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PDBsum entry 2f5n

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Top Page protein dna_rna ligands metals links
Hydrolase/DNA PDB id
2f5n
Jmol
Contents
Protein chain
252 a.a.
DNA/RNA
Ligands
GOL ×2
Metals
_ZN
Waters ×110
HEADER    HYDROLASE/DNA                           26-NOV-05   2F5N
TITLE     MUTM CROSSLINKED TO UNDAMAGED DNA SAMPLING A:T BASE PAIR IC1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3';
COMPND   3 CHAIN: B;
COMPND   4 EC: 3.2.2.23;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: 5'-D(*TP*GP*C*GP*TP*CP*CP*AP*GP*GP*TP*CP*TP*AP*CP*C)-3';
COMPND   8 CHAIN: C;
COMPND   9 ENGINEERED: YES;
COMPND  10 MOL_ID: 3;
COMPND  11 MOLECULE: FORMAMIDOPYRIMIDINE-DNA GLYCOSIDASE;
COMPND  12 CHAIN: A;
COMPND  13 ENGINEERED: YES;
COMPND  14 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: SYNTHETIC DNA;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES;
SOURCE   6 OTHER_DETAILS: SYNTHETIC DNA CONTAINING A BACKBONE MODIFICATION;
SOURCE   7 MOL_ID: 3;
SOURCE   8 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE   9 ORGANISM_TAXID: 1422;
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  12 EXPRESSION_SYSTEM_STRAIN: BL-21 PLYSS;
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS    DISULFIDE CROSSLINK, DNA GLYCOSYLASE, DNA REPAIR, DAMAGE SEARCH,
KEYWDS   2 HYDROLASE-DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BANERJEE,W.L.SANTOS,G.L.VERDINE
REVDAT   3   13-JUL-11 2F5N    1       VERSN
REVDAT   2   24-FEB-09 2F5N    1       VERSN
REVDAT   1   07-MAR-06 2F5N    0
JRNL        AUTH   A.BANERJEE,W.L.SANTOS,G.L.VERDINE
JRNL        TITL   STRUCTURE OF A DNA GLYCOSYLASE SEARCHING FOR LESIONS.
JRNL        REF    SCIENCE                       V. 311  1153 2006
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   16497933
JRNL        DOI    10.1126/SCIENCE.1120288
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) : 32.81
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 296740.440
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.4
REMARK   3   NUMBER OF REFLECTIONS             : 28841
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) : 0.201
REMARK   3   FREE R VALUE                     : 0.248
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1443
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2274
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520
REMARK   3   BIN FREE R VALUE                    : 0.3150
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 119
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1959
REMARK   3   NUCLEIC ACID ATOMS       : 548
REMARK   3   HETEROGEN ATOMS          : 13
REMARK   3   SOLVENT ATOMS            : 110
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.84000
REMARK   3    B22 (A**2) : 5.60000
REMARK   3    B33 (A**2) : -2.76000
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) : 0.18
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) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.025
REMARK   3   BOND ANGLES            (DEGREES) : 2.00
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.54
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) : 3.080 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.840 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.480 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.740 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 50.21
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_PAR.TXT
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_TOP.TXT
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2F5N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-05.
