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PDBsum entry 3e2i

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Transferase PDB id
3e2i
Jmol
Contents
Protein chain
175 a.a.
Ligands
GOL
Metals
_ZN
Waters ×58
HEADER    TRANSFERASE                             05-AUG-08   3E2I
TITLE     CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM S. AUREUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THYMIDINE KINASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 2.7.1.21;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE   3 ORGANISM_TAXID: 1280;
SOURCE   4 GENE: TDK;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS RIPL;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS    ZN-BINDING, ATP-BINDING, DNA SYNTHESIS, KINASE, NUCLEOTIDE-BINDING,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.LAM,K.JOHNS,K.P.BATTAILE,V.ROMANOV,K.LAM,E.F.PAI,N.Y.CHIRGADZE
REVDAT   2   13-JUL-11 3E2I    1       VERSN
REVDAT   1   11-AUG-09 3E2I    0
JRNL        AUTH   R.LAM,K.JOHNS,K.P.BATTAILE,V.ROMANOV,K.LAM,E.F.PAI,
JRNL        AUTH 2 N.Y.CHIRGADZE
JRNL        TITL   CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM S. AUREUS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0043
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) : 2.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.81
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 17194
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) : 0.203
REMARK   3   R VALUE            (WORKING SET) : 0.202
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 871
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) : 2.01
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1176
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020
REMARK   3   BIN FREE R VALUE SET COUNT          : 55
REMARK   3   BIN FREE R VALUE                    : 0.2790
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1341
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 7
REMARK   3   SOLVENT ATOMS            : 58
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.27
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.03000
REMARK   3    B22 (A**2) : 0.03000
REMARK   3    B33 (A**2) : -0.06000
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): 0.151
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.143
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.633
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1377 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1858 ; 1.228 ; 1.964
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   177 ; 4.989 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    58 ;32.164 ;24.138
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   250 ;14.375 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;14.378 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   213 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1016 ; 0.005 ; 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):   875 ; 0.681 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1419 ; 1.309 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   502 ; 2.255 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   437 ; 3.701 ; 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  : 1
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     7        A   192
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9370  13.4810  12.5360
REMARK   3    T TENSOR
REMARK   3      T11:   0.1067 T22:   0.0441
REMARK   3      T33:   0.0789 T12:   0.0002
REMARK   3      T13:  -0.0117 T23:  -0.0359
REMARK   3    L TENSOR
REMARK   3      L11:   1.8770 L22:   0.7463
REMARK   3      L33:   1.8932 L12:  -0.2124
REMARK   3      L13:  -0.0657 L23:  -0.2179
REMARK   3    S TENSOR
REMARK   3      S11:   0.0030 S12:  -0.0797 S13:   0.1575
REMARK   3      S21:   0.1532 S22:  -0.0289 S23:  -0.0553
REMARK   3      S31:  -0.3488 S32:  -0.0403 S33:   0.0258
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   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK   3  U VALUES      : RESIDUAL ONLY
REMARK   4
REMARK   4 3E2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979331
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE-CRYSTAL
REMARK 200                                   MONOCHROMATOR
REMARK 200  OPTICS                         : SI(111) DOUBLE-CRYSTAL
REMARK 200                                   MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17226
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 24.500
REMARK 200  R MERGE                    (I) : 0.06400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 22.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.18300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SUCCINIC ACID PH 7.0, 15%
REMARK 280  PEG3350, CRYO-PROTECTED USING 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z+1/2
REMARK 290       4555   Y,-X,Z+1/2
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z+1/2
REMARK 290       8555   -Y,-X,-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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       48.07200
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       48.07200
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        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.07200
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       48.07200
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000       71.62100
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       71.62100
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 225  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 247  LIES ON A SPECIAL POSITION.
