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PDBsum entry 3s4k

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3s4k
Jmol
Contents
Protein chains
124 a.a.
Ligands
EDO ×4
SO4 ×2
Metals
_CL ×4
Waters ×221
HEADER    HYDROLASE                               19-MAY-11   3S4K
TITLE     STRUCTURE OF A PUTATIVE ESTERASE RV1847/MT1895 FROM MYCOBACTERIUM
TITLE    2 TUBERCULOSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PUTATIVE ESTERASE RV1847/MT1895;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.2.-;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE   3 ORGANISM_TAXID: 1773;
SOURCE   4 GENE: RV1847, MT1895, MTCY359.26C;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, SSGCID,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT   1   01-JUN-11 3S4K    0
JRNL        AUTH   M.C.CLIFTON,T.E.EDWARDS,B.SANKARAN,
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL        AUTH 3 (SSGCID)
JRNL        TITL   STRUCTURE OF A PUTATIVE ESTERASE RV1847/MT1895 FROM
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.82
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2
REMARK   3   NUMBER OF REFLECTIONS             : 27400
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) : 0.173
REMARK   3   R VALUE            (WORKING SET) : 0.171
REMARK   3   FREE R VALUE                     : 0.197
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1376
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) : 1.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1641
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.38
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180
REMARK   3   BIN FREE R VALUE SET COUNT          : 90
REMARK   3   BIN FREE R VALUE                    : 0.2370
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1874
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 221
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.58
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.27000
REMARK   3    B22 (A**2) : -3.57000
REMARK   3    B33 (A**2) : 2.30000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.11000
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): 0.021
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.461
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2002 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1361 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2725 ; 1.357 ; 1.961
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3299 ; 0.862 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   268 ; 5.490 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;31.936 ;22.889
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   325 ;11.469 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;15.880 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   309 ; 0.085 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2278 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   420 ; 0.001 ; 0.020
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):  1264 ; 0.707 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   524 ; 0.200 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2036 ; 1.312 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   738 ; 2.226 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   679 ; 3.494 ; 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    15        A   140
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5582  10.5134  17.7473
REMARK   3    T TENSOR
REMARK   3      T11:   0.0014 T22:   0.0202
REMARK   3      T33:   0.0100 T12:  -0.0010
REMARK   3      T13:   0.0013 T23:   0.0034
REMARK   3    L TENSOR
REMARK   3      L11:   0.3365 L22:   0.2824
REMARK   3      L33:   0.1213 L12:   0.1063
REMARK   3      L13:   0.0836 L23:   0.1448
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0141 S12:   0.0242 S13:   0.0266
REMARK   3      S21:  -0.0138 S22:   0.0036 S23:   0.0040
REMARK   3      S31:  -0.0008 S32:  -0.0118 S33:   0.0105
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    15        B   140
REMARK   3    ORIGIN FOR THE GROUP (A):  28.2898   1.9295  17.6787
REMARK   3    T TENSOR
REMARK   3      T11:   0.0014 T22:   0.0185
REMARK   3      T33:   0.0086 T12:   0.0025
REMARK   3      T13:   0.0025 T23:  -0.0014
REMARK   3    L TENSOR
REMARK   3      L11:   0.3217 L22:   0.2659
REMARK   3      L33:   0.1106 L12:   0.1438
REMARK   3      L13:  -0.0682 L23:  -0.1042
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0161 S12:   0.0194 S13:  -0.0165
REMARK   3      S21:  -0.0032 S22:   0.0058 S23:  -0.0161
REMARK   3      S31:   0.0023 S32:   0.0104 S33:   0.0103
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : 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 RIDING
REMARK   3  POSITIONS. U VALUES: RESIDUAL ONLY
REMARK   4
REMARK   4 3S4K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-MAY-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CURVED CRYSTAL
REMARK 200  OPTICS                         : NULL
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
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27452
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
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     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 4.300
REMARK 200  R MERGE                    (I) : 0.08300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.23500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1Q4T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LICL, 0.1M MES PH 6.0, 20%
REMARK 280  PEG6000. CRYO PROTECTION IN 25% ETHYLENE GLYCOL, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       38.80849
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       60.43581
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 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       38.80849
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       60.43581
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000       50.64200
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       38.80849
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000       50.64200
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       60.43581
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 CL    CL A 143  LIES ON A SPECIAL POSITION.
