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PDBsum entry 4drq

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Isomerase PDB id
4drq
Jmol
Contents
Protein chain
128 a.a.
Ligands
0OS
Waters ×209
HEADER    ISOMERASE                               17-FEB-12   4DRQ
TITLE     EXPLORATION OF PIPECOLATE SULFONAMIDES AS BINDERS OF THE FK506-BINDING
TITLE    2 PROTEINS 51 AND 52: COMPLEX OF FKBP51 WITH 2-(3-((R)-1-((S)-1-(3,5-
TITLE    3 DICHLOROPHENYLSULFONYL)PIPERIDINE-2-CARBONYLOXY)-3-(3,4-DIMETHOXY -
TITLE    4 PHENYL)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,Y.WANG,B.HOOGELAND,A.BRACHER,F.HAUSCH,
AUTHOR   2 S.SCHNEIDER
REVDAT   2   23-MAY-12 4DRQ    1       JRNL
REVDAT   1   18-APR-12 4DRQ    0
JRNL        AUTH   R.GOPALAKRISHNAN,C.KOZANY,Y.WANG,S.SCHNEIDER,B.HOOGELAND,
JRNL        AUTH 2 A.BRACHER,F.HAUSCH
JRNL        TITL   EXPLORATION OF PIPECOLATE SULFONAMIDES AS BINDERS OF THE
JRNL        TITL 2 FK506-BINDING PROTEINS 51 AND 52.
JRNL        REF    J.MED.CHEM.                   V.  55  4123 2012
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   22455398
JRNL        DOI    10.1021/JM201747C
REMARK   2
REMARK   2 RESOLUTION.    1.00 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) : 1.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 66559
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) : 0.138
REMARK   3   R VALUE            (WORKING SET) : 0.138
REMARK   3   FREE R VALUE                     : 0.151
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3503
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) : 1.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.03
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4784
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE SET COUNT          : 252
REMARK   3   BIN FREE R VALUE                    : 0.1870
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          : 35
REMARK   3   SOLVENT ATOMS            : 199
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.94
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.02000
REMARK   3    B22 (A**2) : 0.02000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.022
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.012
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.503
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1159 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):   813 ; 0.003 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1578 ; 1.724 ; 2.018
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1972 ; 0.872 ; 3.004
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   152 ; 7.007 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    43 ;27.154 ;24.651
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   212 ;10.781 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;11.998 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   165 ; 0.387 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1327 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   219 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   213 ; 0.245 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   874 ; 0.206 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   583 ; 0.179 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   580 ; 0.086 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   136 ; 0.243 ; 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):    10 ; 0.127 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.253 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    50 ; 0.302 ; 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):   749 ; 1.636 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   291 ; 0.682 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1168 ; 2.199 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   487 ; 3.047 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   410 ; 3.853 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2176 ; 1.281 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   209 ; 6.850 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1936 ; 3.563 ; 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 4DRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB070698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-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               : SLS
REMARK 200  BEAMLINE                       : X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9116
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70138
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.966
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.03300
REMARK 200   FOR THE DATA SET  : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.06
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.28500
REMARK 200  R SYM FOR SHELL            (I) : 0.28500
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS APO DATA
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3O5Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
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       20.98300
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.29800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.32050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.29800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.98300
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.32050
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     GLU A 140    CG   CD   OE1  OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     LYS A   65   N    CA   C    O    CB   CG   CD
REMARK 480     LYS A   65   CE   NZ
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   391     O    HOH A   402              1.59
REMARK 500   O    HOH A   402     O    HOH A   412              1.65
REMARK 500   O    HOH A   408     O    HOH A   422              2.10
REMARK 500   O    HOH A   395     O    HOH A   408              2.11
REMARK 500   NH2  ARG A    31     O    HOH A   410              2.12
REMARK 500   O    HOH A   421     O    HOH A   439              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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   ATM2   ATM3
REMARK 500    LYS A  65   CD  -  CE  -  NZ  ANGL. DEV. = -14.2 DEGREES
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     -117.00   -138.79
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 462        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A 493        DISTANCE =  7.07 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     0OS A  201
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0OS A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DRK   RELATED DB: PDB
REMARK 900 RELATED ID: 4DRM   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
DBREF  4DRQ A   16   140  UNP    Q13451   FKBP5_HUMAN     16    140
SEQADV 4DRQ GLY A   13  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRQ ALA A   14  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRQ PRO A   15  UNP  Q13451              EXPRESSION TAG
SEQADV 4DRQ 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    0OS  A 201      35
HETNAM     0OS {3-[(1S)-1-[({(2S)-1-[(3,5-DICHLOROPHENYL)
HETNAM   2 0OS  SULFONYL]PIPERIDIN-2-YL}CARBONYL)OXY]-3-(3,4-
HETNAM   3 0OS  DIMETHOXYPHENYL)PROPYL]PHENOXY}ACETIC ACID
FORMUL   2  0OS    C31 H33 CL2 N O9 S
FORMUL   3  HOH   *199(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  THR A   96  1                                  10
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  HIS A  56   O  GLU A 133
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  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  HIS A  56   O  GLU A 133
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         0.46
SITE     1 AC1 12 TYR A  57  PHE A  67  ASP A  68  GLN A  85
SITE     2 AC1 12 VAL A  86  ILE A  87  TRP A  90  TYR A 113
SITE     3 AC1 12 SER A 118  LYS A 121  ILE A 122  PHE A 130
CRYST1   41.966   54.641   56.596  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      0.023829  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018301  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017669        0.00000
      
PROCHECK
Go to PROCHECK summary
 References