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PDBsum entry 1sx8

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Top Page protein dna_rna metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
1sx8
Jmol
Contents
Protein chains
241 a.a.
DNA/RNA
Metals
_MN ×6
Waters ×152
HEADER    HYDROLASE/DNA                           30-MAR-04   1SX8
TITLE     ECORV BOUND TO COGNATE DNA AND MN2+
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*C*AP*AP*GP*AP*TP*AP*TP*CP*TP*T)-3';
COMPND   3 CHAIN: C, D;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: TYPE II RESTRICTION ENZYME ECORV;
COMPND   7 CHAIN: A, B;
COMPND   8 SYNONYM: ENDONUCLEASE ECORV, R.ECORV;
COMPND   9 EC: 3.1.21.4;
COMPND  10 ENGINEERED: YES;
COMPND  11 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: SYNTHETIC;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   6 ORGANISM_TAXID: 562;
SOURCE   7 GENE: ECORVR;
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: MM294 (ENDI-, PRO-, THI-, RK-
SOURCE  11 MK+);
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PBSRV
KEYWDS    HYDROLASE/DNA
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.C.HORTON,J.J.PERONA
REVDAT   3   24-FEB-09 1SX8    1       VERSN
REVDAT   2   29-JUN-04 1SX8    1       JRNL
REVDAT   1   06-APR-04 1SX8    0
JRNL        AUTH   N.C.HORTON,J.J.PERONA
JRNL        TITL   DNA CLEAVAGE BY ECORV ENDONUCLEASE: TWO METAL IONS
JRNL        TITL 2 IN THREE METAL ION BINDING SITES
JRNL        REF    BIOCHEMISTRY                  V.  43  6841 2004
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15170321
JRNL        DOI    10.1021/BI0499056
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : CNS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.2
REMARK   3   NUMBER OF REFLECTIONS             : 23851
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM 5%
REMARK   3   R VALUE            (WORKING SET) : 0.213
REMARK   3   FREE R VALUE                     : 0.254
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1159
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3818
REMARK   3   NUCLEIC ACID ATOMS       : 403
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 152
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 42.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.018
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1SX8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB022063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200  DATA SCALING SOFTWARE          : MOSFLM
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23851
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 0.9
REMARK 200  DATA REDUNDANCY                : 1.800
REMARK 200  R MERGE                    (I) : 0.08900
REMARK 200  R SYM                      (I) : 0.08900
REMARK 200   FOR THE DATA SET  : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.30700
REMARK 200  R SYM FOR SHELL            (I) : 0.30700
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, 0.1M HEPES, 0.15M NACL,
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 100K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   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
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 APPLY THE FOLLOWING TO CHAINS: C, D, 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 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      DC C     1
REMARK 465      DT D    11
REMARK 465     ALA A   142
REMARK 465     THR A   143
REMARK 465     ARG A   144
REMARK 465     LYS B    98
REMARK 465     GLU B    99
REMARK 465     ASN B   100
REMARK 465     GLU B   101
REMARK 465     ALA B   142
REMARK 465     THR B   143
REMARK 465     ARG B   144
REMARK 465     LYS B   145
REMARK 465     SER B   146
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      DA C   2    P    OP1  OP2
REMARK 470     LYS A  17    CG   CD   CE   NZ
REMARK 470     LYS A  58    CG   CD   CE   NZ
REMARK 470     ILE A  62    CG1  CG2  CD1
