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HEADER HYDROLASE 02-JUN-03 1PJA
TITLE THE CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE-2
TITLE 2 REVEALS THE BASIS FOR DIVERGENT SUBSTRATE SPECIFICITIES OF
TITLE 3 THE TWO LYSOSOMAL THIOESTERASES (PPT1 AND PPT2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOYL-PROTEIN THIOESTERASE 2 PRECURSOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PALMITOYL- PROTEIN HYDROLASE 2, PPT-2, G14;
COMPND 5 EC: 3.1.2.22;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: PPT2;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE, GLYCOPROTEIN, LYSOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR G.CALERO,P.GUPTA,M.C.NONATO,S.TANDEL,E.R.BIEHL,S.L.HOFMANN,
AUTHOR 2 J.CLARDY
REVDAT 1 02-SEP-03 1PJA 0
JRNL AUTH G.CALERO,P.GUPTA,M.C.NONATO,S.TANDEL,E.R.BIEHL,
JRNL AUTH 2 S.L.HOFMANN,J.CLARDY
JRNL TITL THE CRYSTAL STRUCTURE OF PALMITOYL PROTEIN
JRNL TITL 2 THIOESTERASE-2 REVEALS THE BASIS FOR DIVERGENT
JRNL TITL 3 SUBSTRATE SPECIFICITIES OF THE TWO LYSOSOMAL
JRNL TITL 4 THIOESTERASES (PPT1 AND PPT2)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 27511
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) : 0.221
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 2161
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 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 1PJA COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-2003.
REMARK 100 THE RCSB ID CODE IS RCSB019357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-2.2M AMMONIUM SULFATE, 8%
REMARK 280 METHYL-PENTANE-DIOL, 100 MM MES , PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,2/3+Z
REMARK 290 6555 X-Y,X,1/3+Z
REMARK 290 7555 Y,X,2/3-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,1/3-Z
REMARK 290 10555 -Y,-X,2/3-Z
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,1/3-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 -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 101.67333
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 50.83667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 101.67333
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 50.83667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.67333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 50.83667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 101.67333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 50.83667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 LEU A 2
REMARK 465 GLY A 3
REMARK 465 LEU A 4
REMARK 465 TRP A 5
REMARK 465 GLY A 6
REMARK 465 GLN A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 TRP A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 17
REMARK 465 LEU A 18
REMARK 465 PRO A 19
REMARK 465 PHE A 20
REMARK 465 LEU A 21
REMARK 465 PRO A 22
REMARK 465 LEU A 23
REMARK 465 LEU A 24
REMARK 465 LEU A 25
REMARK 465 LEU A 26
REMARK 465 ALA A 27
REMARK 465 ALA A 28
REMARK 465 PRO A 29
REMARK 465 ALA A 30
REMARK 465 PRO A 31
REMARK 465 HIS A 32
REMARK 465 ARG A 33
REMARK 465 ALA A 34
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 N GLY A 76 O HOH 11 2.06
REMARK 500 NE2 HIS A 287 O HOH 47 2.15
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 OE2 GLU A 172 OE2 GLU A 172 10665 2.12
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 163 CB ARG A 163 CG 0.045
REMARK 500 ARG A 163 CG ARG A 163 CD 0.047
REMARK 500 ASN A 190 CG ASN A 190 ND2 -0.047
REMARK 500 HIS A 219 CB HIS A 219 CG 0.047
REMARK 500 PRO A 233 C TRP A 234 N 0.094
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 75 N - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 ILE A 108 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASP A 228 N - CA - C ANGL. DEV. =-14.8 DEGREES
