HEADER HYDROLASE 09-AUG-06 2J17
TITLE PTYR BOUND FORM OF SDP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE YIL113W;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 17-198;
COMPND 5 SYNONYM: SDP-1;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: S288C / AB972;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: FB810;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS HYDROLASE, PROTEIN PHOSPHATASE, HYPOTHETICAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.BRIGGS,N.Q.MCDONALD
REVDAT 6 13-DEC-23 2J17 1 LINK
REVDAT 5 08-MAY-19 2J17 1 REMARK
REVDAT 4 28-FEB-18 2J17 1 JRNL
REVDAT 3 24-FEB-09 2J17 1 VERSN
REVDAT 2 29-MAY-07 2J17 1 JRNL
REVDAT 1 22-MAY-07 2J17 0
JRNL AUTH G.C.FOX,M.SHAFIQ,D.C.BRIGGS,P.P.KNOWLES,M.COLLISTER,
JRNL AUTH 2 M.J.DIDMON,V.MAKRANTONI,R.J.DICKINSON,S.HANRAHAN,N.TOTTY,
JRNL AUTH 3 M.J.STARK,S.M.KEYSE,N.Q.MCDONALD
JRNL TITL REDOX-MEDIATED SUBSTRATE RECOGNITION BY SDP1 DEFINES A NEW
JRNL TITL 2 GROUP OF TYROSINE PHOSPHATASES.
JRNL REF NATURE V. 447 487 2007
JRNL REFN ESSN 1476-4687
JRNL PMID 17495930
JRNL DOI 10.1038/NATURE05804
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10016
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 507
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) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 687
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : -0.13000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.377
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.290
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.845
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2382 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3245 ; 1.223 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 5.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 95 ;42.186 ;24.316
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 411 ;17.723 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.085 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 377 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1742 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1085 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1583 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 64 ; 0.138 ; 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): 23 ; 0.217 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.118 ; 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): 1496 ; 0.459 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2363 ; 0.813 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1014 ; 1.035 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 882 ; 1.743 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 47 A 105 6
REMARK 3 1 B 47 B 105 6
REMARK 3 2 A 120 A 196 6
REMARK 3 2 B 120 B 196 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1021 ; .38 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1021 ; 1.65 ; 10.00
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.DISORDER REGIONS AND ATOMS ARE OMITTED.
REMARK 4
REMARK 4 2J17 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029204.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.970
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10632
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.840
