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PDBsum entry 1pjj

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Top Page protein dna_rna ligands metals links
Hydrolase/DNA PDB id
1pjj
Jmol
Contents
Protein chain
271 a.a. *
DNA/RNA
Ligands
GOL ×3
Metals
_ZN
Waters ×278
* Residue conservation analysis
HEADER    HYDROLASE/DNA                           03-JUN-03   1PJJ
TITLE     COMPLEX BETWEEN THE LACTOCOCCUS LACTIS FPG AND AN ABASIC SITE
TITLE    2 CONTAINING DNA.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*CP*TP*CP*TP*TP*TP*(3DR)P*TP*TP*TP*CP*TP*CP*G)-
COMPND   3 3');
COMPND   4 CHAIN: D;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: DNA (5'-D(*GP*CP*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3');
COMPND   8 CHAIN: E;
COMPND   9 ENGINEERED: YES;
COMPND  10 MOL_ID: 3;
COMPND  11 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE;
COMPND  12 CHAIN: A;
COMPND  13 SYNONYM: FAPY-DNA GLYCOSYLASE;
COMPND  14 EC: 3.2.2.23;
COMPND  15 ENGINEERED: YES;
COMPND  16 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 SYNTHETIC: YES;
SOURCE   5 MOL_ID: 3;
SOURCE   6 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS;
SOURCE   7 ORGANISM_TAXID: 1358;
SOURCE   8 GENE: MUTM OR FPG;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PMAL-C
KEYWDS    DNA REPAIR, FPG, MUTM, ABASIC SITE, HYDROLASE-DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.SERRE,K.PEREIRA DE JESUS,S.BOITEUX,C.ZELWER,B.CASTAING
REVDAT   3   13-JUL-11 1PJJ    1       VERSN
REVDAT   2   24-FEB-09 1PJJ    1       VERSN
REVDAT   1   08-JUN-04 1PJJ    0
JRNL        AUTH   K.PEREIRA DE JESUS,L.SERRE,C.ZELWER,B.CASTAING
JRNL        TITL   STRUCTURAL INSIGHTS INTO ABASIC SITE FOR FPG SPECIFIC
JRNL        TITL 2 BINDING AND CATALYSIS: COMPARATIVE HIGH-RESOLUTION
JRNL        TITL 3 CRYSTALLOGRAPHIC STUDIES OF FPG BOUND TO VARIOUS MODELS OF
JRNL        TITL 4 ABASIC SITE ANALOGUES-CONTAINING DNA.
JRNL        REF    NUCLEIC ACIDS RES.            V.  33  5936 2005
JRNL        REFN                   ISSN 0305-1048
JRNL        PMID   16243784
JRNL        DOI    10.1093/NAR/GKI879
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.PEREIRA DE JESUS,L.SERRE,N.HERVOUET,V.BOUCKSON-CASTAING,
REMARK   1  AUTH 2 C.ZELWER,B.CASTAING
REMARK   1  TITL   CRYSTALLIZATION AND PRIMARY X-RAY CRYSTALLOGRAPHIC STUDIES
REMARK   1  TITL 2 OF A COMPLEX BETWEEN TH LACTOCOCCUS LACTIS FPG DNA- REPAIR
REMARK   1  TITL 3 ENZYME AND AN ABASIC SITE CONTAINING DNA
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  58   679 2002
REMARK   1  REFN                   ISSN 0907-4449
REMARK   1  DOI    10.1107/S0907444902001397
REMARK   2
REMARK   2 RESOLUTION.    1.90 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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 48703
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) : 0.202
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2425
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370
REMARK   3   BIN FREE R VALUE                    : 0.4040
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 67
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            : 2164
REMARK   3   NUCLEIC ACID ATOMS       : 557
REMARK   3   HETEROGEN ATOMS          : 19
REMARK   3   SOLVENT ATOMS            : 278
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 27.69
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.00
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) : NULL
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 : ISOTROPIC
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 1PJJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-03.