REMARK 500 GLN A 235 OE1 - CD - NE2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLN A 235 CG - CD - NE2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP A 243 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 THR A 247 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 CYS A 296 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EI9 RELATED DB: PDB
REMARK 900 PALMITOYL PROTEIN THIOESTERASE-1 (PPT1) LYSOSOMAL
REMARK 900 THIOESTERASES
DBREF 1PJA A 1 302 SWS Q9UMR5 PPT2_HUMAN 1 302
SEQRES 1 A 302 MET LEU GLY LEU TRP GLY GLN ARG LEU PRO ALA ALA TRP
SEQRES 2 A 302 VAL LEU LEU LEU LEU PRO PHE LEU PRO LEU LEU LEU LEU
SEQRES 3 A 302 ALA ALA PRO ALA PRO HIS ARG ALA SER TYR LYS PRO VAL
SEQRES 4 A 302 ILE VAL VAL HIS GLY LEU PHE ASP SER SER TYR SER PHE
SEQRES 5 A 302 ARG HIS LEU LEU GLU TYR ILE ASN GLU THR HIS PRO GLY
SEQRES 6 A 302 THR VAL VAL THR VAL LEU ASP LEU PHE ASP GLY ARG GLU
SEQRES 7 A 302 SER LEU ARG PRO LEU TRP GLU GLN VAL GLN GLY PHE ARG
SEQRES 8 A 302 GLU ALA VAL VAL PRO ILE MET ALA LYS ALA PRO GLN GLY
SEQRES 9 A 302 VAL HIS LEU ILE CYS TYR SER GLN GLY GLY LEU VAL CYS
SEQRES 10 A 302 ARG ALA LEU LEU SER VAL MET ASP ASP HIS ASN VAL ASP
SEQRES 11 A 302 SER PHE ILE SER LEU SER SER PRO GLN MET GLY GLN TYR
SEQRES 12 A 302 GLY ASP THR ASP TYR LEU LYS TRP LEU PHE PRO THR SER
SEQRES 13 A 302 MET ARG SER ASN LEU TYR ARG ILE CYS TYR SER PRO TRP
SEQRES 14 A 302 GLY GLN GLU PHE SER ILE CYS ASN TYR TRP HIS ASP PRO
SEQRES 15 A 302 HIS HIS ASP ASP LEU TYR LEU ASN ALA SER SER PHE LEU
SEQRES 16 A 302 ALA LEU ILE ASN GLY GLU ARG ASP HIS PRO ASN ALA THR
SEQRES 17 A 302 VAL TRP ARG LYS ASN PHE LEU ARG VAL GLY HIS LEU VAL
SEQRES 18 A 302 LEU ILE GLY GLY PRO ASP ASP GLY VAL ILE THR PRO TRP
SEQRES 19 A 302 GLN SER SER PHE PHE GLY PHE TYR ASP ALA ASN GLU THR
SEQRES 20 A 302 VAL LEU GLU MET GLU GLU GLN LEU VAL TYR LEU ARG ASP
SEQRES 21 A 302 SER PHE GLY LEU LYS THR LEU LEU ALA ARG GLY ALA ILE
SEQRES 22 A 302 VAL ARG CYS PRO MET ALA GLY ILE SER HIS THR ALA TRP
SEQRES 23 A 302 HIS SER ASN ARG THR LEU TYR GLU THR CYS ILE GLU PRO
SEQRES 24 A 302 TRP LEU SER
HET NAG 2285 14
HET GOL 1614 6
HET GOL 1615 6
HET GOL 1616 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETSYN NAG NAG
FORMUL 2 NAG C8 H15 N1 O6
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *50(H2 O1)
HELIX 1 1 SER A 48 SER A 51 5 4
HELIX 2 2 PHE A 52 HIS A 63 1 12
HELIX 3 3 GLY A 76 ARG A 81 5 6
HELIX 4 4 PRO A 82 ALA A 101 1 20
HELIX 5 5 SER A 111 MET A 124 1 14
HELIX 6 6 THR A 146 PHE A 153 1 8
HELIX 7 7 MET A 157 TYR A 166 1 10
HELIX 8 8 TRP A 169 PHE A 173 5 5
HELIX 9 9 SER A 174 TRP A 179 5 6
HELIX 10 10 HIS A 184 SER A 192 1 9
HELIX 11 11 PHE A 194 ASN A 199 1 6
HELIX 12 12 ASN A 206 LEU A 215 1 10
HELIX 13 13 PRO A 233 PHE A 239 5 7
HELIX 14 14 GLU A 250 GLU A 253 5 4
HELIX 15 15 GLN A 254 ARG A 259 1 6
HELIX 16 16 GLY A 263 ARG A 270 1 8
HELIX 17 17 ASN A 289 ILE A 297 1 9
HELIX 18 18 GLU A 298 LEU A 301 5 4
SHEET 1 A 6 VAL A 68 VAL A 70 0
SHEET 2 A 6 VAL A 39 VAL A 42 1 N VAL A 39 O THR A 69
SHEET 3 A 6 VAL A 105 TYR A 110 1 O TYR A 110 N VAL A 42
SHEET 4 A 6 VAL A 129 LEU A 135 1 O ILE A 133 N LEU A 107
SHEET 5 A 6 HIS A 219 GLY A 224 1 O HIS A 219 N PHE A 132
SHEET 6 A 6 ILE A 273 PRO A 277 1 O CYS A 276 N LEU A 222
SHEET 1 B 2 PHE A 241 TYR A 242 0
SHEET 2 B 2 VAL A 248 LEU A 249 -1 O LEU A 249 N PHE A 241
SSBOND 1 CYS A 109 CYS A 117
SSBOND 2 CYS A 165 CYS A 176
SSBOND 3 CYS A 276 CYS A 296
CISPEP 1 THR A 232 PRO A 233 0 -0.37
CRYST1 148.520 148.520 152.510 90.00 90.00 120.00 P 62 2 2 12
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 0.006733 0.003887 0.000000 0.00000
SCALE2 0.000000 0.007775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006557 0.00000
TER 2162 SER A 302
MASTER 355 0 4 18 8 0 0 6 2243 1 38 24
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