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PDBsum entry 3tc5

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Isomerase/isomerase inhibitor PDB id
3tc5
Jmol
Contents
Protein chain
144 a.a.
Ligands
3T5
P6G
Waters ×266
HEADER    ISOMERASE/ISOMERASE INHIBITOR           08-AUG-11   3TC5
TITLE     SELECTIVE TARGETING OF DISEASE-RELEVANT PROTEIN BINDING DOMAINS BY O-
TITLE    2 PHOSPHORYLATED NATURAL PRODUCT DERIVATIVES
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND   5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PIN1, PPIASE PIN1,
COMPND   6 ROTAMASE 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    PIN1 MUTANT (R14A), ONCOGENIC TRANSFORMATION, SMALL MOLECULE, CELL
KEYWDS   2 CYCLE, ROTAMASE, PHOSPHOPROTEIN, NUCLEUS, ISOMERASE-ISOMERASE
KEYWDS   3 INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.GRAEBER,W.JANCZYK,B.SPERL,N.ELUMALAI,C.KOZANY,F.HAUSCH,T.A.HOLAK,
AUTHOR   2 T.BERG
REVDAT   2   02-NOV-11 3TC5    1       JRNL
REVDAT   1   31-AUG-11 3TC5    0
JRNL        AUTH   M.GRABER,W.JANCZYK,B.SPERL,N.ELUMALAI,C.KOZANY,F.HAUSCH,
JRNL        AUTH 2 T.A.HOLAK,T.BERG
JRNL        TITL   SELECTIVE TARGETING OF DISEASE-RELEVANT PROTEIN BINDING
JRNL        TITL 2 DOMAINS BY O-PHOSPHORYLATED NATURAL PRODUCT DERIVATIVES.
JRNL        REF    ACS CHEM.BIOL.                V.   6  1008 2011
JRNL        REFN                   ISSN 1554-8929
JRNL        PMID   21797253
JRNL        DOI    10.1021/CB2001796
REMARK   2
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.8
REMARK   3   NUMBER OF REFLECTIONS             : 32347
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) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1735
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) : 1.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 934
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 31.97
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1850
REMARK   3   BIN FREE R VALUE SET COUNT          : 51
REMARK   3   BIN FREE R VALUE                    : 0.1970
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1135
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 51
REMARK   3   SOLVENT ATOMS            : 266
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.45
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.069
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.037
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.064
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1213 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):   879 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1635 ; 1.146 ; 1.998
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2057 ; 0.758 ; 3.006
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   142 ; 5.907 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    55 ;32.728 ;22.545
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   203 ;12.303 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;19.902 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   167 ; 0.067 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1308 ; 0.003 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   253 ; 0.001 ; 0.020
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):   715 ; 0.648 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   289 ; 0.205 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1144 ; 1.108 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   498 ; 1.743 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   491 ; 2.679 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2092 ; 0.700 ; 3.000
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3TC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB067299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-10
REMARK 200  TEMPERATURE           (KELVIN) : 77
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42028
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.700
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: 2ZR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2M AMMONIUM SULPHATE, 0.1M HEPES
REMARK 280  BUFFER, 1% PEG 400,PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 277K, VAPOR DIFFUSION, SITTING DROP
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       26.45667