REMARK 100 THE RCSB ID CODE IS RCSB019364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48787
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.700
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 9.600
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : 0.07300
REMARK 200   FOR THE DATA SET  : 5.2000
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     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.51600
REMARK 200  R SYM FOR SHELL            (I) : 0.48800
REMARK 200   FOR SHELL         : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1KFV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE, HEPES, GLYCEROL, PH 8.0,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.21000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       45.94600
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       45.94600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.60500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       45.94600
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       45.94600
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      106.81500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       45.94600
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.94600
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.60500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       45.94600
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.94600
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      106.81500
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       71.21000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A 220    CB   CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR A 221    CB   OG1  CG2
REMARK 470     TYR A 222    CB   CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     TYR A 222    OH
REMARK 470     SER A 223    CB   OG
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    ARG A  74     -129.94     51.64
REMARK 500    ASP A 107      103.17   -161.88
REMARK 500    ARG A 220      -71.32   -144.85
REMARK 500    THR A 221     -172.95     96.02
REMARK 500    TYR A 222      165.31    128.77
REMARK 500    VAL A 237      -37.26   -136.04
REMARK 500    GLN A 269       77.60   -116.46
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     DC D   1         0.06    SIDE CHAIN
REMARK 500     DG E  15         0.05    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 A1220        DISTANCE =  6.98 ANGSTROMS
REMARK 525    HOH A1225        DISTANCE =  5.09 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                              ZN A 300  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 245   SG
REMARK 620 2 CYS A 248   SG  111.8
REMARK 620 3 CYS A 265   SG  111.3  96.8
REMARK 620 4 CYS A 268   SG  107.9 113.7 115.1
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KFV   RELATED DB: PDB
REMARK 900 FIRST CRYSTAL STRUCTURE OBTAINED WITH A BLUNT 13MER DNA
REMARK 900 DUPLEX
REMARK 900 RELATED ID: 1EE8   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FREE FPG
REMARK 900 RELATED ID: 1K82   RELATED DB: PDB
REMARK 900 RELATED ID: 1L1T   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHOR MAINTAINS THAT THE ASP137 IS
REMARK 999 AN ERROR IN THE SEQUENCE DATABASE. THIS
REMARK 999 RESIDUE DOES NOT EXIST.
DBREF  1PJJ A    1   271  UNP    P42371   FPG_LACLC        2    273
DBREF  1PJJ D    1    14  PDB    1PJJ     1PJJ             1     14
DBREF  1PJJ E   15    28  PDB    1PJJ     1PJJ            15     28
SEQADV 1PJJ GLY A    1  UNP  P42371    PRO     2 ENGINEERED
SEQADV 1PJJ     A       UNP  P42371    ASP   138 SEE REMARK 999
SEQRES   1 D   14   DC  DT  DC  DT  DT  DT 3DR  DT  DT  DT  DC  DT  DC
SEQRES   2 D   14   DG
SEQRES   1 E   14   DG  DC  DG  DA  DG  DA  DA  DA  DC  DA  DA  DA  DG
SEQRES   2 E   14   DA
SEQRES   1 A  271  GLY GLU LEU PRO GLU VAL GLU THR VAL ARG ARG GLU LEU
SEQRES   2 A  271  GLU LYS ARG ILE VAL GLY GLN LYS ILE ILE SER ILE GLU
SEQRES   3 A  271  ALA THR TYR PRO ARG MET VAL LEU THR GLY PHE GLU GLN
SEQRES   4 A  271  LEU LYS LYS GLU LEU THR GLY LYS THR ILE GLN GLY ILE
SEQRES   5 A  271  SER ARG ARG GLY LYS TYR LEU ILE PHE GLU ILE GLY ASP
