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PDBsum entry 3o5k

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Isomerase PDB id
3o5k
Jmol
Contents
Protein chains
127 a.a.
HEADER    ISOMERASE                               28-JUL-10   3O5K
TITLE     FK1 DOMAIN OF FKBP51, CRYSTAL FORM VIII
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP5;
COMPND   3 CHAIN: A, B, C, D;
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
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 3O5K    1       JRNL   VERSN
REVDAT   1   01-JUN-11 3O5K    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.    2.70 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) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 12890
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) : 0.227
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.283
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 629
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) : 2.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 872
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.46
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920
REMARK   3   BIN FREE R VALUE SET COUNT          : 46
REMARK   3   BIN FREE R VALUE                    : 0.4610
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3794
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 53.37
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.15000
REMARK   3    B22 (A**2) : -1.44000
REMARK   3    B33 (A**2) : 1.97000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.82000
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): 0.433
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.329
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.643
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3874 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5223 ; 1.223 ; 1.972
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   506 ; 6.637 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   141 ;34.656 ;24.468
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   655 ;16.111 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;12.899 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   572 ; 0.083 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2887 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1589 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2592 ; 0.306 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   122 ; 0.135 ; 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):    79 ; 0.323 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.099 ; 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):  2568 ; 0.353 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3989 ; 0.632 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1466 ; 0.874 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1234 ; 1.403 ; 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  : 4
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):   0.3558   0.5311   5.7032
REMARK   3    T TENSOR
REMARK   3      T11:  -0.2353 T22:  -0.1730
REMARK   3      T33:  -0.2261 T12:  -0.0157
REMARK   3      T13:  -0.0291 T23:   0.0279
REMARK   3    L TENSOR
REMARK   3      L11:   3.5158 L22:   6.4419
REMARK   3      L33:   4.8960 L12:  -1.1230
REMARK   3      L13:  -1.5353 L23:  -0.1998
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0371 S12:  -0.1557 S13:   0.0253
REMARK   3      S21:   0.3183 S22:   0.0080 S23:  -0.0228
REMARK   3      S31:  -0.1158 S32:  -0.0404 S33:   0.0291
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 :   B    13        B   139
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2013   1.1256   4.6837
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1923 T22:  -0.1674
REMARK   3      T33:  -0.1074 T12:  -0.0333
REMARK   3      T13:  -0.0253 T23:  -0.0227
REMARK   3    L TENSOR
REMARK   3      L11:   8.9289 L22:   6.3539
REMARK   3      L33:   2.7548 L12:  -1.6076
REMARK   3      L13:  -1.6037 L23:   0.1533
REMARK   3    S TENSOR
REMARK   3      S11:   0.0569 S12:  -0.2526 S13:   0.4154
REMARK   3      S21:   0.1955 S22:   0.1346 S23:  -0.2532
REMARK   3      S31:  -0.1145 S32:   0.0709 S33:  -0.1915