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       52.91333
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       52.91333
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       26.45667
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 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    -2
REMARK 465     SER A    -1
REMARK 465     HIS 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     SER A    38
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 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     LEU A   7    CB   CG   CD1  CD2
REMARK 470     LYS A  13    CE   NZ
REMARK 470     GLU A  87    CD   OE1  OE2
REMARK 470     LYS A  95    NZ
REMARK 470     GLN A 129    NE2
REMARK 470     ARG A 142    NE   CZ   NH1  NH2
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    ASP A 112       33.31    -82.54
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 A 432        DISTANCE =  6.27 ANGSTROMS
REMARK 525    HOH A 471        DISTANCE =  5.73 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3T5 A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 165
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIN   RELATED DB: PDB
REMARK 900 PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
REMARK 900 RELATED ID: 2ZR6   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MUTANT PIN1 PEPTIDYL-PROLYL CIS-
REMARK 900 TRANS ISOMERASE
REMARK 900 RELATED ID: 2ITK   RELATED DB: PDB
REMARK 900 HUMAN PIN1 BOUND TO D-PEPTIDE
REMARK 900 RELATED ID: 2Q5A   RELATED DB: PDB
REMARK 900 HUMAN PIN1 BOUND TO L-PEPTIDE
DBREF  3TC5 A    1   163  UNP    Q13526   PIN1_HUMAN       1    163
SEQADV 3TC5 GLY A   -2  UNP  Q13526              EXPRESSION TAG
SEQADV 3TC5 SER A   -1  UNP  Q13526              EXPRESSION TAG
SEQADV 3TC5 HIS A    0  UNP  Q13526              EXPRESSION TAG
SEQADV 3TC5 ALA A   14  UNP  Q13526    ARG    14 ENGINEERED MUTATION
SEQRES   1 A  166  GLY SER HIS MET ALA ASP GLU GLU LYS LEU PRO PRO GLY
SEQRES   2 A  166  TRP GLU LYS ALA MET SER ARG SER SER GLY ARG VAL TYR
SEQRES   3 A  166  TYR PHE ASN HIS ILE THR ASN ALA SER GLN TRP GLU ARG
SEQRES   4 A  166  PRO SER GLY ASN SER SER SER GLY GLY LYS ASN GLY GLN
SEQRES   5 A  166  GLY GLU PRO ALA ARG VAL ARG CYS SER HIS LEU LEU VAL
SEQRES   6 A  166  LYS HIS SER GLN SER ARG ARG PRO SER SER TRP ARG GLN
SEQRES   7 A  166  GLU LYS ILE THR ARG THR LYS GLU GLU ALA LEU GLU LEU
SEQRES   8 A  166  ILE ASN GLY TYR ILE GLN LYS ILE LYS SER GLY GLU GLU
SEQRES   9 A  166  ASP PHE GLU SER LEU ALA SER GLN PHE SER ASP CYS SER
SEQRES  10 A  166  SER ALA LYS ALA ARG GLY ASP LEU GLY ALA PHE SER ARG
SEQRES  11 A  166  GLY GLN MET GLN LYS PRO PHE GLU ASP ALA SER PHE ALA
SEQRES  12 A  166  LEU ARG THR GLY GLU MET SER GLY PRO VAL PHE THR ASP
SEQRES  13 A  166  SER GLY ILE HIS ILE ILE LEU ARG THR GLU
HET    3T5  A 164      32
HET    P6G  A 165      19
HETNAM     3T5 (11ALPHA,16ALPHA)-9-FLUORO-11,17-DIHYDROXY-16-METHYL-3,
HETNAM   2 3T5  20-DIOXOPREGNA-1,4-DIEN-21-YL DIHYDROGEN PHOSPHATE
HETNAM     P6G HEXAETHYLENE GLYCOL
HETSYN     3T5 DEXAMETHASONE 21-PHOSPHATE
HETSYN     P6G POLYETHYLENE GLYCOL PEG400
FORMUL   2  3T5    C22 H30 F O8 P
FORMUL   3  P6G    C12 H26 O7
FORMUL   4  HOH   *266(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  TYR A  23   N  ALA A  14
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  PHE A 125  0
SHEET    2   B 4 VAL A  55  VAL A  62 -1  N  CYS A  57   O  LEU A 122
SHEET    3   B 4 GLY A 155  ARG A 161 -1  O  ILE A 156   N  VAL A  62
SHEET    4   B 4 VAL A 150  THR A 152 -1  N  VAL A 150   O  HIS A 157
SITE     1 AC1 13 LYS A  63  ARG A  68  ARG A  69  PHE A 125
SITE     2 AC1 13 GLN A 129  GLN A 131  SER A 154  HIS A 157
SITE     3 AC1 13 HOH A 216  HOH A 263  HOH A 291  HOH A 329
SITE     4 AC1 13 HOH A 462
SITE     1 AC2 12 TYR A  23  ALA A  31  SER A  32  TRP A  34
SITE     2 AC2 12 ILE A  93  LYS A  97  SER A  98  SER A 147
SITE     3 AC2 12 HOH A 202  HOH A 229  HOH A 266  HOH A 296
CRYST1   68.360   68.360   79.370  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      0.014628  0.008446  0.000000        0.00000
SCALE2      0.000000  0.016891  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012599        0.00000
      
PROCHECK
Go to PROCHECK summary
 References