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PDBsum entry 3jxv

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Isomerase PDB id
3jxv
Jmol
Contents
Protein chain
237 a.a.
Waters ×38
HEADER    ISOMERASE                               21-SEP-09   3JXV
TITLE     CRYSTAL STRUCTURE OF THE 3 FKBP DOMAINS OF WHEAT FKBP73
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 70 KDA PEPTIDYL-PROLYL ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, PPIASE, ROTAMASE;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE   3 ORGANISM_COMMON: WHEAT;
SOURCE   4 ORGANISM_TAXID: 4565;
SOURCE   5 GENE: FKBP70;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    FKBP- BINDING DOMAIN FIVE-STRANDED ANTI-PARALLEL BETA-SHEET AND AN
KEYWDS   2 ALPHA-HELIX CROSSING THIS SHEET, STRUCTURAL GENOMICS, ISRAEL
KEYWDS   3 STRUCTURAL PROTEOMICS CENTER, ISPC, CALMODULIN-BINDING, ISOMERASE,
KEYWDS   4 ROTAMASE, STRESS RESPONSE, TPR REPEAT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    O.DYM,A.BREIMAN,ISRAEL STRUCTURAL PROTEOMICS CENTER (ISPC)
REVDAT   2   30-JUN-10 3JXV    1       JRNL
REVDAT   1   16-JUN-10 3JXV    0
JRNL        AUTH   T.UNGER,O.DYM,S.ALBECK,Y.JACOBOVITCH,R.BERNEHIM,D.MAROM,
JRNL        AUTH 2 O.PISANTY,A.BREIMAN
JRNL        TITL   CRYSTAL STRUCTURE OF THE THREE FK506 BINDING PROTEIN
JRNL        TITL 2 DOMAINS OF WHEAT FKBP73: EVIDENCE FOR A UNIQUE WFK73_2
JRNL        TITL 3 DOMAIN.
JRNL        REF    J STRUCT FUNCT GENOMICS       V.  11   113 2010
JRNL        REFN
JRNL        PMID   20306145
JRNL        DOI    10.1007/S10969-010-9085-8
REMARK   2
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0067
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) : 2.08
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.80
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2
REMARK   3   NUMBER OF REFLECTIONS             : 23753
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) : 0.251
REMARK   3   R VALUE            (WORKING SET) : 0.248
REMARK   3   FREE R VALUE                     : 0.287
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1271
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) : 2.08
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1347
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.48
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370
REMARK   3   BIN FREE R VALUE SET COUNT          : 67
REMARK   3   BIN FREE R VALUE                    : 0.2950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1825
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 38
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.91
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.13000
REMARK   3    B22 (A**2) : 2.11000
REMARK   3    B33 (A**2) : -1.36000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.27000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.178
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.693
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1856 ; 0.027 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2503 ; 2.352 ; 1.994
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   235 ; 9.281 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    74 ;36.267 ;26.216
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   350 ;18.092 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;16.544 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   284 ; 0.238 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1357 ; 0.011 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1174 ; 1.544 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1899 ; 2.677 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   682 ; 4.460 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   604 ; 7.723 ; 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 : 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 3JXV COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM14
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25033
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.800
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : 0.06800
REMARK 200  R SYM                      (I) : 0.06200
REMARK 200   FOR THE DATA SET  : 54.3000
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     (%) : 94.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.24300
REMARK 200  R SYM FOR SHELL            (I) : 0.24600
