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PDBsum entry 4drm

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Isomerase PDB id
4drm
Jmol
Contents
Protein chain
128 a.a.
Ligands
0MC
Waters ×228
HEADER    ISOMERASE                               17-FEB-12   4DRM
TITLE     EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND
TITLE    2 FKBP52: COMPLEX OF FKBP51 WITH {3-[(1R)-3-(3,4-DIMETHOXYPHENYL)-1-
TITLE    3 ({[(2S)-1-{[(1S,2R)-2-ETHYL-1-HYDROXYCYCLOHEXYL](OXO)
TITLE    4 ACETYL}PIPERIDIN-2-YL]CARBONYL}OXY)PROPYL]PHENOXY}ACETIC ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP5;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 16-140;
COMPND   5 SYNONYM: PPIASE FKBP5, 51 KDA FK506-BINDING PROTEIN, 51 KDA FKBP,
COMPND   6 FKBP-51, 54 KDA PROGESTERONE RECEPTOR-ASSOCIATED IMMUNOPHILIN,
COMPND   7 ANDROGEN-REGULATED PROTEIN 6, FF1 ANTIGEN, FK506-BINDING PROTEIN 5,
COMPND   8 FKBP-5, FKBP54, P54, HSP90-BINDING IMMUNOPHILIN, ROTAMASE;
COMPND   9 EC: 5.2.1.8;
COMPND  10 ENGINEERED: 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: 469008;
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, IMMUNOPHILIN, PEPTIDYL-
KEYWDS   2 PROLYL ISOMERASE, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.GOPALAKRISHNAN,C.KOZANY,S.GAALI,C.KRESS,B.HOOGELAND,A.BRACHER,
AUTHOR   2 F.HAUSCH
REVDAT   2   23-MAY-12 4DRM    1       JRNL
REVDAT   1   16-MAY-12 4DRM    0
JRNL        AUTH   R.GOPALAKRISHNAN,C.KOZANY,S.GAALI,C.KRESS,B.HOOGELAND,
JRNL        AUTH 2 A.BRACHER,F.HAUSCH
JRNL        TITL   EVALUATION OF SYNTHETIC FK506 ANALOGUES AS LIGANDS FOR THE
JRNL        TITL 2 FK506-BINDING PROTEINS 51 AND 52.
JRNL        REF    J.MED.CHEM.                   V.  55  4114 2012
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   22455444
JRNL        DOI    10.1021/JM201746X
REMARK   2
REMARK   2 RESOLUTION.    1.48 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) : 1.48
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 21603
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) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.208
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1135
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) : 1.48
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1555
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3960
REMARK   3   BIN FREE R VALUE SET COUNT          : 83
REMARK   3   BIN FREE R VALUE                    : 0.4710
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 978
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 46
REMARK   3   SOLVENT ATOMS            : 228
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.31
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.85
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.09000
REMARK   3    B22 (A**2) : 0.25000
REMARK   3    B33 (A**2) : -0.16000
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): 0.075
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.077
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.631
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939
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):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1489 ; 1.604 ; 2.029
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   139 ; 6.691 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    40 ;29.749 ;25.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   196 ;12.881 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;13.721 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   155 ; 0.097 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   832 ; 0.007 ; 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):   674 ; 0.810 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1090 ; 1.453 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   426 ; 2.477 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   399 ; 3.961 ; 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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    13        A   139
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0047  15.3749  -9.6526
REMARK   3    T TENSOR
REMARK   3      T11:   0.0073 T22:   0.0186
REMARK   3      T33:   0.0045 T12:   0.0017
REMARK   3      T13:   0.0009 T23:   0.0015
REMARK   3    L TENSOR
REMARK   3      L11:   0.3789 L22:   0.5329
REMARK   3      L33:   0.3070 L12:  -0.1385
REMARK   3      L13:   0.0217 L23:   0.0008
REMARK   3    S TENSOR
