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PDBsum entry 1r2z

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Top Page protein dna_rna metals links
Hydrolase/DNA PDB id
1r2z
Jmol
Contents
Protein chain
273 a.a. *
DNA/RNA
Metals
_ZN
Waters ×318
* Residue conservation analysis
HEADER    HYDROLASE/DNA                           30-SEP-03   1R2Z
TITLE     MUTM (FPG) BOUND TO 5,6-DIHYDROURACIL (DHU) CONTAINING DNA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-
COMPND   3 D(*AP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3';
COMPND   4 CHAIN: B;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: 5'-D(*TP*GP*CP*GP*TP*CP*CP*AP*(DHU)
COMPND   8 P*GP*TP*CP*TP*AP*CP*C)-3';
COMPND   9 CHAIN: C;
COMPND  10 ENGINEERED: YES;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: MUTM;
COMPND  13 CHAIN: A;
COMPND  14 SYNONYM: FPG;
COMPND  15 ENGINEERED: YES;
COMPND  16 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: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE   7 ORGANISM_TAXID: 1422;
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: PET24B
KEYWDS    DNA REPAIR, DNA GLYCOSYLASE, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.C.FROMME,G.L.VERDINE
REVDAT   4   24-FEB-09 1R2Z    1       VERSN
REVDAT   3   06-JAN-04 1R2Z    1       JRNL
REVDAT   2   21-OCT-03 1R2Z    1       MODRES
REVDAT   1   14-OCT-03 1R2Z    0
JRNL        AUTH   J.C.FROMME,G.L.VERDINE
JRNL        TITL   DNA LESION RECOGNITION BY THE BACTERIAL REPAIR
JRNL        TITL 2 ENZYME MUTM.
JRNL        REF    J.BIOL.CHEM.                  V. 278 51543 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   14525999
JRNL        DOI    10.1074/JBC.M307768200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.63 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) : 1.63
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 314184.800
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.9
REMARK   3   NUMBER OF REFLECTIONS             : 52398
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) : 0.208
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2656
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           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.63
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4149
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470
REMARK   3   BIN FREE R VALUE                    : 0.2490
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 239
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2106
REMARK   3   NUCLEIC ACID ATOMS       : 483
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 318
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.54000
REMARK   3    B22 (A**2) : -1.54000
REMARK   3    B33 (A**2) : -2.01000
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) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : 0.09
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) : 0.21
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.09
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88
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) : 1.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.770 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.470 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.370 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 49.73
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  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  5  : DHU.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   : DHU.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1R2Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-03.
REMARK 100 THE RCSB ID CODE IS RCSB020372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
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 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53944
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : 0.04800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.35700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1L1T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MAGNESIUM ACETATE, SODIUM
REMARK 280  CACODYLATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
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       22.29550
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.09000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.11300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.09000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.29550
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.11300