REMARK 200 RESOLUTION RANGE LOW (A) : 61.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: PDB ENTRY 2J16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 400, 0.1M HEPES, PH 7.5, 0.2M
REMARK 280 CACL2, 7MG/ML PROTEIN, 15MM PHOSPHOTYROSINE, 1:1 SITTING DROP
REMARK 280 VAPOUR DIFFUSION, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 108.78100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.83050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.83050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 163.17150
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.83050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.83050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.39050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.83050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.83050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 163.17150
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.83050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.83050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 54.39050
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 108.78100
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PQS
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 140 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 140 TO SER
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 SER A 17
REMARK 465 GLY A 18
REMARK 465 GLN A 19
REMARK 465 ARG A 20
REMARK 465 PRO A 21
REMARK 465 SER A 22
REMARK 465 LEU A 23
REMARK 465 PRO A 24
REMARK 465 MET A 25
REMARK 465 LEU A 26
REMARK 465 ALA A 27
REMARK 465 THR A 28
REMARK 465 ASP A 29
REMARK 465 GLU A 30
REMARK 465 ARG A 31
REMARK 465 SER A 32
REMARK 465 THR A 33
REMARK 465 ASP A 34
REMARK 465 LYS A 35
REMARK 465 GLU A 36
REMARK 465 SER A 37
REMARK 465 PRO A 38
REMARK 465 ASN A 39
REMARK 465 GLU A 40
REMARK 465 ASP A 41
REMARK 465 ARG A 42
REMARK 465 GLU A 43
REMARK 465 PHE A 44
REMARK 465 VAL A 45
REMARK 465 PRO A 46
REMARK 465 SER A 48
REMARK 465 SER A 49
REMARK 465 LEU A 50
REMARK 465 ASP A 51
REMARK 465 VAL A 52
REMARK 465 ARG A 53
REMARK 465 THR A 198
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 GLN B 19
REMARK 465 ARG B 20
REMARK 465 PRO B 21
REMARK 465 SER B 22
REMARK 465 LEU B 23
REMARK 465 PRO B 24
REMARK 465 MET B 25
REMARK 465 LEU B 26
REMARK 465 ALA B 27
REMARK 465 THR B 28
REMARK 465 ASP B 29
REMARK 465 GLU B 30
REMARK 465 ARG B 31
REMARK 465 SER B 32
REMARK 465 THR B 33
REMARK 465 ASP B 34
REMARK 465 LYS B 35
REMARK 465 GLU B 36
REMARK 465 SER B 37
REMARK 465 PRO B 38
REMARK 465 ASN B 39
REMARK 465 GLU B 40
REMARK 465 ASP B 41
REMARK 465 ARG B 42
REMARK 465 GLU B 43
REMARK 465 PHE B 44
REMARK 465 VAL B 45
REMARK 465 PRO B 46
REMARK 465 SER B 48
REMARK 465 SER B 49
REMARK 465 LEU B 50
REMARK 465 ASP B 51
REMARK 465 VAL B 52
REMARK 465 THR B 198
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 ARG A 54 CD NE CZ NH1 NH2
REMARK 470 LYS A 58 CD CE NZ
REMARK 470 ARG A 108 CZ NH1 NH2
REMARK 470 ARG A 133 NE CZ NH1 NH2
REMARK 470 LYS A 171 NZ
REMARK 470 ASP A 175 CG OD1 OD2
REMARK 470 LYS A 176 CD CE NZ
REMARK 470 LYS A 197 CA C O CB CG CD CE
REMARK 470 LYS A 197 NZ
REMARK 470 ARG B 53 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 54 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 108 NE CZ NH1 NH2
REMARK 470 ARG B 133 CD NE CZ NH1 NH2
REMARK 470 LYS B 197 CA C O CB CG CD CE
REMARK 470 LYS B 197 NZ
