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PDBsum entry 3o5i

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Isomerase PDB id
3o5i
Jmol
Contents
Protein chains
128 a.a.
Ligands
GOL
ACT
Waters ×164
HEADER    ISOMERASE                               28-JUL-10   3O5I
TITLE     FK1 DOMAIN OF FKBP51, CRYSTAL FORM II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP5;
COMPND   3 CHAIN: A, B;
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 3O5I    1       JRNL   VERSN
REVDAT   1   01-JUN-11 3O5I    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.    1.80 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) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 23530
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) : 0.205
REMARK   3   R VALUE            (WORKING SET) : 0.203
REMARK   3   FREE R VALUE                     : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 1213
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) : 1.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1591
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060
REMARK   3   BIN FREE R VALUE SET COUNT          : 99
REMARK   3   BIN FREE R VALUE                    : 0.2830
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1944
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 164
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.22
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.48
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): 0.139
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.269
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1992 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2676 ; 1.382 ; 1.979
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   254 ; 6.903 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    77 ;30.593 ;24.805
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   355 ;12.927 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;11.318 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   288 ; 0.096 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1478 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   906 ; 0.204 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1379 ; 0.307 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   172 ; 0.125 ; 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):    68 ; 0.269 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    34 ; 0.106 ; 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):  1306 ; 0.745 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2014 ; 1.108 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   784 ; 2.144 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   662 ; 3.060 ; 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   140
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4036  25.3913  48.4873
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1324 T22:  -0.1574
REMARK   3      T33:  -0.1419 T12:  -0.0135
REMARK   3      T13:  -0.0065 T23:   0.0271
REMARK   3    L TENSOR
REMARK   3      L11:   3.1272 L22:   1.8351
REMARK   3      L33:   2.9913 L12:   0.6001
REMARK   3      L13:  -0.6645 L23:  -0.4833
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0148 S12:   0.0675 S13:  -0.0393
REMARK   3      S21:  -0.1494 S22:   0.0849 S23:   0.0965
REMARK   3      S31:  -0.1387 S32:  -0.2030 S33:  -0.0700
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   140
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1315  24.6238 139.0279
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1038 T22:  -0.1715
REMARK   3      T33:  -0.1095 T12:  -0.0393
REMARK   3      T13:  -0.0013 T23:   0.0008
REMARK   3    L TENSOR
REMARK   3      L11:   3.2608 L22:   1.9092
REMARK   3      L33:   4.3871 L12:   0.6749
REMARK   3      L13:  -0.8282 L23:  -0.8488
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0602 S12:   0.0944 S13:  -0.0182
REMARK   3      S21:  -0.0605 S22:   0.0834 S23:   0.0466
REMARK   3      S31:  -0.0852 S32:  -0.1084 S33:  -0.0232
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 3O5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060690.
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   : 23588
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.193
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : 0.09400
REMARK 200  R SYM                      (I) : 0.09400
REMARK 200   FOR THE DATA SET  : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.41700
REMARK 200  R SYM FOR SHELL            (I) : 0.41700
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   (%): 43.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG3350, 0.2 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 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       60.15933
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      120.31867
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      120.31867
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       60.15933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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     ASN A  42    CG   OD1  ND2
REMARK 470     GLU B  44    CG   CD   OE1  OE2
REMARK 470     LYS B  52    CG   CD   CE   NZ
REMARK 470     LYS B  83    CG   CD   CE   NZ
REMARK 470     LYS B 138    CG   CD   CE   NZ
REMARK 470     GLU B 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   OH   TYR A    57     OD2  ASP A    68              2.02
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    ASN A  74       58.85     35.17
REMARK 500    ALA A 112     -111.92   -136.08
REMARK 500    GLU B  44      -30.57     71.26
REMARK 500    ALA B 112     -110.73   -132.91
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 GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 141
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: 3O5J   RELATED DB: PDB
REMARK 900 RELATED ID: 3O5K   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  3O5I A   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
DBREF  3O5I B   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
SEQADV 3O5I GLY A   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5I ALA A   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5I PRO A   15  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5I GLY B   13  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5I ALA B   14  UNP  Q13451              EXPRESSION TAG
SEQADV 3O5I PRO B   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
HET    GOL  B   1       6
HET    ACT  B 141       4
HETNAM     GOL GLYCEROL
HETNAM     ACT ACETATE ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  GOL    C3 H8 O3
FORMUL   4  ACT    C2 H3 O2 1-
FORMUL   5  HOH   *164(H2 O)
HELIX    1   1 GLY A   13  GLY A   22  1                                  10
HELIX    2   2 ILE A   87  ALA A   95  1                                   9
HELIX    3   3 PRO A  109  ALA A  112  5                                   4
HELIX    4   4 GLY B   13  GLY B   22  1                                  10
HELIX    5   5 HIS B   71  ASN B   74  5                                   4
HELIX    6   6 ILE B   87  ALA B   95  1                                   9
HELIX    7   7 PRO B  109  ALA B  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  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  79   N  VAL A  53
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  HIS B  56   O  GLU B 133
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  HIS B  56   O  GLU B 133
SHEET    6   D 6 PHE B  77  SER B  80 -1  O  PHE B  79   N  VAL B  53
CISPEP   1 LEU A  119    PRO A  120          0         9.07
CISPEP   2 LEU B  119    PRO B  120          0        -0.25
SITE     1 AC1  8 HIS B  56  TYR B  57  LYS B  58  HIS B  71
SITE     2 AC1  8 ILE B 102  GLU B 131  GLU B 133  HOH B 152
SITE     1 AC2  7 LYS A  58  LYS A  60  LYS A  66  SER A  69
SITE     2 AC2  7 HOH A 199  GLU B  45  THR B  46
CRYST1   48.353   48.353  180.478  90.00  90.00 120.00 P 31 2 1     12
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      0.020681  0.011940  0.000000        0.00000
SCALE2      0.000000  0.023881  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005541        0.00000
      
PROCHECK
Go to PROCHECK summary
 References