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PDBsum entry 2b0e

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Top Page protein dna_rna metals Protein-protein interface(s) links
Hydrolase/DNA PDB id
2b0e
Jmol
Contents
Protein chains
233 a.a.
DNA/RNA
Metals
_CA ×2
Waters ×253
HEADER    HYDROLASE/DNA                           13-SEP-05   2B0E
TITLE     ECORV RESTRICTION ENDONUCLEASE/GAAUTC/CA2+
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*AP*AP*AP*GP*AP*AP*(DU)P*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
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 GENE: ECORVR;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: MM294;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBSRV
KEYWDS    PROTEIN-NUCLEIC ACID RECOGNITION, INDIRECT READOUT,
KEYWDS   2 RESTRICTION ENZYME, SUBSTRATE SPECIFICITY, NONCOGNATE,
KEYWDS   3 HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.A.HILLER,A.M.RODRIGUEZ,J.J.PERONA
REVDAT   3   24-FEB-09 2B0E    1       VERSN
REVDAT   2   22-NOV-05 2B0E    1       JRNL
REVDAT   1   27-SEP-05 2B0E    0
JRNL        AUTH   D.A.HILLER,A.M.RODRIGUEZ,J.J.PERONA
JRNL        TITL   NON-COGNATE ENZYME-DNA COMPLEX: STRUCTURAL AND
JRNL        TITL 2 KINETIC ANALYSIS OF ECORV ENDONUCLEASE BOUND TO
JRNL        TITL 3 THE ECORI RECOGNITION SITE GAATTC
JRNL        REF    J.MOL.BIOL.                   V. 354   121 2005
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16236314
JRNL        DOI    10.1016/J.JMB.2005.09.046
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   A.M.MARTIN,M.D.SAM,N.O.REICH,J.J.PERONA
REMARK   1  TITL   STRUCTURAL AND ENERGETIC ORIGINS OF INDIRECT
REMARK   1  TITL 2 READOUT IN SITE-SPECIFIC DNA CLEAVAGE BY A
REMARK   1  TITL 3 RESTRICTION ENDONUCLEASE
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   6   269 1999
REMARK   1  REFN                   ISSN 1072-8368
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.A.HILLER,J.M.FOGG,A.M.MARTIN,J.M.BEECHEM,
REMARK   1  AUTH 2 N.O.REICH,J.J.PERONA
REMARK   1  TITL   SIMULTANEOUS DNA BINDING AND BENDING BY ECORV
REMARK   1  TITL 2 ENDONUCLEASE OBSERVED BY REAL-TIME FLUORESCENCE
REMARK   1  REF    BIOCHEMISTRY                  V.  42 14375 2003
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 3
REMARK   1  AUTH   N.C.HORTON,J.J.PERONA
REMARK   1  TITL   DNA CLEAVAGE BY ECORV ENDONUCLEASE: TWO METAL IONS
REMARK   1  TITL 2 IN THREE METAL ION BINDING SITES
REMARK   1  REF    BIOCHEMISTRY                  V.  43  6841 2004
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    1.90 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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 69729
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.234
REMARK   3   FREE R VALUE                     : 0.314
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 3732
REMARK   3   NUCLEIC ACID ATOMS       : 444
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 253
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.62
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.80
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 2B0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-05.
