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PDBsum entry 1jr4

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Transferase PDB id
1jr4
Jmol
Contents
Protein chain
212 a.a. *
Ligands
CL4
Metals
_MG
Waters ×16
* Residue conservation analysis
HEADER    TRANSFERASE                             10-AUG-01   1JR4
TITLE     CATECHOL O-METHYLTRANSFERASE BISUBSTRATE-INHIBITOR COMPLEX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE, SOLUBLE FORM;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: S-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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TRANSFERASE, METHYLTRANSFERASE, NEUROTRANSMITTER
KEYWDS   2 DEGRADATION, BISUBSTRATE INHIBITOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.RUF,M.STIHLE
REVDAT   2   24-FEB-09 1JR4    1       VERSN
REVDAT   1   10-AUG-02 1JR4    0
JRNL        AUTH   C.LERNER,A.RUF,V.GRAMLICH,B.MASJOST,G.ZURCHER,
JRNL        AUTH 2 R.JAKOB-ROETNE,E.BORRONI,F.DIEDERICH
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF A BISUBSTRATE INHIBITOR
JRNL        TITL 2 BOUND TO THE ENZYME CATECHOL-O-METHYLTRANSFERASE:
JRNL        TITL 3 A DRAMATIC EFFECT OF INHIBITOR PREORGANIZATION ON
JRNL        TITL 4 BINDING AFFINITY.
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  40  4040 2001
JRNL        REFN                   ISSN 1433-7851
JRNL        PMID   12404486
JRNL        DOI    10.1002/1521-3773(20011105)40:21<4040::AID-ANIE4040
JRNL        DOI  2 >3.0.CO;2-C
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.MASJOST,P.BALLMER,E.BORRONI,G.ZUERCHER,
REMARK   1  AUTH 2 F.K.WINKLER,R.JAKOB-ROETNE,F.DIEDERICH
REMARK   1  TITL   STRUCTURE-BASED DESIGN, SYNTHESIS, AND IN VITRO
REMARK   1  TITL 2 EVALUATION OF BISUBSTRATE INHIBITORS FOR CATECHOL
REMARK   1  TITL 3 O-METHYLTRANSFERASE (COMT)
REMARK   1  REF    CHEMISTRY                     V.   6   971 2000
REMARK   1  REFN                   ISSN 0947-6539
REMARK   1  DOI    10.1002/(SICI)1521-3765(20000317)6:6<971::AID-CHEM9
REMARK   1  DOI  2 71>3.0.CO;2-0
REMARK   2
REMARK   2 RESOLUTION.    2.63 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNX 2000
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  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.21
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1108477.130
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 7809
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 + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.223
REMARK   3   FREE R VALUE                     : 0.280
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 759
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 7835
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) : 2.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.40
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 934
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300
REMARK   3   BIN FREE R VALUE                    : 0.4230
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 101
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1672
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 35
REMARK   3   SOLVENT ATOMS            : 16
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 5.46000
REMARK   3    B22 (A**2) : 5.46000
REMARK   3    B33 (A**2) : -10.92000
REMARK   3    B12 (A**2) : 6.84000
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) : 0.36
REMARK   3   ESD FROM SIGMAA              (A) : 0.43
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) : 0.48
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.56
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.68
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) : 2.140 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.400 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.140 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.480 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : CL45.PRX
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ION.TOP
REMARK   3  TOPOLOGY FILE  4   : CL45.TPX
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1JR4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-01.
