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PDBsum entry 3hvj

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3hvj
Jmol
Contents
Protein chains
213 a.a.
Ligands
705 ×2
BTB
Metals
_MG ×2
_CL
Waters ×406
HEADER    TRANSFERASE                             16-JUN-09   3HVJ
TITLE     RAT CATECHOL O-METHYLTRANSFERASE IN COMPLEX WITH A CATECHOL-TYPE, N6-
TITLE    2 PROPYLADENINE-CONTAINING BISUBSTRATE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND   3 CHAIN: A, B;
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 3HVJ    1       JRNL   VERSN  TITLE
REVDAT   1   13-OCT-09 3HVJ    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.    1.79 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) : 1.79
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.04
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1
REMARK   3   NUMBER OF REFLECTIONS             : 39165
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) : 0.186
REMARK   3   R VALUE            (WORKING SET) : 0.183
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2078
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) : 1.79
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2284
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.23
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840
REMARK   3   BIN FREE R VALUE SET COUNT          : 94
REMARK   3   BIN FREE R VALUE                    : 0.3520
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3362
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 99
REMARK   3   SOLVENT ATOMS            : 406
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.33
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.41000
REMARK   3    B22 (A**2) : -1.08000
REMARK   3    B33 (A**2) : 0.66000
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): 0.139
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.108
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3582 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2365 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4871 ; 1.530 ; 2.015
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5810 ; 0.959 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   441 ; 5.353 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;38.626 ;24.870
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   626 ;14.221 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;22.135 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   541 ; 0.098 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3927 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   662 ; 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):  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):  2151 ; 0.886 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   869 ; 0.246 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3474 ; 1.540 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1431 ; 2.520 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1389 ; 3.873 ; 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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3HVJ 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 RCSB053634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-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) : 1.0075
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   : 42379
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.040
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10900
REMARK 200   FOR THE DATA SET  : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.52900
REMARK 200   FOR SHELL         : 2.000
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   (%): 45.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
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       27.67300
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.25000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.70700
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.25000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.67300
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.70700
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 465     MET B    44
REMARK 465     SER B   259
REMARK 465     SER B   260
REMARK 465     PRO B   261
REMARK 465     ASP B   262
REMARK 465     LYS B   263
REMARK 465     SER B   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   O    HOH B   286     O    HOH B   317              2.14
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    19     O    HOH B   338     1565     2.19
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    ARG A 118   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 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    LYS A  79     -114.56   -137.40
REMARK 500    TYR A 111     -114.60     58.61
REMARK 500    ASP A 176      -76.17    -92.73
REMARK 500    ASP A 184       28.47   -157.17
REMARK 500    HIS A 185     -149.63   -100.76
REMARK 500    SER A 239     -141.71   -150.51
REMARK 500    MET B  83       47.89    -77.79
REMARK 500    SER B 101       66.23     26.00
REMARK 500    TYR B 111     -113.86     51.08
REMARK 500    ASP B 176      -75.81    -92.64
REMARK 500    ASP B 184       37.89   -147.84
REMARK 500    HIS B 185     -151.74   -110.24
REMARK 500    SER B 239     -143.11   -154.24
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 265  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 184   OD1
REMARK 620 2 ASP A 212   OD2  89.0
REMARK 620 3 ASN A 213   OD1  90.5  80.9
REMARK 620 4 705 A   1   O34 170.1 100.6  89.1
REMARK 620 5 705 A   1   O32  90.2 168.3  87.4  79.9
REMARK 620 6 HOH A 401   O    92.7  92.9 173.0  88.9  98.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 265  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 184   OD1
REMARK 620 2 ASP B 212   OD2  93.4
REMARK 620 3 ASN B 213   OD1  90.5  81.8
REMARK 620 4 705 B   2   O34 165.8 100.7  90.2
REMARK 620 5 705 B   2   O32  89.7 167.4  86.0  76.2
REMARK 620 6 HOH B 433   O    95.8  95.8 173.4  84.3  96.1
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 705 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 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 BTB A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 705 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HVH   RELATED DB: PDB
REMARK 900 RELATED ID: 3HVI   RELATED DB: PDB
REMARK 900 RELATED ID: 3HVK   RELATED DB: PDB
