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HEADER HYDROLASE 07-JUL-09 3I6M
TITLE 3D STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
TITLE 2 COMPLEXED WITH N-PIPERIDINOPROPYL-GALANTHAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 23-556;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787
KEYWDS SERINE HYDROLASE, CHOLINESTERASE, NEUROTRANSMITTER
KEYWDS 2 DEGRADATION, ALZHEIMER'S DISEASE, BIS-FUNCTIONAL
KEYWDS 3 GALANTHAMINE DERIVATIVE, ALTERNATIVE SPLICING, CELL
KEYWDS 4 JUNCTION, CELL MEMBRANE, DISULFIDE BOND, GLYCOPROTEIN, GPI-
KEYWDS 5 ANCHOR, HYDROLASE, LIPOPROTEIN, MEMBRANE, SERINE ESTERASE,
KEYWDS 6 SYNAPSE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LAMBA,C.BARTOLUCCI
REVDAT 1 12-JAN-10 3I6M 0
JRNL AUTH C.BARTOLUCCI,L.A.HALLER,U.JORDIS,G.FELS,D.LAMBA
JRNL TITL PROBING TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
JRNL TITL 2 CATALYTIC GORGE WITH TWO NOVEL BIS-FUNCTIONAL
JRNL TITL 3 GALANTHAMINE DERIVATIVES.
JRNL REF J.MED.CHEM. 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 20025280
JRNL DOI 10.1021/JM901296P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.M.GREENBLATT,C.GUILLOU,D.GUENARD,A.ARGAMAN,
REMARK 1 AUTH 2 S.BOTTI,B.BADET,C.THAL,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL THE COMPLEX OF A BIVALENT DERIVATIVE OF
REMARK 1 TITL 2 GALANTHAMINE WITH TORPEDO ACETYLCHOLINESTERASE
REMARK 1 TITL 3 DISPLAYS DRASTIC DEFORMATION OF THE ACTIVE-SITE
REMARK 1 TITL 4 GORGE: IMPLICATIONS FOR STRUCTURE-BASED DRUG DESIGN
REMARK 1 REF J.AM.CHEM.SOC. V. 126 15405 2004
REMARK 1 REFN ISSN 0002-7863
REMARK 1 PMID 15563167
REMARK 1 DOI 10.1021/JA0466154
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.M.GREENBLATT,G.KRYGER,T.LEWIS,I.SILMAN,
REMARK 1 AUTH 2 J.L.SUSSMAN
REMARK 1 TITL STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 1 TITL 2 (-)-GALANTHAMINE AT 2.3A RESOLUTION
REMARK 1 REF FEBS LETT. V. 463 321 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 10606746
REMARK 1 DOI 10.1016/S0014-5793(99)01637-3
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.BARTOLUCCI,E.PEROLA,C.PILGER,G.FELS,D.LAMBA
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF A COMPLEX OF
REMARK 1 TITL 2 GALANTHAMINE (NIVALIN) WITH ACETYLCHOLINESTERASE
REMARK 1 TITL 3 FROM TORPEDO CALIFORNICA: IMPLICATIONS FOR THE
REMARK 1 TITL 4 DESIGN OF NEW ANTI-ALZHEIMER DRUGS
REMARK 1 REF PROTEINS V. 42 182 2001
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 11119642
REMARK 1 DOI 10.1002/1097-0134
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.PILGER,C.BARTOLUCCI,D.LAMBA,A.TROPSHA,G.FELS
REMARK 1 TITL ACCURATE PREDICTION OF THE BOUND CONFORMATION OF
REMARK 1 TITL 2 GALANTHAMINE IN THE ACTIVE SITE OF TORPEDO
REMARK 1 TITL 3 CALIFORNICA ACETYLCHOLINESTERASE USING MOLECULAR
REMARK 1 TITL 4 DOCKING
REMARK 1 REF J.MOL.GRAPH.MODEL. V. 19 288 2001
REMARK 1 REFN ISSN 1093-3263
REMARK 1 PMID 11449566
REMARK 1 DOI 10.1016/S1093-3263(00)00056-5
REMARK 1 REFERENCE 5
REMARK 1 AUTH E.LUTTMANN,E.LINNEMANN,G.FELS
REMARK 1 TITL GALANTHAMINE AS BIS-FUNCTIONAL LIGAND FOR THE
REMARK 1 TITL 2 ACETYLCHOLINESTERASE.