REMARK 470     LYS A  67    CG   CD   CE   NZ
REMARK 470     GLN A  68    CG   CD   OE1  NE2
REMARK 470     LYS A  98    CG   CD   CE   NZ
REMARK 470     GLU A  99    CG   CD   OE1  OE2
REMARK 470     ASN A 100    CG   OD1  ND2
REMARK 470     LYS A 104    CG   CD   CE   NZ
REMARK 470     ARG A 140    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 145    CG   CD   CE   NZ
REMARK 470     LYS A 149    CD   CE   NZ
REMARK 470     LYS A 203    CG   CD   CE   NZ
REMARK 470     SER A 223    OG
REMARK 470     GLN A 224    CG   CD   OE1  NE2
REMARK 470     ASN A 227    CG   OD1  ND2
REMARK 470     ASP A 228    CG   OD1  OD2
REMARK 470     ASN A 231    CG   OD1  ND2
REMARK 470     LYS B  17    CD   CE   NZ
REMARK 470     LYS B  38    CG   CD   CE   NZ
REMARK 470     LYS B  67    CG   CD   CE   NZ
REMARK 470     GLN B  68    CG   CD   OE1  NE2
REMARK 470     LYS B  85    CE   NZ
REMARK 470     TYR B  95    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS B 104    CG   CD   CE   NZ
REMARK 470     ASN B 116    CG   OD1  ND2
REMARK 470     ARG B 140    CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 149    CG   CD   CE   NZ
REMARK 470     ASN B 154    CG   OD1  ND2
REMARK 470     LYS B 197    CG   CD   CE   NZ
REMARK 470     LYS B 203    CD   CE   NZ
REMARK 470     GLN B 224    CG   CD   OE1  NE2
REMARK 470     LEU B 225    CG   CD1  CD2
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 B   214     OH   TYR B   236              2.19
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     DT C   6   C2     DT C   6   N3      0.088
REMARK 500     DT C   6   C4     DT C   6   C5      0.062
REMARK 500     DT C   6   C5     DT C   6   C6      0.044
REMARK 500     DT C   8   N1     DT C   8   C2      0.049
REMARK 500     DT C   8   C4     DT C   8   O4     -0.063
REMARK 500     DT D   6   C4     DT D   6   C5      0.061
REMARK 500     DT D   6   C4     DT D   6   O4      0.058
REMARK 500    ALA A  88   CA    ALA A  88   CB      0.128
REMARK 500    PHE A 105   CZ    PHE A 105   CE2     0.118
REMARK 500    PHE A 125   CZ    PHE A 125   CE2     0.172
REMARK 500    TYR A 136   CE1   TYR A 136   CZ      0.080
REMARK 500    TYR A 163   CB    TYR A 163   CG      0.090
REMARK 500    PHE A 169   CE2   PHE A 169   CD2     0.154
REMARK 500    VAL A 200   CB    VAL A 200   CG1     0.173
REMARK 500    PHE A 206   CE2   PHE A 206   CD2     0.173
REMARK 500    PHE A 212   CE1   PHE A 212   CZ      0.117
REMARK 500    GLU A 235   CG    GLU A 235   CD      0.113
REMARK 500    TYR A 236   CE1   TYR A 236   CZ      0.094
REMARK 500    ARG A 244   CB    ARG A 244   CG      0.171
REMARK 500    TYR B  12   CG    TYR B  12   CD2     0.084
REMARK 500    TYR B  12   CZ    TYR B  12   CE2     0.079
REMARK 500    TYR B  12   CE2   TYR B  12   CD2     0.094
REMARK 500    ILE B  23   CB    ILE B  23   CG2     0.201
REMARK 500    SER B  41   CA    SER B  41   CB      0.101
REMARK 500    GLU B  64   CG    GLU B  64   CD      0.101
REMARK 500    TYR B  72   CD1   TYR B  72   CE1     0.129
REMARK 500    TYR B  72   CZ    TYR B  72   CE2     0.096
REMARK 500    THR B  94   CA    THR B  94   CB      0.171
REMARK 500    PHE B 105   CE1   PHE B 105   CZ      0.118
REMARK 500    PHE B 169   CG    PHE B 169   CD1     0.095
REMARK 500    GLU B 211   CD    GLU B 211   OE1     0.077
REMARK 500    GLU B 211   CD    GLU B 211   OE2     0.067
REMARK 500    PHE B 212   CD1   PHE B 212   CE1     0.133
REMARK 500    TYR B 230   CG    TYR B 230   CD1     0.093
REMARK 500    TYR B 230   CZ    TYR B 230   CE2     0.115
REMARK 500    TYR B 241   CZ    TYR B 241   CE2     0.078
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     DT C   6   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DC C   9   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DC C   9   O3' -  P   -  OP2 ANGL. DEV. =   7.1 DEGREES
REMARK 500     DT D   8   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES
