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PDBsum entry 3b7x

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Isomerase PDB id
3b7x
Jmol
Contents
Protein chain
117 a.a.
Waters ×55
HEADER    ISOMERASE                               31-OCT-07   3B7X
TITLE     CRYSTAL STRUCTURE OF HUMAN FK506-BINDING PROTEIN 6
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FK506-BINDING PROTEIN 6;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: PPIASE FKBP-TYPE DOMAIN: RESIDUES 12-144;
COMPND   5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, PPIASE,
COMPND   6 ROTAMASE, 36 KDA FK506-BINDING PROTEIN, FKBP-36,
COMPND   7 IMMUNOPHILIN FKBP36;
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: FKBP6, FKBP36;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-MHL
KEYWDS    ISOMERASE, REPEAT, ROTAMASE, TPR REPEAT, WILLIAMS-BEUREN
KEYWDS   2 SYNDROME, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.R.WALKER,T.DAVIS,C.BUTLER-COLE,R.PARAMANATHAN,J.WEIGELT,
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT   2   24-FEB-09 3B7X    1       VERSN
REVDAT   1   27-NOV-07 3B7X    0
JRNL        AUTH   J.R.WALKER,T.DAVIS,C.BUTLER-COLE,R.PARAMANATHAN,
JRNL        AUTH 2 J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,
JRNL        AUTH 3 S.DHE-PAGANON
JRNL        TITL   HUMAN FK506-BINDING PROTEIN 6.
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3
REMARK   3   NUMBER OF REFLECTIONS             : 10261
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) : 0.258
REMARK   3   R VALUE            (WORKING SET) : 0.256
REMARK   3   FREE R VALUE                     : 0.282
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 549
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 722
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.97
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000
REMARK   3   BIN FREE R VALUE SET COUNT          : 46
REMARK   3   BIN FREE R VALUE                    : 0.2960
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 922
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 55
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.58
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.41000
REMARK   3    B22 (A**2) : 3.41000
REMARK   3    B33 (A**2) : -6.83000
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): 0.215
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.186
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.153
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.637
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   939 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1268 ; 1.489 ; 2.012
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   114 ; 6.843 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    42 ;35.571 ;23.333
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   163 ;19.583 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;21.694 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   142 ; 0.108 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   703 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   401 ; 0.210 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   632 ; 0.312 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    59 ; 0.157 ; 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):    38 ; 0.256 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.169 ; 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):   598 ; 0.840 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   925 ; 1.481 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   389 ; 1.883 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   343 ; 3.021 ; 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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3B7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-07.
REMARK 100 THE RCSB ID CODE IS RCSB045190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X25
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : SI 111
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10831
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 9.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05400
REMARK 200   FOR THE DATA SET  : 46.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.36500
REMARK 200   FOR SHELL         : 6.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1KT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXED EQUAL VOLUMES OF 1.6M MGSO4,
REMARK 280  0.1M MES PH 6.5, AND 10 MG/ML PROTEIN. CRYSTALS WERE
REMARK 280  CRYOPROTECTED BY TRANSFERRING THE CRYSTALS TO A DROP
REMARK 280  CONTAINING MOTHER LIQUOR TO WHICH GLYCEROL WAS ADDED TO A
REMARK 280  FINAL CONCENTRATION OF 20%, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       3555   -Y,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   -X+1/2,Y,-Z+3/4
REMARK 290       6555   X,-Y+1/2,-Z+1/4
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X,-Y,Z
REMARK 290      11555   -Y+1/2,X,Z+3/4
