spacer
spacer

PDBsum entry 3a42

Go to PDB code: 
Top Page protein ligands links
Hydrolase PDB id
3a42
Jmol
Contents
Protein chain
282 a.a.
Ligands
GOL ×3
SO4
Waters ×82
HEADER    HYDROLASE                               30-JUN-09   3A42
TITLE     CRYSTAL STRUCTURE OF MVNEI1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: FAPY-DNA GLYCOSYLASE, DNA-(APURINIC OR APYRIMIDINIC SITE)
COMPND   5 LYASE, AP LYASE, ENDONUCLEASE VIII MVNEI1;
COMPND   6 EC: 3.2.2.23;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ACANTHAMOEBA POLYPHAGA MIMIVIRUS;
SOURCE   3 ORGANISM_COMMON: APMV;
SOURCE   4 ORGANISM_TAXID: 212035;
SOURCE   5 GENE: L315, MIMI_L315;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS    HELIX TWO TURNS HELIX, ZINC-LESS FINGER, HYDROLASE, DNA DAMAGE, DNA
KEYWDS   2 REPAIR, DNA-BINDING, GLYCOSIDASE, LYASE, MULTIFUNCTIONAL ENZYME
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.IMAMURA,S.WALLACE,S.DOUBLIE
REVDAT   3   13-JUL-11 3A42    1       VERSN
REVDAT   2   29-SEP-09 3A42    1       JRNL
REVDAT   1   21-JUL-09 3A42    0
JRNL        AUTH   K.IMAMURA,S.S.WALLACE,S.DOUBLIE
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF A VIRAL NEIL1 ORTHOLOG
JRNL        TITL 2 UNLIGANDED AND BOUND TO ABASIC SITE-CONTAINING DNA
JRNL        REF    J.BIOL.CHEM.                  V. 284 26174 2009
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   19625256
JRNL        DOI    10.1074/JBC.M109.021907
REMARK   2
REMARK   2 RESOLUTION.    2.60 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) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
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             : 12144
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.209
REMARK   3   FREE R VALUE                     : 0.268
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300
REMARK   3   FREE R VALUE TEST SET COUNT      : 1256
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) : 2.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260
REMARK   3   BIN FREE R VALUE                    : 0.3930
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 : 0.031
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2337
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 23
REMARK   3   SOLVENT ATOMS            : 82
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 66.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.73
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.65300
REMARK   3    B22 (A**2) : 0.65300
REMARK   3    B33 (A**2) : -1.30700
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33
REMARK   3   ESD FROM SIGMAA              (A) : 0.39
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.33
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) : 1.510 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.618 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.876 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.953 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 49.07
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : GOL_XPLOR_PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : GOL_XPLOR_TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3A42 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB028784.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.3
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 RU300
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : MAR MIRRORS
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12173
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 11.800
REMARK 200  R MERGE                    (I) : 0.05900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 44.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000MME, AMMONIUM SULFATE, PH6.3,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.89933
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       14.94967
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       22.42450
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        7.47483
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       37.37417
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A     1
REMARK 465     GLY A   271
REMARK 465     SER A   272
REMARK 465     GLY A   273
REMARK 465     LYS A   274
REMARK 465     ASN A   275
REMARK 465     LYS A   276
REMARK 465     HIS A   290
REMARK 465     HIS A   291
REMARK 465     HIS A   292
REMARK 465     HIS A   293
REMARK 465     HIS A   294
REMARK 465     HIS A   295
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    GLU A  37      156.34    -38.86
REMARK 500    LYS A  72        0.31    -66.74
REMARK 500    ASP A 112       79.71   -165.23
REMARK 500    LYS A 120      133.51   -170.42
REMARK 500    ASP A 144       48.26   -153.81
REMARK 500    ASP A 146       79.37   -105.31
REMARK 500    LYS A 149        3.17    -59.47