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    13        C   140
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4581  -2.0425 -29.1122
REMARK   3    T TENSOR
REMARK   3      T11:   0.0336 T22:  -0.0622
REMARK   3      T33:  -0.1560 T12:  -0.1235
REMARK   3      T13:   0.0421 T23:   0.0067
REMARK   3    L TENSOR
REMARK   3      L11:   6.4196 L22:  10.2130
REMARK   3      L33:   7.5405 L12:  -1.6386
REMARK   3      L13:  -2.8950 L23:  -0.9713
REMARK   3    S TENSOR
REMARK   3      S11:   0.1733 S12:  -0.4281 S13:   0.3485
REMARK   3      S21:   0.5633 S22:  -0.1869 S23:  -0.4056
REMARK   3      S31:  -0.6566 S32:   0.4473 S33:   0.0137
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    13        D   140
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0764 -17.1129  29.6999
REMARK   3    T TENSOR
REMARK   3      T11:   0.2776 T22:   0.2098
REMARK   3      T33:   0.5160 T12:   0.0550
REMARK   3      T13:   0.1002 T23:  -0.0051
REMARK   3    L TENSOR
REMARK   3      L11:  10.9260 L22:   8.9858
REMARK   3      L33:   5.6545 L12:   2.7082
REMARK   3      L13:   3.7135 L23:   0.6313
REMARK   3    S TENSOR
REMARK   3      S11:   0.0914 S12:   0.9356 S13:  -1.1258
REMARK   3      S21:  -0.9339 S22:   0.4225 S23:  -1.6293
REMARK   3      S31:   0.1119 S32:   0.4085 S33:  -0.5139
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 3O5K 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 RCSB060692.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-09
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                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.886
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12932
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.505
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.08800
REMARK 200  R SYM                      (I) : 0.08800
REMARK 200   FOR THE DATA SET  : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200
REMARK 200  R SYM FOR SHELL            (I) : 0.39200
REMARK 200   FOR SHELL         : 1.900
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 3O5I, CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32 % PEG3350, 0.05 M NH4OAC, 0.1 M
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       24.21500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
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: D
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     GLU A   140
REMARK 465     GLU B   140
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  20    CG   CD   OE1  OE2
REMARK 470     GLU A  23    CG   CD   OE1  OE2
REMARK 470     GLU A  44    CG   CD   OE1  OE2
REMARK 470     GLU A  75    CG   CD   OE1  OE2
REMARK 470     GLU B  44    CG   CD   OE1  OE2
REMARK 470     ARG B  73    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B  75    CG   CD   OE1  OE2
REMARK 470     LEU B 119    CG   CD1  CD2
REMARK 470     LYS B 138    CG   CD   CE   NZ
REMARK 470     GLU C  20    CG   CD   OE1  OE2
REMARK 470     GLN C  21    CG   CD   OE1  NE2
REMARK 470     ASN C  42    CG   OD1  ND2
REMARK 470     GLU C  44    CG   CD   OE1  OE2
REMARK 470     LYS C  52    CG   CD   CE   NZ
REMARK 470     LYS C  65    CG   CD   CE   NZ
REMARK 470     LYS C 121    CG   CD   CE   NZ
REMARK 470     LYS C 138    CG   CD   CE   NZ
REMARK 470     GLU C 140    CG   CD   OE1  OE2
REMARK 470     GLN D  21    CG   CD   OE1  NE2
REMARK 470     GLU D  23    CG   CD   OE1  OE2
REMARK 470     ASN D  42    CG   OD1  ND2
REMARK 470     GLU D  44    CG   CD   OE1  OE2
REMARK 470     GLU D  45    CG   CD   OE1  OE2
REMARK 470     LYS D  52    CG   CD   CE   NZ
REMARK 470     LYS D  58    CG   CD   CE   NZ
REMARK 470     LYS D  60    CG   CD   CE   NZ
REMARK 470     LEU D  61    CG   CD1  CD2
REMARK 470     LYS D  65    CG   CD   CE   NZ
REMARK 470     LYS D  66    CG   CD   CE   NZ
REMARK 470     LYS D  83    CG   CD   CE   NZ
REMARK 470     LYS D  99    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLY C  13   N     GLY C  13   CA      0.208
REMARK 500    GLU D  75   CD    GLU D  75   OE1     0.108
REMARK 500    GLU D  75   CD    GLU D  75   OE2     0.115
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  14       85.24     31.23