DBREF  3HVJ A   44   264  UNP    P22734   COMT_RAT        44    264
DBREF  3HVJ B   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
SEQRES   1 B  221  MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES   2 B  221  GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES   3 B  221  GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES   4 B  221  MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES   5 B  221  VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES   6 B  221  GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES   7 B  221  LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU MET
SEQRES   8 B  221  ASN PRO ASP TYR ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES   9 B  221  PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES  10 B  221  ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES  11 B  221  ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES  12 B  221  LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES  13 B  221  CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES  14 B  221  ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES  15 B  221  VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES  16 B  221  SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES  17 B  221  LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
HET    705  A   1      41
HET     MG  A 265       1
HET     CL  A 266       1
HET    BTB  A 267      14
HET    705  B   2      41
HET     MG  B 265       1
HETNAM     705 N-[(E)-3-[(2R,3S,4R,5R)-3,4-DIHYDROXY-5-(6-
HETNAM   2 705  PROPYLAMINOPURIN-9-YL)OXOLAN-2-YL]PROP-2-ENYL]-5-(4-
HETNAM   3 705  FLUOROPHENYL)-2,3-DIHYDROXY-BENZAMIDE
HETNAM      MG MAGNESIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM   2 BTB  PROPANE-1,3-DIOL
HETSYN     BTB BIS-TRIS BUFFER
FORMUL   3  705    2(C28 H29 F N6 O6)
FORMUL   4   MG    2(MG 2+)
FORMUL   5   CL    CL 1-
FORMUL   6  BTB    C8 H19 N O5
FORMUL   9  HOH   *406(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
HELIX   11  11 THR B   47  ALA B   60  1                                  14
HELIX   12  12 ASP B   64  LYS B   79  1                                  16
HELIX   13  13 VAL B   85  SER B  101  1                                  17
HELIX   14  14 GLY B  113  ARG B  121  1                                   9
HELIX   15  15 ASN B  135  GLY B  150  1                                  16
HELIX   16  16 ALA B  161  ILE B  166  1                                   6
HELIX   17  17 GLN B  168  ASP B  174  1                                   7
HELIX   18  18 TRP B  186  ASP B  188  5                                   3
HELIX   19  19 ARG B  189  CYS B  200  1                                  12
HELIX   20  20 THR B  219  SER B  229  1                                  11
SHEET    1   A 7 VAL A 155  ASN A 159  0
SHEET    2   A 7 ARG A 128  GLU A 133  1  N  THR A 131   O  LEU A 158
SHEET    3   A 7 LEU A 104  LEU A 108  1  N  GLU A 107   O  LEU A 130
SHEET    4   A 7 LEU A 178  LEU A 183  1  O  PHE A 182   N  LEU A 106
SHEET    5   A 7 LEU A 203  ALA A 211  1  O  LEU A 210   N  VAL A 181
SHEET    6   A 7 VAL A 247  TYR A 255 -1  O  TYR A 255   N  GLY A 206
SHEET    7   A 7 PHE A 232  TYR A 240 -1  N  SER A 239   O  ASP A 248
SHEET    1   B 7 VAL B 155  ASN B 159  0
SHEET    2   B 7 ARG B 128  GLU B 133  1  N  THR B 131   O  LEU B 158
SHEET    3   B 7 LEU B 104  LEU B 108  1  N  VAL B 105   O  LEU B 130
SHEET    4   B 7 LEU B 178  LEU B 183  1  O  PHE B 182   N  LEU B 106
SHEET    5   B 7 LEU B 203  ALA B 211  1  O  VAL B 208   N  VAL B 181
SHEET    6   B 7 VAL B 247  TYR B 255 -1  O  TYR B 255   N  GLY B 206
SHEET    7   B 7 PHE B 232  TYR B 240 -1  N  THR B 235   O  LYS B 252
LINK         OD1 ASP A 184                MG    MG A 265     1555   1555  2.08
LINK         OD2 ASP A 212                MG    MG A 265     1555   1555  2.17
LINK         OD1 ASN A 213                MG    MG A 265     1555   1555  2.11
LINK         OD1 ASP B 184                MG    MG B 265     1555   1555  1.99
LINK         OD2 ASP B 212                MG    MG B 265     1555   1555  2.04
LINK         OD1 ASN B 213                MG    MG B 265     1555   1555  2.09
LINK         O34 705 A   1                MG    MG A 265     1555   1555  2.09
LINK         O32 705 A   1                MG    MG A 265     1555   1555  2.11
LINK         O34 705 B   2                MG    MG B 265     1555   1555  2.18
LINK         O32 705 B   2                MG    MG B 265     1555   1555  2.15
LINK        MG    MG A 265                 O   HOH A 401     1555   1555  2.09
LINK        MG    MG B 265                 O   HOH B 433     1555   1555  2.10
CISPEP   1 VAL A  216    PRO A  217          0        -0.72
CISPEP   2 VAL B  216    PRO B  217          0         0.06
SITE     1 AC1 27 HOH A  40  MET A  83  GLY A 109  TYR A 111
SITE     2 AC1 27 GLU A 133  MET A 134  TYR A 138  GLY A 160
SITE     3 AC1 27 ALA A 161  SER A 162  GLN A 163  ASP A 184
SITE     4 AC1 27 HIS A 185  TRP A 186  LYS A 187  ARG A 189
SITE     5 AC1 27 ASP A 212  ASN A 213  GLU A 242   MG A 265
SITE     6 AC1 27 HOH A 317  HOH A 324  HOH A 401  705 B   2
SITE     7 AC1 27 TRP B  81  LEU B 241  MET B 244
SITE     1 AC2  5 705 A   1  ASP A 184  ASP A 212  ASN A 213
SITE     2 AC2  5 HOH A 401
SITE     1 AC3  3 ASP A  87  ALA A  88  TYR A 243
SITE     1 AC4 11 CYS A  76  THR A  77  LYS A  79  TRP A  81
SITE     2 AC4 11 HOH A 433  705 B   2  TRP B 186  LYS B 187
SITE     3 AC4 11 ASP B 188  PRO B 217  HOH B 373
SITE     1 AC5 30 705 A   1  TRP A  81  LEU A 241  MET A 244
SITE     2 AC5 30 BTB A 267  HOH A 425  TRP B  81  MET B  83
SITE     3 AC5 30 GLY B 109  TYR B 111  GLU B 133  MET B 134
SITE     4 AC5 30 ASN B 135  TYR B 138  GLY B 160  ALA B 161
SITE     5 AC5 30 SER B 162  GLN B 163  ASP B 184  HIS B 185
SITE     6 AC5 30 TRP B 186  LYS B 187  ARG B 189  ASP B 212
SITE     7 AC5 30 ASN B 213  PRO B 217  GLU B 242   MG B 265
SITE     8 AC5 30 HOH B 345  HOH B 433
SITE     1 AC6  5 705 B   2  ASP B 184  ASP B 212  ASN B 213
SITE     2 AC6  5 HOH B 433
CRYST1   55.346   61.414  132.500  90.00  90.00  90.00 P 21 21 21    8
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      0.018068  0.000000  0.000000        0.00000
SCALE2      0.000000  0.016283  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007547        0.00000
      
PROCHECK
Go to PROCHECK summary
 References