REMARK 100 THE RCSB ID CODE IS RCSB014092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-00
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 5.5
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          : ENRAF-NONIUS FR571
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS
REMARK 200  OPTICS                         : OSMIC MIRRORS
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   : 22407
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
REMARK 200  DATA REDUNDANCY                : 2.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.03800
REMARK 200   FOR THE DATA SET  : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.23900
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: UNPUBLISHED COMT TERNARY COMPLEX (WINKLER, F.)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 100MM AMMONIUM
REMARK 280  SULFATE, 100 MM BIS-TRIS, PH 5.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 293K
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      111.80000
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       55.90000
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       55.90000
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      111.80000
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     PRO A   215
REMARK 465     SER A   216
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    PRO A  19      150.00    -46.30
REMARK 500    LYS A  36     -102.66   -141.29
REMARK 500    SER A  58       65.24     32.33
REMARK 500    TYR A  68     -115.08     55.94
REMARK 500    ASP A 131       73.50     55.57
REMARK 500    ASP A 133      -65.10   -109.21
REMARK 500    ASP A 141       17.10   -150.02
REMARK 500    HIS A 142     -153.12    -91.06
REMARK 500    SER A 196     -141.34   -140.23
REMARK 500    MET A 201      157.84    149.67
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                              MG A 300  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 169   OD2
REMARK 620 2 HOH A 302   O   123.3
REMARK 620 3 ASP A 141   OD1 103.0  64.5
REMARK 620 4 ASP A 141   OD2 106.8 104.3  50.8
REMARK 620 5 ASN A 170   OD1  78.2 146.9 140.7  90.7
REMARK 620 6 CL4 A 301   O28  94.0  76.0 140.1 153.7  77.8
REMARK 620 7 CL4 A 301   O29 151.4  80.7 101.6  78.2  73.5  75.9
REMARK 620 N                    1     2     3     4     5     6
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 CL4 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VID   RELATED DB: PDB
REMARK 900 1VID CONTAINS THE SAME PROTEIN WITHOUT LIGAND
DBREF  1JR4 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    CL4  A 301      34
HETNAM      MG MAGNESIUM ION
HETNAM     CL4 N-{3-[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-
HETNAM   2 CL4  FURAN-2-YL]-ALLYL}-2,3-DIHYDROXY-5-NITRO-BENZAMIDE
FORMUL   2   MG    MG 2+
FORMUL   3  CL4    C19 H19 N7 O8
FORMUL   4  HOH   *16(H2 O)
HELIX    1   1 THR A    4  ALA A   17  1                                  14
HELIX    2   2 ASP A   21  LYS A   36  1                                  16
HELIX    3   3 VAL A   42  SER A   58  1                                  17
HELIX    4   4 GLY A   70  ARG A   78  1                                   9
HELIX    5   5 ASN A   92  ALA A  106  1                                  15
HELIX    6   6 GLY A  107  ASP A  110  5                                   4
HELIX    7   7 ALA A  118  ILE A  123  1                                   6
HELIX    8   8 GLN A  125  ASP A  131  1                                   7
HELIX    9   9 TRP A  143  ASP A  145  5                                   3
HELIX   10  10 ARG A  146  CYS A  157  1                                  12
HELIX   11  11 THR A  176  SER A  186  1                                  11
SHEET    1   A 7 VAL A 112  ASN A 116  0
SHEET    2   A 7 ARG A  85  GLU A  90  1  N  LEU A  86   O  THR A 113
SHEET    3   A 7 LEU A  61  LEU A  65  1  N  GLU A  64   O  LEU A  87
SHEET    4   A 7 MET A 137  LEU A 140  1  O  PHE A 139   N  LEU A  63
SHEET    5   A 7 VAL A 165  ALA A 168  1  O  LEU A 167   N  VAL A 138
SHEET    6   A 7 VAL A 204  TYR A 212 -1  O  ALA A 210   N  LEU A 166
SHEET    7   A 7 PHE A 189  TYR A 197 -1  N  THR A 192   O  LYS A 209
LINK        MG    MG A 300                 OD2 ASP A 169     1555   1555  1.81
LINK        MG    MG A 300                 O   HOH A 302     1555   1555  2.12
LINK        MG    MG A 300                 OD1 ASP A 141     1555   1555  2.84
LINK        MG    MG A 300                 OD2 ASP A 141     1555   1555  1.86
LINK        MG    MG A 300                 OD1 ASN A 170     1555   1555  2.20
LINK        MG    MG A 300                 O28 CL4 A 301     1555   1555  1.96
LINK        MG    MG A 300                 O29 CL4 A 301     1555   1555  2.33
CISPEP   1 VAL A  173    PRO A  174          0        -0.07
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  CL4 A 301
SITE     2 AC1  5 HOH A 302
SITE     1 AC2 25 TRP A  38  MET A  40  GLY A  66  TYR A  68
SITE     2 AC2 25 MET A  89  GLU A  90  MET A  91  ASN A  92
SITE     3 AC2 25 TYR A  95  GLY A 117  ALA A 118  SER A 119
SITE     4 AC2 25 GLN A 120  ASP A 141  HIS A 142  TRP A 143
SITE     5 AC2 25 LYS A 144  ASP A 169  ASN A 170  PRO A 174
SITE     6 AC2 25 LEU A 198  GLU A 199   MG A 300  HOH A 302
SITE     7 AC2 25 HOH A 309
CRYST1   50.600   50.600  167.700  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      0.019776  0.011418  0.000000        0.00000
SCALE2      0.000000  0.022835  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005962        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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