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PDBsum entry 1pji

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Top Page protein dna_rna ligands metals links
Hydrolase/DNA PDB id
1pji
Jmol
Contents
Protein chain
267 a.a. *
DNA/RNA
Ligands
GOL ×4
Metals
_ZN
Waters ×223
* Residue conservation analysis
HEADER    HYDROLASE/DNA                           03-JUN-03   1PJI
TITLE     CRYSTAL STRUCTURE OF WILD TYPE LACTOCOCCUS LACTIS FPG COMPLEXED TO A
TITLE    2 1,3 PROPANEDIOL CONTAINING DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA (5'-D(*CP*TP*CP*TP*TP*TP*(PDI)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
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: SYNTHETIC;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES;
SOURCE   6 OTHER_DETAILS: SYNTHETIC;
SOURCE   7 MOL_ID: 3;
SOURCE   8 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS SUBSP. CREMORIS;
SOURCE   9 ORGANISM_TAXID: 1359;
SOURCE  10 STRAIN: SUBSP. CREMORIS;
SOURCE  11 GENE: MUTM OR FPG;
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PMAL-C
KEYWDS    DNA REPAIR, FPG, MUTM, ABASIC SITE, HYDROLASE-DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.PEREIRA,L.SERRE,C.ZELWER,B.CASTAING
REVDAT   3   13-JUL-11 1PJI    1       VERSN
REVDAT   2   24-FEB-09 1PJI    1       VERSN
REVDAT   1   03-AUG-04 1PJI    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  TITL   CRYSTAL STRUCTURE OF THE LACTOCOCCUS LACTIS FPG BOUND TO AN
REMARK   1  TITL 2 ABASIC SITE ANALOGUE CONTAINING DNA
REMARK   1  REF    EMBO J.                       V.  21  2854 2002
REMARK   1  REFN                   ISSN 0261-4189
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) : 40.00
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)   (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 48299
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) : 0.210
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 4766
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) (%) : 98.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3041
REMARK   3   BIN FREE R VALUE                    : 0.3475
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 100
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            : 2143
REMARK   3   NUCLEIC ACID ATOMS       : 554
REMARK   3   HETEROGEN ATOMS          : 25
REMARK   3   SOLVENT ATOMS            : 223
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 30.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.50
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) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.24
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  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: THE WATER 218 IS LOCATED CLOSE TO A
REMARK   3  SPECIAL POSITION IN THE CRYSTAL
REMARK   4
REMARK   4 1PJI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-03.
REMARK 100 THE RCSB ID CODE IS RCSB019363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-03
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                       : BM30A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48727
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06200
REMARK 200   FOR THE DATA SET  : 16.5000
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) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.53000
REMARK 200   FOR SHELL         : 1.000
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: 1KFV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CITRATE, HEPES, GLYCEROL, PH 8.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
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       71.03800
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       45.97750
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       45.97750
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       35.51900
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       45.97750
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       45.97750
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      106.55700
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       45.97750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.97750
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       35.51900
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       45.97750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.97750
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      106.55700
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       71.03800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY CORRESPONDS TO ONE FPG AND ONE DNA
REMARK 300 DUPLEX
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 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     ILE A   219
REMARK 465     ARG A   220
REMARK 465     THR A   221
REMARK 465     TYR A   222
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 470     ARG A  88    CG   CD   NE   CZ   NH1  NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1191     O    HOH A  1191     8555     0.31
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    ARG A  74     -126.35     50.83
REMARK 500    ALA A 224      107.50   -173.75
REMARK 500    VAL A 237      -37.81   -137.82
REMARK 500    GLN A 269       77.65   -116.47
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 A1128        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH A1190        DISTANCE =  5.03 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  112.4
REMARK 620 3 CYS A 265   SG  112.3  97.7
REMARK 620 4 CYS A 268   SG  105.4 114.5 114.7
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
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 RELATED ID: 1NNJ   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHOR MAINTAINS THAT THE SEQUENCE
REMARK 999 DATABASE RESIDUE ASP139 IS AN ERROR. THIS
REMARK 999 RESIDUE DOES NOT EXIST.
DBREF  1PJI A    1   271  UNP    P42371   FPG_LACLC        2    273
DBREF  1PJI D    1    14  PDB    1PJI     1PJI             1     14
DBREF  1PJI E   15    28  PDB    1PJI     1PJI            15     28
SEQADV 1PJI     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  PRO 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  A1001       6
HET    GOL  A1002       6
HET    GOL  A1003       6
HET    GOL  A1004      12
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    4(C3 H8 O3)
FORMUL   9  HOH   *223(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  SER A  152  1                                  12
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  PHE A  98 -1  O  LYS A  97   N  SER A  24
SHEET    3   A 4 GLY A 101  ALA A 106 -1  O  GLY A 101   N  PHE A  98
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  2.42
LINK        ZN    ZN A 300                 SG  CYS A 248     1555   1555  2.50
LINK        ZN    ZN A 300                 SG  CYS A 265     1555   1555  2.18
LINK        ZN    ZN A 300                 SG  CYS A 268     1555   1555  2.41
LINK         OG  PDI D   7                 P    DT D   8     1555   1555  1.59
LINK         P   PDI D   7                 O3'  DT D   6     1555   1555  1.60
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  GOL A1002
SITE     3 AC2 11 HOH A1063   DT D   9   DT D  10
SITE     1 AC3  7 ARG A  74  CYS A 248  GOL A1001  HOH A1093
SITE     2 AC3  7 HOH A1165   DT D  10  HOH E  61
SITE     1 AC4  8 ARG A  16  GLN A  20  LEU A  81  THR A  83
SITE     2 AC4  8 ASP A  85  PHE A  98  ASP A 100  GLY A 101
SITE     1 AC5 10 GLY A 259  ARG A 260  HOH A1082  HOH A1182
SITE     2 AC5 10  DT D   6   DT D   8   DT D   9  HOH D  18
SITE     3 AC5 10  DA E  20   DA E  21
CRYST1   91.955   91.955  142.076  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      0.010875  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010875  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007038        0.00000
      
PROCHECK
Go to PROCHECK summary
 References