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PDBsum entry 3bwm

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Transferase PDB id
3bwm
Jmol
Contents
Protein chain
214 a.a.
Ligands
SAM
DNC
Metals
_MG
__K
Waters ×110
HEADER    TRANSFERASE                             09-JAN-08   3BWM
TITLE     CRYSTAL STRUCTURE OF HUMAN CATECHOL O-METHYLTRANSFERASE
TITLE    2 WITH BOUND SAM AND DNC
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 2.1.1.6;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 GENE: COMT;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B(+)
KEYWDS    COMT, ROSSMANN FOLD, SAM, DNC, ALTERNATIVE INITIATION,
KEYWDS   2 CATECHOLAMINE METABOLISM, CYTOPLASM, MAGNESIUM, MEMBRANE,
KEYWDS   3 METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION,
KEYWDS   4 POLYMORPHISM, S-ADENOSYL-L-METHIONINE, TRANSFERASE,
KEYWDS   5 TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.RUTHERFORD,I.LE TRONG,R.E.STENKAMP,W.W.PARSON
REVDAT   3   24-FEB-09 3BWM    1       VERSN
REVDAT   2   24-JUN-08 3BWM    1       JRNL
REVDAT   1   03-JUN-08 3BWM    0
JRNL        AUTH   K.RUTHERFORD,I.LE TRONG,R.E.STENKAMP,W.W.PARSON
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN 108V AND 108M CATECHOL
JRNL        TITL 2 O-METHYLTRANSFERASE.
JRNL        REF    J.MOL.BIOL.                   V. 380   120 2008
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   18486144
JRNL        DOI    10.1016/J.JMB.2008.04.040
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0066
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.31
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.3
REMARK   3   NUMBER OF REFLECTIONS             : 10559
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) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.225
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 549
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.98
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 32
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 3.35
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130
REMARK   3   BIN FREE R VALUE SET COUNT          : 2
REMARK   3   BIN FREE R VALUE                    : 0.2260
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1695
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 43
REMARK   3   SOLVENT ATOMS            : 110
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.98
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.60000
REMARK   3    B22 (A**2) : 1.17000
REMARK   3    B33 (A**2) : 0.44000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.292
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.206
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.288
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1769 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1172 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2402 ; 1.269 ; 2.002
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2890 ; 0.912 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   213 ; 5.152 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    80 ;36.825 ;25.125
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   312 ;13.331 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;15.114 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   274 ; 0.067 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1933 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   321 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    65 ; 0.128 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.075 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    32 ; 0.257 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.151 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1071 ; 0.581 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   434 ; 0.103 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1735 ; 1.119 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   698 ; 1.626 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   667 ; 2.716 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 3BWM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB046047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-06
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 10.5
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          : RIGAKU MICROMAX-007
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11145
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970
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     (%) : 76.8
REMARK 200  DATA REDUNDANCY                : 5.400
REMARK 200  R MERGE                    (I) : 0.08000
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) : 1.97
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04
REMARK 200  COMPLETENESS FOR SHELL     (%) : 3.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.44800
REMARK 200  R SYM FOR SHELL            (I) : 2.30000
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1H1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, NACL, MGCL2, DTT, CAPS, NA, K
REMARK 280  PO4, LISO4, SAM, DNC, PH 10.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
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       21.64200
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.02300
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.32400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.02300
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.64200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.32400
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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       36.41    -87.26