REMARK 500    GLY A 165   C   -  N   -  CA  ANGL. DEV. = -20.9 DEGREES
REMARK 500    LEU A 180   CB  -  CG  -  CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 237   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ILE B  43   CG1 -  CB  -  CG2 ANGL. DEV. = -15.8 DEGREES
REMARK 500    ARG B  49   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    PRO B  66   C   -  N   -  CA  ANGL. DEV. = -10.2 DEGREES
REMARK 500    ASP B  74   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 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    SER A 112     -114.27   -104.65
REMARK 500    ASN A 117      -30.05    -26.45
REMARK 500    SER A 146       -1.46    -58.71
REMARK 500    PRO A 162        9.16    -55.99
REMARK 500    LYS A 164      -22.27   -153.22
REMARK 500    THR A 187       66.40     22.29
REMARK 500    LYS A 229      -95.40   -111.94
REMARK 500    ASP B  36      175.71    -58.99
REMARK 500    LYS B  85       68.38   -116.54
REMARK 500    SER B 112     -110.43    -97.60
REMARK 500    ASN B 117      -25.01    -15.57
REMARK 500    PRO B 162       19.14    -69.14
REMARK 500    THR B 187       71.50     27.63
REMARK 500    LYS B 203       74.17   -101.24
REMARK 500    LYS B 229      -83.98   -130.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500     DA C   2         0.09    SIDE_CHAIN
REMARK 500     DT C   6         0.07    SIDE_CHAIN
REMARK 500     DT D   6         0.07    SIDE_CHAIN
REMARK 500     DT D  10         0.07    SIDE_CHAIN
REMARK 500    TYR B  78         0.08    SIDE_CHAIN
REMARK 500    TYR B 219         0.09    SIDE_CHAIN
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 B 272        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH A 295        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH A 319        DISTANCE =  6.54 ANGSTROMS
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                              MN A 246  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  DA C   7   OP1
REMARK 620 2 HOH A 258   O   112.5
REMARK 620 3 ASP A  74   OD1 159.4  68.0
REMARK 620 4 ASP A  74   OD2 151.1  90.4  45.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 246  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  DT C  11   OP1
REMARK 620 2 HIS B  71   NE2  88.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 247  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  74   OD2
REMARK 620 2 ASP B  90   OD2  89.4
REMARK 620 3 HOH B 274   O    70.3  96.8
REMARK 620 4 HOH B 257   O    96.1 172.3  80.1
REMARK 620 5  DA D   7   OP1 167.3  84.4  99.4  89.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN B 248  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  74   OD1
REMARK 620 2 GLU B  45   OE1  87.0
REMARK 620 3 HOH B 258   O    81.6  86.9
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 246
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 247
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 248
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 246
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 247
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 248
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SX5   RELATED DB: PDB
DBREF  1SX8 A    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  1SX8 B    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  1SX8 C    1    11  PDB    1SX8     1SX8             1     11
DBREF  1SX8 D    1    11  PDB    1SX8     1SX8             1     11
SEQADV 1SX8 ALA A   92  UNP  P04390    LYS    91 ENGINEERED
SEQADV 1SX8 ALA B   92  UNP  P04390    LYS    91 ENGINEERED
SEQRES   1 C   11   DC  DA  DA  DG  DA  DT  DA  DT  DC  DT  DT
SEQRES   1 D   11   DC  DA  DA  DG  DA  DT  DA  DT  DC  DT  DT
SEQRES   1 A  244  SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP GLU
SEQRES   2 A  244  ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA GLU
SEQRES   3 A  244  GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL LEU
