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PDBsum entry 3hvi

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Transferase PDB id
3hvi
Jmol
Contents
Protein chain
213 a.a.
Ligands
619
D1D
Metals
_MG
_NA
_CL
Waters ×329
HEADER    TRANSFERASE                             16-JUN-09   3HVI
TITLE     RAT CATECHOL O-METHYLTRANSFERASE IN COMPLEX WITH A CATECHOL-TYPE, N6-
TITLE    2 ETHYLADENINE-CONTAINING BISUBSTRATE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: SOLUBLE FORM, UNP RESIDUES 44-264;
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: RAT;
SOURCE   4 ORGANISM_TAXID: 10116;
SOURCE   5 TISSUE: LIVER;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDS56/RBSII
KEYWDS    METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, ALTERNATIVE
KEYWDS   2 INITIATION, CATECHOLAMINE METABOLISM, CELL MEMBRANE, MAGNESIUM,
KEYWDS   3 MEMBRANE, METAL-BINDING, PHOSPHOPROTEIN, S-ADENOSYL-L-METHIONINE,
KEYWDS   4 SIGNAL-ANCHOR, TRANSFERASE, TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.EHLER,D.SCHLATTER,M.STIHLE,J.BENZ,M.G.RUDOLPH
REVDAT   2   08-AUG-12 3HVI    1       JRNL   VERSN  TITLE
REVDAT   1   13-OCT-09 3HVI    0
JRNL        AUTH   M.ELLERMANN,R.JAKOB-ROETNE,C.LERNER,E.BORRONI,D.SCHLATTER,
JRNL        AUTH 2 D.ROTH,A.EHLER,M.G.RUDOLPH,F.DIEDERICH
JRNL        TITL   MOLECULAR RECOGNITION AT THE ACTIVE SITE OF
JRNL        TITL 2 CATECHOL-O-METHYLTRANSFERASE: ENERGETICALLY FAVORABLE
JRNL        TITL 3 REPLACEMENT OF A WATER MOLECULE IMPORTED BY A BISUBSTRATE
JRNL        TITL 4 INHIBITOR.
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  48  9092 2009
JRNL        REFN                   ISSN 1433-7851
JRNL        PMID   19882607
JRNL        DOI    10.1002/ANIE.200904410
REMARK   2
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
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) : 1.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.45
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.1
REMARK   3   NUMBER OF REFLECTIONS             : 62693
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) : 0.132
REMARK   3   R VALUE            (WORKING SET) : 0.131
REMARK   3   FREE R VALUE                     : 0.161
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3331
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) : 1.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3845
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.62
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740
REMARK   3   BIN FREE R VALUE SET COUNT          : 213
REMARK   3   BIN FREE R VALUE                    : 0.3110
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          : 51
REMARK   3   SOLVENT ATOMS            : 325
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 9.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.45
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.70000
REMARK   3    B22 (A**2) : 0.74000
REMARK   3    B33 (A**2) : -0.05000
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): 0.037
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.038
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.210
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1943 ; 0.017 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1326 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2672 ; 1.926 ; 2.014
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3277 ; 1.039 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   260 ; 5.386 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;38.352 ;24.713
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   355 ;10.590 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;22.095 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   299 ; 0.152 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2177 ; 0.011 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   380 ; 0.003 ; 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):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  1149 ; 1.804 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   460 ; 0.873 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1883 ; 2.568 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   794 ; 3.549 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   767 ; 4.940 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3269 ; 1.642 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   334 ;10.145 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3205 ; 4.430 ; 3.000
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3HVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053633.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SADABS
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68810
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06000
REMARK 200   FOR THE DATA SET  : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.58000
REMARK 200   FOR SHELL         : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COMO
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 0.1M BT PH 5.5, 0.1M
REMARK 280  AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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       24.92850
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.30850
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.35300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.30850
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.92850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.35300
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 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    44
REMARK 465     GLY A    45
REMARK 465     SER A   259
REMARK 465     SER A   260
REMARK 465     PRO A   261
REMARK 465     ASP A   262
REMARK 465     LYS A   263
REMARK 465     SER A   264
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NE2  GLN A    66     O    HOH A   304              2.15
REMARK 500   O    HOH A   518     O    HOH A   520              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   425     O    HOH A   459     3545     2.05