REMARK 200   FOR SHELL         : 6.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KNO3   0.1 BIS TRIXPROPANE PH=8.5
REMARK 280  20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
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       15.66100
REMARK 290   SMTRY3   2  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 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     LYS A    31
REMARK 465     VAL A    32
REMARK 465     GLY A    33
REMARK 465     GLU A    34
REMARK 465     GLU A    35
REMARK 465     ASN A    36
REMARK 465     GLU A    37
REMARK 465     ILE A    38
REMARK 465     GLY A    39
REMARK 465     LYS A    40
REMARK 465     GLN A    41
REMARK 465     GLY A    42
REMARK 465     LEU A    43
REMARK 465     LYS A    44
REMARK 465     LYS A    45
REMARK 465     LYS A    46
REMARK 465     LEU A    47
REMARK 465     LEU A    48
REMARK 465     LYS A    49
REMARK 465     GLU A    50
REMARK 465     GLY A    51
REMARK 465     GLU A    52
REMARK 465     GLY A    53
REMARK 465     TRP A    54
REMARK 465     ASP A    55
REMARK 465     THR A    56
REMARK 465     PRO A    57
REMARK 465     GLU A    58
REMARK 465     VAL A    59
REMARK 465     GLY A    60
REMARK 465     ASP A    61
REMARK 465     GLU A    62
REMARK 465     VAL A    63
REMARK 465     GLU A    64
REMARK 465     VAL A    65
REMARK 465     HIS A    66
REMARK 465     TYR A    67
REMARK 465     THR A    68
REMARK 465     GLY A    69
REMARK 465     THR A    70
REMARK 465     LEU A    71
REMARK 465     LEU A    72
REMARK 465     ASP A    73
REMARK 465     GLY A    74
REMARK 465     LYS A    75
REMARK 465     LYS A    76
REMARK 465     PHE A    77
REMARK 465     ASP A    78
REMARK 465     SER A    79
REMARK 465     SER A    80
REMARK 465     ARG A    81
REMARK 465     ASP A    82
REMARK 465     ARG A    83
REMARK 465     ASP A    84
REMARK 465     ASP A    85
REMARK 465     THR A    86
REMARK 465     PHE A    87
REMARK 465     LYS A    88
REMARK 465     PHE A    89
REMARK 465     LYS A    90
REMARK 465     LEU A    91
REMARK 465     GLY A    92
REMARK 465     GLN A    93
REMARK 465     GLY A    94
REMARK 465     GLN A    95
REMARK 465     VAL A    96
REMARK 465     ILE A    97
REMARK 465     LYS A    98
REMARK 465     GLY A    99
REMARK 465     TRP A   100
REMARK 465     ASP A   101
REMARK 465     GLN A   102
REMARK 465     GLY A   103
REMARK 465     ILE A   104
REMARK 465     LYS A   105
REMARK 465     THR A   106
REMARK 465     MET A   107
REMARK 465     LYS A   108
REMARK 465     LYS A   109
REMARK 465     GLY A   110
REMARK 465     GLU A   111
REMARK 465     ASN A   112
REMARK 465     ALA A   113
REMARK 465     LEU A   114
REMARK 465     PHE A   115
REMARK 465     THR A   116
REMARK 465     ILE A   117
REMARK 465     PRO A   118
REMARK 465     PRO A   119
REMARK 465     GLU A   120
REMARK 465     LEU A   121
REMARK 465     ALA A   122
REMARK 465     TYR A   123
REMARK 465     GLY A   124
REMARK 465     GLU A   125
REMARK 465     SER A   126
REMARK 465     GLY A   127
REMARK 465     SER A   128
REMARK 465     PRO A   129
REMARK 465     PRO A   130
REMARK 465     THR A   131
REMARK 465     ILE A   132
REMARK 465     PRO A   133
REMARK 465     ALA A   134
REMARK 465     ASN A   135
REMARK 465     ALA A   136
REMARK 465     THR A   137
REMARK 465     LEU A   138
REMARK 465     GLN A   139
REMARK 465     PHE A   140
REMARK 465     ASP A   141
REMARK 465     VAL A   142
REMARK 465     GLU A   143
REMARK 465     LEU A   144
REMARK 465     LEU A   145
REMARK 465     SER A   146
REMARK 465     TRP A   147
REMARK 465     GLU A   245
REMARK 465     GLY A   246
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   OD2  ASP A   273     OH   TYR A   355              1.61
REMARK 500
REMARK 500 REMARK: NULL
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 A 307   N     GLY A 307   CA      0.097
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    ASP A 306   O   -  C   -  N   ANGL. DEV. = -10.5 DEGREES
REMARK 500    GLY A 307   C   -  N   -  CA  ANGL. DEV. = -22.6 DEGREES
REMARK 500    VAL A 374   CG1 -  CB  -  CG2 ANGL. DEV. =  13.1 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    LYS A 169     -163.94     87.68
REMARK 500    LEU A 208      -66.44     72.30
REMARK 500    ALA A 243      -50.24    163.78
REMARK 500    TYR A 287      133.48     39.44
REMARK 500    GLU A 288      131.05    105.70
REMARK 500    ALA A 356     -112.79   -131.75