SEQRES   6 A  271  ASP PHE ARG LEU ILE SER HIS LEU ARG MET GLU GLY LYS
SEQRES   7 A  271  TYR ARG LEU ALA THR LEU ASP ALA PRO ARG GLU LYS HIS
SEQRES   8 A  271  ASP HIS LEU THR MET LYS PHE ALA ASP GLY GLN LEU ILE
SEQRES   9 A  271  TYR ALA ASP VAL ARG LYS PHE GLY THR TRP GLU LEU ILE
SEQRES  10 A  271  SER THR ASP GLN VAL LEU PRO TYR PHE LEU LYS LYS LYS
SEQRES  11 A  271  ILE GLY PRO GLU PRO THR TYR GLU ASP PHE ASP GLU LYS
SEQRES  12 A  271  LEU PHE ARG GLU LYS LEU ARG LYS SER THR LYS LYS ILE
SEQRES  13 A  271  LYS PRO TYR LEU LEU GLU GLN THR LEU VAL ALA GLY LEU
SEQRES  14 A  271  GLY ASN ILE TYR VAL ASP GLU VAL LEU TRP LEU ALA LYS
SEQRES  15 A  271  ILE HIS PRO GLU LYS GLU THR ASN GLN LEU ILE GLU SER
SEQRES  16 A  271  SER ILE HIS LEU LEU HIS ASP SER ILE ILE GLU ILE LEU
SEQRES  17 A  271  GLN LYS ALA ILE LYS LEU GLY GLY SER SER ILE ARG THR
SEQRES  18 A  271  TYR SER ALA LEU GLY SER THR GLY LYS MET GLN ASN GLU
SEQRES  19 A  271  LEU GLN VAL TYR GLY LYS THR GLY GLU LYS CYS SER ARG
SEQRES  20 A  271  CYS GLY ALA GLU ILE GLN LYS ILE LYS VAL ALA GLY ARG
SEQRES  21 A  271  GLY THR HIS PHE CYS PRO VAL CYS GLN GLN LYS
HET    3DR  D   7      11
HET     ZN  A 300       1
HET    GOL  A1002       6
HET    GOL  A1003       6
HET    GOL  A1004      12
HETNAM     3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETSYN     3DR ABASIC DIDEOXYRIBOSE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  3DR    C5 H11 O6 P
FORMUL   4   ZN    ZN 2+
FORMUL   5  GOL    3(C3 H8 O3)
FORMUL   8  HOH   *278(H2 O)
HELIX    1   1 GLU A    2  VAL A   18  1                                  17
HELIX    2   2 TYR A   29  VAL A   33  5                                   5
HELIX    3   3 GLY A   36  THR A   45  1                                  10
HELIX    4   4 GLN A  121  LYS A  130  1                                  10
HELIX    5   5 ASP A  141  LYS A  151  1                                  11
HELIX    6   6 LYS A  155  GLU A  162  1                                   8
HELIX    7   7 GLY A  170  ALA A  181  1                                  12
HELIX    8   8 GLU A  188  LEU A  192  5                                   5
HELIX    9   9 ILE A  193  LEU A  214  1                                  22
HELIX   10  10 LYS A  230  LEU A  235  5                                   6
SHEET    1   A 4 SER A  24  ALA A  27  0
SHEET    2   A 4 ASP A  92  LYS A  97 -1  O  LYS A  97   N  SER A  24
SHEET    3   A 4 GLN A 102  ALA A 106 -1  O  TYR A 105   N  LEU A  94
SHEET    4   A 4 LYS A  78  ALA A  82 -1  N  LYS A  78   O  ALA A 106
SHEET    1   B 4 ILE A  49  ARG A  55  0
SHEET    2   B 4 TYR A  58  ILE A  63 -1  O  ILE A  60   N  SER A  53
SHEET    3   B 4 PHE A  67  HIS A  72 -1  O  SER A  71   N  LEU A  59
SHEET    4   B 4 THR A 113  SER A 118 -1  O  GLU A 115   N  ILE A  70
SHEET    1   C 2 GLN A 253  VAL A 257  0
SHEET    2   C 2 ARG A 260  PHE A 264 -1  O  THR A 262   N  ILE A 255
LINK        ZN    ZN A 300                 SG  CYS A 245     1555   1555  2.40
LINK        ZN    ZN A 300                 SG  CYS A 248     1555   1555  2.46
LINK        ZN    ZN A 300                 SG  CYS A 265     1555   1555  2.19
LINK        ZN    ZN A 300                 SG  CYS A 268     1555   1555  2.37
LINK         O3'  DT D   6                 P   3DR D   7     1555   1555  1.60
LINK         O3' 3DR D   7                 P    DT D   8     1555   1555  1.60
SITE     1 AC1  4 CYS A 245  CYS A 248  CYS A 265  CYS A 268
SITE     1 AC2  7 ARG A  16  GLN A  20  LEU A  81  THR A  83
SITE     2 AC2  7 ASP A  85  ASP A 100  GLY A 101
SITE     1 AC3  8 GLY A 259  HOH A1202  HOH A1209  HOH A1211
SITE     2 AC3  8  DT D   8   DA E  21  HOH E 220  HOH E 268
SITE     1 AC4 12 LEU A  34  TYR A  58  HIS A  72  ARG A  74
SITE     2 AC4 12 THR A 113  GLU A 115  TYR A 125  LYS A 129
SITE     3 AC4 12 HOH A1065  HOH A1159   DT D   9   DT D  10
CRYST1   91.892   91.892  142.420  90.00  90.00  90.00 P 41 21 2     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      0.010882  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010882  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007021        0.00000
      
PROCHECK
Go to PROCHECK summary
 References