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PDBsum entry 3kag

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Isomerase PDB id
3kag
Jmol
Contents
Protein chain
145 a.a.
Ligands
4D7
12P
Waters ×121
HEADER    ISOMERASE                               19-OCT-09   3KAG
TITLE     STRUCTURE-GUIDED DESIGN OF ALPHA-AMINO ACID-DERIVED PIN1
TITLE    2 INHIBITORS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-
COMPND   3 INTERACTING 1;
COMPND   4 CHAIN: A;
COMPND   5 SYNONYM: ROTAMASE PIN1, PPIASE PIN1;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES;
COMPND   8 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: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    SBDD, PPIASE, ISOMERASE, ROTAMASE, SMALL MOLECULE, PROLINE
KEYWDS   2 DIRECTED KINASE, CELL CYCLE, ONCOGENIC TRANSFORMATION,
KEYWDS   3 NUCLEUS, PHOSPHOPROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.M.BAKER,P.DOKURNO,D.A.ROBINSON,A.E.SURGENOR,J.B.MURRAY,
AUTHOR   2 A.J.POTTER,J.D.MOORE
REVDAT   2   05-JAN-10 3KAG    1       JRNL
REVDAT   1   22-DEC-09 3KAG    0
JRNL        AUTH   A.J.POTTER,S.RAY,L.GUERITZ,C.L.NUNNS,C.J.BRYANT,
JRNL        AUTH 2 S.F.SCRACE,N.MATASSOVA,L.M.BAKER,P.DOKURNO,
JRNL        AUTH 3 D.A.ROBINSON,A.E.SURGENOR,B.DAVIS,J.B.MURRAY,
JRNL        AUTH 4 C.M.RICHARDSON,J.D.MOORE
JRNL        TITL   STRUCTURE-GUIDED DESIGN OF ALPHA-AMINO ACID-DERIVED
JRNL        TITL 2 PIN1 INHIBITORS
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20   586 2010
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   19969456
JRNL        DOI    10.1016/J.BMCL.2009.11.090
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8
REMARK   3   NUMBER OF REFLECTIONS             : 15750
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) : 0.205
REMARK   3   R VALUE            (WORKING SET) : 0.202
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 842
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1011
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.02
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3940
REMARK   3   BIN FREE R VALUE SET COUNT          : 56
REMARK   3   BIN FREE R VALUE                    : 0.4850
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1170
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 45
REMARK   3   SOLVENT ATOMS            : 121
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.79
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.69000
REMARK   3    B22 (A**2) : 0.69000
REMARK   3    B33 (A**2) : -1.03000
REMARK   3    B12 (A**2) : 0.34000
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): 0.143
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.795
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1243 ; 0.025 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1665 ; 1.974 ; 1.979
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   147 ; 7.385 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    60 ;31.593 ;22.500
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   216 ;16.113 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;19.189 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   165 ; 0.155 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   951 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):   727 ; 1.362 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1167 ; 2.353 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   516 ; 3.682 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   496 ; 6.043 ; 4.500
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 : NULL
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3KAG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
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                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200  DATA SCALING SOFTWARE          : D*TREK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16604
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9
REMARK 200  DATA REDUNDANCY                : 2.000
REMARK 200  R MERGE                    (I) : 0.05700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   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: PDB ENTRY 1PIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMMONIUM SULPHATE, 0.1M HEPES
REMARK 280  BUFFER, 1% PEG 400, 5MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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       26.52000
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       53.04000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       53.04000
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       26.52000
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 214  LIES ON A SPECIAL POSITION.
