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PDBsum entry 1vid

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Transferase (methyltransferase) PDB id
1vid
Jmol
Contents
Protein chain
213 a.a.
Ligands
SAM
DNC
Metals
_MG
Waters ×139
HEADER    TRANSFERASE (METHYLTRANSFERASE)         05-JAN-96   1VID
TITLE     CATECHOL O-METHYLTRANSFERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: COMT;
COMPND   5 EC: 2.1.1.6;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 TISSUE: LIVER;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TRANSFERASE, METHYLTRANSFERASE, NEUROTRANSMITTER
KEYWDS   2 DEGRADATION, TRANSFERASE (METHYLTRANSFERASE)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.VIDGREN,L.A.SVENSSON,A.LILJAS
REVDAT   2   24-FEB-09 1VID    1       VERSN
REVDAT   1   11-JUL-96 1VID    0
JRNL        AUTH   J.VIDGREN,L.A.SVENSSON,A.LILJAS
JRNL        TITL   CRYSTAL STRUCTURE OF CATECHOL O-METHYLTRANSFERASE.
JRNL        REF    NATURE                        V. 368   354 1994
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   8127373
JRNL        DOI    10.1038/368354A0
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.VIDGREN,C.TILGMANN,K.LUNDSTROM,A.LILJAS
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY
REMARK   1  TITL 2 INVESTIGATION OF A RECOMBINANT FORM OF RAT
REMARK   1  TITL 3 CATECHOL O-METHYLTRANSFERASE
REMARK   1  REF    PROTEINS                      V.  11   233 1991
REMARK   1  REFN                   ISSN 0887-3585
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
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)   (%) : 85.0
REMARK   3   NUMBER OF REFLECTIONS             : 15300
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
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 : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1679
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 41
REMARK   3   SOLVENT ATOMS            : 139
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 1.87
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.43
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21
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  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: NULL
REMARK   4
REMARK   4 1VID COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : AUG-93
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX9.5
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91
REMARK 200  MONOCHROMATOR                  : NULL
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          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16005
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.08300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+1/3
REMARK 290       6555   -X,-X+Y,-Z+2/3
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      112.33333
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       56.16667
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.16667
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      112.33333
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 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     2
REMARK 465     ASP A     3
REMARK 465     SER A   217
REMARK 465     PRO A   218
REMARK 465     ASP A   219
REMARK 465     LYS A   220
REMARK 465     SER A   221
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    MET A  40       42.72    -76.72
REMARK 500    TYR A  68     -104.71     61.58
REMARK 500    ASP A 133      -80.39    -93.25
REMARK 500    ASP A 141       38.83   -159.37
REMARK 500    HIS A 142     -155.67   -107.09
REMARK 500    SER A 196     -146.95   -153.01
REMARK 500    MET A 201      167.70    174.59
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 A 459        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH A 472        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH A 479        DISTANCE =  6.01 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                              MG A 300  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141   OD1
REMARK 620 2 ASP A 169   OD2  90.6
REMARK 620 3 ASN A 170   OD1  85.6  91.0
REMARK 620 4 DNC A 302   O1  157.3 110.9  86.9
REMARK 620 5 DNC A 302   O2   82.1 168.1  79.1  75.5
REMARK 620 6 HOH A 400   O    97.0  85.4 175.5  92.0 104.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 301
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNC A 302
DBREF  1VID A    1   221  UNP    P22734   COMT_RAT        44    264
SEQRES   1 A  221  MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES   2 A  221  GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES   3 A  221  GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES   4 A  221  MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES   5 A  221  VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES   6 A  221  GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES   7 A  221  LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU MET
SEQRES   8 A  221  ASN PRO ASP TYR ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES   9 A  221  PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES  10 A  221  ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES  11 A  221  ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES  12 A  221  LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES  13 A  221  CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES  14 A  221  ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES  15 A  221  VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES  16 A  221  SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES  17 A  221  LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
HET     MG  A 300       1
HET    SAM  A 301      27
HET    DNC  A 302      14
HETNAM      MG MAGNESIUM ION
HETNAM     SAM S-ADENOSYLMETHIONINE
HETNAM     DNC 3,5-DINITROCATECHOL
FORMUL   2   MG    MG 2+
FORMUL   3  SAM    C15 H22 N6 O5 S
FORMUL   4  DNC    C6 H4 N2 O6
FORMUL   5  HOH   *139(H2 O)
HELIX    1   1 LYS A    5  ASN A   16  1                                  12
HELIX    2   2 PRO A   22  GLN A   35  1                                  14
HELIX    3   3 GLY A   43  TYR A   57  1                                  15
HELIX    4   4 TYR A   71  LEU A   79  1                                   9
HELIX    5   5 PRO A   93  ALA A  106  1                                  14
HELIX    6   6 SER A  119  TYR A  130  1                                  12
HELIX    7   7 LYS A  144  LYS A  156  5                                  13
HELIX    8   8 PRO A  177  GLY A  185  1                                   9
SHEET    1   A 7 PHE A 189  TYR A 197  0
SHEET    2   A 7 VAL A 204  TYR A 212 -1  N  ILE A 211   O  GLU A 190
SHEET    3   A 7 VAL A 165  ALA A 168 -1  N  ALA A 168   O  GLU A 208
SHEET    4   A 7 MET A 137  LEU A 140  1  N  VAL A 138   O  VAL A 165
SHEET    5   A 7 LEU A  61  LEU A  65  1  N  LEU A  63   O  MET A 137
SHEET    6   A 7 ARG A  85  GLU A  90  1  N  ARG A  85   O  VAL A  62
SHEET    7   A 7 VAL A 112  ASN A 116  1  N  THR A 113   O  LEU A  86
LINK        MG    MG A 300                 OD1 ASP A 141     1555   1555  2.28
LINK        MG    MG A 300                 OD2 ASP A 169     1555   1555  2.30
LINK        MG    MG A 300                 OD1 ASN A 170     1555   1555  2.34
LINK        MG    MG A 300                 O1  DNC A 302     1555   1555  2.25
LINK        MG    MG A 300                 O2  DNC A 302     1555   1555  2.26
LINK        MG    MG A 300                 O   HOH A 400     1555   1555  2.41
CISPEP   1 VAL A  173    PRO A  174          0        -0.05
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  DNC A 302
SITE     2 AC1  5 HOH A 400
SITE     1 AC2 22 MET A  40  ASN A  41  VAL A  42  GLY A  66
SITE     2 AC2 22 ALA A  67  TYR A  68  TYR A  71  SER A  72
SITE     3 AC2 22 GLU A  90  MET A  91  TYR A  95  GLY A 117
SITE     4 AC2 22 ALA A 118  SER A 119  GLN A 120  ASP A 141
SITE     5 AC2 22 HIS A 142  TRP A 143  DNC A 302  HOH A 359
SITE     6 AC2 22 HOH A 384  HOH A 444
SITE     1 AC3  8 TRP A  38  ASP A 141  TRP A 143  LYS A 144
SITE     2 AC3  8 ASN A 170  GLU A 199   MG A 300  SAM A 301
CRYST1   51.300   51.300  168.500  90.00  90.00 120.00 P 32 2 1      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      0.019493  0.011254  0.000000        0.00000
SCALE2      0.000000  0.022509  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005935        0.00000
      
PROCHECK
Go to PROCHECK summary
 References