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    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 128   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 128   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG A 204   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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    MET A  83       49.91    -81.90
REMARK 500    SER A 101       58.93     36.23
REMARK 500    TYR A 111     -109.01     66.32
REMARK 500    ASP A 176      -80.18    -94.00
REMARK 500    ASP A 184       38.76   -155.80
REMARK 500    HIS A 185     -151.55   -110.58
REMARK 500    SER A 239     -144.69   -154.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    LEU A 158         12.46
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 295        DISTANCE =  6.38 ANGSTROMS
REMARK 525    HOH A 315        DISTANCE =  6.44 ANGSTROMS
REMARK 525    HOH A 316        DISTANCE =  6.46 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   1  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 184   OD1
REMARK 620 2 ASP A 212   OD2  90.2
REMARK 620 3 ASN A 213   OD1  93.7  82.4
REMARK 620 4 619 A 267   O34 166.3 103.5  87.7
REMARK 620 5 619 A 267   O32  88.6 166.2  84.0  78.0
REMARK 620 6 HOH A 445   O    90.4  91.0 172.2  90.0 102.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA A 265  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 226   O
REMARK 620 2 ARG A 227   O    81.2
REMARK 620 3 SER A 229   O    89.8 113.3
REMARK 620 4 PHE A 232   O    98.3 168.9  77.8
REMARK 620 5 HOH A 497   O   160.6  87.8  79.9  95.5
REMARK 620 6 HOH A 327   O   109.8  84.4 155.9  85.3  84.9
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 619 A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D1D A 268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HVH   RELATED DB: PDB
REMARK 900 RELATED ID: 3HVJ   RELATED DB: PDB
REMARK 900 RELATED ID: 3HVK   RELATED DB: PDB
DBREF  3HVI A   44   264  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   1       1
HET     NA  A 265       1
HET     CL  A 266       1
HET    619  A 267      40
HET    D1D  A 268       8
HETNAM      MG MAGNESIUM ION
HETNAM      NA SODIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     619 N-[(E)-3-[(2R,3S,4R,5R)-5-(6-ETHYLAMINOPURIN-9-YL)-3,4-
HETNAM   2 619  DIHYDROXY-OXOLAN-2-YL]PROP-2-ENYL]-5-(4-FLUOROPHENYL)-
HETNAM   3 619  2,3-DIHYDROXY-BENZAMIDE
HETNAM     D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL
FORMUL   2   MG    MG 2+
FORMUL   3   NA    NA 1+
FORMUL   4   CL    CL 1-
FORMUL   5  619    C27 H27 F N6 O6
FORMUL   6  D1D    C4 H8 O2 S2
FORMUL   7  HOH   *325(H2 O)
HELIX    1   1 THR A   47  ALA A   60  1                                  14
HELIX    2   2 ASP A   64  LYS A   79  1                                  16
HELIX    3   3 VAL A   85  SER A  101  1                                  17
HELIX    4   4 GLY A  113  ARG A  121  1                                   9
HELIX    5   5 ASN A  135  GLY A  150  1                                  16
HELIX    6   6 ALA A  161  ILE A  166  1                                   6
HELIX    7   7 GLN A  168  ASP A  174  1                                   7
HELIX    8   8 TRP A  186  ASP A  188  5                                   3
HELIX    9   9 ARG A  189  CYS A  200  1                                  12
HELIX   10  10 THR A  219  SER A  229  1                                  11
SHEET    1   A 7 VAL A 155  LEU A 158  0
SHEET    2   A 7 ARG A 128  MET A 132  1  N  THR A 131   O  LEU A 158
SHEET    3   A 7 LEU A 104  LEU A 108  1  N  VAL A 105   O  LEU A 130
SHEET    4   A 7 MET A 180  LEU A 183  1  O  PHE A 182   N  LEU A 108
SHEET    5   A 7 VAL A 208  ALA A 211  1  O  LEU A 210   N  VAL A 181
SHEET    6   A 7 VAL A 247  TYR A 255 -1  O  ALA A 253   N  LEU A 209
SHEET    7   A 7 PHE A 232  TYR A 240 -1  N  SER A 239   O  ASP A 248
LINK         OD1 ASP A 184                MG    MG A   1     1555   1555  2.08
LINK         OD2 ASP A 212                MG    MG A   1     1555   1555  2.07
LINK         OD1 ASN A 213                MG    MG A   1     1555   1555  2.15
LINK         O   VAL A 226                NA    NA A 265     1555   1555  2.56
LINK         O   ARG A 227                NA    NA A 265     1555   1555  2.80
LINK         O   SER A 229                NA    NA A 265     1555   1555  2.54
LINK         O   PHE A 232                NA    NA A 265     1555   1555  2.42
LINK        MG    MG A   1                 O34 619 A 267     1555   1555  2.07
LINK        MG    MG A   1                 O32 619 A 267     1555   1555  2.14
LINK        MG    MG A   1                 O   HOH A 445     1555   1555  2.05
LINK        NA    NA A 265                 O   HOH A 497     1555   1555  2.31
LINK        NA    NA A 265                 O   HOH A 327     1555   1555  2.73
CISPEP   1 VAL A  216    PRO A  217          0        -4.09
SITE     1 AC1  5 ASP A 184  ASP A 212  ASN A 213  619 A 267
SITE     2 AC1  5 HOH A 445
SITE     1 AC2  6 VAL A 226  ARG A 227  SER A 229  PHE A 232
SITE     2 AC2  6 HOH A 327  HOH A 497
SITE     1 AC3  3 ASP A  87  ALA A  88  TYR A 243
SITE     1 AC4 30  MG A   1  HOH A  42  MET A  83  GLY A 109
SITE     2 AC4 30 TYR A 111  GLU A 133  MET A 134  ASN A 135
SITE     3 AC4 30 TYR A 138  ALA A 140  GLN A 143  GLN A 144
SITE     4 AC4 30 GLY A 160  ALA A 161  SER A 162  GLN A 163
SITE     5 AC4 30 ASP A 184  HIS A 185  TRP A 186  LYS A 187
SITE     6 AC4 30 ARG A 189  ASP A 212  ASN A 213  PRO A 217
SITE     7 AC4 30 GLU A 242  D1D A 268  HOH A 367  HOH A 371
SITE     8 AC4 30 HOH A 443  HOH A 445
SITE     1 AC5  8 TRP A  81  ALA A 140  GLN A 143  ILE A 157
SITE     2 AC5  8 ASN A 159  MET A 244  619 A 267  HOH A 447
CRYST1   49.857   54.706   80.617  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      0.020057  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018280  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012404        0.00000
      
PROCHECK
Go to PROCHECK summary
 References