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PDBsum entry 1az3

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Top Page protein Protein-protein interface(s) links
Endonuclease PDB id
1az3
Jmol
Contents
Protein chains
186 a.a.
215 a.a.
Waters ×38
HEADER    ENDONUCLEASE                            24-NOV-97   1AZ3
TITLE     ECORV ENDONUCLEASE, UNLIGANDED, FORM B
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ECORV ENDONUCLEASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 3.1.21.4
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562
KEYWDS    ENDONUCLEASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.PERONA,A.MARTIN
REVDAT   3   24-FEB-09 1AZ3    1       VERSN
REVDAT   2   01-APR-03 1AZ3    1       JRNL
REVDAT   1   27-MAY-98 1AZ3    0
JRNL        AUTH   J.J.PERONA,A.M.MARTIN
JRNL        TITL   CONFORMATIONAL TRANSITIONS AND STRUCTURAL
JRNL        TITL 2 DEFORMABILITY OF ECORV ENDONUCLEASE REVEALED BY
JRNL        TITL 3 CRYSTALLOGRAPHIC ANALYSIS.
JRNL        REF    J.MOL.BIOL.                   V. 273   207 1997
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9367757
JRNL        DOI    10.1006/JMBI.1997.1315
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   F.K.WINKLER,D.W.BANNER,C.OEFNER,D.TSERNOGLOU,
REMARK   1  AUTH 2 R.S.BROWN,S.P.HEATHMAN,R.K.BRYAN,P.D.MARTIN,
REMARK   1  AUTH 3 K.PETRATOS,K.S.WILSON
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF ECORV ENDONUCLEASE AND OF
REMARK   1  TITL 2 ITS COMPLEXES WITH COGNATE AND NON-COGNATE DNA
REMARK   1  TITL 3 FRAGMENTS
REMARK   1  REF    EMBO J.                       V.  12  1781 1993
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1 REFERENCE 2
REMARK   1  AUTH   F.K.WINKLER
REMARK   1  TITL   STRUCTURE AND FUNCTION OF RESTRICTION ENDONUCLEASES
REMARK   1  REF    CURR.OPIN.STRUCT.BIOL.        V.   2    93 1992
REMARK   1  REFN                   ISSN 0959-440X
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.0
REMARK   3   NUMBER OF REFLECTIONS             : 16499
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) : 0.223
REMARK   3   FREE R VALUE                     : 0.315
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
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) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060
REMARK   3   BIN FREE R VALUE                    : 0.3910
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            : 3136
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 49
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 35.80
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) : 0.50
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) : 1.98
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.16
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.46
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1AZ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : SEP-96
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 4
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
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   (%): 48.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-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       36.85000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.95000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.40000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       29.95000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.85000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.40000
REMARK 290   SMTRY3   4  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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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     ALA A    10
REMARK 465     LEU A    11
REMARK 465     TYR A    12
REMARK 465     ASP A    13
REMARK 465     GLU A    14
REMARK 465     ASN A    15
REMARK 465     GLN A    16
REMARK 465     LYS A    17
REMARK 465     GLY A    34