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     MET A     1
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     GLU A  88    CD   OE1  OE2
REMARK 470     GLU A 133    CG   CD   OE1  OE2
REMARK 470     GLU A 150    CG   CD   OE1  OE2
REMARK 470     LYS A 154    CD   CE   NZ
REMARK 470     LYS A 156    CD   CE   NZ
REMARK 470     SER A 197    OG
REMARK 470     LYS A 198    CD   CE   NZ
REMARK 470     GLU A 201    CG   CD   OE1  OE2
REMARK 470     GLU A 205    CD   OE1  OE2
REMARK 470     LYS A 217    CD   CE   NZ
REMARK 470     ARG A 223    CD   NE   CZ   NH1  NH2
REMARK 470     THR A 224    CB   OG1  CG2
REMARK 470     ARG A 251    CD   NE   CZ   NH1  NH2
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     -137.74   -104.75
REMARK 500    ARG A  76     -120.84     51.79
REMARK 500    ASP A 110       94.22   -161.14
REMARK 500    VAL A 153       36.67    -75.08
REMARK 500    LYS A 154       -9.65   -141.27
REMARK 500    ARG A 223      -68.06   -130.51
REMARK 500    THR A 224       -1.99   -149.68
REMARK 500    VAL A 241      -34.55   -135.22
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 320  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 252   SG
REMARK 620 2 CYS A 269   SG   98.0
REMARK 620 3 CYS A 272   SG  112.0 116.5
REMARK 620 4 CYS A 249   SG  109.9 111.0 109.1
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 320
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L1T   RELATED DB: PDB
REMARK 900 MUTM (FPG) BOUND TO ABASIC-SITE CONTAINING DNA
REMARK 900 RELATED ID: 1L1Z   RELATED DB: PDB
REMARK 900 MUTM (FPG) COVALENT-DNA INTERMEDIATE
REMARK 900 RELATED ID: 1L2B   RELATED DB: PDB
REMARK 900 MUTM (FPG) DNA END-PRODUCT STRUCTURE
REMARK 900 RELATED ID: 1L2C   RELATED DB: PDB
REMARK 900 MUTM (FPG)-DNA ESTRANGED THYMINE MISMATCH RECOGNITION
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1L2D   RELATED DB: PDB
REMARK 900 MUTM (FPG)-DNA ESTRANGED GUANINE MISMATCH RECOGNITION
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1R2Y   RELATED DB: PDB
REMARK 900 MUTM (FPG) BOUND TO 8-OXOGUANINE (OXOG) CONTAINING DNA
REMARK 999
REMARK 999 SEQUENCE THE SEQUENCE OF THIS PROTEIN IS NOT AVAILABLE IN ANY
REMARK 999 REFERENCE SEQUENCE DATABASE.
DBREF  1R2Z A    1   274  UNP    P84131   P84131_BACST     1    274
DBREF  1R2Z B    1    12  PDB    1R2Z     1R2Z             1     12
DBREF  1R2Z C   13    24  PDB    1R2Z     1R2Z            13     24
SEQRES   1 B   12   DG  DT  DA  DG  DA  DC  DC  DT  DG  DG  DA  DC
SEQRES   1 C   12   DG  DT  DC  DC  DA UMP  DG  DT  DC  DT  DA  DC
SEQRES   1 A  274  MET PRO GLN 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 GLN 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
MODRES 1R2Z UMP C   18    U  2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HET    UMP  C  18      19
HET     ZN  A 320       1
HETNAM     UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETNAM      ZN ZINC ION
HETSYN     UMP DUMP
FORMUL   2  UMP    C9 H13 N2 O8 P
FORMUL   4   ZN    ZN 2+
FORMUL   5  HOH   *318(H2 O)
HELIX    1   1 GLN 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  LYS A  217  1                                  22
HELIX   10  10 THR A  234  LEU A  239  5                                   6
SHEET    1   A 4 ILE A  23  ILE A  28  0
SHEET    2   A 4 THR A  94  PHE A 100 -1  O  VAL A  97   N  ARG A  27
SHEET    3   A 4 SER A 104  ARG A 109 -1  O  TYR A 108   N  VAL A  96
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  VAL A 119   N  HIS A  36
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         O3' UMP C  18                 P    DG C  19     1555   1555  1.58
LINK         P   UMP C  18                 O3'  DA C  17     1555   1555  1.59
LINK        ZN    ZN A 320                 SG  CYS A 252     1555   1555  2.33
LINK        ZN    ZN A 320                 SG  CYS A 269     1555   1555  2.37
LINK        ZN    ZN A 320                 SG  CYS A 272     1555   1555  2.33
LINK        ZN    ZN A 320                 SG  CYS A 249     1555   1555  2.37
CISPEP   1 HIS A   36    PRO A   37          0        -0.74
CISPEP   2 PRO A  129    PRO A  130          0         0.24
SITE     1 AC1  4 CYS A 249  CYS A 252  CYS A 269  CYS A 272
CRYST1   44.591   94.226  102.180  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      0.022426  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010613  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009787        0.00000
      
PROCHECK
Go to PROCHECK summary
 References