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PDBsum entry 3o5l

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Isomerase PDB id
3o5l
Jmol
Contents
Protein chain
128 a.a.
Ligands
1PE
Waters ×168
HEADER    ISOMERASE                               28-JUL-10   3O5L
TITLE     FK1 DOMAIN MUTANT A19T OF FKBP51, CRYSTAL FORM I
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP5;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PPIASE FKBP5, FK506-BINDING PROTEIN 5, FKBP-5, ROTAMASE, 51
COMPND   5 KDA FK506-BINDING PROTEIN, 51 KDA FKBP, FKBP-51, 54 KDA PROGESTERONE
COMPND   6 RECEPTOR-ASSOCIATED IMMUNOPHILIN, FKBP54, P54, FF1 ANTIGEN, HSP90-
COMPND   7 BINDING IMMUNOPHILIN, ANDROGEN-REGULATED PROTEIN 6;
COMPND   8 EC: 5.2.1.8;
COMPND   9 ENGINEERED: YES;
COMPND  10 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: AIG6, FKBP5, FKBP51;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+ RIL;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTB
KEYWDS    FK-506 BINDING DOMAIN, HSP90 COCHAPERONE, IMMUNOPHILINE, PEPTIDYL-
KEYWDS   2 PROLYL ISOMERASE, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BRACHER,C.KOZANY,A.-K.THOST,F.HAUSCH
REVDAT   2   28-MAR-12 3O5L    1       JRNL   VERSN
REVDAT   1   01-JUN-11 3O5L    0
JRNL        AUTH   A.BRACHER,C.KOZANY,A.K.THOST,F.HAUSCH
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF THE PPIASE DOMAIN OF FKBP51,
JRNL        TITL 2 A COCHAPERONE OF HUMAN HSP90.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  67   549 2011
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   21636895
JRNL        DOI    10.1107/S0907444911013862
REMARK   2
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8
REMARK   3   NUMBER OF REFLECTIONS             : 29516
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) : 0.173
REMARK   3   R VALUE            (WORKING SET) : 0.172
REMARK   3   FREE R VALUE                     : 0.206
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1487
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) : 1.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2028
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.24
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280
REMARK   3   BIN FREE R VALUE SET COUNT          : 95
REMARK   3   BIN FREE R VALUE                    : 0.2910
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 982
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 161
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 14.32
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.74
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.01000
REMARK   3    B22 (A**2) : 0.01000
REMARK   3    B33 (A**2) : -0.02000
REMARK   3    B12 (A**2) : 0.01000
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): 0.058
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.917
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1100 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):   788 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1480 ; 1.554 ; 1.982
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1941 ; 0.885 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   143 ; 7.970 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    43 ;28.539 ;24.651
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   204 ;13.730 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ; 9.673 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   154 ; 0.092 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1235 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   212 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   249 ; 0.281 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   908 ; 0.204 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   569 ; 0.181 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   620 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   131 ; 0.221 ; 0.200
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):    15 ; 0.268 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    33 ; 0.269 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.282 ; 0.200
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):   731 ; 1.745 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   283 ; 0.912 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1102 ; 2.264 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   455 ; 3.006 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   378 ; 3.993 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2101 ; 1.473 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   168 ; 8.811 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1861 ; 5.452 ; 3.000
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   : 1.20
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 3O5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
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) : 0.9723
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29538
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.559
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : 0.06300
REMARK 200  R SYM                      (I) : 0.06300
REMARK 200   FOR THE DATA SET  : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900
REMARK 200  R SYM FOR SHELL            (I) : 0.39900
REMARK 200   FOR SHELL         : 1.800
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: PDB ENTRY 3O5P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % JEFFAMINE ED-2001, 0.1 M HEPES,
REMARK 280  PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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       59.33200
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       29.66600
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       29.66600
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       59.33200
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 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  45    CG   CD   OE1  OE2
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   NZ   LYS A    58     O    HOH A   171              1.76
REMARK 500   O    HOH A   223     O    HOH A   244              1.95
REMARK 500   O    HOH A   238     O    HOH A   244              2.04
REMARK 500   O    HOH A   247     O    HOH A   256              2.06
REMARK 500   NZ   LYS A    60     O    HOH A   171              2.09
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   NZ   LYS A    58     O    HOH A   241     4455     1.89
REMARK 500   OE1  GLU A    44     O    HOH A   152     4565     2.04
REMARK 500   O    HOH A   254     O    HOH A   264     6454     2.18
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 112     -114.45   -137.60
REMARK 500    SER A 118       78.15   -151.74
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 243        DISTANCE =  5.01 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 AUTHORS STATE THAT 1PE IS PROBABLY A STRUCTURED FRAGMENT OF
REMARK 600 JEFFAMINE ED-2001.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O5D   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5E   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5F   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5G   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5I   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5J   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5K   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5M   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5O   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5P   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5Q   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5R   RELATED DB: PDB
REMARK 900 RELATED ID: 1KT0   RELATED DB: PDB
REMARK 900 STRUCTURE OF FULL-LENGTH FKBP51
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT A19T IS A MUTATION, BUT NOT A NATURALLY
REMARK 999 OCCURRING ALLELE.
