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PDBsum entry 1eo3

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Top Page protein dna_rna ligands metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
1eo3
Jmol
Contents
Protein chains
241 a.a. *
DNA/RNA
Ligands
ACY ×2
Metals
_MG ×4
Waters ×297
* Residue conservation analysis
HEADER    HYDROLASE/DNA                           21-MAR-00   1EO3
TITLE     INHIBITION OF ECORV ENDONUCLEASE BY DEOXYRIBO-3'-S-
TITLE    2 PHOSPHOROTHIOLATES: A HIGH RESOLUTION X-RAY
TITLE    3 CRYSTALLOGRAPHIC STUDY
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*CP*AP*AP*GP*AP*(TSP)P*AP*TP*CP*TP*T)-
COMPND   3 3');
COMPND   4 CHAIN: C, D;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: TYPE II RESTRICTION ENZYME ECORV;
COMPND   8 CHAIN: A, B;
COMPND   9 SYNONYM: ENDONUCLEASE ECORV, R.ECORV;
COMPND  10 EC: 3.1.21.4;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   5 ORGANISM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    PROTEIN-DNA COMPLEX, RESTRICTION ENDONUCLEASE, DNA ANALOG,
KEYWDS   2 HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.C.HORTON,B.A.CONNOLLY,J.J.PERONA
REVDAT   3   24-FEB-09 1EO3    1       VERSN
REVDAT   2   08-FEB-05 1EO3    1       JRNL   REMARK
REVDAT   1   04-APR-00 1EO3    0
JRNL        AUTH   N.C.HORTON,B.A.CONNOLLY,J.J.PERONA
JRNL        TITL   INHIBITION OF ECORV ENDONUCLEASE BY
JRNL        TITL 2 DEOXYRIBO-3'-S-PHOSPHOROTHIOLATES: A
JRNL        TITL 3 HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STUDY
JRNL        REF    J.AM.CHEM.SOC.                V. 122  3314 2000
JRNL        REFN                   ISSN 0002-7863
JRNL        DOI    10.1021/JA993719J
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 4.90
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.5
REMARK   3   NUMBER OF REFLECTIONS             : 29583
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 SET) : 0.196
REMARK   3   FREE R VALUE                     : 0.290
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1514
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            : 3814
REMARK   3   NUCLEIC ACID ATOMS       : 410
REMARK   3   HETEROGEN ATOMS          : 4
REMARK   3   SOLVENT ATOMS            : 305
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.20
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) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 2.12
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  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 1EO3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-00.
REMARK 100 THE RCSB ID CODE IS RCSB010754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-98
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
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS II
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31662
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8
REMARK 200  DATA REDUNDANCY                : 1.770
REMARK 200  R MERGE                    (I) : 0.13100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.35800
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: NULL
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   (%): 39.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.1M HEPES, 0.15M
REMARK 280  NACL, 50 MM MGCL2, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 290K
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER COMPOSED OF CHAINS A
REMARK 300 AND B
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     MET A     1
REMARK 465     ARG A   144
REMARK 465     ASN A   154
REMARK 465     GLU A   155
REMARK 465     MET B     1
REMARK 465     LYS B    98
REMARK 465     GLU B    99
REMARK 465     ASN B   100
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      DT D  11    C5'  C4'  O4'  C3'  O3'  C2'  C1'
REMARK 470      DT D  11    N1   C2   O2   N3   C4   O4   C5
REMARK 470      DT D  11    C7   C6
REMARK 470     GLN A  16    CG   CD   OE1  NE2
REMARK 470     LYS A  17    CG   CD   CE   NZ
REMARK 470     LYS A  38    CG   CD   CE   NZ
REMARK 470     GLU A  57    CG   CD   OE1  OE2