REMARK 1 REF J.MOL.MODEL. V. 8 208 2002
REMARK 1 REFN ESSN 0948-5023
REMARK 1 PMID 12140604
REMARK 1 REFERENCE 6
REMARK 1 AUTH L.ALISARAIE,G.FELS
REMARK 1 TITL A QXP-BASED MULTISTEP DOCKING PROCEDURE FOR
REMARK 1 TITL 2 ACCURATE PREDICTION OF PROTEIN-LIGAND COMPLEXES
REMARK 1 REF J.CHEM.INF.MODEL. V. 46 1174 2006
REMARK 1 REFN ISSN 1549-9596
REMARK 1 PMID 16711737
REMARK 1 DOI 10.1021/CI050343M
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1997132.140
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 46822
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 SET) : 0.180
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4701
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3572
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 397
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4263
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 398
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.30000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 8.30000
REMARK 3 B13 (A**2) : -16.60000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.02
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED INDIVIDUAL ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.733 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.525 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.789 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.908 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 62.80
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3I6M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : THREE-SEGMENT PT-COATED
REMARK 200 TOROIDAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46878
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 19.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41800
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 42% PEG200, 100MM MES PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.73133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.46267
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.46267
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.73133
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 137.19400
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 2 CG OD1 OD2
REMARK 480 HIS A 3 CG ND1 CD2 CE1 NE2
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 HIS A 3 -40.49 -155.13
REMARK 500 LEU A 23 53.07 38.67
REMARK 500 PHE A 45 -11.84 81.24
REMARK 500 ALA A 60 50.25 -108.56
REMARK 500 SER A 108 74.63 -162.24
REMARK 500 ASN A 131 109.48 -58.37
REMARK 500 LEU A 158 78.93 -119.72
REMARK 500 SER A 200 -119.95 57.64
REMARK 500 GLU A 299 -71.63 -120.21
REMARK 500 THR A 317 -158.87 -158.31
REMARK 500 ASP A 326 66.36 -119.74
REMARK 500 TRP A 378 1.22 -69.96
REMARK 500 ASP A 380 51.66 -155.35
REMARK 500 VAL A 400 -60.86 -125.99
REMARK 500 HIS A 486 -0.30 73.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 442 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 536
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 537
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 538
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE G3X A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C.3.1.1.7) COMPLEXED WITH
REMARK 900 GALANTHAMINE
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1DX6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE WITH (-)-GALANTHAMINE AT
REMARK 900 2.3A RESOLUTION
REMARK 900 RELATED ID: 3I6Z RELATED DB: PDB
REMARK 900 3D STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 COMPLEXED WITH N-SACCHARINOHEXYL-GALANTHAMINE
DBREF 3I6M A 2 535 UNP P04058 ACES_TORCA 23 556
SEQRES 1 A 534 ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS
SEQRES 2 A 534 VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE
SEQRES 3 A 534 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 A 534 GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO
SEQRES 5 A 534 TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN
SEQRES 6 A 534 CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER
SEQRES 7 A 534 GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU
SEQRES 8 A 534 ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG
SEQRES 9 A 534 PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY
SEQRES 10 A 534 GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN
SEQRES 11 A 534 GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL
SEQRES 12 A 534 SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA
SEQRES 13 A 534 LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 A 534 LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN
SEQRES 15 A 534 ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE
SEQRES 16 A 534 PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS
SEQRES 17 A 534 ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA
SEQRES 18 A 534 ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER
SEQRES 19 A 534 VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU
SEQRES 20 A 534 GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU
SEQRES 21 A 534 LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU
SEQRES 22 A 534 ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE
SEQRES 23 A 534 PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE
SEQRES 24 A 534 PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN
SEQRES 25 A 534 PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP
SEQRES 26 A 534 GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE
SEQRES 27 A 534 SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE
SEQRES 28 A 534 MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP
SEQRES 29 A 534 LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP
SEQRES 30 A 534 MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU
SEQRES 31 A 534 ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU
SEQRES 32 A 534 MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY
SEQRES 33 A 534 THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU
SEQRES 34 A 534 VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU
SEQRES 35 A 534 ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU
SEQRES 36 A 534 ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE
SEQRES 37 A 534 MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO
SEQRES 38 A 534 ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE
SEQRES 39 A 534 THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU
SEQRES 40 A 534 PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS
SEQRES 41 A 534 VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA
SEQRES 42 A 534 THR
MODRES 3I6M ASN A 59 ASN GLYCOSYLATION SITE
MODRES 3I6M ASN A 416 ASN GLYCOSYLATION SITE
HET NAG A 536 14
HET NAG A 537 14
HET NAG A 538 14
HET G3X A 1 29
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM G3X (4AS,6R,8AS)-3-METHOXY-11-(3-PIPERIDIN-1-YLPROPYL)-5,6,
HETNAM 2 G3X 9,10,11,12-HEXAHYDRO-4AH-[1]BENZOFURO[3A,3,2-
HETNAM 3 G3X EF][2]BENZAZEPIN-6-OL
HETSYN NAG NAG
HETSYN G3X (4AS,6R,8AS)-4A,5,9,10,11,12-HEXAHYDRO-3-METHOXY-11-[3-
HETSYN 2 G3X (1-PIPERIDINYL)PROPYL]-6H-BENZOFURO[3A,3,2-
HETSYN 3 G3X EF][2]BENZAZEPIN-6-OL
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 4 G3X C24 H34 N2 O3
FORMUL 5 HOH *398(H2 O)
HELIX 1 1 VAL A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASN A 131 5 5
HELIX 4 4 GLY A 132 GLU A 140 1 9
HELIX 5 5 VAL A 150 LEU A 156 1 7
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 GLN A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 SER A 215 PHE A 219 5 5
HELIX 10 10 SER A 237 LEU A 252 1 16
HELIX 11 11 SER A 258 LYS A 269 1 12
HELIX 12 12 LYS A 270 GLU A 278 1 9
HELIX 13 13 TRP A 279 LEU A 282 5 4
HELIX 14 14 SER A 304 GLY A 312 1 9
HELIX 15 15 GLY A 328 ALA A 336 1 9
HELIX 16 16 SER A 348 VAL A 360 1 13
HELIX 17 17 ASN A 364 THR A 376 1 13
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 GLY A 415 1 16
HELIX 20 20 PRO A 433 GLY A 437 5 5
HELIX 21 21 GLU A 443 PHE A 448 1 6
HELIX 22 22 GLY A 449 ASN A 457 5 9
HELIX 23 23 THR A 459 GLY A 480 1 22
HELIX 24 24 ARG A 517 GLN A 526 1 10
HELIX 25 25 GLN A 526 THR A 535 1 10
SHEET 1 A 3 LEU A 7 THR A 10 0
SHEET 2 A 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 A 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 B11 THR A 18 VAL A 22 0
SHEET 2 B11 SER A 25 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 B11 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 B11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 B11 THR A 109 ILE A 115 1 N TRP A 114 O VAL A 144
SHEET 6 B11 GLY A 189 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 B11 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 B11 GLN A 318 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 B11 GLY A 417 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 B11 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 B11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.06
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.05
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A 536 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A 537 1555 1555 1.45
LINK O4 NAG A 537 C1 NAG A 538 1555 1555 1.40
CISPEP 1 SER A 103 PRO A 104 0 0.31
SITE 1 AC1 3 ASN A 59 SER A 61 HOH A 906
SITE 1 AC2 5 ASN A 416 NAG A 538 HOH A 732 HOH A 894
SITE 2 AC2 5 HOH A 918
SITE 1 AC3 2 NAG A 537 HOH A 918
SITE 1 AC4 13 TRP A 84 GLY A 117 GLY A 118 GLY A 119
SITE 2 AC4 13 TYR A 121 GLU A 199 SER A 200 PHE A 290
SITE 3 AC4 13 PHE A 330 PHE A 331 TYR A 334 HIS A 440
SITE 4 AC4 13 HOH A 547
CRYST1 112.194 112.194 137.194 90.00 90.00 120.00 P 31 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008913 0.005146 0.000000 0.00000
SCALE2 0.000000 0.010292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007289 0.00000
TER 4264 THR A 535
MASTER 371 0 4 25 14 0 8 6 4732 1 79 42
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