REMARK 375 CL    CL B 143  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 173  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 186  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 165  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     GLY A    -3
REMARK 465     PRO A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     GLN A     2
REMARK 465     PRO A     3
REMARK 465     SER A     4
REMARK 465     PRO A     5
REMARK 465     ASP A     6
REMARK 465     SER A     7
REMARK 465     PRO A     8
REMARK 465     ALA A     9
REMARK 465     PRO A    10
REMARK 465     LEU A    11
REMARK 465     ASN A    12
REMARK 465     VAL A    13
REMARK 465     THR A    14
REMARK 465     HIS A    74
REMARK 465     GLY A    75
REMARK 465     GLY B    -3
REMARK 465     PRO B    -2
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     MET B     1
REMARK 465     GLN B     2
REMARK 465     PRO B     3
REMARK 465     SER B     4
REMARK 465     PRO B     5
REMARK 465     ASP B     6
REMARK 465     SER B     7
REMARK 465     PRO B     8
REMARK 465     ALA B     9
REMARK 465     PRO B    10
REMARK 465     LEU B    11
REMARK 465     ASN B    12
REMARK 465     VAL B    13
REMARK 465     THR B    14
REMARK 465     HIS B    74
REMARK 465     GLY B    75
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     ARG A  40    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A  46    CG   CD1  CD2
REMARK 470     GLU A  76    CG   CD   OE1  OE2
REMARK 470     LEU B  46    CG   CD1  CD2
REMARK 470     GLU B  76    CG   CD   OE1  OE2
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    GLN A  45     -164.29   -106.86
REMARK 500    GLN B  45     -164.92   -110.67
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 231        DISTANCE =  5.36 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 142
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 145
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 144
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYTUD.17673.A   RELATED DB: TARGETDB
DBREF  3S4K A    1   140  UNP    P95162   Y1847_MYCTU      1    140
DBREF  3S4K B    1   140  UNP    P95162   Y1847_MYCTU      1    140
SEQADV 3S4K GLY A   -3  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K PRO A   -2  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K GLY A   -1  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K SER A    0  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K GLY B   -3  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K PRO B   -2  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K GLY B   -1  UNP  P95162              EXPRESSION TAG
SEQADV 3S4K SER B    0  UNP  P95162              EXPRESSION TAG
SEQRES   1 A  144  GLY PRO GLY SER MET GLN PRO SER PRO ASP SER PRO ALA
SEQRES   2 A  144  PRO LEU ASN VAL THR VAL PRO PHE ASP SER GLU LEU GLY
SEQRES   3 A  144  LEU GLN PHE THR GLU LEU GLY PRO ASP GLY ALA ARG ALA
SEQRES   4 A  144  GLN LEU ASP VAL ARG PRO LYS LEU LEU GLN LEU THR GLY
SEQRES   5 A  144  VAL VAL HIS GLY GLY VAL TYR CYS ALA MET ILE GLU SER
SEQRES   6 A  144  ILE ALA SER MET ALA ALA PHE ALA TRP LEU ASN SER HIS
SEQRES   7 A  144  GLY GLU GLY GLY SER VAL VAL GLY VAL ASN ASN ASN THR
SEQRES   8 A  144  ASP PHE VAL ARG SER ILE SER SER GLY MET VAL TYR GLY
SEQRES   9 A  144  THR ALA GLU PRO LEU HIS ARG GLY ARG ARG GLN GLN LEU
SEQRES  10 A  144  TRP LEU VAL THR ILE THR ASP ASP THR ASP ARG VAL VAL