DBREF  3O5L A   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
SEQADV 3O5L GLY A   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5L ALA A   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5L PRO A   15  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5L THR A   19  UNP  Q13451    ALA    19 SEE REMARK 999
SEQRES   1 A  128  GLY ALA PRO ALA THR VAL THR GLU GLN GLY GLU ASP ILE
SEQRES   2 A  128  THR SER LYS LYS ASP ARG GLY VAL LEU LYS ILE VAL LYS
SEQRES   3 A  128  ARG VAL GLY ASN GLY GLU GLU THR PRO MET ILE GLY ASP
SEQRES   4 A  128  LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU SER ASN GLY
SEQRES   5 A  128  LYS LYS PHE ASP SER SER HIS ASP ARG ASN GLU PRO PHE
SEQRES   6 A  128  VAL PHE SER LEU GLY LYS GLY GLN VAL ILE LYS ALA TRP
SEQRES   7 A  128  ASP ILE GLY VAL ALA THR MET LYS LYS GLY GLU ILE CYS
SEQRES   8 A  128  HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR GLY SER ALA
SEQRES   9 A  128  GLY SER LEU PRO LYS ILE PRO SER ASN ALA THR LEU PHE
SEQRES  10 A  128  PHE GLU ILE GLU LEU LEU ASP PHE LYS GLY GLU
HET    1PE  A   1      16
HETNAM     1PE PENTAETHYLENE GLYCOL
HETSYN     1PE PEG400
FORMUL   2  1PE    C10 H22 O6
FORMUL   3  HOH   *161(H2 O)
HELIX    1   1 GLY A   13  GLY A   22  1                                  10
HELIX    2   2 HIS A   71  ARG A   73  5                                   3
HELIX    3   3 ILE A   87  ALA A   95  1                                   9
HELIX    4   4 PRO A  109  ALA A  112  5                                   4
SHEET    1   A 6 GLU A  23  ASP A  24  0
SHEET    2   A 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  GLU A  23
SHEET    3   A 6 ILE A 102  CYS A 107 -1  O  ILE A 102   N  LYS A  38
SHEET    4   A 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107
SHEET    5   A 6 LYS A  52  LEU A  61 -1  N  LYS A  60   O  PHE A 129
SHEET    6   A 6 LYS A  66  SER A  69 -1  O  PHE A  67   N  GLY A  59
SHEET    1   B 6 GLU A  23  ASP A  24  0
SHEET    2   B 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  GLU A  23
SHEET    3   B 6 ILE A 102  CYS A 107 -1  O  ILE A 102   N  LYS A  38
SHEET    4   B 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107
SHEET    5   B 6 LYS A  52  LEU A  61 -1  N  LYS A  60   O  PHE A 129
SHEET    6   B 6 PHE A  77  SER A  80 -1  O  PHE A  79   N  VAL A  53
CISPEP   1 LEU A  119    PRO A  120          0         4.76
SITE     1 AC1  9 TYR A  57  PHE A  67  ASP A  68  VAL A  86
SITE     2 AC1  9 ILE A  87  TRP A  90  TYR A 113  HOH A 229
SITE     3 AC1  9 HOH A 262
CRYST1   47.978   47.978   88.998  90.00  90.00 120.00 P 32 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      0.020843  0.012034  0.000000        0.00000
SCALE2      0.000000  0.024067  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011236        0.00000
      
PROCHECK
Go to PROCHECK summary
 References