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 ILE A 55 -61.36 86.59
REMARK 500 GLU A 66 28.99 -74.99
REMARK 500 SER A 72 -162.44 -71.68
REMARK 500 ASN A 93 131.76 -39.33
REMARK 500 SER A 140 -142.09 -123.66
REMARK 500 SER A 145 -70.51 -104.95
REMARK 500 ARG B 54 73.91 49.29
REMARK 500 GLU B 66 40.89 -76.21
REMARK 500 SER B 72 -162.71 -73.22
REMARK 500 SER B 140 -147.51 -118.60
REMARK 500 SER B 145 -70.34 -122.69
REMARK 500 ASN B 178 75.66 -156.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PTR A 1199
REMARK 610 PTR B 1200
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 MG A1197 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 73 OE1
REMARK 620 2 GLU A 73 OE2 49.8
REMARK 620 3 ASN A 93 OD1 116.8 74.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1198 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 110 OE1
REMARK 620 2 HOH A2009 O 74.9
REMARK 620 3 HOH A2010 O 51.7 65.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1197 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 73 OE1
REMARK 620 2 GLU B 73 OE2 50.5
REMARK 620 3 ASN B 93 ND2 121.1 72.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1199 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 99 O
REMARK 620 2 PRO B 100 O 153.3
REMARK 620 3 PRO B 100 O 72.4 121.1
REMARK 620 4 VAL B 102 O 88.9 74.7 74.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1198 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 134 OE2
REMARK 620 2 HOH B2005 O 72.0
REMARK 620 3 HOH B2005 O 84.0 121.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTR A1199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTR B1200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2J16 RELATED DB: PDB
REMARK 900 APO & SULPHATE BOUND FORMS OF SDP-1
DBREF 2J17 A 17 198 UNP P40479 YIL3_YEAST 17 198
DBREF 2J17 B 17 198 UNP P40479 YIL3_YEAST 17 198
SEQADV 2J17 SER A 140 UNP P40479 CYS 140 ENGINEERED MUTATION
SEQADV 2J17 SER B 140 UNP P40479 CYS 140 ENGINEERED MUTATION
SEQRES 1 A 182 SER GLY GLN ARG PRO SER LEU PRO MET LEU ALA THR ASP
SEQRES 2 A 182 GLU ARG SER THR ASP LYS GLU SER PRO ASN GLU ASP ARG
SEQRES 3 A 182 GLU PHE VAL PRO CYS SER SER LEU ASP VAL ARG ARG ILE
SEQRES 4 A 182 TYR PRO LYS GLY PRO LEU LEU VAL LEU PRO GLU LYS ILE
SEQRES 5 A 182 TYR LEU TYR SER GLU PRO THR VAL LYS GLU LEU LEU PRO
SEQRES 6 A 182 PHE ASP VAL VAL ILE ASN VAL ALA GLU GLU ALA ASN ASP
SEQRES 7 A 182 LEU ARG MET GLN VAL PRO ALA VAL GLU TYR HIS HIS TYR
SEQRES 8 A 182 ARG TRP GLU HIS ASP SER GLN ILE ALA LEU ASP LEU PRO
SEQRES 9 A 182 SER LEU THR SER ILE ILE HIS ALA ALA THR THR LYS ARG
SEQRES 10 A 182 GLU LYS ILE LEU ILE HIS SER GLN CYS GLY LEU SER ARG
SEQRES 11 A 182 SER ALA THR LEU ILE ILE ALA TYR ILE MET LYS TYR HIS
SEQRES 12 A 182 ASN LEU SER LEU ARG HIS SER TYR ASP LEU LEU LYS SER
SEQRES 13 A 182 ARG ALA ASP LYS ILE ASN PRO SER ILE GLY LEU ILE PHE
SEQRES 14 A 182 GLN LEU MET GLU TRP GLU VAL ALA LEU ASN ALA LYS THR
SEQRES 1 B 182 SER GLY GLN ARG PRO SER LEU PRO MET LEU ALA THR ASP
SEQRES 2 B 182 GLU ARG SER THR ASP LYS GLU SER PRO ASN GLU ASP ARG
SEQRES 3 B 182 GLU PHE VAL PRO CYS SER SER LEU ASP VAL ARG ARG ILE
SEQRES 4 B 182 TYR PRO LYS GLY PRO LEU LEU VAL LEU PRO GLU LYS ILE
SEQRES 5 B 182 TYR LEU TYR SER GLU PRO THR VAL LYS GLU LEU LEU PRO
SEQRES 6 B 182 PHE ASP VAL VAL ILE ASN VAL ALA GLU GLU ALA ASN ASP
