HEADER HYDROLASE 20-JUL-04 1U32
TITLE CRYSTAL STRUCTURE OF A PROTEIN PHOSPHATASE-1: CALCINEURIN HYBRID BOUND
TITLE 2 TO OKADAIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 6-298;
COMPND 6 SYNONYM: PROTEIN PHOSPHATASE-1: CALCINEURIN HYBRID, PP-1G, PROTEIN
COMPND 7 PHOSPHATASE 1C CATALYTIC SUBUNIT;
COMPND 8 EC: 3.1.3.16;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPP1CC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.MAYNES,K.R.PERREAULT,M.M.CHERNEY,H.A.LUU,M.N.G.JAMES,C.F.B.HOLMES
REVDAT 5 25-OCT-23 1U32 1 REMARK
REVDAT 4 10-NOV-21 1U32 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1U32 1 VERSN
REVDAT 2 19-OCT-04 1U32 1 JRNL
REVDAT 1 17-AUG-04 1U32 0
JRNL AUTH J.T.MAYNES,K.R.PERREAULT,M.M.CHERNEY,H.A.LUU,M.N.G.JAMES,
JRNL AUTH 2 C.F.B.HOLMES
JRNL TITL CRYSTAL STRUCTURE AND MUTAGENESIS OF A PROTEIN
JRNL TITL 2 PHOSPHATASE-1:CALCINEURIN HYBRID ELUCIDATE THE ROLE OF THE
JRNL TITL 3 {BETA}12-{BETA}13 LOOP IN INHIBITOR BINDING
JRNL REF J.BIOL.CHEM. V. 279 43198 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15280359
JRNL DOI 10.1074/JBC.M407184200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 36.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1946384.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 21272
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) : 0.218
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1250
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3254
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 199
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2371
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 37.25
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 : BME.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : DAM.PARAM
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : BME.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : DAM.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023182.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36900
REMARK 200 R SYM FOR SHELL (I) : 0.36000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.020
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 ID 1JK7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, TRIS, PEG 400,
REMARK 280 MERCAPTOETHANOL, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 49.37950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.37950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.09000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.37950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.37950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.09000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.37950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.37950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.09000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.37950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.37950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.09000
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 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: MONOMERIC
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 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 585 O HOH A 585 8666 1.20
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 ASP A 194 N - CA - C ANGL. DEV. = -17.6 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 ASP A 95 148.60 80.78
REMARK 500 ARG A 96 -48.94 71.31
REMARK 500 GLU A 126 50.54 -94.35
REMARK 500 TYR A 144 -110.44 -136.62
REMARK 500 GLU A 167 15.85 54.90
REMARK 500 SER A 224 -156.53 62.65
REMARK 500 ALA A 247 -123.19 -135.24
REMARK 500 HIS A 248 -28.46 73.46
REMARK 500 ASP A 274 -2.58 64.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HIS A 66 NE2 107.4
REMARK 620 3 ASP A 92 OD2 91.9 98.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 400 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 92 OD2
REMARK 620 2 ASN A 124 OD1 100.9
REMARK 620 3 HIS A 173 NE2 81.2 89.3
REMARK 620 4 HIS A 248 ND1 159.9 97.3 90.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OKA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 303
DBREF 1U32 A 6 298 UNP P36873 PP1G_HUMAN 6 298
SEQADV 1U32 LEU A 273 UNP P36873 CYS 273 ENGINEERED MUTATION
SEQADV 1U32 ASP A 274 UNP P36873 GLY 274 ENGINEERED MUTATION
SEQADV 1U32 VAL A 275 UNP P36873 GLU 275 ENGINEERED MUTATION
SEQADV 1U32 TYR A 276 UNP P36873 PHE 276 ENGINEERED MUTATION
SEQADV 1U32 ASN A 277 UNP P36873 ASP 277 ENGINEERED MUTATION
SEQRES 1 A 293 LYS LEU ASN ILE ASP SER ILE ILE GLN ARG LEU LEU GLU