REMARK 100 THE RCSB ID CODE IS RCSB034518.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-00
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) : NULL
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          : RIGAKU RAXIS II
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69729
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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   (%): 37.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K, HEPES, NACL, CACL2, PH 7.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K
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     MET A     1
REMARK 465     ASN A    97
REMARK 465     LYS A    98
REMARK 465     GLU A    99
REMARK 465     ASN A   100
REMARK 465     GLU A   101
REMARK 465     ALA A   142
REMARK 465     THR A   143
REMARK 465     ARG A   144
REMARK 465     LYS A   145
REMARK 465     SER A   146
REMARK 465     SER A   147
REMARK 465     MET B     1
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     LYS A  17    CG   CD   CE   NZ
REMARK 470     SER A  35    OG
REMARK 470     LYS A  38    CG   CD   CE   NZ
REMARK 470     LYS A  54    CG   CD   CE   NZ
REMARK 470     GLU A  57    CG   CD   OE1  OE2
REMARK 470     LYS A  67    CG   CD   CE   NZ
REMARK 470     GLN A  69    CG   CD   OE1  NE2
REMARK 470     ASN A  84    CG   OD1  ND2
REMARK 470     LYS A  85    CG   CD   CE   NZ
REMARK 470     ARG A 140    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 149    CG   CD   CE   NZ
REMARK 470     ASN A 152    CG   OD1  ND2
REMARK 470     ASN A 154    CG   OD1  ND2
REMARK 470     LYS A 161    CG   CD   CE   NZ
REMARK 470     LYS A 164    CG   CD   CE   NZ
REMARK 470     LYS A 197    CG   CD   CE   NZ
REMARK 470     LYS A 203    CG   CD   CE   NZ
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 A 245    CG   CD   CE   NZ
REMARK 470     LYS B  17    CG   CD   CE   NZ
REMARK 470     SER B  35    OG
REMARK 470     GLU B  45    CG   CD   OE1  OE2
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     GLN B  69    CG   CD   OE1  NE2
REMARK 470     ASN B  84    CG   OD1  ND2
REMARK 470     ASN B  97    CG   OD1  ND2
REMARK 470     LYS B  98    CG   CD   CE   NZ
REMARK 470     LYS B 102    CG   CD   CE   NZ
REMARK 470     ARG B 140    CG   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     GLU B 158    CG   CD   OE1  OE2
REMARK 470     LYS B 164    CG   CD   CE   NZ
REMARK 470     LYS B 197    CG   CD   CE   NZ
REMARK 470     LYS B 203    CG   CD   CE   NZ
REMARK 470     GLN B 224    CG   CD   OE1  NE2
REMARK 470     ASP B 228    CG   OD1  OD2
REMARK 470     LYS B 245    CG   CD   CE   NZ
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   O4' -  C1' -  N9  ANGL. DEV. =   2.4 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    CYS A  21       -3.38   -141.38
REMARK 500    LEU A 107       35.32    -94.78
REMARK 500    SER A 112     -105.42   -102.23
REMARK 500    ASN A 117      -37.17    -38.13
REMARK 500    ASN A 154        1.41    -64.67
REMARK 500    PRO A 162       21.08    -70.93
REMARK 500    LYS A 164      -67.36   -100.48
REMARK 500    THR A 187       69.95     21.74
REMARK 500    LYS A 229      -97.55   -146.63
REMARK 500    SER B 112     -121.01    -95.73
REMARK 500    THR B 187       64.34     28.74
REMARK 500    TYR B 196      -36.69    -36.58
REMARK 500    ASP B 228       44.99   -106.86
REMARK 500    LYS B 229      -78.86   -164.49
REMARK 500    TYR B 230      141.21   -171.23
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   6         0.09    SIDE_CHAIN
REMARK 500     DA D   1         0.07    SIDE_CHAIN
REMARK 500     DA D   2         0.08    SIDE_CHAIN
REMARK 500     DC D   9         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 B 281        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 366        DISTANCE =  6.12 ANGSTROMS
REMARK 525    HOH A 371        DISTANCE =  5.08 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                              CA A 307  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  45   OE1
REMARK 620 2 HOH A 376   O   137.0
REMARK 620 3 HOH A 432   O    71.4  85.6
REMARK 620 4 ASP A  74   OD2  79.9  63.6  89.4
REMARK 620 5 HOH A 381   O    63.1 156.5  92.7 139.9
REMARK 620 6 HOH A 385   O   147.5  68.5  96.3 131.1  88.4
REMARK 620 7 HOH A 386   O   109.3  97.4 173.8  96.7  82.4  79.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 322  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A  91   O
