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PDBsum entry 1nnj

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Top Page protein dna_rna ligands metals links
Hydrolase PDB id
1nnj
Jmol
Contents
Protein chain
267 a.a. *
DNA/RNA
Ligands
GOL ×2
Metals
_ZN
Waters ×227
* Residue conservation analysis
HEADER    HYDROLASE                               14-JAN-03   1NNJ
TITLE     CRYSTAL STRUCTURE COMPLEX BETWEEN THE LACTOCOCCUS LACTIS FPG AND AN
TITLE    2 ABASIC SITE CONTAINING DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*CP*TP*CP*TP*TP*TP*(PDI)P*TP*TP*TP*CP*TP*CP*G)-3';
COMPND   3 CHAIN: D;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: 5'-D(*GP*CP*GP*AP*GP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3';
COMPND   7 CHAIN: E;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE;
COMPND  11 CHAIN: A;
COMPND  12 SYNONYM: FAPY-DNA GLYCOSYLASE;
COMPND  13 EC: 3.2.2.23;
COMPND  14 ENGINEERED: YES;
COMPND  15 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;
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
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.SERRE,K.PEREIRA DE JESUS,S.BOITEUX,C.ZELWER,B.CASTAING
REVDAT   3   13-JUL-11 1NNJ    1       VERSN
REVDAT   2   24-FEB-09 1NNJ    1       VERSN
REVDAT   1   11-FEB-03 1NNJ    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 THE 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 1.1
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) : 0.215
REMARK   3   FREE R VALUE                     : 0.236
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) : 0.2660
REMARK   3   BIN FREE R VALUE                    : 0.2900
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 102
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            : 2148
REMARK   3   NUCLEIC ACID ATOMS       : 554
REMARK   3   HETEROGEN ATOMS          : 13
REMARK   3   SOLVENT ATOMS            : 227
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 28.30
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 1NNJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-03.
REMARK 100 THE RCSB ID CODE IS RCSB018035.
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                             : 8.5
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   : 56858
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6
REMARK 200  DATA REDUNDANCY                : 11.600
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : 0.07400
REMARK 200   FOR THE DATA SET  : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.66500
REMARK 200  R SYM FOR SHELL            (I) : 0.62700
REMARK 200   FOR SHELL         : 1.200
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   (%): 65.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE, HEPES, GLYCEROL, PH 8.5,
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       71.26500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.07500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.07500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.63250
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.07500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.07500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      106.89750
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.07500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.07500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.63250
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.07500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.07500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      106.89750
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       71.26500
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 389  LIES ON A SPECIAL POSITION.
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     ARG A   220
REMARK 465     THR A   221
REMARK 465     TYR A   222
REMARK 465     SER A   223
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     PDI D   7    O3P
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     -131.56     51.58
REMARK 500    ASP A 107      101.95   -160.78
REMARK 500    SER A 227       33.34    -77.24
REMARK 500    VAL A 237      -35.02   -134.55
REMARK 500    GLN A 269       78.04   -117.67
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         0.07    SIDE CHAIN
REMARK 500     DG E  15         0.05    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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  112.7
REMARK 620 3 CYS A 265   SG  110.0  95.3
REMARK 620 4 CYS A 268   SG  107.5 115.1 116.0
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KFV   RELATED DB: PDB
REMARK 900 FIRST CRYSTAL STRUCTURE OBTAINED WITH A BLUNT 13 MER 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
DBREF  1NNJ A    1   271  UNP    P42371   FPG_LACLC        2    273
DBREF  1NNJ D    1    14  PDB    1NNJ     1NNJ             1     14
DBREF  1NNJ E   15    28  PDB    1NNJ     1NNJ            15     28
SEQADV 1NNJ GLY A    1  UNP  P42371    PRO     2 ENGINEERED
SEQADV 1NNJ     A       UNP  P42371    ASP   139 SEE REMARK 999
SEQRES   1 D   14   DC  DT  DC  DT  DT  DT PDI  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    PDI  D   7       8
HET     ZN  A 300       1
HET    GOL  A 301       6
HET    GOL  D 302       6
HETNAM     PDI PHOSPHORIC ACID MONO-(3-HYDROXY-PROPYL) ESTER
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   1  PDI    C3 H9 O5 P
FORMUL   4   ZN    ZN 2+
FORMUL   5  GOL    2(C3 H8 O3)
FORMUL   7  HOH   *227(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  GLU A  234  5                                   5
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  PHE A 264   N  GLN A 253
LINK         O3'  DT D   6                 P   PDI D   7     1555   1555  1.60
LINK         P    DT D   8                 OG  PDI D   7     1555   1555  1.59
LINK         SG  CYS A 245                ZN    ZN A 300     1555   1555  2.41
LINK         SG  CYS A 248                ZN    ZN A 300     1555   1555  2.48
LINK         SG  CYS A 265                ZN    ZN A 300     1555   1555  2.19
LINK         SG  CYS A 268                ZN    ZN A 300     1555   1555  2.42
SITE     1 AC1  4 CYS A 245  CYS A 248  CYS A 265  CYS A 268
SITE     1 AC2 11 TYR A  58  HIS A  72  ARG A  74  THR A 113
SITE     2 AC2 11 GLU A 115  TYR A 125  LYS A 129  HOH A 341
SITE     3 AC2 11 HOH A 434   DT D   9   DT D  10
SITE     1 AC3  8 GLY A 259   DT D   6   DT D   8   DT D   9
SITE     2 AC3  8 HOH D 312  HOH D 319  HOH D 329   DA E  21
CRYST1   92.150   92.150  142.530  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      0.010852  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010852  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007016        0.00000
      
PROCHECK
Go to PROCHECK summary
 References