REMARK 465     SER A    35
REMARK 465     ASP A    36
REMARK 465     THR A    37
REMARK 465     LYS A    38
REMARK 465     VAL A    39
REMARK 465     LEU A    40
REMARK 465     ASN A    97
REMARK 465     LYS A    98
REMARK 465     ILE A   103
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     LEU A   148
REMARK 465     SER A   183
REMARK 465     GLY A   184
REMARK 465     ASN A   185
REMARK 465     THR A   186
REMARK 465     THR A   187
REMARK 465     ASN A   218
REMARK 465     TYR A   219
REMARK 465     GLU A   220
REMARK 465     ARG A   221
REMARK 465     THR A   222
REMARK 465     SER A   223
REMARK 465     GLN A   224
REMARK 465     LEU A   225
REMARK 465     ARG A   226
REMARK 465     ASN A   227
REMARK 465     ASP A   228
REMARK 465     LYS A   229
REMARK 465     TYR A   230
REMARK 465     ASN A   231
REMARK 465     ASN A   232
REMARK 465     ILE A   233
REMARK 465     SER A   234
REMARK 465     GLU A   235
REMARK 465     TYR A   236
REMARK 465     ARG A   237
REMARK 465     ASN A   238
REMARK 465     TRP A   239
REMARK 465     ILE A   240
REMARK 465     TYR A   241
REMARK 465     ARG A   242
REMARK 465     GLY A   243
REMARK 465     ARG A   244
REMARK 465     LYS A   245
REMARK 465     ASN B    15
REMARK 465     GLN B    16
REMARK 465     LYS B    17
REMARK 465     TYR B    18
REMARK 465     THR B    37
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 465     SER B   147
REMARK 465     LEU B   148
REMARK 465     SER B   183
REMARK 465     GLY B   184
REMARK 465     ASN B   185
REMARK 465     THR B   186
REMARK 465     THR B   187
REMARK 465     ARG B   221
REMARK 465     THR B   222
REMARK 465     SER B   223
REMARK 465     GLN B   224
REMARK 465     LEU B   225
REMARK 465     ARG B   226
REMARK 465     ASN B   227
REMARK 465     ASP B   228
REMARK 465     ARG B   242
REMARK 465     GLY B   243
REMARK 465     ARG B   244
REMARK 465     LYS B   245
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     VAL A  20    CG1  CG2
REMARK 470     GLU A  27    CG   CD   OE1  OE2
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  68    CG   CD   OE1  NE2
REMARK 470     GLN A  69    CG   CD   OE1  NE2
REMARK 470     ASN A  70    CG   OD1  ND2
REMARK 470     LYS A  85    CG   CD   CE   NZ
REMARK 470     GLU A  99    CG   CD   OE1  OE2
REMARK 470     GLU A 101    CG   CD   OE1  OE2
REMARK 470     LYS A 102    CG   CD   CE   NZ
REMARK 470     LYS A 104    CG   CD   CE   NZ
REMARK 470     ARG A 115    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASN A 116    CG   OD1  ND2
REMARK 470     THR A 118    OG1  CG2
REMARK 470     LYS A 119    CG   CD   CE   NZ
REMARK 470     ARG A 140    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A 141    CG1  CG2
REMARK 470     GLU A 155    CG   CD   OE1  OE2
REMARK 470     GLU A 158    CG   CD   OE1  OE2
REMARK 470     LYS A 161    CG   CD   CE   NZ
REMARK 470     TYR A 163    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS A 164    CG   CD   CE   NZ
REMARK 470     LEU A 180    CG   CD1  CD2
REMARK 470     ASN A 188    CG   OD1  ND2
REMARK 470     HIS A 193    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A 197    CG   CD   CE   NZ
REMARK 470     LYS A 203    CG   CD   CE   NZ
REMARK 470     ASP A 207    CG   OD1  OD2
REMARK 470     ASP A 210    CG   OD1  OD2
REMARK 470     GLU B  14    CG   CD   OE1  OE2
REMARK 470     ASP B  19    CG   OD1  OD2
REMARK 470     LYS B  29    CG   CD   CE   NZ
REMARK 470     ASP B  36    CG   OD1  OD2
REMARK 470     LYS B  38    CG   CD   CE   NZ
REMARK 470     LYS B  54    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  69    CG   CD   OE1  NE2
REMARK 470     ASN B  70    CG   OD1  ND2
REMARK 470     ASN B  84    CG   OD1  ND2
REMARK 470     LYS B  98    CG   CD   CE   NZ
REMARK 470     LYS B 102    CG   CD   CE   NZ
REMARK 470     LYS B 104    CG   CD   CE   NZ
REMARK 470     LYS B 119    CG   CD   CE   NZ