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    -3
REMARK 465     SER A    -2
REMARK 465     HIS A    -1
REMARK 465     GLY A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     ASP A     3
REMARK 465     GLU A     4
REMARK 465     GLU A     5
REMARK 465     LYS A     6
REMARK 465     GLY A    39
REMARK 465     ASN A    40
REMARK 465     SER A    41
REMARK 465     SER A    42
REMARK 465     SER A    43
REMARK 465     GLY 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 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           DISTANCE
REMARK 500   NH2  ARG A   142     OE1  GLU A   145              1.97
REMARK 500   O14  4D7 A   164     O    HOH A   196              2.01
REMARK 500   OE2  GLU A   101     O    HOH A   203              2.15
REMARK 500
REMARK 500 REMARK: NULL
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    GLU A 145   CD    GLU A 145   OE1     0.072
REMARK 500    GLU A 145   CD    GLU A 145   OE2     0.067
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    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 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    ASN A  30       15.50     59.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP A 102        24.8      L          L   OUTSIDE RANGE
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     12P A  165
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4D7 A 164
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12P A 165
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KAB   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAC   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAD   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAF   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAH   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAI   RELATED DB: PDB
DBREF  3KAG A    1   163  UNP    Q13526   PIN1_HUMAN       1    163
SEQADV 3KAG GLY A   -3  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAG SER A   -2  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAG HIS A   -1  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAG GLY A    0  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAG ALA A   14  UNP  Q13526    ARG    14 ENGINEERED
SEQRES   1 A  167  GLY SER HIS GLY MET ALA ASP GLU GLU LYS LEU PRO PRO
SEQRES   2 A  167  GLY TRP GLU LYS ALA MET SER ARG SER SER GLY ARG VAL
SEQRES   3 A  167  TYR TYR PHE ASN HIS ILE THR ASN ALA SER GLN TRP GLU
SEQRES   4 A  167  ARG PRO SER GLY ASN SER SER SER GLY GLY LYS ASN GLY
SEQRES   5 A  167  GLN GLY GLU PRO ALA ARG VAL ARG CYS SER HIS LEU LEU
SEQRES   6 A  167  VAL LYS HIS SER GLN SER ARG ARG PRO SER SER TRP ARG
SEQRES   7 A  167  GLN GLU LYS ILE THR ARG THR LYS GLU GLU ALA LEU GLU
SEQRES   8 A  167  LEU ILE ASN GLY TYR ILE GLN LYS ILE LYS SER GLY GLU
SEQRES   9 A  167  GLU ASP PHE GLU SER LEU ALA SER GLN PHE SER ASP CYS
SEQRES  10 A  167  SER SER ALA LYS ALA ARG GLY ASP LEU GLY ALA PHE SER
SEQRES  11 A  167  ARG GLY GLN MET GLN LYS PRO PHE GLU ASP ALA SER PHE
SEQRES  12 A  167  ALA LEU ARG THR GLY GLU MET SER GLY PRO VAL PHE THR
SEQRES  13 A  167  ASP SER GLY ILE HIS ILE ILE LEU ARG THR GLU
HET    4D7  A 164      23
HET    12P  A 165      22
HETNAM     4D7 3-(1H-BENZIMIDAZOL-2-YL)-N-[(2-METHYLFURAN-3-YL)
HETNAM   2 4D7  CARBONYL]-D-ALANINE
HETNAM     12P DODECAETHYLENE GLYCOL
HETSYN     4D7 (R)-3-(1H-BENZOIMIDAZOL-2-YL)-2-[(2-METHYL-FURAN-3-
HETSYN   2 4D7  CARBONYL)-AMINO]-PROPIONIC ACID
HETSYN     12P POLYETHYLENE GLYCOL PEG400
FORMUL   2  4D7    C16 H15 N3 O4
FORMUL   3  12P    C24 H50 O13
FORMUL   4  HOH   *121(H2 O)
HELIX    1   1 THR A   81  SER A   98  1                                  18
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  LEU A  141  1                                  11
SHEET    1   A 3 TRP A  11  MET A  15  0
SHEET    2   A 3 VAL A  22  ASN A  26 -1  O  PHE A  25   N  GLU A  12
SHEET    3   A 3 SER A  32  GLN A  33 -1  O  GLN A  33   N  TYR A  24
SHEET    1   B 4 ASP A 121  SER A 126  0
SHEET    2   B 4 ARG A  54  VAL A  62 -1  N  CYS A  57   O  LEU A 122
SHEET    3   B 4 GLY A 155  GLU A 163 -1  O  LEU A 160   N  SER A  58
SHEET    4   B 4 VAL A 150  THR A 152 -1  N  VAL A 150   O  HIS A 157
SITE     1 AC1 13 HIS A  59  LEU A  61  LYS A  63  ARG A  69
SITE     2 AC1 13 CYS A 113  SER A 114  GLN A 131  SER A 154
SITE     3 AC1 13 HIS A 157  HOH A 176  HOH A 195  HOH A 196
SITE     4 AC1 13 HOH A 198
SITE     1 AC2 15 TYR A  23  ALA A  31  SER A  32  GLN A  33
SITE     2 AC2 15 TRP A  34  ILE A  93  LYS A  97  SER A  98
SITE     3 AC2 15 MET A 146  SER A 147  GLY A 148  HOH A 179
SITE     4 AC2 15 HOH A 182  HOH A 219  HOH A 249
CRYST1   68.504   68.504   79.560  90.00  90.00 120.00 P 31 2 1      6
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      0.014598  0.008428  0.000000        0.00000
SCALE2      0.000000  0.016856  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012569        0.00000
      
PROCHECK
Go to PROCHECK summary
 References