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     ASN A 116    CG   OD1  ND2
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 161    CG   CD   CE   NZ
REMARK 470     LYS A 197    CG   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     SER B  35    OG
REMARK 470     LYS B  38    CG   CD   CE   NZ
REMARK 470     GLU B  57    CG   CD   OE1  OE2
REMARK 470     LYS B  67    CG   CD   CE   NZ
REMARK 470     GLN B  68    CG   CD   OE1  NE2
REMARK 470     GLU B  82    CG   CD   OE1  OE2
REMARK 470     LYS B  85    CE   NZ
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     LEU B 148    CG   CD1  CD2
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     LEU B 225    CG   CD1  CD2
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     DG D   4   C4' -  C3' -  O3' ANGL. DEV. = -15.9 DEGREES
REMARK 500     DG D   4   O4' -  C1' -  C2' ANGL. DEV. =   3.5 DEGREES
REMARK 500     DG D   4   N9  -  C1' -  C2' ANGL. DEV. =   8.8 DEGREES
REMARK 500     DT D   8   O4' -  C1' -  C2' ANGL. DEV. =   3.1 DEGREES
REMARK 500     DT D   8   O4' -  C1' -  N1  ANGL. DEV. =   2.0 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    LEU A 107       43.18    -95.93
REMARK 500    SER A 112     -105.38   -106.98
REMARK 500    ASN A 117      -39.37    -38.50
REMARK 500    PRO A 162       22.50    -76.26
REMARK 500    THR A 187       65.26     32.03
REMARK 500    LYS A 229      -84.84   -118.11
REMARK 500    SER B  35       75.74   -105.14
REMARK 500    SER B 112     -121.73    -92.74
REMARK 500    THR B 187       66.57     27.15
REMARK 500    ASN B 227        4.08    -67.48
REMARK 500    LYS B 229      -86.09   -132.66
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     DG C   4         0.07    SIDE_CHAIN
REMARK 500     DA D   2         0.09    SIDE_CHAIN
REMARK 500     DT D   8         0.07    SIDE_CHAIN
REMARK 500     DC D   9         0.08    SIDE_CHAIN
REMARK 500     DT D  10         0.07    SIDE_CHAIN
REMARK 500    TYR B 163         0.07    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 C  23        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH B 692        DISTANCE =  6.50 ANGSTROMS
REMARK 525    HOH B 703        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH A 705        DISTANCE =  6.70 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                              MG A 501  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  45   OE2
REMARK 620 2 ASP A  74   OD1 100.0
REMARK 620 3 HOH A 610   O   176.6  76.7
REMARK 620 4 HOH A 666   O    98.8  74.6  79.5
REMARK 620 5 HOH A 708   O    85.5 159.9  97.3  85.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 502  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  74   OD2
REMARK 620 2 HOH C  27   O   132.6
REMARK 620 3 HOH A 611   O   105.9 101.4
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 503  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B  45   OE1
REMARK 620 2 ASP B  74   OD1  93.6
REMARK 620 3 HOH B 619   O   174.5  88.2
REMARK 620 4 HOH B 618   O    90.2 108.7  84.3
REMARK 620 5 HOH B 622   O    86.7  81.2  98.7 169.9
REMARK 620 6 HOH B 668   O    91.4 164.2  88.2  86.2  84.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 504  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  74   OD2
REMARK 620 2 ILE B  91   O   108.5
REMARK 620 3 HOH B 625   O   128.1  79.0
REMARK 620 4 HOH B 623   O    82.0 167.9  89.7
REMARK 620 5 HOH B 699   O   128.3 103.1  97.2  73.6
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 503
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 504
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 601
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 602
DBREF  1EO3 A    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  1EO3 B    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  1EO3 C    1    11  PDB    1EO3     1EO3             1     11
DBREF  1EO3 D    1    11  PDB    1EO3     1EO3             1     11
SEQRES   1 C   11   DC  DA  DA  DG  DA TSP  DA  DT  DC  DT  DT
SEQRES   1 D   11   DC  DA  DA  DG  DA TSP  DA  DT  DC  DT  DT
SEQRES   1 A  245  MET SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP
SEQRES   2 A  245  GLU ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA
SEQRES   3 A  245  GLU GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL
SEQRES   4 A  245  LEU SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE
SEQRES   5 A  245  ASN LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU
SEQRES   6 A  245  PRO LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR
SEQRES   7 A  245  LYS PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE
SEQRES   8 A  245  LYS THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS
SEQRES   9 A  245  PHE THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN
SEQRES  10 A  245  THR LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA
SEQRES  11 A  245  HIS TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR
SEQRES  12 A  245  ARG LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU
SEQRES  13 A  245  ASN GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE
SEQRES  14 A  245  LEU GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY
SEQRES  15 A  245  SER GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS
SEQRES  16 A  245  TYR LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER
SEQRES  17 A  245  GLU ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG
SEQRES  18 A  245  THR SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER
SEQRES  19 A  245  GLU TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
SEQRES   1 B  245  MET SER LEU ARG SER ASP LEU ILE ASN ALA LEU TYR ASP
SEQRES   2 B  245  GLU ASN GLN LYS TYR ASP VAL CYS GLY ILE ILE SER ALA
SEQRES   3 B  245  GLU GLY LYS ILE TYR PRO LEU GLY SER ASP THR LYS VAL
SEQRES   4 B  245  LEU SER THR ILE PHE GLU LEU PHE SER ARG PRO ILE ILE
SEQRES   5 B  245  ASN LYS ILE ALA GLU LYS HIS GLY TYR ILE VAL GLU GLU
SEQRES   6 B  245  PRO LYS GLN GLN ASN HIS TYR PRO ASP PHE THR LEU TYR
SEQRES   7 B  245  LYS PRO SER GLU PRO ASN LYS LYS ILE ALA ILE ASP ILE
SEQRES   8 B  245  LYS THR THR TYR THR ASN LYS GLU ASN GLU LYS ILE LYS
SEQRES   9 B  245  PHE THR LEU GLY GLY TYR THR SER PHE ILE ARG ASN ASN
SEQRES  10 B  245  THR LYS ASN ILE VAL TYR PRO PHE ASP GLN TYR ILE ALA
SEQRES  11 B  245  HIS TRP ILE ILE GLY TYR VAL TYR THR ARG VAL ALA THR
SEQRES  12 B  245  ARG LYS SER SER LEU LYS THR TYR ASN ILE ASN GLU LEU
SEQRES  13 B  245  ASN GLU ILE PRO LYS PRO TYR LYS GLY VAL LYS VAL PHE
SEQRES  14 B  245  LEU GLN ASP LYS TRP VAL ILE ALA GLY ASP LEU ALA GLY
SEQRES  15 B  245  SER GLY ASN THR THR ASN ILE GLY SER ILE HIS ALA HIS
SEQRES  16 B  245  TYR LYS ASP PHE VAL GLU GLY LYS GLY ILE PHE ASP SER
SEQRES  17 B  245  GLU ASP GLU PHE LEU ASP TYR TRP ARG ASN TYR GLU ARG
SEQRES  18 B  245  THR SER GLN LEU ARG ASN ASP LYS TYR ASN ASN ILE SER
SEQRES  19 B  245  GLU TYR ARG ASN TRP ILE TYR ARG GLY ARG LYS
MODRES 1EO3 TSP C    6    T  3'-THIO-THYMIDINE-5'-PHOSPHATE
MODRES 1EO3 TSP D    6    T  3'-THIO-THYMIDINE-5'-PHOSPHATE
HET    TSP  C   6      20
HET    TSP  D   6      20
HET     MG  A 501       1
HET     MG  A 502       1
HET     MG  B 503       1
HET     MG  B 504       1
HET    ACY  A 601       4
HET    ACY  B 602       4
HETNAM     TSP 3'-THIO-THYMIDINE-5'-PHOSPHATE
HETNAM      MG MAGNESIUM ION
HETNAM     ACY ACETIC ACID
FORMUL   1  TSP    2(C10 H15 N2 O7 P S)
FORMUL   5   MG    4(MG 2+)
FORMUL   9  ACY    2(C2 H4 O2)
FORMUL  11  HOH   *297(H2 O)
HELIX    1   1 SER A    2  GLN A   16  1                                  15
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 LYS A  173  ILE A  176  1                                   4
HELIX    6   6 HIS A  195  GLY A  202  1                                   8
HELIX    7   7 SER A  208  ASN A  218  1                                  11
HELIX    8   8 THR A  222  ASN A  227  1                                   6
HELIX    9   9 ASN A  232  ARG A  242  1                                  11
HELIX   10  10 SER B    2  TYR B   18  1                                  17
HELIX   11  11 ASP B   36  HIS B   59  1                                  24
HELIX   12  12 PRO B  124  ASP B  126  5                                   3
HELIX   13  13 ASN B  154  LEU B  156  5                                   3
