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PDBsum entry 3ikd

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
3ikd
Jmol
Contents
Protein chain
113 a.a.
Ligands
J9Z ×2
Waters ×474
HEADER    ISOMERASE                               05-AUG-09   3IKD
TITLE     STRUCTURE-BASED DESIGN OF NOVEL PIN1 INHIBITORS (I)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-
COMPND   3 INTERACTING 1;
COMPND   4 CHAIN: A, B;
COMPND   5 FRAGMENT: UNP RESIDUES 45-163, PIN1 PPIASE DOMAIN;
COMPND   6 SYNONYM: ROTAMASE PIN1, PPIASE PIN1;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PIN1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    SBDD, PPIASE, CELL CYCLE, ISOMERASE, SMALL MOLECULE,
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.MATTHEWS,S.GREASLEY,R.FERRE,H.PARGE
REVDAT   1   22-SEP-09 3IKD    0
JRNL        AUTH   C.GUO,X.HOU,L.DONG,E.DAGOSTINO,S.GREASLEY,R.FERRE,
JRNL        AUTH 2 J.MARAKOVITS,M.C.JOHNSON,D.MATTHEWS,B.MROCZKOWSKI,
JRNL        AUTH 3 H.PARGE,T.VANARSDALE,I.POPOFF,J.PIRAINO,
JRNL        AUTH 4 S.MARGOSIAK,J.THOMSON,G.LOS,B.W.MURRAY
JRNL        TITL   STRUCTURE-BASED DESIGN OF NOVEL HUMAN PIN1
JRNL        TITL 2 INHIBITORS (I).
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  5613 2009
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   19729306
JRNL        DOI    10.1016/J.BMCL.2009.08.034
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00
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             : 12666
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NONE SELECTED
REMARK   3   R VALUE            (WORKING SET) : 0.203
REMARK   3   FREE R VALUE                     : 0.203
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.08
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2706
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     : 0
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            : 2183
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 84
REMARK   3   SOLVENT ATOMS            : 474
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  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 3IKD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB054520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-NOV-00
REMARK 200  TEMPERATURE           (KELVIN) : 93
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 RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14274
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.05800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 24.3300
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     (%) : 94.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.42
REMARK 200  R MERGE FOR SHELL          (I) : 0.17100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 7.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 36.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.9M NA
REMARK 280  CITRATE, 5MM TCEP, 100MM HEPES: COMPOUND @ 500UM SOAKED INTO
REMARK 280  APO CRYSTAL FOR 60HRS. , PH 8.0 , VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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   X+1/2,Y+1/2,Z
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        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  1.000000  0.000000  0.000000       58.67700
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.01400
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.67700
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.01400
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 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: PISA
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: PISA
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 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     GLY A    41
REMARK 465     SER A    42
REMARK 465     HIS A    43
REMARK 465     MET A    44
REMARK 465     GLY A    45
REMARK 465     LYS A    46
REMARK 465     ASN A    47
REMARK 465     GLY A    48
REMARK 465     GLN A    49
REMARK 465     GLY A    50
REMARK 465     GLY B    41
REMARK 465     SER B    42
REMARK 465     HIS B    43
REMARK 465     MET B    44
REMARK 465     GLY B    45
REMARK 465     LYS B    46
REMARK 465     ASN B    47
REMARK 465     GLY B    48
REMARK 465     GLN B    49
REMARK 465     GLY B    50
REMARK 465     GLU B    51
REMARK 465     PRO B    52
REMARK 465     ALA B    53
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     GLU A  87    CG   CD   OE1  OE2
REMARK 470     GLN B  94    CG   CD   OE1  NE2
REMARK 470     LYS B  95    CD   CE   NZ
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),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    HIS A  64   CG    HIS A  64   CD2     0.056
REMARK 500    HIS B  59   CG    HIS B  59   CD2     0.061
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    VAL A  62   CG1 -  CB  -  CG2 ANGL. DEV. = -10.3 DEGREES
REMARK 500    ARG A  68   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES
REMARK 500    ARG A  68   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A  80   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 127   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG B  56   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 119   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG B 127   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 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    ALA A 118       32.60    -91.73