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     MSE A   -19
REMARK 465     GLY A   -18
REMARK 465     SER A   -17
REMARK 465     SER A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     SER A    -9
REMARK 465     SER A    -8
REMARK 465     GLY A    -7
REMARK 465     LEU A    -6
REMARK 465     VAL A    -5
REMARK 465     PRO A    -4
REMARK 465     ARG A    -3
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MSE A     1
REMARK 465     TYR A     2
REMARK 465     GLU A     3
REMARK 465     THR A     4
REMARK 465     TYR A     5
REMARK 465     HIS A     6
REMARK 465     ILE A    46
REMARK 465     ASP A    47
REMARK 465     ASP A    48
REMARK 465     ARG A    49
REMARK 465     TYR A    50
REMARK 465     HIS A    51
REMARK 465     LYS A    52
REMARK 465     GLU A    53
REMARK 465     LYS A    54
REMARK 465     VAL A    55
REMARK 465     VAL A    56
REMARK 465     ASP A   193
REMARK 465     ASN A   194
REMARK 465     ASN A   195
REMARK 465     LYS A   196
REMARK 465     GLU A   197
REMARK 465     GLU A   198
REMARK 465     LEU A   199
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    CYS A  12   CB    CYS A  12   SG     -0.102
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 143     -160.53   -105.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 200  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 145   SG
REMARK 620 2 CYS A 148   SG  109.5
REMARK 620 3 CYS A 183   SG  113.9 116.6
REMARK 620 4 HIS A 186   ND1 115.9 111.0  88.8
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 201
DBREF  3E2I A    1   199  UNP    Q0H0G9   Q0H0G9_STAAU     1    199
SEQADV 3E2I MSE A  -19  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I GLY A  -18  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I SER A  -17  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I SER A  -16  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -15  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -14  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -13  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -12  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -11  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A  -10  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I SER A   -9  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I SER A   -8  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I GLY A   -7  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I LEU A   -6  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I VAL A   -5  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I PRO A   -4  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I ARG A   -3  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I GLY A   -2  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I SER A   -1  UNP  Q0H0G9              EXPRESSION TAG
SEQADV 3E2I HIS A    0  UNP  Q0H0G9              EXPRESSION TAG
SEQRES   1 A  219  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  219  LEU VAL PRO ARG GLY SER HIS MSE TYR GLU THR TYR HIS
SEQRES   3 A  219  SER GLY TRP ILE GLU CYS ILE THR GLY SER MSE PHE SER
SEQRES   4 A  219  GLY LYS SER GLU GLU LEU ILE ARG ARG LEU ARG ARG GLY
SEQRES   5 A  219  ILE TYR ALA LYS GLN LYS VAL VAL VAL PHE LYS PRO ALA
SEQRES   6 A  219  ILE ASP ASP ARG TYR HIS LYS GLU LYS VAL VAL SER HIS
SEQRES   7 A  219  ASN GLY ASN ALA ILE GLU ALA ILE ASN ILE SER LYS ALA
SEQRES   8 A  219  SER GLU ILE MSE THR HIS ASP LEU THR ASN VAL ASP VAL
SEQRES   9 A  219  ILE GLY ILE ASP GLU VAL GLN PHE PHE ASP ASP GLU ILE
SEQRES  10 A  219  VAL SER ILE VAL GLU LYS LEU SER ALA ASP GLY HIS ARG
SEQRES  11 A  219  VAL ILE VAL ALA GLY LEU ASP MSE ASP PHE ARG GLY GLU
SEQRES  12 A  219  PRO PHE GLU PRO MSE PRO LYS LEU MSE ALA VAL SER GLU
