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PDBsum entry 3nwb

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Transferase/transferase inhibitor PDB id
3nwb
Jmol
Contents
Protein chain
213 a.a.
Ligands
659
NHE
SO4
Metals
_MG
_CL ×3
Waters ×220
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-JUL-10   3NWB
TITLE     RAT COMT IN COMPLEX WITH A FLUORINATED DESOXYRIBOSE-CONTAINING
TITLE    2 BISUBSTRATE INHIBITOR AVOIDS HYDROXYL GROUP
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 GENE: COMT;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 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, TRANSMEMBRANE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS   5 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.EHLER,D.SCHLATTER,M.STIHLE,J.BENZ,M.G.RUDOLPH
REVDAT   3   11-APR-12 3NWB    1       JRNL
REVDAT   2   22-FEB-12 3NWB    1       JRNL
REVDAT   1   03-AUG-11 3NWB    0
JRNL        AUTH   M.ELLERMANN,C.LERNER,G.BURGY,A.EHLER,C.BISSANTZ,
JRNL        AUTH 2 R.JAKOB-ROETNE,R.PAULINI,O.ALLEMANN,H.TISSOT,D.GRUNSTEIN,
JRNL        AUTH 3 M.STIHLE,F.DIEDERICH,M.G.RUDOLPH
JRNL        TITL   CATECHOL-O-METHYLTRANSFERASE IN COMPLEX WITH SUBSTITUTED
JRNL        TITL 2 3'-DEOXYRIBOSE BISUBSTRATE INHIBITORS
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   253 2012
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   22349227
JRNL        DOI    10.1107/S0907444912001138
REMARK   2
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_764)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.42
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 54209
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.134
REMARK   3   R VALUE            (WORKING SET) : 0.132
REMARK   3   FREE R VALUE                     : 0.164
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040
REMARK   3   FREE R VALUE TEST SET COUNT      : 2730
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 23.4248 -  3.4638    0.88     2618   121  0.1608 0.1625
REMARK   3     2  3.4638 -  2.7507    1.00     2857   142  0.1427 0.1828
REMARK   3     3  2.7507 -  2.4034    1.00     2770   167  0.1299 0.1683
REMARK   3     4  2.4034 -  2.1838    1.00     2787   156  0.1146 0.1479
REMARK   3     5  2.1838 -  2.0274    1.00     2788   143  0.1055 0.1431
REMARK   3     6  2.0274 -  1.9079    1.00     2772   143  0.1034 0.1360
REMARK   3     7  1.9079 -  1.8124    1.00     2750   142  0.1004 0.1432
REMARK   3     8  1.8124 -  1.7335    1.00     2759   133  0.0976 0.1309
REMARK   3     9  1.7335 -  1.6668    1.00     2751   156  0.1005 0.1447
REMARK   3    10  1.6668 -  1.6093    1.00     2756   153  0.0967 0.1405
REMARK   3    11  1.6093 -  1.5590    1.00     2724   150  0.1027 0.1626
REMARK   3    12  1.5590 -  1.5144    1.00     2719   160  0.1124 0.1566
REMARK   3    13  1.5144 -  1.4746    1.00     2708   157  0.1187 0.1684
REMARK   3    14  1.4746 -  1.4386    1.00     2737   147  0.1373 0.1789
REMARK   3    15  1.4386 -  1.4059    1.00     2762   125  0.1471 0.2067
REMARK   3    16  1.4059 -  1.3760    1.00     2739   153  0.1696 0.2302
REMARK   3    17  1.3760 -  1.3485    0.99     2699   135  0.2018 0.2292
REMARK   3    18  1.3485 -  1.3230    0.94     2540   131  0.2300 0.2452
REMARK   3    19  1.3230 -  1.2994    0.81     2243   116  0.2852 0.3096
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 1.01
REMARK   3   K_SOL              : 0.48
REMARK   3   B_SOL              : 52.39
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.180
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 14.87
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.05050
REMARK   3    B22 (A**2) : -0.80110
REMARK   3    B33 (A**2) : -0.24950
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.012           1976
REMARK   3   ANGLE     :  1.466           2715
REMARK   3   CHIRALITY :  0.089            301
REMARK   3   PLANARITY :  0.009            343
REMARK   3   DIHEDRAL  : 13.919            761
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3NWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9
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   : 54289
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.170
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9
REMARK 200  DATA REDUNDANCY                : 6.630
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06740
REMARK 200   FOR THE DATA SET  : 13.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.33
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.13
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.61440
REMARK 200   FOR SHELL         : 1.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CHES, PH 9, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 300K
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       25.19450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.67800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.67550
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.67800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.19450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.67550