REMARK 620 2 HOH A 430   O   169.7
REMARK 620 3 HOH A 431   O    86.9  93.1
REMARK 620 4 ASP A  74   OD1  95.6  91.3 137.1
REMARK 620 5 HOH A 400   O    82.8  87.1 100.1 122.8
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 CA A 307
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 322
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AZ0   RELATED DB: PDB
REMARK 900 RELATED ID: 1BSU   RELATED DB: PDB
REMARK 900 RELATED ID: 2B0E   RELATED DB: PDB
DBREF  2B0E A    1   245  UNP    P04390   T2E5_ECOLI       0    244
DBREF  2B0E B    1   245  UNP    P04390   T2E5_ECOLI       0    244
DBREF  2B0E C    1    11  PDB    2B0E     2B0E             1     11
DBREF  2B0E D    1    11  PDB    2B0E     2B0E             1     11
SEQRES   1 C   11   DA  DA  DA  DG  DA  DA  DU  DT  DC  DT  DT
SEQRES   1 D   11   DA  DA  DA  DG  DA  DA  DU  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
HET     CA  A 307       1
HET     CA  A 322       1
HETNAM      CA CALCIUM ION
FORMUL   5   CA    2(CA 2+)
FORMUL   7  HOH   *253(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 ASN A  152  LEU A  156  5                                   5
HELIX    5   5 LYS A  173  ALA A  177  1                                   5
HELIX    6   6 HIS A  195  GLU A  201  1                                   7
HELIX    7   7 SER A  208  ASN A  218  1                                  11
HELIX    8   8 GLN A  224  LYS A  229  5                                   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  152  ILE B  159  5                                   8
HELIX   14  14 LYS B  173  ILE B  176  1                                   4
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  ASP B  228  1                                   7
HELIX   18  18 ASN B  232  ARG B  242  1                                  11
SHEET    1   A 4 ILE A  30  PRO A  32  0
SHEET    2   A 4 VAL A  20  SER A  25 -1  N  ILE A  23   O  TYR A  31
SHEET    3   A 4 VAL B  20  SER B  25 -1  O  ILE B  24   N  GLY A  22
SHEET    4   A 4 ILE B  30  PRO B  32 -1  O  TYR B  31   N  ILE B  23
SHEET    1   B 5 ILE A  62  GLU A  64  0
SHEET    2   B 5 PHE A  75  TYR A  78 -1  O  THR A  76   N  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  O  TRP A 132   N  ALA A  88
SHEET    5   B 5 LYS A 167  ASP A 172 -1  O  GLN A 171   N  ILE A 133
SHEET    1   C 2 THR A 106  GLY A 109  0
SHEET    2   C 2 ASN A 188  GLY A 190 -1  O  ILE A 189   N  GLY A 108
SHEET    1   D 5 ILE B  62  GLU B  64  0
SHEET    2   D 5 PHE B  75  TYR B  78 -1  O  TYR B  78   N  ILE B  62
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  GLY B 108
SHEET    3   E 3 ALA B 177  SER B 183 -1  N  GLY B 182   O  ASN B 188
LINK        CA    CA A 307                 OE1 GLU A  45     1555   1555  2.54
LINK        CA    CA A 307                 O   HOH A 376     1555   1555  2.67
LINK        CA    CA A 307                 O   HOH A 432     1555   1555  2.42
LINK        CA    CA A 307                 OD2 ASP A  74     1555   1555  2.47
LINK        CA    CA A 307                 O   HOH A 381     1555   1555  2.27
LINK        CA    CA A 307                 O   HOH A 385     1555   1555  2.17
LINK        CA    CA A 307                 O   HOH A 386     1555   1555  2.32
LINK        CA    CA A 322                 O   ILE A  91     1555   1555  2.52
LINK        CA    CA A 322                 O   HOH A 430     1555   1555  2.07
LINK        CA    CA A 322                 O   HOH A 431     1555   1555  2.31
LINK        CA    CA A 322                 OD1 ASP A  74     1555   1555  2.33
LINK        CA    CA A 322                 O   HOH A 400     1555   1555  2.34
CISPEP   1 TYR A   72    PRO A   73          0        -0.77
CISPEP   2 TYR B   72    PRO B   73          0         0.31
SITE     1 AC1  7 GLU A  45  ASP A  74  HOH A 376  HOH A 381
SITE     2 AC1  7 HOH A 385  HOH A 386  HOH A 432
SITE     1 AC2  6 GLU A  45  ASP A  74  ILE A  91  HOH A 400
SITE     2 AC2  6 HOH A 430  HOH A 431
CRYST1   48.100   48.500   63.900  97.00 109.00 106.70 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      0.020790  0.006237  0.008898        0.00000
SCALE2      0.000000  0.021526  0.005272        0.00000
SCALE3      0.000000  0.000000  0.017040        0.00000
      
PROCHECK
Go to PROCHECK summary
 References