SEQRES  13 A  219  GLN VAL THR LYS LEU GLN ALA VAL CYS ALA VAL CYS GLY
SEQRES  14 A  219  SER SER SER SER ARG THR GLN ARG LEU ILE ASN GLY LYS
SEQRES  15 A  219  PRO ALA LYS ILE ASP ASP PRO ILE ILE LEU VAL GLY ALA
SEQRES  16 A  219  ASN GLU SER TYR GLU PRO ARG CYS ARG ALA HIS HIS ILE
SEQRES  17 A  219  VAL ALA PRO SER ASP ASN ASN LYS GLU GLU LEU
MODRES 3E2I MSE A   17  MET  SELENOMETHIONINE
MODRES 3E2I MSE A   75  MET  SELENOMETHIONINE
MODRES 3E2I MSE A  118  MET  SELENOMETHIONINE
MODRES 3E2I MSE A  128  MET  SELENOMETHIONINE
MODRES 3E2I MSE A  132  MET  SELENOMETHIONINE
HET    MSE  A  17       8
HET    MSE  A  75       8
HET    MSE  A 118       8
HET    MSE  A 128      13
HET    MSE  A 132       8
HET     ZN  A 200       1
HET    GOL  A 201       6
HETNAM     MSE SELENOMETHIONINE
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  MSE    5(C5 H11 N O2 SE)
FORMUL   2   ZN    ZN 2+
FORMUL   3  GOL    C3 H8 O3
FORMUL   4  HOH   *58(H2 O)
HELIX    1   1 GLY A   20  ALA A   35  1                                  16
HELIX    2   2 LYS A   70  HIS A   77  5                                   8
HELIX    3   3 GLU A   89  ASP A   94  5                                   6
HELIX    4   4 ASP A   95  ASP A  107  1                                  13
HELIX    5   5 PRO A  127  SER A  135  1                                   9
HELIX    6   6 CYS A  183  HIS A  187  5                                   5
SHEET    1   A 6 GLU A  64  ILE A  68  0
SHEET    2   A 6 VAL A  39  PRO A  44  1  N  VAL A  41   O  ILE A  66
SHEET    3   A 6 VAL A  84  ILE A  87  1  O  GLY A  86   N  VAL A  40
SHEET    4   A 6 ARG A 110  LEU A 116  1  O  ARG A 110   N  ILE A  85
SHEET    5   A 6 TRP A   9  GLY A  15  1  N  ILE A  13   O  VAL A 113
SHEET    6   A 6 GLN A 137  LEU A 141  1  O  LEU A 141   N  THR A  14
SHEET    1   B 2 ALA A 143  VAL A 144  0
SHEET    2   B 2 SER A 151  SER A 152 -1  O  SER A 152   N  ALA A 143
SHEET    1   C 3 LYS A 162  PRO A 163  0
SHEET    2   C 3 ARG A 154  ILE A 159 -1  N  ILE A 159   O  LYS A 162
SHEET    3   C 3 GLU A 177  ARG A 182 -1  O  SER A 178   N  LEU A 158
LINK         C   SER A  16                 N   MSE A  17     1555   1555  1.33
LINK         C   MSE A  17                 N   PHE A  18     1555   1555  1.33
LINK         C   ILE A  74                 N   MSE A  75     1555   1555  1.32
LINK         C   MSE A  75                 N   THR A  76     1555   1555  1.34
LINK         C   ASP A 117                 N   MSE A 118     1555   1555  1.33
LINK         C   MSE A 118                 N   ASP A 119     1555   1555  1.33
LINK         C   PRO A 127                 N   MSE A 128     1555   1555  1.33
LINK         C   MSE A 128                 N   PRO A 129     1555   1555  1.35
LINK         C   LEU A 131                 N   MSE A 132     1555   1555  1.33
LINK         C   MSE A 132                 N   ALA A 133     1555   1555  1.33
LINK         SG  CYS A 145                ZN    ZN A 200     1555   1555  2.36
LINK         SG  CYS A 148                ZN    ZN A 200     1555   1555  2.31
LINK         SG  CYS A 183                ZN    ZN A 200     1555   1555  2.22
LINK         ND1 HIS A 186                ZN    ZN A 200     1555   1555  2.25
CISPEP   1 GLU A  126    PRO A  127          0        -0.30
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 183  HIS A 186
SITE     1 AC2  9 SER A  16  MSE A  17  PHE A  18  SER A  19
SITE     2 AC2  9 GLY A  20  LYS A  21  SER A  22  ARG A  31
SITE     3 AC2  9 HOH A 227
CRYST1   71.621   71.621   96.144  90.00  90.00  90.00 P 42 2 2      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      0.013962  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013962  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010401        0.00000
      
PROCHECK
Go to PROCHECK summary
 References