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PDBsum entry 2f5p

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Top Page protein dna_rna metals links
Hydrolase/DNA PDB id
2f5p
Jmol
Contents
Protein chain
254 a.a.
DNA/RNA
Metals
_ZN
Waters ×166
HEADER    HYDROLASE/DNA                           26-NOV-05   2F5P
TITLE     MUTM CROSSLINKED TO UNDAMAGED DNA SAMPLING A:T BASE PAIR IC2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-
COMPND   3 D(*AP*GP*GP*TP*AP*GP*AP*CP*TP*TP*GP*GP*AP*CP*GP*C)-3';
COMPND   4 CHAIN: C;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: 5'-
COMPND   8 D(*TP*GP*CP*G*TP*CP*CP*AP*AP*GP*TP*CP*TP*AP*CP*C)-3';
COMPND   9 CHAIN: D;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSIDASE;
COMPND  13 CHAIN: A;
COMPND  14 SYNONYM: MUTM;
COMPND  15 EC: 3.2.2.23;
COMPND  16 ENGINEERED: YES;
COMPND  17 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 SYNTHETIC: YES;
SOURCE   5 OTHER_DETAILS: SYNTHETIC DNA;
SOURCE   6 MOL_ID: 3;
SOURCE   7 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE   8 ORGANISM_TAXID: 1422;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL-21 PLYSS;
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS    DISULFIDE CROSSLINK, DNA GLYCOSYLASE, DNA REPAIR, DAMAGE
KEYWDS   2 SEARCH, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BANERJEE,W.L.SANTOS,G.L.VERDINE
REVDAT   2   24-FEB-09 2F5P    1       VERSN
REVDAT   1   07-MAR-06 2F5P    0
JRNL        AUTH   A.BANERJEE,W.L.SANTOS,G.L.VERDINE
JRNL        TITL   STRUCTURE OF A DNA GLYCOSYLASE SEARCHING FOR
JRNL        TITL 2 LESIONS.
JRNL        REF    SCIENCE                       V. 311  1153 2006
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   16497933
JRNL        DOI    10.1126/SCIENCE.1120288
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.72
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 324043.430
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 28890
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) : 0.205
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500
REMARK   3   FREE R VALUE TEST SET COUNT      : 2176
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4071
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320
REMARK   3   BIN FREE R VALUE                    : 0.2760
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 344
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2009
REMARK   3   NUCLEIC ACID ATOMS       : 507
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 166
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 15.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.46000
REMARK   3    B22 (A**2) : -2.09000
REMARK   3    B33 (A**2) : -0.37000
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) : 0.23
REMARK   3   ESD FROM SIGMAA              (A) : 0.13
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) : 0.27
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.890 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.620 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.870 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.050 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 43.98
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  : 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   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2F5P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-06.
REMARK 100 THE RCSB ID CODE IS RCSB035482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-04
REMARK 200  TEMPERATURE           (KELVIN) : 77
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X25
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30052
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : 0.11700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.40300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1R2Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, PH
REMARK 280  7.0, TEMPERATURE 350K, TEMPERATURE 277K
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       22.68600
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.06250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.99100
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.06250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.68600
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.99100
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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      DC C    15
REMARK 465      DG C    16
REMARK 465      DC C    17
REMARK 465      DT D    -1
REMARK 465      DG D     0
REMARK 465      DC D     1
REMARK 465      DG D     2
REMARK 465     MET A     1
REMARK 465     LYS A   217
REMARK 465     GLY A   218
REMARK 465     GLY A   219
REMARK 465     SER A   220
REMARK 465     THR A   221
REMARK 465     VAL A   222
REMARK 465     ARG A   223
REMARK 465     THR A   224
REMARK 465     TYR A   225
REMARK 465     VAL A   226
REMARK 465     ASN A   227
REMARK 465     THR A   228
REMARK 465     GLN A   229
REMARK 465     GLY A   230
REMARK 465     GLU A   231
REMARK 465     ALA A   232
REMARK 465     GLY A   233
REMARK 465     THR A   234
REMARK 465     PHE A   235
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      DT D   3    P    OP1  OP2
REMARK 470     VAL A 153    CG1  CG2