SEQRES 7 B 182 LEU ARG MET GLN VAL PRO ALA VAL GLU TYR HIS HIS TYR
SEQRES 8 B 182 ARG TRP GLU HIS ASP SER GLN ILE ALA LEU ASP LEU PRO
SEQRES 9 B 182 SER LEU THR SER ILE ILE HIS ALA ALA THR THR LYS ARG
SEQRES 10 B 182 GLU LYS ILE LEU ILE HIS SER GLN CYS GLY LEU SER ARG
SEQRES 11 B 182 SER ALA THR LEU ILE ILE ALA TYR ILE MET LYS TYR HIS
SEQRES 12 B 182 ASN LEU SER LEU ARG HIS SER TYR ASP LEU LEU LYS SER
SEQRES 13 B 182 ARG ALA ASP LYS ILE ASN PRO SER ILE GLY LEU ILE PHE
SEQRES 14 B 182 GLN LEU MET GLU TRP GLU VAL ALA LEU ASN ALA LYS THR
HET MG A1197 1
HET MG A1198 1
HET PTR A1199 11
HET MG B1197 1
HET MG B1198 1
HET MG B1199 1
HET PTR B1200 11
HETNAM MG MAGNESIUM ION
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 3 MG 5(MG 2+)
FORMUL 5 PTR 2(C9 H12 N O6 P)
FORMUL 10 HOH *24(H2 O)
HELIX 1 1 VAL A 76 LEU A 80 5 5
HELIX 2 2 GLN A 114 LEU A 117 5 4
HELIX 3 3 ASP A 118 LYS A 132 1 15
HELIX 4 4 SER A 145 HIS A 159 1 15
HELIX 5 5 SER A 162 ALA A 174 1 13
HELIX 6 6 SER A 180 ALA A 196 1 17
HELIX 7 7 VAL B 76 LEU B 80 5 5
HELIX 8 8 GLN B 114 LEU B 117 5 4
HELIX 9 9 ASP B 118 LYS B 132 1 15
HELIX 10 10 SER B 145 HIS B 159 1 15
HELIX 11 11 SER B 162 SER B 172 1 11
HELIX 12 12 SER B 180 ALA B 196 1 17
SHEET 1 AA 5 LEU A 61 LEU A 64 0
SHEET 2 AA 5 ILE A 68 TYR A 71 -1 O ILE A 68 N VAL A 63
SHEET 3 AA 5 ILE A 136 HIS A 139 1 O ILE A 136 N TYR A 69
SHEET 4 AA 5 VAL A 84 ASN A 87 1 O VAL A 84 N LEU A 137
SHEET 5 AA 5 GLU A 103 HIS A 106 1 O GLU A 103 N VAL A 85
SHEET 1 BA 5 LEU B 61 LEU B 64 0
SHEET 2 BA 5 ILE B 68 TYR B 71 -1 O ILE B 68 N VAL B 63
SHEET 3 BA 5 ILE B 136 HIS B 139 1 O ILE B 136 N TYR B 69
SHEET 4 BA 5 VAL B 84 ASN B 87 1 O VAL B 84 N LEU B 137
SHEET 5 BA 5 GLU B 103 HIS B 106 1 O GLU B 103 N VAL B 85
SSBOND 1 CYS A 47 CYS A 142 1555 1555 2.04
SSBOND 2 CYS B 47 CYS B 142 1555 1555 2.03
LINK OE1 GLU A 73 MG MG A1197 1555 1555 2.66
LINK OE2 GLU A 73 MG MG A1197 1555 1555 2.56
LINK OD1 ASN A 93 MG MG A1197 1555 1555 1.98
LINK OE1 GLU A 110 MG MG A1198 1555 1555 2.90
LINK MG MG A1198 O HOH A2009 1555 1555 2.96
LINK MG MG A1198 O HOH A2010 1555 1555 3.14
LINK OE1 GLU B 73 MG MG B1197 1555 1555 2.71
LINK OE2 GLU B 73 MG MG B1197 1555 1555 2.42
LINK ND2 ASN B 93 MG MG B1197 1555 1555 2.20
LINK O VAL B 99 MG MG B1199 7555 1555 3.09
LINK O PRO B 100 MG MG B1199 1555 1555 2.77
LINK O PRO B 100 MG MG B1199 7555 1555 2.91
LINK O VAL B 102 MG MG B1199 7555 1555 2.35
LINK OE2 GLU B 134 MG MG B1198 1555 1555 2.63
LINK MG MG B1198 O HOH B2005 1555 1555 2.57
LINK MG MG B1198 O HOH B2005 1555 7555 2.38
SITE 1 AC1 2 GLU A 73 ASN A 93
SITE 1 AC2 3 GLU A 110 ASP A 112 HOH A2009
SITE 1 AC3 2 GLU B 73 ASN B 93
SITE 1 AC4 2 GLU B 134 HOH B2005
SITE 1 AC5 3 VAL B 99 PRO B 100 VAL B 102
SITE 1 AC6 8 HIS A 111 SER A 140 GLN A 141 CYS A 142
SITE 2 AC6 8 GLY A 143 LEU A 144 SER A 145 ARG A 146
SITE 1 AC7 8 HIS B 111 SER B 140 GLN B 141 CYS B 142
SITE 2 AC7 8 GLY B 143 LEU B 144 SER B 145 ARG B 146
CRYST1 61.661 61.661 217.562 90.00 90.00 90.00 P 43 21 2 16
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 0.016218 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004596 0.00000
MTRIX1 1 0.960500 -0.221100 -0.168800 16.03100 1
MTRIX2 1 -0.210400 -0.974400 0.078700 78.49500 1
MTRIX3 1 -0.181900 -0.040000 -0.982500 75.75810 1
(ATOM LINES ARE NOT SHOWN.)
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