REMARK 100 THE RCSB ID CODE IS RCSB035480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-03
REMARK 200  TEMPERATURE           (KELVIN) : 200
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   : 29774
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : 0.09400
REMARK 200  R SYM                      (I) : 0.15200
REMARK 200   FOR THE DATA SET  : NULL
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     (%) : 90.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.48400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.780
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   (%): 54.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       22.68950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.59750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.47350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.59750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.68950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.47350
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: B, C, 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      DG B    15
REMARK 465      DC B    16
REMARK 465      DT C     0
REMARK 465      DG C     1
REMARK 465      DC C     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 465     GLN A   236
REMARK 465     HIS A   237
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      DG C   3    P    OP1  OP2
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  80    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A  91    CD   OE1  OE2
REMARK 470     VAL A 153    CG1  CG2
REMARK 470     LYS A 154    CD   CE   NZ
REMARK 470     LYS A 156    CG   CD   CE   NZ
REMARK 470     LYS A 198    CD   CE   NZ
REMARK 470     GLU A 205    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ALA A  45   CA    ALA A  45   CB      0.134
REMARK 500    MET A  47   CB    MET A  47   CG      0.207
REMARK 500    PHE A  64   CE1   PHE A  64   CZ      0.115
REMARK 500    CYS A 272   CB    CYS A 272   SG      0.133
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500     DA B   1   O5' -  C5' -  C4' ANGL. DEV. = -11.9 DEGREES
REMARK 500    ARG A  58   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
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    LEU A  66     -153.43   -108.35
REMARK 500    ARG A  76     -143.28     51.85
REMARK 500    ASP A 110      104.77   -160.08
REMARK 500    LYS A 154      -12.28    167.78
REMARK 500    VAL A 241      -39.87   -130.96
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     DA B   1         0.09    SIDE CHAIN
REMARK 500    TYR A 176         0.07    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 249   SG
REMARK 620 2 CYS A 252   SG  112.6
REMARK 620 3 CYS A 269   SG  116.8 103.1
REMARK 620 4 CYS A 272   SG  133.3  91.4  94.0
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 A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F5O   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5P   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5Q   RELATED DB: PDB
REMARK 900 RELATED ID: 2F5S   RELATED DB: PDB
DBREF  2F5N A    1   274  UNP    P84131   P84131_BACST     1    274
DBREF  2F5N B    1    16  PDB    2F5N     2F5N             1     16
DBREF  2F5N C    0    15  PDB    2F5N     2F5N             0     15
SEQADV 2F5N CYS A  166  UNP  P84131    GLN   166 ENGINEERED
SEQRES   1 B   16   DA  DG  DG  DT  DA  DG  DA  DC  DC  DT  DG  DG  DA
SEQRES   2 B   16   DC  DG  DC
SEQRES   1 C   16   DT  DG  DC  DG  DT  DC  DC  DA  DG  DG  DT  DC  DT
SEQRES   2 C   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
HET    GOL  A 301       6
HET    GOL  A 302       6
HETNAM      ZN ZINC ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   4   ZN    ZN 2+
FORMUL   5  GOL    2(C3 H8 O3)
FORMUL   7  HOH   *110(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 LYS A  122  ASP A  126  1                                   5
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  MET A  216  1                                  21
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  ALA A  70   O  TYR A 120
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  GLY A  54   O  LEU A  65
SHEET    1   C 2 GLU A 257  VAL A 261  0
SHEET    2   C 2 ARG A 264  TYR A 268 -1  O  TYR A 268   N  GLU A 257
LINK        ZN    ZN A 300                 SG  CYS A 249     1555   1555  2.34
LINK        ZN    ZN A 300                 SG  CYS A 252     1555   1555  2.30
LINK        ZN    ZN A 300                 SG  CYS A 269     1555   1555  2.34
LINK         SG  CYS A 272                ZN    ZN A 300     1555   1555  2.97
CISPEP   1 HIS A   36    PRO A   37          0        -1.03
CISPEP   2 PRO A  129    PRO A  130          0         0.04
SITE     1 AC1  4 CYS A 249  CYS A 252  CYS A 269  CYS A 272
SITE     1 AC2  5 ASP A  25  GLU A  41  ALA A  44  ALA A  45
SITE     2 AC2  5 ILE A  48
SITE     1 AC3  7 ARG A  53  GLY A  54  LEU A  55  GLU A  56
SITE     2 AC3  7 LEU A  65  HOH A 335  HOH A 397
CRYST1   45.379   92.947  105.195  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      0.022037  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010759  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009506        0.00000
      
PROCHECK
Go to PROCHECK summary
 References