REMARK 500    LYS A 154       49.45    -92.92
REMARK 500    MET A 222       -2.06     81.23
REMARK 500    PRO A 239       -1.83    -59.68
REMARK 500    ASN A 260       10.46    -66.20
REMARK 500    ALA A 266       49.88    -90.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
DBREF  3A42 A    1   287  UNP    Q5UQ00   FPG_MIMIV        1    287
SEQADV 3A42 LEU A  288  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 GLU A  289  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  290  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  291  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  292  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  293  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  294  UNP  Q5UQ00              EXPRESSION TAG
SEQADV 3A42 HIS A  295  UNP  Q5UQ00              EXPRESSION TAG
SEQRES   1 A  295  MET PRO GLU GLY PRO GLU VAL ALA LEU THR ALA ASP ILE
SEQRES   2 A  295  LEU GLU LYS TYR PHE LYS GLY LYS THR LEU GLU TYR ILE
SEQRES   3 A  295  ASP PHE ILE SER GLY ARG TYR SER LYS SER GLU PRO GLU
SEQRES   4 A  295  GLY TYR ASP ASP PHE ILE ALA ASN LEU PRO LEU LYS VAL
SEQRES   5 A  295  SER ASN VAL ASP THR LYS GLY LYS PHE LEU TRP PHE GLU
SEQRES   6 A  295  LEU PHE ASP PRO ASN ASP LYS SER ASN LYS TRP TYR ILE
SEQRES   7 A  295  TRP ASN THR PHE GLY LEU THR GLY MET TRP SER LEU PHE
SEQRES   8 A  295  GLU ALA LYS TYR THR ARG ALA VAL LEU SER PHE ASP ASN
SEQRES   9 A  295  GLU LEU MET ALA TYR PHE SER ASP MET ARG ASN PHE GLY
SEQRES  10 A  295  THR PHE LYS PHE SER ASN SER GLU LYS GLU LEU LYS ARG
SEQRES  11 A  295  LYS LEU ASN GLU LEU GLY PRO ASP PHE LEU LYS ASN ASP
SEQRES  12 A  295  ASP ILE ASP ILE SER LYS ILE LYS LYS TYR LYS GLN PRO
SEQRES  13 A  295  ILE VAL ALA LEU LEU MET ASP GLN LYS LYS ILE GLY SER
SEQRES  14 A  295  GLY LEU GLY ASN TYR LEU VAL ALA GLU ILE LEU TYR ARG
SEQRES  15 A  295  ALA LYS ILE ASP PRO HIS LYS LEU GLY SER ASN LEU THR
SEQRES  16 A  295  ASP GLN GLU ILE GLU ASN LEU TRP TYR TRP ILE LYS TYR
SEQRES  17 A  295  GLU THR LYS LEU ALA TYR ASP SER ASN HIS ILE GLY TYR
SEQRES  18 A  295  MET VAL ASN LEU GLU ASN GLU SER SER LYS ILE GLY ARG
SEQRES  19 A  295  LYS ASN TYR HIS PRO ASN ILE HIS PRO THR GLU LYS GLU
SEQRES  20 A  295  PHE ASP PHE LEU VAL TYR ARG LYS LYS LYS ASP PRO ASN
SEQRES  21 A  295  GLY ASN LYS VAL ILE ALA ASP LYS ILE ILE GLY SER GLY
SEQRES  22 A  295  LYS ASN LYS ARG THR THR TYR TRP ALA PRO ALA ILE GLN
SEQRES  23 A  295  LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET    GOL  A 401       6
HET    GOL  A 402       6
HET    GOL  A 403       6
HET    SO4  A 504       5
HETNAM     GOL GLYCEROL
HETNAM     SO4 SULFATE ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  GOL    3(C3 H8 O3)
FORMUL   5  SO4    O4 S 2-
FORMUL   6  HOH   *82(H2 O)
HELIX    1   1 GLU A    3  LYS A   19  1                                  17
HELIX    2   2 GLY A   31  SER A   36  1                                   6
HELIX    3   3 GLY A   40  ALA A   46  1                                   7
HELIX    4   4 GLU A  125  ASN A  133  1                                   9
HELIX    5   5 ASP A  146  LYS A  151  5                                   6
HELIX    6   6 PRO A  156  ASP A  163  1                                   8
HELIX    7   7 GLY A  172  LYS A  184  1                                  13
HELIX    8   8 LEU A  190  LEU A  194  5                                   5
HELIX    9   9 THR A  195  SER A  216  1                                  22
HELIX   10  10 MET A  222  ASN A  224  5                                   3
HELIX   11  11 LEU A  225  SER A  230  1                                   6
SHEET    1   A 8 GLY A  86  SER A  89  0
SHEET    2   A 8 MET A 107  ASP A 112 -1  O  TYR A 109   N  SER A  89
SHEET    3   A 8 THR A  96  PHE A 102 -1  N  LEU A 100   O  ALA A 108
SHEET    4   A 8 THR A  22  PHE A  28 -1  N  TYR A  25   O  SER A 101
SHEET    5   A 8 LEU A  50  LYS A  58 -1  O  LEU A  50   N  LEU A  23
SHEET    6   A 8 PHE A  61  PHE A  67 -1  O  GLU A  65   N  SER A  53
SHEET    7   A 8 LYS A  75  THR A  81 -1  O  TRP A  76   N  LEU A  66
SHEET    8   A 8 THR A 118  SER A 122 -1  O  LYS A 120   N  TRP A  79
CISPEP   1 LEU A   48    PRO A   49          0         0.40
SITE     1 AC1  5 LYS A  16  TYR A  17  LYS A  94  TYR A  95
SITE     2 AC1  5 LYS A 231
SITE     1 AC2  3 SER A 124  GLU A 125  LYS A 126
SITE     1 AC3  3 ASN A 201  TYR A 204  TRP A 205
SITE     1 AC4  5 TRP A  79  LYS A 120  ARG A 130  LYS A 131
SITE     2 AC4  5 HOH A 341
CRYST1  123.241  123.241   44.849  90.00  90.00 120.00 P 65          6
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      0.008114  0.004685  0.000000        0.00000
SCALE2      0.000000  0.009369  0.000000        0.00000
SCALE3      0.000000  0.000000  0.022297        0.00000
      
PROCHECK
Go to PROCHECK summary
 References