITE 2 AC4 5 HOH A2646
SITE 1 AC5 7 TYR A 239 PRO A 243 GLN A 244 LYS A 270
SITE 2 AC5 7 HOH A2064 HOH A2211 HOH A2498
SITE 1 AC6 6 LYS A 83 PHE A 289 PHE A 294 LYS A 297
SITE 2 AC6 6 IHP A1900 HOH A2639
SITE 1 AC7 27 ARG B 57 ARG B 68 ASP B 153 LYS B 189
SITE 2 AC7 27 ASP B 223 HIS B 224 SER B 252 GLU B 253
SITE 3 AC7 27 ALA B 254 GLY B 255 VAL B 256 GLY B 257
SITE 4 AC7 27 ARG B 258 LYS B 305 TYR B 309 LYS B 312
SITE 5 AC7 27 GOL B 403 ACT B1500 HOH B2026 HOH B2069
SITE 6 AC7 27 HOH B2183 HOH B2598 HOH B2627 HOH B2628
SITE 7 AC7 27 HOH B2629 HOH B2865 HOH B2885
SITE 1 AC8 9 ASP B 223 SER B 252 GLU B 253 ALA B 254
SITE 2 AC8 9 GLY B 255 VAL B 256 GLY B 257 ARG B 258
SITE 3 AC8 9 HOH B2069
SITE 1 AC9 7 HIS B 224 LYS B 305 TYR B 308 TYR B 309
SITE 2 AC9 7 LYS B 312 IHP B1901 HOH B2628
SITE 1 BC1 5 TYR B 42 ARG B 310 GLU B 311 ALA B 346
SITE 2 BC1 5 HOH B2407
SITE 1 BC2 8 TYR B 239 PRO B 243 GLN B 244 LYS B 270
SITE 2 BC2 8 GOL B 404 HOH B2035 HOH B2236 HOH B2370
SITE 1 BC3 8 LYS B 83 PHE B 289 PHE B 294 ILE B 296
SITE 2 BC3 8 LYS B 297 TYR B 309 IHP B1901 HOH B2821
SITE 1 BC4 6 THR B 34 LEU B 242 PRO B 243 GLN B 244
SITE 2 BC4 6 GOL B 402 HOH B2798
SITE 1 BC5 1 THR B 333
CRYST1 46.130 136.950 79.910 90.00 102.95 90.00 P 1 21 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 0.021678 0.000000 0.004985 0.00000
SCALE2 0.000000 0.007302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