HELIX   14  14 LYS B  173  ALA B  177  1                                   5
HELIX   15  15 HIS B  195  GLY B  202  1                                   8
HELIX   16  16 SER B  208  ASN B  218  1                                  11
HELIX   17  17 THR B  222  ASN B  227  1                                   6
HELIX   18  18 ASN B  232  ARG B  242  1                                  11
SHEET    1   A 5 ILE A  30  PRO A  32  0
SHEET    2   A 5 VAL A  20  SER A  25 -1  O  ILE A  23   N  TYR A  31
SHEET    3   A 5 VAL B  20  SER B  25 -1  N  CYS B  21   O  ILE A  24
SHEET    4   A 5 LYS B  29  PRO B  32 -1  O  LYS B  29   N  SER B  25
SHEET    5   A 5 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  N  THR A  76   O  GLU A  64
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  N  ILE A 129   O  LYS A  86
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  N  ILE A 189   O  GLY A 108
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  N  THR B  76   O  GLU B  64
SHEET    3   D 5 LYS B  86  THR B  96 -1  N  ILE B  87   O  LEU B  77
SHEET    4   D 5 TYR B 128  THR B 139  1  N  ILE B 129   O  LYS B  86
SHEET    5   D 5 GLY B 165  ASP B 172 -1  O  GLY B 165   N  THR B 139
SHEET    1   E 2 THR B 106  GLY B 109  0
SHEET    2   E 2 ASN B 188  GLY B 190 -1  O  ILE B 189   N  LEU B 107
LINK         S3' TSP C   6                 P    DA C   7     1555   1555  1.97
LINK         S3' TSP D   6                 P    DA D   7     1555   1555  1.99
LINK         O3'  DA C   5                 P   TSP C   6     1555   1555  1.59
LINK         O3'  DA D   5                 P   TSP D   6     1555   1555  1.59
LINK         OE2 GLU A  45                MG    MG A 501     1555   1555  1.98
LINK         OD1 ASP A  74                MG    MG A 501     1555   1555  2.39
LINK         OD2 ASP A  74                MG    MG A 502     1555   1555  2.21
LINK         OE1 GLU B  45                MG    MG B 503     1555   1555  2.01
LINK         OD1 ASP B  74                MG    MG B 503     1555   1555  2.08
LINK         OD2 ASP B  74                MG    MG B 504     1555   1555  2.19
LINK         O   ILE B  91                MG    MG B 504     1555   1555  2.21
LINK        MG    MG A 501                 O   HOH A 610     1555   1555  2.11
LINK        MG    MG A 501                 O   HOH A 666     1555   1555  2.21
LINK        MG    MG A 501                 O   HOH A 708     1555   1555  2.04
LINK        MG    MG A 502                 O   HOH C  27     1555   1555  2.33
LINK        MG    MG A 502                 O   HOH A 611     1555   1555  2.18
LINK        MG    MG B 503                 O   HOH B 619     1555   1555  1.93
LINK        MG    MG B 503                 O   HOH B 618     1555   1555  2.17
LINK        MG    MG B 503                 O   HOH B 622     1555   1555  2.03
LINK        MG    MG B 503                 O   HOH B 668     1555   1555  2.14
LINK        MG    MG B 504                 O   HOH B 625     1555   1555  2.13
LINK        MG    MG B 504                 O   HOH B 623     1555   1555  2.13
LINK        MG    MG B 504                 O   HOH B 699     1555   1555  2.09
CISPEP   1 TYR A   72    PRO A   73          0         0.48
CISPEP   2 TYR B   72    PRO B   73          0        -0.89
SITE     1 AC1  5 GLU A  45  ASP A  74  HOH A 610  HOH A 666
SITE     2 AC1  5 HOH A 708
SITE     1 AC2  4 ASP A  74  ILE A  91  HOH A 611  HOH C  27
SITE     1 AC3  6 GLU B  45  ASP B  74  HOH B 618  HOH B 619
SITE     2 AC3  6 HOH B 622  HOH B 668
SITE     1 AC4  5 ASP B  74  ILE B  91  HOH B 623  HOH B 625
SITE     2 AC4  5 HOH B 699
SITE     1 AC5  6 TYR A  18  ASP A  19  VAL A  20  PHE A  47
SITE     2 AC5  6 TYR A 163  VAL A 166
SITE     1 AC6  6 TYR B  18  ASP B  19  VAL B  20  PHE B  44
SITE     2 AC6  6 TYR B 163  VAL B 166
CRYST1   48.000   48.500   63.800  97.00 108.90 106.30 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      0.020833  0.006092  0.008806        0.00000
SCALE2      0.000000  0.021482  0.005178        0.00000
SCALE3      0.000000  0.000000  0.017042        0.00000
      
PROCHECK
Go to PROCHECK summary
 References