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PDBsum entry 3kac

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
3kac
Jmol
Contents
Protein chain
113 a.a.
Ligands
4BX ×2
Waters ×224
HEADER    ISOMERASE                               19-OCT-09   3KAC
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, B;
COMPND   5 FRAGMENT: 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: 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 3KAC    1       JRNL
REVDAT   1   22-DEC-09 3KAC    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.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.49
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1
REMARK   3   NUMBER OF REFLECTIONS             : 13240
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) : 0.172
REMARK   3   R VALUE            (WORKING SET) : 0.168
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 726
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 792
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.18
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220
REMARK   3   BIN FREE R VALUE SET COUNT          : 41
REMARK   3   BIN FREE R VALUE                    : 0.3090
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1795
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 28
REMARK   3   SOLVENT ATOMS            : 224
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.04000
REMARK   3    B22 (A**2) : -0.05000
REMARK   3    B33 (A**2) : 0.04000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.11000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.222
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.683
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1855 ; 0.021 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2487 ; 1.805 ; 1.968
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   226 ; 7.427 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;39.358 ;23.333
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   334 ;15.858 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.053 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   257 ; 0.129 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1432 ; 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):  1131 ; 1.073 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1809 ; 1.834 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   724 ; 3.173 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   678 ; 4.846 ; 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 3KAC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
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   : 15369
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1
REMARK 200  DATA REDUNDANCY                : 2.600
REMARK 200  R MERGE                    (I) : 0.06200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 6.1000
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     (%) : 92.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.32300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.100
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   (%): 38.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM CITRATE, 0.1M TRIS
REMARK 280  BUFFER, 5MM DTT, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
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       59.03200
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.28800
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.03200
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.28800
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 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 272  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    41
REMARK 465     SER A    42
REMARK 465     HIS 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 465     GLY B    41
REMARK 465     SER B    42
REMARK 465     HIS B    43
REMARK 465     GLY B    44
REMARK 465     GLY B    45
REMARK 465     LYS B    46
REMARK 465     ASN B    47
REMARK 465     GLY B    48
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   OE1  GLN A   131     O    HOH A   269              2.13
REMARK 500
REMARK 500 REMARK: NULL
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 B   225     O    HOH B   242     2656     2.15
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  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG B 142   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
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 173        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH A 274        DISTANCE =  6.48 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4BX A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4BX B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KAB   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAD   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAF   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAG   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAH   RELATED DB: PDB
REMARK 900 RELATED ID: 3KAI   RELATED DB: PDB
DBREF  3KAC A   45   163  UNP    Q13526   PIN1_HUMAN      45    163
DBREF  3KAC B   45   163  UNP    Q13526   PIN1_HUMAN      45    163
SEQADV 3KAC GLY A   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC SER A   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC HIS A   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC GLY A   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC GLN A   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3KAC GLN A   82  UNP  Q13526    LYS    82 ENGINEERED
SEQADV 3KAC GLY B   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC SER B   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC HIS B   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC GLY B   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3KAC GLN B   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3KAC GLN B   82  UNP  Q13526    LYS    82 ENGINEERED
SEQRES   1 A  123  GLY SER HIS GLY 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 GLY 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    4BX  A   1      14
HET    4BX  B   1      14
HETNAM     4BX 3-(1H-BENZIMIDAZOL-2-YL)PROPANOIC ACID
FORMUL   3  4BX    2(C10 H10 N2 O2)
FORMUL   5  HOH   *224(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  LEU A  141  1                                  11
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  ILE B 156   N  VAL B  62
SHEET    4   B 4 VAL B 150  THR B 152 -1  N  THR B 152   O  GLY B 155
SITE     1 AC1  9 HOH A  38  HIS A  59  LEU A  61  LYS A  63
SITE     2 AC1  9 ARG A  69  CYS A 113  PHE A 134  SER A 154
SITE     3 AC1  9 HOH A 249
SITE     1 AC2 10 HIS B  59  LEU B  61  LYS B  63  ARG B  69
SITE     2 AC2 10 CYS B 113  GLN B 131  PHE B 134  SER B 154
SITE     3 AC2 10 HIS B 157  HOH B 233
CRYST1  118.064   36.576   51.328  90.00 101.11  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      0.008470  0.000000  0.001663        0.00000
SCALE2      0.000000  0.027340  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019855        0.00000
      
PROCHECK
Go to PROCHECK summary
 References