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     1
REMARK 465     GLY A     2
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: 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   HZ2  LYS A   156     O    HOH A   301              1.58
REMARK 500   O2   NHE A   227     O    HOH A   286              1.88
REMARK 500   OE2  GLU A    64     OG   SER A    72              2.03
REMARK 500   OD2  ASP A    94     O    HOH A   416              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   360     O    HOH A   415     4455     1.89
REMARK 500   O    HOH A   310     O    HOH A   383     3545     2.08
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  40       44.18    -82.93
REMARK 500    SER A  58       57.11     31.54
REMARK 500    TYR A  68     -111.04     63.19
REMARK 500    ASP A 133      -79.32    -91.12
REMARK 500    ASP A 141       30.94   -153.06
REMARK 500    HIS A 142     -151.35   -102.37
REMARK 500    SER A 196     -147.42   -154.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 LIGAND NHE COULD BE IN THE PROTONATED FORM
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 222  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 336   O
REMARK 620 2 659 A 226   O22  89.7
REMARK 620 3 ASP A 141   OD1  92.9 166.5
REMARK 620 4 ASP A 169   OD2  90.3 102.3  90.9
REMARK 620 5 659 A 226   O21 103.0  78.2  88.3 166.7
REMARK 620 6 ASN A 170   OD1 171.4  87.4  91.9  82.5  84.3
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 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 659 A 226
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 228
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NW9   RELATED DB: PDB
REMARK 900 RELATED ID: 3NWE   RELATED DB: PDB
REMARK 900 RELATED ID: 3OZR   RELATED DB: PDB
REMARK 900 RELATED ID: 3OZS   RELATED DB: PDB
REMARK 900 RELATED ID: 3OZT   RELATED DB: PDB
DBREF  3NWB 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 222       1
HET     CL  A 223       1
HET     CL  A 224       1
HET     CL  A 225       1
HET    659  A 226      63
HET    NHE  A 227      28
HET    SO4  A 228       5
HETNAM      MG MAGNESIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     659 N-[(E)-3-[(2R,3R,4S,5R)-3-FLUORO-4-HYDROXY-5-[6-
HETNAM   2 659  (METHYLAMINO)PURIN-9-YL]OXOLAN-2-YL]PROP-2-ENYL]-5-(4-
HETNAM   3 659  FLUOROPHENYL)-2,3-DIHYDROXY-BENZAMIDE
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETNAM     SO4 SULFATE ION
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL   2   MG    MG 2+
FORMUL   3   CL    3(CL 1-)
FORMUL   6  659    C26 H24 F2 N6 O5
FORMUL   7  NHE    C8 H17 N O3 S
FORMUL   8  SO4    O4 S 2-
FORMUL   9  HOH   *219(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 LEU A  108  ASP A  110  5                                   3
HELIX    7   7 ALA A  118  ILE A  123  1                                   6
HELIX    8   8 GLN A  125  TYR A  130  1                                   6
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  LEU A 115  0
SHEET    2   A 7 ARG A  85  MET A  89  1  N  THR A  88   O  LEU A 115
SHEET    3   A 7 LEU A  61  LEU A  65  1  N  VAL A  62   O  LEU A  87
SHEET    4   A 7 LEU A 135  LEU A 140  1  O  PHE A 139   N  LEU A  65
SHEET    5   A 7 LEU A 160  ALA A 168  1  O  LEU A 167   N  VAL A 138
SHEET    6   A 7 VAL A 204  TYR A 212 -1  O  TYR A 212   N  GLY A 163
SHEET    7   A 7 PHE A 189  TYR A 197 -1  N  SER A 196   O  ASP A 205
LINK        MG    MG A 222                 O   HOH A 336     1555   1555  2.03
LINK        MG    MG A 222                 O22 659 A 226     1555   1555  2.08
LINK         OD1 ASP A 141                MG    MG A 222     1555   1555  2.08
LINK         OD2 ASP A 169                MG    MG A 222     1555   1555  2.09
LINK        MG    MG A 222                 O21 659 A 226     1555   1555  2.10
LINK         OD1 ASN A 170                MG    MG A 222     1555   1555  2.14
CISPEP   1 VAL A  173    PRO A  174          0        -0.01
SITE     1 AC1  5 ASP A 141  ASP A 169  ASN A 170  659 A 226
SITE     2 AC1  5 HOH A 336
SITE     1 AC2  3 ASN A  41  VAL A  42  SER A  72
SITE     1 AC3  4 ASP A  44  ALA A  45  TYR A 200  HOH A 348
SITE     1 AC4  1 GLY A  83
SITE     1 AC5 26 MET A  40  GLY A  66  GLU A  90  MET A  91
SITE     2 AC5 26 ASN A  92  TYR A  95  ALA A  97  GLN A 100
SITE     3 AC5 26 GLN A 101  GLY A 117  ALA A 118  SER A 119
SITE     4 AC5 26 GLN A 120  ASP A 141  HIS A 142  TRP A 143
SITE     5 AC5 26 LYS A 144  ARG A 146  ASP A 169  ASN A 170
SITE     6 AC5 26 GLU A 199   MG A 222  HOH A 268  HOH A 311
SITE     7 AC5 26 HOH A 336  HOH A 379
SITE     1 AC6  8 GLU A  37  TRP A  38  ALA A  96  GLN A 100
SITE     2 AC6  8 ILE A 114  MET A 201  HOH A 286  HOH A 388
SITE     1 AC7  4 ASP A   3  THR A   4  LYS A   5  ARG A   8
CRYST1   50.389   55.351   79.356  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      0.019846  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018067  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012601        0.00000
      
PROCHECK
Go to PROCHECK summary
 References