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 4 13-SEP-23 3TC5 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3TC5 1 REMARK
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,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) : 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 498 ; 1.743 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 491 ; 2.679 ; 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): 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 DEPOSITION ID IS D_1000067299.
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> 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 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-TRANS
REMARK 900 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
(ATOM LINES ARE NOT SHOWN.)
END