REMARK 500    TYR A  68     -108.47     53.38
REMARK 500    ASP A 133      -69.57    -97.18
REMARK 500    ASP A 141       41.62   -155.00
REMARK 500    HIS A 142     -156.49   -109.52
REMARK 500    SER A 196     -143.13   -157.92
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 504        DISTANCE =  5.93 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  92.6
REMARK 620 3 ASN A 170   OD1  85.9  85.2
REMARK 620 4 HOH A 411   O    97.3  93.4 176.5
REMARK 620 5 DNC A 302   O1  165.0  97.3  83.7  93.4
REMARK 620 6 DNC A 302   O2   85.6 161.0  75.8 105.7  81.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A 303   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 184   O
REMARK 620 2 SER A 186   O   107.8
REMARK 620 3 PHE A 189   O   158.7  83.9
REMARK 620 4 HOH A 425   O    93.2 158.7  75.1
REMARK 620 5 HOH A 426   O    79.9  70.6 121.2 117.7
REMARK 620 N                    1     2     3     4
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 K A 303
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 301
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNC A 302
DBREF  3BWM A    2   215  UNP    P21964   COMT_HUMAN      52    265
SEQRES   1 A  214  GLY ASP THR LYS GLU GLN ARG ILE LEU ASN HIS VAL LEU
SEQRES   2 A  214  GLN HIS ALA GLU PRO GLY ASN ALA GLN SER VAL LEU GLU
SEQRES   3 A  214  ALA ILE ASP THR TYR CYS GLU GLN LYS GLU TRP ALA MET
SEQRES   4 A  214  ASN VAL GLY ASP LYS LYS GLY LYS ILE VAL ASP ALA VAL
SEQRES   5 A  214  ILE GLN GLU HIS GLN PRO SER VAL LEU LEU GLU LEU GLY
SEQRES   6 A  214  ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG LEU
SEQRES   7 A  214  LEU SER PRO GLY ALA ARG LEU ILE THR ILE GLU ILE ASN
SEQRES   8 A  214  PRO ASP CYS ALA ALA ILE THR GLN ARG MET VAL ASP PHE
SEQRES   9 A  214  ALA GLY VAL LYS ASP LYS VAL THR LEU VAL VAL GLY ALA
SEQRES  10 A  214  SER GLN ASP ILE ILE PRO GLN LEU LYS LYS LYS TYR ASP
SEQRES  11 A  214  VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP LYS
SEQRES  12 A  214  ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU GLU CYS
SEQRES  13 A  214  GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP ASN
SEQRES  14 A  214  VAL ILE CYS PRO GLY ALA PRO ASP PHE LEU ALA HIS VAL
SEQRES  15 A  214  ARG GLY SER SER CYS PHE GLU CYS THR HIS TYR GLN SER
SEQRES  16 A  214  PHE LEU GLU TYR ARG GLU VAL VAL ASP GLY LEU GLU LYS
SEQRES  17 A  214  ALA ILE TYR LYS GLY PRO
HET     MG  A 300       1
HET      K  A 303       1
HET    SAM  A 301      27
HET    DNC  A 302      14
HETNAM      MG MAGNESIUM ION
HETNAM       K POTASSIUM ION
HETNAM     SAM S-ADENOSYLMETHIONINE
HETNAM     DNC 3,5-DINITROCATECHOL
FORMUL   2   MG    MG 2+
FORMUL   3    K    K 1+
FORMUL   4  SAM    C15 H22 N6 O5 S
FORMUL   5  DNC    C6 H4 N2 O6
FORMUL   6  HOH   *110(H2 O)
HELIX    1   1 THR A    4  ALA A   17  1                                  14
HELIX    2   2 ASN A   21  LYS A   36  1                                  16
HELIX    3   3 VAL A   42  GLN A   58  1                                  17
HELIX    4   4 GLY A   70  ARG A   78  1                                   9
HELIX    5   5 ASN A   92  GLY A  107  1                                  16
HELIX    6   6 VAL A  108  ASP A  110  5                                   3
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 ALA A  176  SER A  186  1                                  11
SHEET    1   A 7 VAL A 112  VAL A 116  0
SHEET    2   A 7 ARG A  85  GLU A  90  1  N  THR A  88   O  VAL A 115
SHEET    3   A 7 VAL A  61  LEU A  65  1  N  LEU A  62   O  ILE 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  LEU A 140
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  PHE A 197 -1  N  SER A 196   O  ASP A 205
LINK         OD1 ASP A 141                MG    MG A 300     1555   1555  2.13
LINK         OD2 ASP A 169                MG    MG A 300     1555   1555  2.35
LINK         OD1 ASN A 170                MG    MG A 300     1555   1555  2.24
LINK         O   ARG A 184                 K     K A 303     1555   1555  2.91
LINK         O   SER A 186                 K     K A 303     1555   1555  2.48
LINK         O   PHE A 189                 K     K A 303     1555   1555  2.62
LINK        MG    MG A 300                 O   HOH A 411     1555   1555  2.05
LINK        MG    MG A 300                 O1  DNC A 302     1555   1555  2.13
LINK        MG    MG A 300                 O2  DNC A 302     1555   1555  2.21
LINK         K     K A 303                 O   HOH A 425     1555   1555  2.76
LINK         K     K A 303                 O   HOH A 426     1555   1555  2.92
CISPEP   1 CYS A  173    PRO A  174          0        -0.67
SITE     1 AC1  4 ASP A 141  ASP A 169  ASN A 170  HOH A 411
SITE     1 AC2  5 ARG A 184  SER A 186  PHE A 189  HOH A 425
SITE     2 AC2  5 HOH A 426
SITE     1 AC3 19 MET A  40  ASN A  41  GLY A  66  ALA A  67
SITE     2 AC3 19 TYR A  68  TYR A  71  SER A  72  GLU A  90
SITE     3 AC3 19 ILE A  91  GLY A 117  ALA A 118  SER A 119
SITE     4 AC3 19 GLN A 120  ASP A 141  HIS A 142  TRP A 143
SITE     5 AC3 19 HOH A 402  HOH A 441  HOH A 458
SITE     1 AC4 10 TRP A  38  ASP A 141  HIS A 142  TRP A 143
SITE     2 AC4 10 LYS A 144  ASP A 169  ASN A 170  LEU A 198
SITE     3 AC4 10 GLU A 199  HOH A 411
CRYST1   43.284   66.648   68.046  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      0.023103  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015004  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014696        0.00000
      
PROCHECK
Go to PROCHECK summary
 References