REMARK 470     LYS B 149    CG   CD   CE   NZ
REMARK 470     ASN B 152    CG   OD1  ND2
REMARK 470     GLU B 158    CG   CD   OE1  OE2
REMARK 470     LYS B 203    CG   CD   CE   NZ
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   5      -74.99    -66.33
REMARK 500    ASP A  19       42.51   -105.82
REMARK 500    CYS A  21       46.18   -148.94
REMARK 500    LYS A  85       50.30   -149.97
REMARK 500    ASN A 100       79.60     72.62
REMARK 500    LEU A 107     -126.14    -89.32
REMARK 500    SER A 112     -135.85    -76.84
REMARK 500    PHE A 113      -29.59    -35.18
REMARK 500    ASN A 117      -30.32    -28.01
REMARK 500    ASN A 120       16.78     59.86
REMARK 500    LEU A 156      -75.41    -39.68
REMARK 500    ASN A 157       20.42    -66.50
REMARK 500    LYS A 203       55.80   -117.79
REMARK 500    TRP A 216       43.41    -92.70
REMARK 500    GLN B  69      -60.48      3.65
REMARK 500    ASN B  70        6.85    -52.93
REMARK 500    LYS B  85       53.28   -114.43
REMARK 500    LYS B 102      133.24    -39.10
REMARK 500    SER B 112     -118.05    -88.47
REMARK 500    ASN B 117      -30.01     71.51
REMARK 500    ASN B 120       17.79     51.88
REMARK 500    LEU B 156      -40.92    -28.73
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    TYR B 219         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1AZ3 A    2   245  UNP    P04390   T2E5_ECOLI       1    244
DBREF  1AZ3 B    2   245  UNP    P04390   T2E5_ECOLI       1    244
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 LYS
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 LYS
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
FORMUL   3  HOH   *38(H2 O)
HELIX    1   1 LEU A    3  ILE A    8  1                                   6
HELIX    2   2 ILE A   43  HIS A   59  1                                  17
HELIX    3   3 PHE A  125  GLN A  127  5                                   3
HELIX    4   4 ILE A  153  GLU A  158  5                                   6
HELIX    5   5 LYS A  173  ILE A  176  1                                   4
HELIX    6   6 TYR A  196  GLU A  201  1                                   6
HELIX    7   7 GLU A  209  TYR A  215  1                                   7
HELIX    8   8 LEU B    3  TYR B   12  1                                  10
HELIX    9   9 VAL B   39  HIS B   59  1                                  21
HELIX   10  10 PHE B  113  ASN B  116  1                                   4
HELIX   11  11 PHE B  125  GLN B  127  5                                   3
HELIX   12  12 TRP B  174  ILE B  176  5                                   3
HELIX   13  13 TYR B  196  VAL B  200  1                                   5
HELIX   14  14 GLU B  209  ARG B  217  1                                   9
HELIX   15  15 ILE B  233  TRP B  239  1                                   7
SHEET    1   A 5 ILE A  62  GLU A  65  0
SHEET    2   A 5 PHE A  75  TYR A  78 -1  N  TYR A  78   O  ILE A  62
SHEET    3   A 5 LYS A  86  THR A  96 -1  N  ILE A  89   O  PHE A  75
SHEET    4   A 5 TYR A 128  THR A 139  1  N  ILE A 129   O  LYS A  86
SHEET    5   A 5 LYS A 167  ASP A 172 -1  N  GLN A 171   O  ILE A 133
SHEET    1   B 5 TYR B  61  GLU B  64  0
SHEET    2   B 5 PHE B  75  LYS B  79 -1  N  TYR B  78   O  ILE B  62
SHEET    3   B 5 LYS B  86  THR B  96 -1  N  ILE B  89   O  PHE B  75
SHEET    4   B 5 TYR B 128  THR B 139  1  N  ILE B 129   O  LYS B  86
SHEET    5   B 5 VAL B 166  ASP B 172 -1  N  GLN B 171   O  ILE B 133
CISPEP   1 TYR A   72    PRO A   73          0        -2.14
CISPEP   2 TYR B   72    PRO B   73          0        -0.71
CRYST1   73.700  122.800   59.900  90.00  90.00  90.00 P 21 21 21    8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013569  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008143  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016694        0.00000
      
PROCHECK
Go to PROCHECK summary
 References