REMARK 500    ALA A 112     -101.58   -125.19
REMARK 500    ASP B  68      142.87   -175.79
REMARK 500    ALA B 112     -115.11   -144.22
REMARK 500    SER B 118      109.93   -162.91
REMARK 500    LYS B 121       35.26   -143.18
REMARK 500    SER B 124      126.83    -35.48
REMARK 500    SER C  62        0.91    -61.05
REMARK 500    ASN C  74       53.66     33.24
REMARK 500    ALA C 112     -104.93   -127.57
REMARK 500    SER C 118       97.11   -169.11
REMARK 500    LYS C 121      -70.82    -78.98
REMARK 500    ASN C 125       79.47     81.23
REMARK 500    ASP D  68      144.33   -174.86
REMARK 500    ILE D  87      153.01    -49.51
REMARK 500    ALA D 112     -108.58    -99.31
REMARK 500    SER D 118       88.94   -179.39
REMARK 500    LYS D 121      -70.93    -66.01
REMARK 500
REMARK 500 REMARK: NULL
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: 3O5L   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
DBREF  3O5K A   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
DBREF  3O5K B   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
DBREF  3O5K C   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
DBREF  3O5K D   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
SEQADV 3O5K GLY A   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K ALA A   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K PRO A   15  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K GLY B   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K ALA B   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K PRO B   15  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K GLY C   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K ALA C   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K PRO C   15  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K GLY D   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K ALA D   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5K PRO D   15  UNP  Q13451              EXPRESSION TAG
SEQRES   1 A  128  GLY ALA PRO ALA THR VAL ALA 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
SEQRES   1 B  128  GLY ALA PRO ALA THR VAL ALA GLU GLN GLY GLU ASP ILE
SEQRES   2 B  128  THR SER LYS LYS ASP ARG GLY VAL LEU LYS ILE VAL LYS
SEQRES   3 B  128  ARG VAL GLY ASN GLY GLU GLU THR PRO MET ILE GLY ASP
SEQRES   4 B  128  LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU SER ASN GLY
SEQRES   5 B  128  LYS LYS PHE ASP SER SER HIS ASP ARG ASN GLU PRO PHE
SEQRES   6 B  128  VAL PHE SER LEU GLY LYS GLY GLN VAL ILE LYS ALA TRP
SEQRES   7 B  128  ASP ILE GLY VAL ALA THR MET LYS LYS GLY GLU ILE CYS
SEQRES   8 B  128  HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR GLY SER ALA
SEQRES   9 B  128  GLY SER LEU PRO LYS ILE PRO SER ASN ALA THR LEU PHE
SEQRES  10 B  128  PHE GLU ILE GLU LEU LEU ASP PHE LYS GLY GLU
SEQRES   1 C  128  GLY ALA PRO ALA THR VAL ALA GLU GLN GLY GLU ASP ILE
SEQRES   2 C  128  THR SER LYS LYS ASP ARG GLY VAL LEU LYS ILE VAL LYS
SEQRES   3 C  128  ARG VAL GLY ASN GLY GLU GLU THR PRO MET ILE GLY ASP
SEQRES   4 C  128  LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU SER ASN GLY
SEQRES   5 C  128  LYS LYS PHE ASP SER SER HIS ASP ARG ASN GLU PRO PHE
SEQRES   6 C  128  VAL PHE SER LEU GLY LYS GLY GLN VAL ILE LYS ALA TRP
SEQRES   7 C  128  ASP ILE GLY VAL ALA THR MET LYS LYS GLY GLU ILE CYS
SEQRES   8 C  128  HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR GLY SER ALA
SEQRES   9 C  128  GLY SER LEU PRO LYS ILE PRO SER ASN ALA THR LEU PHE
SEQRES  10 C  128  PHE GLU ILE GLU LEU LEU ASP PHE LYS GLY GLU
SEQRES   1 D  128  GLY ALA PRO ALA THR VAL ALA GLU GLN GLY GLU ASP ILE
SEQRES   2 D  128  THR SER LYS LYS ASP ARG GLY VAL LEU LYS ILE VAL LYS
SEQRES   3 D  128  ARG VAL GLY ASN GLY GLU GLU THR PRO MET ILE GLY ASP
SEQRES   4 D  128  LYS VAL TYR VAL HIS TYR LYS GLY LYS LEU SER ASN GLY
SEQRES   5 D  128  LYS LYS PHE ASP SER SER HIS ASP ARG ASN GLU PRO PHE
SEQRES   6 D  128  VAL PHE SER LEU GLY LYS GLY GLN VAL ILE LYS ALA TRP
SEQRES   7 D  128  ASP ILE GLY VAL ALA THR MET LYS LYS GLY GLU ILE CYS
SEQRES   8 D  128  HIS LEU LEU CYS LYS PRO GLU TYR ALA TYR GLY SER ALA
SEQRES   9 D  128  GLY SER LEU PRO LYS ILE PRO SER ASN ALA THR LEU PHE