SEQRES  11 A  144  ALA ARG GLY GLN VAL ARG LEU GLN ASN LEU GLU ALA ARG
SEQRES  12 A  144  PRO
SEQRES   1 B  144  GLY PRO GLY SER MET GLN PRO SER PRO ASP SER PRO ALA
SEQRES   2 B  144  PRO LEU ASN VAL THR VAL PRO PHE ASP SER GLU LEU GLY
SEQRES   3 B  144  LEU GLN PHE THR GLU LEU GLY PRO ASP GLY ALA ARG ALA
SEQRES   4 B  144  GLN LEU ASP VAL ARG PRO LYS LEU LEU GLN LEU THR GLY
SEQRES   5 B  144  VAL VAL HIS GLY GLY VAL TYR CYS ALA MET ILE GLU SER
SEQRES   6 B  144  ILE ALA SER MET ALA ALA PHE ALA TRP LEU ASN SER HIS
SEQRES   7 B  144  GLY GLU GLY GLY SER VAL VAL GLY VAL ASN ASN ASN THR
SEQRES   8 B  144  ASP PHE VAL ARG SER ILE SER SER GLY MET VAL TYR GLY
SEQRES   9 B  144  THR ALA GLU PRO LEU HIS ARG GLY ARG ARG GLN GLN LEU
SEQRES  10 B  144  TRP LEU VAL THR ILE THR ASP ASP THR ASP ARG VAL VAL
SEQRES  11 B  144  ALA ARG GLY GLN VAL ARG LEU GLN ASN LEU GLU ALA ARG
SEQRES  12 B  144  PRO
HET    EDO  A 141       4
HET    EDO  A 142       4
HET     CL  A 143       1
HET     CL  A 144       1
HET    SO4  A 145       5
HET    EDO  B 141       4
HET    EDO  B 142       4
HET     CL  B 143       1
HET    SO4  B 144       5
HET     CL  B 145       1
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM      CL CHLORIDE ION
HETNAM     SO4 SULFATE ION
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  EDO    4(C2 H6 O2)
FORMUL   5   CL    4(CL 1-)
FORMUL   7  SO4    2(O4 S 2-)
FORMUL  13  HOH   *221(H2 O)
HELIX    1   1 VAL A   15  GLY A   22  1                                   8
HELIX    2   2 ARG A   40  LEU A   44  5                                   5
HELIX    3   3 HIS A   51  ASN A   72  1                                  22
HELIX    4   4 VAL B   15  GLY B   22  1                                   8
HELIX    5   5 ARG B   40  LEU B   44  5                                   5
HELIX    6   6 HIS B   51  ASN B   72  1                                  22
SHEET    1   A12 GLN A  24  GLY A  29  0
SHEET    2   A12 GLY A  32  VAL A  39 -1  O  ARG A  34   N  THR A  26
SHEET    3   A12 GLY A  96  ARG A 107 -1  O  GLY A 100   N  ALA A  35
SHEET    4   A12 GLN A 111  THR A 119 -1  O  LEU A 115   N  GLU A 103
SHEET    5   A12 VAL A 125  LEU A 136 -1  O  ALA A 127   N  ILE A 118
SHEET    6   A12 SER A  79  PHE A  89 -1  N  ASP A  88   O  ARG A 128
SHEET    7   A12 SER B  79  PHE B  89 -1  O  THR B  87   N  ASN A  85
SHEET    8   A12 VAL B 125  LEU B 136 -1  O  ARG B 128   N  ASP B  88
SHEET    9   A12 GLN B 111  THR B 119 -1  N  ILE B 118   O  ALA B 127
SHEET   10   A12 GLY B  96  ARG B 107 -1  N  GLU B 103   O  LEU B 115
SHEET   11   A12 GLY B  32  VAL B  39 -1  N  ALA B  35   O  GLY B 100
SHEET   12   A12 GLN B  24  GLY B  29 -1  N  THR B  26   O  ARG B  34
SITE     1 AC1  6 GLY A  82  HOH A 206  HOH A 223  SER B  92
SITE     2 AC1  6 ARG B 139  HOH B 167
SITE     1 AC2  6 SER A  92  ARG A 139  HOH A 180  GLY B  82
SITE     2 AC2  6 HOH B 198  HOH B 221
SITE     1 AC3  2 PHE A  89  HOH B 171
SITE     1 AC4  2 HOH A 202  PHE B  89
SITE     1 AC5  2 ARG A 110  GLN A 111
SITE     1 AC6  2 ARG B 110  GLN B 111
SITE     1 AC7  3 PRO A 104  HIS A 106  ARG A 107
SITE     1 AC8  3 PRO B 104  HIS B 106  ARG B 107
CRYST1   41.722   50.642   60.506  90.00  92.76  90.00 P 1 2 1       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      0.023968  0.000000  0.001157        0.00000
SCALE2      0.000000  0.019746  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016547        0.00000
      
PROCHECK
Go to PROCHECK summary
 References