SEQRES   4 A  244  SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE ASN
SEQRES   5 A  244  LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU PRO
SEQRES   6 A  244  LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR LYS
SEQRES   7 A  244  PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE ALA
SEQRES   8 A  244  THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS PHE
SEQRES   9 A  244  THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN THR
SEQRES  10 A  244  LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA HIS
SEQRES  11 A  244  TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR ARG
SEQRES  12 A  244  LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU ASN
SEQRES  13 A  244  GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE LEU
SEQRES  14 A  244  GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY SER
SEQRES  15 A  244  GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS TYR
SEQRES  16 A  244  LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER GLU
SEQRES  17 A  244  ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG THR
SEQRES  18 A  244  SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER GLU
SEQRES  19 A  244  TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
SEQRES   1 B  244  SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP GLU
SEQRES   2 B  244  ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA GLU
SEQRES   3 B  244  GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL LEU
SEQRES   4 B  244  SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE ASN
SEQRES   5 B  244  LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU PRO
SEQRES   6 B  244  LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR LYS
SEQRES   7 B  244  PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE ALA
SEQRES   8 B  244  THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS PHE
SEQRES   9 B  244  THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN THR
SEQRES  10 B  244  LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA HIS
SEQRES  11 B  244  TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR ARG
SEQRES  12 B  244  LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU ASN
SEQRES  13 B  244  GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE LEU
SEQRES  14 B  244  GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY SER
SEQRES  15 B  244  GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS TYR
SEQRES  16 B  244  LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER GLU
SEQRES  17 B  244  ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG THR
SEQRES  18 B  244  SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER GLU
SEQRES  19 B  244  TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
HET     MN  A 246       1
HET     MN  A 247       1
HET     MN  A 248       1
HET     MN  B 246       1
HET     MN  B 247       1
HET     MN  B 248       1
HETNAM      MN MANGANESE (II) ION
FORMUL   5   MN    6(MN 2+)
FORMUL  11  HOH   *152(H2 O)
HELIX    1   1 SER A    2  TYR A   18  1                                  17
HELIX    2   2 ASP A   36  HIS A   59  1                                  24
HELIX    3   3 PRO A  124  ASP A  126  5                                   3
HELIX    4   4 LYS A  145  LYS A  149  5                                   5
HELIX    5   5 ASN A  154  ILE A  159  5                                   6
HELIX    6   6 LYS A  173  ILE A  176  1                                   4
HELIX    7   7 HIS A  195  GLY A  202  1                                   8
HELIX    8   8 SER A  208  ASN A  218  1                                  11
HELIX    9   9 THR A  222  ASN A  227  1                                   6
HELIX   10  10 ASN A  232  ARG A  242  1                                  11
HELIX   11  11 SER B    2  TYR B   18  1                                  17
HELIX   12  12 ASP B   36  LYS B   58  1                                  23
HELIX   13  13 PRO B  124  ASP B  126  5                                   3