SEQRES  10 D  128  PHE GLU ILE GLU LEU LEU ASP PHE LYS GLY GLU
HELIX    1   1 ALA A   14  GLY A   22  1                                   9
HELIX    2   2 SER A   70  ASN A   74  1                                   5
HELIX    3   3 ILE A   87  THR A   96  1                                  10
HELIX    4   4 PRO A  109  ALA A  112  5                                   4
HELIX    5   5 GLY B   13  GLY B   22  1                                  10
HELIX    6   6 ILE B   87  VAL B   94  1                                   8
HELIX    7   7 ALA B   95  MET B   97  5                                   3
HELIX    8   8 PRO B  109  ALA B  112  5                                   4
HELIX    9   9 PRO C   15  GLY C   22  1                                   8
HELIX   10  10 HIS C   71  ARG C   73  5                                   3
HELIX   11  11 ILE C   87  ALA C   95  1                                   9
HELIX   12  12 PRO C  109  ALA C  112  5                                   4
HELIX   13  13 GLY D   13  GLY D   22  1                                  10
HELIX   14  14 ILE D   87  THR D   96  1                                  10
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  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  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  77   N  VAL A  55
SHEET    1   C 6 GLU B  23  ASP B  24  0
SHEET    2   C 6 VAL B  33  ARG B  39 -1  O  LYS B  35   N  GLU B  23
SHEET    3   C 6 ILE B 102  CYS B 107 -1  O  ILE B 102   N  LYS B  38
SHEET    4   C 6 LEU B 128  LYS B 138 -1  O  LEU B 128   N  CYS B 107
SHEET    5   C 6 LYS B  52  LEU B  61 -1  N  LYS B  60   O  PHE B 129
SHEET    6   C 6 LYS B  66  SER B  69 -1  O  ASP B  68   N  GLY B  59
SHEET    1   D 6 GLU B  23  ASP B  24  0
SHEET    2   D 6 VAL B  33  ARG B  39 -1  O  LYS B  35   N  GLU B  23
SHEET    3   D 6 ILE B 102  CYS B 107 -1  O  ILE B 102   N  LYS B  38
SHEET    4   D 6 LEU B 128  LYS B 138 -1  O  LEU B 128   N  CYS B 107
SHEET    5   D 6 LYS B  52  LEU B  61 -1  N  LYS B  60   O  PHE B 129
SHEET    6   D 6 PHE B  77  SER B  80 -1  O  PHE B  77   N  VAL B  55
SHEET    1   E 6 GLU C  23  ASP C  24  0
SHEET    2   E 6 VAL C  33  ARG C  39 -1  O  LYS C  35   N  GLU C  23
SHEET    3   E 6 ILE C 102  CYS C 107 -1  O  HIS C 104   N  ILE C  36
SHEET    4   E 6 LEU C 128  LYS C 138 -1  O  LEU C 128   N  CYS C 107
SHEET    5   E 6 LYS C  52  LEU C  61 -1  N  HIS C  56   O  GLU C 133
SHEET    6   E 6 LYS C  66  SER C  69 -1  O  ASP C  68   N  GLY C  59
SHEET    1   F 6 GLU C  23  ASP C  24  0
SHEET    2   F 6 VAL C  33  ARG C  39 -1  O  LYS C  35   N  GLU C  23
SHEET    3   F 6 ILE C 102  CYS C 107 -1  O  HIS C 104   N  ILE C  36
SHEET    4   F 6 LEU C 128  LYS C 138 -1  O  LEU C 128   N  CYS C 107
SHEET    5   F 6 LYS C  52  LEU C  61 -1  N  HIS C  56   O  GLU C 133
SHEET    6   F 6 PHE C  77  SER C  80 -1  O  PHE C  77   N  VAL C  55
SHEET    1   G 6 GLU D  23  ASP D  24  0
SHEET    2   G 6 VAL D  33  ARG D  39 -1  O  LYS D  35   N  GLU D  23
SHEET    3   G 6 ILE D 102  CYS D 107 -1  O  ILE D 102   N  LYS D  38
SHEET    4   G 6 LEU D 128  LYS D 138 -1  O  LEU D 128   N  CYS D 107
SHEET    5   G 6 LYS D  52  LEU D  61 -1  N  HIS D  56   O  GLU D 133
SHEET    6   G 6 LYS D  66  SER D  69 -1  O  ASP D  68   N  GLY D  59
SHEET    1   H 6 GLU D  23  ASP D  24  0
SHEET    2   H 6 VAL D  33  ARG D  39 -1  O  LYS D  35   N  GLU D  23
SHEET    3   H 6 ILE D 102  CYS D 107 -1  O  ILE D 102   N  LYS D  38
SHEET    4   H 6 LEU D 128  LYS D 138 -1  O  LEU D 128   N  CYS D 107
SHEET    5   H 6 LYS D  52  LEU D  61 -1  N  HIS D  56   O  GLU D 133
SHEET    6   H 6 PHE D  77  SER D  80 -1  O  PHE D  79   N  VAL D  53
CISPEP   1 LEU A  119    PRO A  120          0         3.10
CISPEP   2 LEU B  119    PRO B  120          0         2.79
CISPEP   3 LEU C  119    PRO C  120          0        -6.60
CISPEP   4 LEU D  119    PRO D  120          0       -13.93
CRYST1   69.802   48.430   76.317  90.00 114.50  90.00 P 1 21 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      0.014326  0.000000  0.006527        0.00000
SCALE2      0.000000  0.020648  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014399        0.00000
      
PROCHECK
Go to PROCHECK summary
 References