REMARK 290      12555   Y,-X+1/2,Z+1/4
REMARK 290      13555   -X,Y+1/2,-Z+1/4
REMARK 290      14555   X+1/2,-Y,-Z+3/4
REMARK 290      15555   Y,X,-Z
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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       27.52950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       27.52950
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.98250
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.49125
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.52950
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      172.47375
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      172.47375
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.52950
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       57.49125
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       27.52950
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      114.98250
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       27.52950
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      114.98250
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       27.52950
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      172.47375
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       57.49125
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       27.52950
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       57.49125
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      172.47375
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       27.52950
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       27.52950
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      114.98250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     GLY A    11
REMARK 465     GLU A    12
REMARK 465     GLY A    13
REMARK 465     ASP A    14
REMARK 465     ASP A    15
REMARK 465     ALA A    16
REMARK 465     PRO A    17
REMARK 465     GLY A    18
REMARK 465     TYR A    76
REMARK 465     PHE A    77
REMARK 465     ARG A    78
REMARK 465     LYS A    79
REMARK 465     THR A    80
REMARK 465     PRO A    81
REMARK 465     ARG A    82
REMARK 465     GLY A    87
REMARK 465     ASP A   144
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  85    CG   CD   CE   NZ
REMARK 470     ILE A  90    CG1  CG2  CD1
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    PRO A  53      -19.14    -43.47
REMARK 500    MET A  84      114.19   -163.25
REMARK 500    ALA A 117     -107.71   -128.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF  3B7X A   12   144  UNP    O75344   FKBP6_HUMAN     12    144
SEQADV 3B7X GLY A   11  UNP  O75344              EXPRESSION TAG
SEQRES   1 A  134  GLY GLU GLY ASP ASP ALA PRO GLY GLN SER LEU TYR GLU
SEQRES   2 A  134  ARG LEU SER GLN ARG MET LEU ASP ILE SER GLY ASP ARG
SEQRES   3 A  134  GLY VAL LEU LYS ASP VAL ILE ARG GLU GLY ALA GLY ASP
SEQRES   4 A  134  LEU VAL ALA PRO ASP ALA SER VAL LEU VAL LYS TYR SER
SEQRES   5 A  134  GLY TYR LEU GLU HIS MET ASP ARG PRO PHE ASP SER ASN
SEQRES   6 A  134  TYR PHE ARG LYS THR PRO ARG LEU MET LYS LEU GLY GLU
SEQRES   7 A  134  ASP ILE THR LEU TRP GLY MET GLU LEU GLY LEU LEU SER
SEQRES   8 A  134  MET ARG ARG GLY GLU LEU ALA ARG PHE LEU PHE LYS PRO
SEQRES   9 A  134  ASN TYR ALA TYR GLY THR LEU GLY CYS PRO PRO LEU ILE
SEQRES  10 A  134  PRO PRO ASN THR THR VAL LEU PHE GLU ILE GLU LEU LEU
SEQRES  11 A  134  ASP PHE LEU ASP
FORMUL   2  HOH   *55(H2 O)
HELIX    1   1 SER A   20  SER A   26  1                                   7
HELIX    2   2 LEU A   92  SER A  101  1                                  10
HELIX    3   3 PRO A  114  ALA A  117  5                                   4
SHEET    1   A 6 LEU A  30  ASP A  31  0
SHEET    2   A 6 VAL A  38  ARG A  44 -1  O  LYS A  40   N  LEU A  30
SHEET    3   A 6 LEU A 107  PHE A 112 -1  O  ARG A 109   N  ASP A  41
SHEET    4   A 6 VAL A 133  LEU A 143 -1  O  ILE A 137   N  ALA A 108
SHEET    5   A 6 SER A  56  TYR A  64 -1  N  LEU A  58   O  ASP A 141
SHEET    6   A 6 ASP A  73  SER A  74 -1  O  ASP A  73   N  GLY A  63
SHEET    1   B 6 LEU A  30  ASP A  31  0
SHEET    2   B 6 VAL A  38  ARG A  44 -1  O  LYS A  40   N  LEU A  30
SHEET    3   B 6 LEU A 107  PHE A 112 -1  O  ARG A 109   N  ASP A  41
SHEET    4   B 6 VAL A 133  LEU A 143 -1  O  ILE A 137   N  ALA A 108
SHEET    5   B 6 SER A  56  TYR A  64 -1  N  LEU A  58   O  ASP A 141
SHEET    6   B 6 MET A  84  LYS A  85 -1  O  MET A  84   N  VAL A  57
SHEET    1   C 2 ALA A  47  LEU A  50  0
SHEET    2   C 2 ARG A 103  ARG A 104 -1  O  ARG A 104   N  ALA A  47
CISPEP   1 PRO A  124    PRO A  125          0        -3.01
CRYST1   55.059   55.059  229.965  90.00  90.00  90.00 I 41 2 2     16
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      0.018162  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018162  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004348        0.00000
      
PROCHECK
Go to PROCHECK summary
 References