REMARK   3      S11:   0.0102 S12:   0.0239 S13:  -0.0216
REMARK   3      S21:  -0.0137 S22:   0.0114 S23:   0.0222
REMARK   3      S31:  -0.0047 S32:   0.0251 S33:  -0.0216
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   201        A   201
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8301  12.1577 -19.7162
REMARK   3    T TENSOR
REMARK   3      T11:   0.0533 T22:   0.0642
REMARK   3      T33:   0.0189 T12:   0.0115
REMARK   3      T13:  -0.0106 T23:  -0.0046
REMARK   3    L TENSOR
REMARK   3      L11:   8.0737 L22:   0.2799
REMARK   3      L33:   3.4017 L12:  -0.5969
REMARK   3      L13:  -4.9406 L23:  -0.2231
REMARK   3    S TENSOR
REMARK   3      S11:   0.1031 S12:   0.3429 S13:  -0.1068
REMARK   3      S21:  -0.1122 S22:  -0.1392 S23:   0.0209
REMARK   3      S31:   0.0617 S32:  -0.0757 S33:   0.0361
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 U VALUES : RESIDUAL ONLY
REMARK   4
REMARK   4 4DRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22844
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.162
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.06600
REMARK 200  R SYM                      (I) : 0.06600
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.47700
REMARK 200  R SYM FOR SHELL            (I) : 0.47700
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS APO STRUCTURE
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3O5Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 37.5 % PEG3350, 0.1 M NH4OAC, 0.1 M
REMARK 280  HEPES PH 7.5, 10 % DMSO, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       21.08100
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.41100
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.63600
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.41100
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.08100
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.63600
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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 300 REMARK: BIOLOGICAL UNIT IS A MONOMER
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     LYS A  65    CG   CD   CE   NZ
REMARK 470     GLU A 140    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   O    HOH A   359     O    HOH A   491              2.14
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     -117.85   -135.12
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 0MC A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DRK   RELATED DB: PDB
REMARK 900 RELATED ID: 4DRN   RELATED DB: PDB
REMARK 900 RELATED ID: 4DRO   RELATED DB: PDB
REMARK 900 RELATED ID: 4DRP   RELATED DB: PDB
REMARK 900 RELATED ID: 4DRQ   RELATED DB: PDB
DBREF  4DRM A   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
SEQADV 4DRM GLY A   13  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRM ALA A   14  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRM PRO A   15  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRM THR A   19  UNP  Q13451    ALA    19 CONFLICT
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    0MC  A 201      46
HETNAM     0MC {3-[(1R)-3-(3,4-DIMETHOXYPHENYL)-1-({[(2S)-1-{[(1S,2R)-
HETNAM   2 0MC  2-ETHYL-1-HYDROXYCYCLOHEXYL](OXO)ACETYL}PIPERIDIN-2-
HETNAM   3 0MC  YL]CARBONYL}OXY)PROPYL]PHENOXY}ACETIC ACID
FORMUL   2  0MC    C35 H45 N O10
FORMUL   3  HOH   *228(H2 O)
HELIX    1   1 GLY A   13  GLY A   22  1                                  10
HELIX    2   2 HIS A   71  ASN A   74  5                                   4
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  LEU A 106   N  LEU A  34
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  52   O  LYS A 138
SHEET    6   A 6 LYS A  66  SER A  69 -1  O  ASP A  68   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  LEU A 106   N  LEU A  34
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  52   O  LYS A 138
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         3.99
SITE     1 AC1 13 TYR A  57  PHE A  67  ASP A  68  PHE A  77
SITE     2 AC1 13 GLY A  84  GLN A  85  VAL A  86  ILE A  87
SITE     3 AC1 13 TRP A  90  TYR A 113  HOH A 377  HOH A 434
SITE     4 AC1 13 HOH A 435
CRYST1   42.162   55.272   56.822  90.00  90.00  90.00 P 21 21 21    4
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      0.023718  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018092  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017599        0.00000
      
PROCHECK
Go to PROCHECK summary
 References