REMARK 500    ALA B 118       31.86    -98.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 214        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH B 221        DISTANCE =  5.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J9Z A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE J9Z B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I6C   RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 3IK8   RELATED DB: PDB
REMARK 900 SAME PROTEIN: APO STRUCTURE
REMARK 900 RELATED ID: 3IKG   RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH SMALL MOLECULE INHIBITOR
DBREF  3IKD A   45   163  UNP    Q13526   PIN1_HUMAN      45    163
DBREF  3IKD B   45   163  UNP    Q13526   PIN1_HUMAN      45    163
SEQADV 3IKD GLY A   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD SER A   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD HIS A   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD MET A   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD GLN A   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3IKD GLN A   82  UNP  Q13526    LYS    82 ENGINEERED
SEQADV 3IKD GLY B   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD SER B   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD HIS B   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD MET B   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3IKD GLN B   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3IKD GLN B   82  UNP  Q13526    LYS    82 ENGINEERED
SEQRES   1 A  123  GLY SER HIS MET GLY LYS ASN GLY GLN GLY GLU PRO ALA
SEQRES   2 A  123  ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER GLN
SEQRES   3 A  123  SER ARG ARG PRO SER SER TRP ARG GLN GLU GLN ILE THR
SEQRES   4 A  123  ARG THR GLN GLU GLU ALA LEU GLU LEU ILE ASN GLY TYR
SEQRES   5 A  123  ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU SER
SEQRES   6 A  123  LEU ALA SER GLN PHE SER ASP CYS SER SER ALA LYS ALA
SEQRES   7 A  123  ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET GLN
SEQRES   8 A  123  LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR GLY
SEQRES   9 A  123  GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE HIS
SEQRES  10 A  123  ILE ILE LEU ARG THR GLU
SEQRES   1 B  123  GLY SER HIS MET GLY LYS ASN GLY GLN GLY GLU PRO ALA
SEQRES   2 B  123  ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER GLN
SEQRES   3 B  123  SER ARG ARG PRO SER SER TRP ARG GLN GLU GLN ILE THR
SEQRES   4 B  123  ARG THR GLN GLU GLU ALA LEU GLU LEU ILE ASN GLY TYR
SEQRES   5 B  123  ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU SER
SEQRES   6 B  123  LEU ALA SER GLN PHE SER ASP CYS SER SER ALA LYS ALA
SEQRES   7 B  123  ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET GLN
SEQRES   8 B  123  LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR GLY
SEQRES   9 B  123  GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE HIS
SEQRES  10 B  123  ILE ILE LEU ARG THR GLU
HET    J9Z  A 501      42
HET    J9Z  B 502      42
HETNAM     J9Z (2R)-2-[(1-BENZOTHIOPHEN-2-YLCARBONYL)AMINO]-3-
HETNAM   2 J9Z  PHENYLPROPYL PHOSPHATE
FORMUL   3  J9Z    2(C18 H16 N O5 P S 2-)
FORMUL   5  HOH   *158(H2 O)
HELIX    1   1 THR A   81  GLY A   99  1                                  19
HELIX    2   2 ASP A  102  SER A  111  1                                  10
HELIX    3   3 CYS A  113  ARG A  119  5                                   7
HELIX    4   4 GLN A  131  ALA A  140  1                                  10
HELIX    5   5 THR B   81  SER B   98  1                                  18
HELIX    6   6 ASP B  102  SER B  111  1                                  10
HELIX    7   7 CYS B  113  ARG B  119  5                                   7
HELIX    8   8 GLN B  131  ALA B  140  1                                  10
SHEET    1   A 4 ASP A 121  PHE A 125  0
SHEET    2   A 4 VAL A  55  VAL A  62 -1  N  CYS A  57   O  LEU A 122
SHEET    3   A 4 GLY A 155  GLU A 163 -1  O  ILE A 156   N  VAL A  62
SHEET    4   A 4 VAL A 150  THR A 152 -1  N  VAL A 150   O  HIS A 157
SHEET    1   B 4 ASP B 121  PHE B 125  0
SHEET    2   B 4 VAL B  55  VAL B  62 -1  N  CYS B  57   O  LEU B 122
SHEET    3   B 4 GLY B 155  GLU B 163 -1  O  LEU B 160   N  SER B  58
SHEET    4   B 4 VAL B 150  THR B 152 -1  N  VAL B 150   O  HIS B 157
SITE     1 AC1 14 HIS A  59  LEU A  61  LYS A  63  ARG A  68
SITE     2 AC1 14 ARG A  69  CYS A 113  SER A 114  LEU A 122
SITE     3 AC1 14 GLN A 131  PHE A 134  SER A 154  HIS A 157
SITE     4 AC1 14 HOH A 165  HOH A 216
SITE     1 AC2  9 LYS B  63  ARG B  68  ARG B  69  CYS B 113
SITE     2 AC2  9 LEU B 122  SER B 154  HIS B 157  HOH B 165
SITE     3 AC2  9 HOH B 175
CRYST1  117.354   36.028   51.281  90.00 100.30  90.00 C 1 2 1       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      0.008521  0.000000  0.001548        0.00000
SCALE2      0.000000  0.027756  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019820        0.00000
      
PROCHECK
Go to PROCHECK summary
 References