REMARK 470     GLN A 236    CG   CD   OE1  NE2
REMARK 470     HIS A 237    CG   ND1  CD2  CE1  NE2
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    LEU A  66     -151.76   -105.51
REMARK 500    ARG A  76     -134.66     56.90
REMARK 500    ASP A 110      110.76   -166.02
REMARK 500    GLU A 133       -6.60     77.63
REMARK 500    LYS A 154       -8.51    179.74
REMARK 500    HIS A 237      129.90     64.52
REMARK 500    VAL A 241      -40.04   -130.62
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 272   SG
REMARK 620 2 CYS A 249   SG  111.9
REMARK 620 3 CYS A 252   SG  110.0 108.3
REMARK 620 4 CYS A 269   SG  119.2 109.4  96.6
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R2Y   RELATED DB: PDB
REMARK 900 RELATED ID: 1L1T   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5N   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5O   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5Q   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5S   RELATED DB: PDB
DBREF  2F5P A    1   274  UNP    P84131   P84131_BACST     1    274
DBREF  2F5P C    2    17  PDB    2F5P     2F5P             2     17
DBREF  2F5P D   -1    14  PDB    2F5P     2F5P            -1     14
SEQADV 2F5P CYS A  166  UNP  P84131    GLN   166 ENGINEERED
SEQRES   1 C   16   DA  DG  DG  DT  DA  DG  DA  DC  DT  DT  DG  DG  DA
SEQRES   2 C   16   DC  DG  DC
SEQRES   1 D   16   DT  DG  DC  DG  DT  DC  DC  DA  DA  DG  DT  DC  DT
SEQRES   2 D   16   DA  DC  DC
SEQRES   1 A  274  MET PRO GLU LEU PRO GLU VAL GLU THR ILE ARG ARG THR
SEQRES   2 A  274  LEU LEU PRO LEU ILE VAL GLY LYS THR ILE GLU ASP VAL
SEQRES   3 A  274  ARG ILE PHE TRP PRO ASN ILE ILE ARG HIS PRO ARG ASP
SEQRES   4 A  274  SER GLU ALA PHE ALA ALA ARG MET ILE GLY GLN THR VAL
SEQRES   5 A  274  ARG GLY LEU GLU ARG ARG GLY LYS PHE LEU LYS PHE LEU
SEQRES   6 A  274  LEU ASP ARG ASP ALA LEU ILE SER HIS LEU ARG MET GLU
SEQRES   7 A  274  GLY ARG TYR ALA VAL ALA SER ALA LEU GLU PRO LEU GLU
SEQRES   8 A  274  PRO HIS THR HIS VAL VAL PHE CYS PHE THR ASP GLY SER
SEQRES   9 A  274  GLU LEU ARG TYR ARG ASP VAL ARG LYS PHE GLY THR MET
SEQRES  10 A  274  HIS VAL TYR ALA LYS GLU GLU ALA ASP ARG ARG PRO PRO
SEQRES  11 A  274  LEU ALA GLU LEU GLY PRO GLU PRO LEU SER PRO ALA PHE
SEQRES  12 A  274  SER PRO ALA VAL LEU ALA GLU ARG ALA VAL LYS THR LYS
SEQRES  13 A  274  ARG SER VAL LYS ALA LEU LEU LEU ASP CYS THR VAL VAL
SEQRES  14 A  274  ALA GLY PHE GLY ASN ILE TYR VAL ASP GLU SER LEU PHE
SEQRES  15 A  274  ARG ALA GLY ILE LEU PRO GLY ARG PRO ALA ALA SER LEU
SEQRES  16 A  274  SER SER LYS GLU ILE GLU ARG LEU HIS GLU GLU MET VAL
SEQRES  17 A  274  ALA THR ILE GLY GLU ALA VAL MET LYS GLY GLY SER THR
SEQRES  18 A  274  VAL ARG THR TYR VAL ASN THR GLN GLY GLU ALA GLY THR
SEQRES  19 A  274  PHE GLN HIS HIS LEU TYR VAL TYR GLY ARG GLN GLY ASN
SEQRES  20 A  274  PRO CYS LYS ARG CYS GLY THR PRO ILE GLU LYS THR VAL
SEQRES  21 A  274  VAL ALA GLY ARG GLY THR HIS TYR CYS PRO ARG CYS GLN
SEQRES  22 A  274  ARG
HET     ZN  A 300       1
HETNAM      ZN ZINC ION
FORMUL   4   ZN    ZN 2+
FORMUL   5  HOH   *166(H2 O)
HELIX    1   1 GLU A    3  VAL A   19  1                                  17
HELIX    2   2 TRP A   30  ASN A   32  5                                   3
HELIX    3   3 ASP A   39  ILE A   48  1                                  10
HELIX    4   4 GLU A  123  ARG A  128  5                                   6
HELIX    5   5 SER A  144  VAL A  153  1                                  10
HELIX    6   6 SER A  158  ASP A  165  1                                   8
HELIX    7   7 GLY A  173  GLY A  185  1                                  13
HELIX    8   8 PRO A  191  LEU A  195  5                                   5
HELIX    9   9 SER A  196  VAL A  215  1                                  20
SHEET    1   A 4 ILE A  23  ILE A  28  0
SHEET    2   A 4 THR A  94  PHE A 100 -1  O  CYS A  99   N  GLU A  24
SHEET    3   A 4 SER A 104  ARG A 109 -1  O  LEU A 106   N  PHE A  98
SHEET    4   A 4 ARG A  80  SER A  85 -1  N  ALA A  82   O  ARG A 107
SHEET    1   B 5 ILE A  34  HIS A  36  0
SHEET    2   B 5 THR A 116  ALA A 121  1  O  MET A 117   N  ARG A  35
SHEET    3   B 5 ASP A  69  HIS A  74 -1  N  ILE A  72   O  HIS A 118
SHEET    4   B 5 PHE A  61  LEU A  65 -1  N  PHE A  64   O  LEU A  71
SHEET    5   B 5 GLY A  54  ARG A  58 -1  N  GLU A  56   O  LYS A  63
SHEET    1   C 2 GLU A 257  VAL A 261  0
SHEET    2   C 2 ARG A 264  TYR A 268 -1  O  THR A 266   N  THR A 259
LINK        ZN    ZN A 300                 SG  CYS A 272     1555   1555  2.29
LINK        ZN    ZN A 300                 SG  CYS A 249     1555   1555  2.34
LINK        ZN    ZN A 300                 SG  CYS A 252     1555   1555  2.40
LINK        ZN    ZN A 300                 SG  CYS A 269     1555   1555  2.31
CISPEP   1 HIS A   36    PRO A   37          0        -0.51
CISPEP   2 PRO A  129    PRO A  130          0         0.01
SITE     1 AC1  4 CYS A 249  CYS A 252  CYS A 269  CYS A 272
CRYST1   45.372   91.982  106.125  90.00  90.00  90.00 P 21 21 21    4
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      0.022040  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010872  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009423        0.00000
      
PROCHECK
Go to PROCHECK summary
 References