REMARK 500    GLN A 364     -144.59   -119.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU A  285     GLY A  286                 -108.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR A 308        19.6      L          L   OUTSIDE RANGE
REMARK 500    THR A 373        24.4      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
DBREF  3JXV A   31   386  UNP    Q43207   FKB70_WHEAT     31    386
SEQRES   1 A  356  LYS VAL GLY GLU GLU ASN GLU ILE GLY LYS GLN GLY LEU
SEQRES   2 A  356  LYS LYS LYS LEU LEU LYS GLU GLY GLU GLY TRP ASP THR
SEQRES   3 A  356  PRO GLU VAL GLY ASP GLU VAL GLU VAL HIS TYR THR GLY
SEQRES   4 A  356  THR LEU LEU ASP GLY LYS LYS PHE ASP SER SER ARG ASP
SEQRES   5 A  356  ARG ASP ASP THR PHE LYS PHE LYS LEU GLY GLN GLY GLN
SEQRES   6 A  356  VAL ILE LYS GLY TRP ASP GLN GLY ILE LYS THR MET LYS
SEQRES   7 A  356  LYS GLY GLU ASN ALA LEU PHE THR ILE PRO PRO GLU LEU
SEQRES   8 A  356  ALA TYR GLY GLU SER GLY SER PRO PRO THR ILE PRO ALA
SEQRES   9 A  356  ASN ALA THR LEU GLN PHE ASP VAL GLU LEU LEU SER TRP
SEQRES  10 A  356  THR SER VAL ARG ASP ILE ALA LYS ASP GLY GLY ILE PHE
SEQRES  11 A  356  LYS LYS ILE LEU LYS GLU GLY ASP LYS TRP GLU ASN PRO
SEQRES  12 A  356  LYS ASP PRO ASP GLU VAL PHE VAL LYS TYR GLU ALA ARG
SEQRES  13 A  356  LEU GLU ASP GLY THR VAL VAL SER LYS SER GLU GLY VAL
SEQRES  14 A  356  GLU PHE THR VAL LYS ASP GLY HIS LEU CYS PRO ALA LEU
SEQRES  15 A  356  ALA LYS ALA VAL LYS THR MET LYS LYS GLY GLU LYS VAL
SEQRES  16 A  356  LEU LEU ALA VAL LYS PRO GLN TYR GLY PHE GLY GLU MET
SEQRES  17 A  356  GLY ARG PRO ALA ALA GLY GLU GLY GLY ALA VAL PRO PRO
SEQRES  18 A  356  ASN ALA SER LEU VAL ILE ASP LEU GLU LEU VAL SER TRP
SEQRES  19 A  356  LYS THR VAL THR GLU ILE GLY ASP ASP LYS LYS ILE LEU
SEQRES  20 A  356  LYS LYS VAL LEU LYS GLU UNK GLU GLY TYR GLU ARG PRO
SEQRES  21 A  356  ASN GLU GLY ALA VAL VAL THR VAL LYS ILE THR GLY LYS
SEQRES  22 A  356  LEU GLN ASP GLY THR VAL PHE LEU LYS LYS GLY HIS ASP
SEQRES  23 A  356  GLU GLN GLU PRO PHE GLU PHE LYS THR ASP GLU GLU ALA
SEQRES  24 A  356  VAL ILE GLU GLY LEU ASP ARG ALA VAL LEU ASN MET LYS
SEQRES  25 A  356  LYS GLY GLU VAL ALA LEU VAL THR ILE PRO PRO GLU TYR
SEQRES  26 A  356  ALA TYR GLY SER THR GLU SER LYS GLN ASP ALA ILE VAL
SEQRES  27 A  356  PRO PRO ASN SER THR VAL ILE TYR GLU VAL GLU LEU VAL
SEQRES  28 A  356  SER PHE VAL LYS ASP
FORMUL   2  HOH   *38(H2 O)
HELIX    1   1 LYS A  204  GLY A  206  5                                   3
HELIX    2   2 CYS A  209  LYS A  217  1                                   9
HELIX    3   3 PRO A  231  GLY A  234  5                                   4
HELIX    4   4 ILE A  331  LEU A  339  1                                   9
HELIX    5   5 PRO A  352  ALA A  356  5                                   5
SHEET    1   A 6 VAL A 150  ASP A 152  0
SHEET    2   A 6 ILE A 159  LYS A 165 -1  O  LYS A 161   N  ARG A 151
SHEET    3   A 6 LYS A 224  VAL A 229 -1  O  LEU A 226   N  LYS A 162
SHEET    4   A 6 LEU A 255  LYS A 265 -1  O  LEU A 259   N  VAL A 225
SHEET    5   A 6 GLU A 178  LEU A 187 -1  N  ARG A 186   O  VAL A 256
SHEET    6   A 6 VAL A 192  THR A 202 -1  O  SER A 194   N  ALA A 185
SHEET    1   B 6 VAL A 267  ILE A 270  0
SHEET    2   B 6 ILE A 276  LYS A 282 -1  O  ILE A 276   N  ILE A 270
SHEET    3   B 6 VAL A 346  ILE A 351 -1  O  LEU A 348   N  LYS A 279
SHEET    4   B 6 VAL A 374  VAL A 384 -1  O  TYR A 376   N  VAL A 349
SHEET    5   B 6 VAL A 295  LEU A 304 -1  N  LYS A 303   O  ILE A 375
SHEET    6   B 6 VAL A 309  LYS A 313 -1  O  PHE A 310   N  GLY A 302
SHEET    1   C 6 VAL A 267  ILE A 270  0
SHEET    2   C 6 ILE A 276  LYS A 282 -1  O  ILE A 276   N  ILE A 270
SHEET    3   C 6 VAL A 346  ILE A 351 -1  O  LEU A 348   N  LYS A 279
SHEET    4   C 6 VAL A 374  VAL A 384 -1  O  TYR A 376   N  VAL A 349
SHEET    5   C 6 VAL A 295  LEU A 304 -1  N  LYS A 303   O  ILE A 375
SHEET    6   C 6 GLU A 322  LYS A 324 -1  O  PHE A 323   N  VAL A 296
SHEET    1   D 2 SER A 362  LYS A 363  0
SHEET    2   D 2 ILE A 367  VAL A 368 -1  O  VAL A 368   N  SER A 362
CRYST1   69.168   31.322   96.716  90.00  98.46  90.00 P 1 21 1      2
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      0.014458  0.000000  0.002150        0.00000
SCALE2      0.000000  0.031926  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010453        0.00000
      
PROCHECK
Go to PROCHECK summary
 References