SEQRES 2 A 293 VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN LEU GLN
SEQRES 3 A 293 GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER ARG GLU
SEQRES 4 A 293 ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU GLU ALA
SEQRES 5 A 293 PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN TYR TYR
SEQRES 6 A 293 ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE PRO PRO
SEQRES 7 A 293 GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL ASP ARG
SEQRES 8 A 293 GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU LEU ALA
SEQRES 9 A 293 TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU LEU ARG
SEQRES 10 A 293 GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE TYR GLY
SEQRES 11 A 293 PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE LYS LEU
SEQRES 12 A 293 TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU PRO ILE
SEQRES 13 A 293 ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS HIS GLY
SEQRES 14 A 293 GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN ILE ARG
SEQRES 15 A 293 ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN GLY LEU
SEQRES 16 A 293 LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS ASP VAL
SEQRES 17 A 293 LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER PHE THR
SEQRES 18 A 293 PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS LYS HIS
SEQRES 19 A 293 ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL VAL GLU
SEQRES 20 A 293 ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU VAL THR
SEQRES 21 A 293 LEU PHE SER ALA PRO ASN TYR LEU ASP VAL TYR ASN ASN
SEQRES 22 A 293 ALA GLY ALA MET MET SER VAL ASP GLU THR LEU MET CYS
SEQRES 23 A 293 SER PHE GLN ILE LEU LYS PRO
HET MN A 400 1
HET MN A 401 1
HET OKA A 501 57
HET BME A 301 4
HET BME A 302 4
HET BME A 303 4
HETNAM MN MANGANESE (II) ION
HETNAM OKA OKADAIC ACID
HETNAM BME BETA-MERCAPTOETHANOL
HETSYN OKA 9,10-DEEPITHIO-9,10-DIDEHYDROACANTHIFOLICIN
FORMUL 2 MN 2(MN 2+)
FORMUL 4 OKA C44 H68 O13
FORMUL 5 BME 3(C2 H6 O S)
FORMUL 8 HOH *89(H2 O)
HELIX 1 1 ASN A 8 GLU A 18 1 11
HELIX 2 2 GLN A 31 GLN A 49 1 19
HELIX 3 3 GLN A 68 GLY A 80 1 13
HELIX 4 4 GLN A 99 TYR A 114 1 16
HELIX 5 5 CYS A 127 ARG A 132 1 6
HELIX 6 6 GLY A 135 TYR A 144 1 10
HELIX 7 7 ASN A 145 ASN A 157 1 13
HELIX 8 8 SER A 182 ARG A 188 1 7
HELIX 9 9 GLY A 199 SER A 207 1 9
HELIX 10 10 GLY A 228 HIS A 239 1 12
HELIX 11 11 ASN A 271 VAL A 275 5 5
SHEET 1 A 6 LEU A 52 LEU A 55 0
SHEET 2 A 6 ALA A 162 VAL A 165 1 O ILE A 164 N LEU A 53
SHEET 3 A 6 ILE A 169 CYS A 171 -1 O CYS A 171 N ALA A 163
SHEET 4 A 6 LEU A 243 ARG A 246 1 O CYS A 245 N PHE A 170
SHEET 5 A 6 LEU A 263 LEU A 266 1 O LEU A 266 N ARG A 246
SHEET 6 A 6 TYR A 255 PHE A 258 -1 N GLU A 256 O THR A 265
SHEET 1 B 5 PHE A 118 LEU A 120 0
SHEET 2 B 5 TYR A 87 PHE A 89 1 N TYR A 87 O PHE A 119
SHEET 3 B 5 LEU A 59 CYS A 62 1 N CYS A 62 O LEU A 88
SHEET 4 B 5 GLY A 280 VAL A 285 -1 O MET A 283 N ILE A 61
SHEET 5 B 5 CYS A 291 LEU A 296 -1 O LEU A 296 N GLY A 280
SHEET 1 C 3 ASP A 208 PRO A 209 0
SHEET 2 C 3 PHE A 225 PHE A 227 1 O PHE A 227 N ASP A 208
SHEET 3 C 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
LINK SG CYS A 127 S2 BME A 303 1555 1555 2.03
LINK SG CYS A 202 S2 BME A 301 1555 1555 2.04
LINK SG CYS A 291 S2 BME A 302 1555 1555 2.03
LINK OD2 ASP A 64 MN MN A 401 1555 1555 2.09
LINK NE2 HIS A 66 MN MN A 401 1555 1555 2.28
LINK OD2 ASP A 92 MN MN A 400 1555 1555 2.20
LINK OD2 ASP A 92 MN MN A 401 1555 1555 2.22
LINK OD1 ASN A 124 MN MN A 400 1555 1555 2.17
LINK NE2 HIS A 173 MN MN A 400 1555 1555 2.26
LINK ND1 HIS A 248 MN MN A 400 1555 1555 2.27
CISPEP 1 ALA A 57 PRO A 58 0 -0.28
CISPEP 2 PRO A 82 PRO A 83 0 0.21
CISPEP 3 ARG A 191 PRO A 192 0 0.23
SITE 1 AC1 6 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC1 6 MN A 401 HOH A 505
SITE 1 AC2 4 ASP A 64 HIS A 66 ASP A 92 MN A 400
SITE 1 AC3 15 ARG A 96 HIS A 125 ILE A 130 TYR A 134
SITE 2 AC3 15 GLN A 181 ARG A 188 ARG A 221 LYS A 234
SITE 3 AC3 15 HIS A 237 TYR A 272 LEU A 273 TYR A 276
SITE 4 AC3 15 BME A 301 HOH A 556 HOH A 566
SITE 1 AC4 6 VAL A 195 CYS A 202 TRP A 206 HIS A 237
SITE 2 AC4 6 BME A 303 OKA A 501
SITE 1 AC5 3 ILE A 169 LEU A 289 CYS A 291
SITE 1 AC6 5 ARG A 122 CYS A 127 VAL A 195 TRP A 206
SITE 2 AC6 5 BME A 301
CRYST1 98.759 98.759 62.180 90.00 90.00 90.00 P 42 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 0.010126 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016082 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