HELIX   14  14 ASN B  154  ILE B  159  5                                   6
HELIX   15  15 LYS B  173  ILE B  176  1                                   4
HELIX   16  16 HIS B  195  GLY B  202  1                                   8
HELIX   17  17 SER B  208  ASN B  218  1                                  11
HELIX   18  18 THR B  222  TYR B  230  1                                   9
HELIX   19  19 ASN B  232  ARG B  242  1                                  11
SHEET    1   A 6 TYR A 151  ASN A 152  0
SHEET    2   A 6 LYS A  29  TYR A  31 -1  N  ILE A  30   O  TYR A 151
SHEET    3   A 6 VAL A  20  SER A  25 -1  N  ILE A  23   O  TYR A  31
SHEET    4   A 6 VAL B  20  SER B  25 -1  O  GLY B  22   N  ILE A  24
SHEET    5   A 6 LYS B  29  PRO B  32 -1  O  TYR B  31   N  ILE B  23
SHEET    6   A 6 TYR B 151  ASN B 152 -1  O  TYR B 151   N  ILE B  30
SHEET    1   B 5 ILE A  62  GLU A  64  0
SHEET    2   B 5 PHE A  75  TYR A  78 -1  O  TYR A  78   N  ILE A  62
SHEET    3   B 5 LYS A  86  THR A  96 -1  O  ILE A  87   N  LEU A  77
SHEET    4   B 5 TYR A 128  THR A 139  1  O  ILE A 134   N  ASP A  90
SHEET    5   B 5 LYS A 167  ASP A 172 -1  O  LYS A 167   N  VAL A 137
SHEET    1   C 3 THR A 106  GLY A 109  0
SHEET    2   C 3 ASN A 188  SER A 191 -1  O  ILE A 189   N  LEU A 107
SHEET    3   C 3 ALA A 177  ALA A 181 -1  N  GLY A 178   O  GLY A 190
SHEET    1   D 5 ILE B  62  GLU B  64  0
SHEET    2   D 5 PHE B  75  TYR B  78 -1  O  THR B  76   N  GLU B  64
SHEET    3   D 5 LYS B  86  THR B  96 -1  O  ILE B  87   N  LEU B  77
SHEET    4   D 5 TYR B 128  ARG B 140  1  O  TRP B 132   N  ALA B  88
SHEET    5   D 5 TYR B 163  ASP B 172 -1  O  GLN B 171   N  ILE B 133
SHEET    1   E 3 THR B 106  GLY B 109  0
SHEET    2   E 3 ASN B 188  SER B 191 -1  O  ILE B 189   N  LEU B 107
SHEET    3   E 3 ALA B 177  SER B 183 -1  N  GLY B 182   O  ASN B 188
LINK        MN    MN A 246                 OP1  DA C   7     1555   1555  2.11
LINK        MN    MN A 246                 O   HOH A 258     1555   1555  2.56
LINK        MN    MN A 246                 OD1 ASP A  74     1555   1555  2.73
LINK        MN    MN A 246                 OD2 ASP A  74     1555   1555  2.58
LINK        MN    MN A 247                 O   HOH A 257     1555   1555  2.40
LINK        MN    MN A 248                 NE2 HIS A  71     1555   1555  2.60
LINK        MN    MN B 246                 OP1  DT C  11     1555   1555  2.33
LINK        MN    MN B 246                 NE2 HIS B  71     1555   1555  2.21
LINK        MN    MN B 247                 OD2 ASP B  74     1555   1555  2.69
LINK        MN    MN B 247                 OD2 ASP B  90     1555   1555  2.47
LINK        MN    MN B 247                 O   HOH B 274     1555   1555  2.24
LINK        MN    MN B 247                 O   HOH B 257     1555   1555  2.49
LINK        MN    MN B 247                 OP1  DA D   7     1555   1555  2.25
LINK        MN    MN B 248                 OD1 ASP B  74     1555   1555  2.50
LINK        MN    MN B 248                 OE1 GLU B  45     1555   1555  2.40
LINK        MN    MN B 248                 O   HOH B 258     1555   1555  2.21
CISPEP   1 TYR A   72    PRO A   73          0        -0.41
CISPEP   2 TYR B   72    PRO B   73          0         1.42
SITE     1 AC1  5 ASP A  74  ASP A  90  HOH A 258   DT C   6
SITE     2 AC1  5  DA C   7
SITE     1 AC2  3 GLU A  45  ASP A  74  HOH A 257
SITE     1 AC3  1 HIS A  71
SITE     1 AC4  2 HIS B  71   DT C  11
SITE     1 AC5  5 ASP B  74  ASP B  90  HOH B 257  HOH B 274
SITE     2 AC5  5  DA D   7
SITE     1 AC6  3 GLU B  45  ASP B  74  HOH B 258
CRYST1   47.800   49.100   63.700  96.90 108.90 107.10 P 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      0.020921  0.006436  0.008953        0.00000
SCALE2      0.000000  0.021309  0.005226        0.00000
SCALE3      0.000000  0.000000  0.017085        0.00000
      
PROCHECK
Go to PROCHECK summary
 References