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HEADER HYDROLASE 18-DEC-08 2W6C
TITLE ACHE IN COMPLEX WITH A BIS-(-)-NOR-MEPTAZINOL DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: X;
COMPND 4 SYNONYM: ACHE;
COMPND 5 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;
SOURCE 5 ORGAN: ELECTRIC ORGAN
KEYWDS CATALYTIC TRIAD, SERINE HYDROLASE, ALZHEIMER'S DISEASE,
KEYWDS 2 CELL MEMBRANE, CHOLINESTERASE, SERINE ESTERASE,
KEYWDS 3 NEUROTRANSMITTER DEGRADATION, NERVE, MUSCLE, SYNAPSE,
KEYWDS 4 MEMBRANE, HYDROLASE, ALTERNATIVE SPLICING,
KEYWDS 5 BIS-(-)-NOR-MEPTAZINOL, GPI-ANCHOR, GLYCOPROTEIN, CELL
KEYWDS 6 JUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAZ,Q.XIE,H.M.GREENBLATT,W.FU,Y.TANG,I.SILMAN,Z.QIU,
AUTHOR 2 J.L.SUSSMAN
REVDAT 1 07-APR-09 2W6C 0
JRNL AUTH A.PAZ,Q.XIE,H.M.GREENBLATT,W.FU,Y.TANG,I.SILMAN,
JRNL AUTH 2 Z.QIU,J.L.SUSSMAN
JRNL TITL THE CRYSTAL STRUCTURE OF A COMPLEX OF
JRNL TITL 2 ACETYLCHOLINESTERASE WITH A BIS-(-)-NOR-MEPTAZINOL
JRNL TITL 3 DERIVATIVE REVEALS DISRUPTION OF THE CATALYTIC
JRNL TITL 4 TRIAD.
JRNL REF J.MED.CHEM. 2009
JRNL REFN ESSN 1520-4804
JRNL PMID 19326912
JRNL DOI 10.1021/JM801657V
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
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) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26745
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1456
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) : 2.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1917
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4171
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.02000
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): 0.348
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.261
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.167
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.060
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4382 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5954 ; 2.112 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 526 ; 6.459 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 197 ;32.624 ;23.959
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 686 ;18.162 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;15.689 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 634 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3343 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2626 ; 0.800 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4239 ; 1.548 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1756 ; 2.465 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1715 ; 3.898 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2W6C COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-08.
REMARK 100 THE PDBE ID CODE IS EBI-38287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.69
REMARK 200 RESOLUTION RANGE LOW (A) : 39.68
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.4
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.4
REMARK 200 R MERGE FOR SHELL (I) : 0.05
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: LOCAL MODEL DERIVED FROM PDB ENTRY 1EA5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 40% PEG 200, 150 MM MES, PH 7.4, AND CRYSTALS WERE SOAKED
REMARK 280 IN 1 MM OF INHIBITOR SOLUTION
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 45.85600
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 91.71200
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 91.71200
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 45.85600
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 137.56800
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 X -20
REMARK 465 ASN X -19
REMARK 465 LEU X -18
REMARK 465 LEU X -17
REMARK 465 VAL X -16
REMARK 465 THR X -15
REMARK 465 SER X -14
REMARK 465 SER X -13
REMARK 465 LEU X -12
REMARK 465 GLY X -11
REMARK 465 VAL X -10
REMARK 465 LEU X -9
REMARK 465 LEU X -8
REMARK 465 HIS X -7
REMARK 465 LEU X -6
REMARK 465 VAL X -5
REMARK 465 VAL X -4
REMARK 465 LEU X -3
REMARK 465 CYS X -2
REMARK 465 GLN X -1
REMARK 465 ALA X 0
REMARK 465 ASP X 1
REMARK 465 ASP X 2
REMARK 465 HIS X 3
REMARK 465 HIS X 486
REMARK 465 SER X 487
REMARK 465 GLN X 488
REMARK 465 GLU X 489
REMARK 465 ALA X 536
REMARK 465 CYS X 537
REMARK 465 ASP X 538
REMARK 465 GLY X 539
REMARK 465 GLU X 540
REMARK 465 LEU X 541
REMARK 465 SER X 542
REMARK 465 SER X 543
REMARK 465 SER X 544
REMARK 465 GLY X 545
REMARK 465 THR X 546
REMARK 465 SER X 547
REMARK 465 SER X 548
REMARK 465 SER X 549
REMARK 465 LYS X 550
REMARK 465 GLY X 551
REMARK 465 ILE X 552
REMARK 465 ILE X 553
REMARK 465 PHE X 554
REMARK 465 TYR X 555
REMARK 465 VAL X 556
REMARK 465 LEU X 557
REMARK 465 PHE X 558
REMARK 465 SER X 559
REMARK 465 ILE X 560
REMARK 465 LEU X 561
REMARK 465 TYR X 562
REMARK 465 LEU X 563
REMARK 465 ILE X 564
REMARK 465 PHE X 565
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN X 42 CG OD1 ND2
REMARK 470 ARG X 46 CZ NH1 NH2
REMARK 470 ARG X 250 CZ NH1 NH2
REMARK 470 ASN X 257 CG OD1 ND2
REMARK 470 GLU X 260 OE1 OE2
REMARK 470 GLU X 268 OE1 OE2
REMARK 470 LYS X 270 CD CE NZ
REMARK 470 GLU X 344 OE1 OE2
REMARK 470 LYS X 357 NZ
REMARK 470 ASP X 365 OD1 OD2
REMARK 470 LYS X 413 CD CE NZ
REMARK 470 LYS X 498 CG CD CE NZ
REMARK 470 GLU X 508 CD OE1 OE2
REMARK 470 ARG X 515 CZ NH1 NH2
REMARK 470 GLN X 526 OE1 NE2
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 CB THR X 497 - O HOH X 2106 1.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU X 260 CB GLU X 260 CG 0.129
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 LEU X 143 CA - CB - CG ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO X 191 C - N - CA ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG X 243 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG X 244 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 VAL X 295 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 LYS X 325 CD - CE - NZ ANGL. DEV. = -14.5 DEGREES
REMARK 500 LEU X 430 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 LEU X 494 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 VAL X 518 CB - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU X 531 CA - CB - CG ANGL. DEV. = 16.0 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 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 ASN X 42 0.92 -61.08
REMARK 500 PHE X 45 -9.50 66.00
REMARK 500 ALA X 60 51.67 -104.91
REMARK 500 ARG X 105 123.42 -35.25
REMARK 500 SER X 108 60.44 -158.90
REMARK 500 PHE X 155 13.82 -141.34
REMARK 500 SER X 200 -125.00 56.56
REMARK 500 PRO X 294 153.77 -48.76
REMARK 500 GLU X 299 -80.76 -120.09
REMARK 500 ASP X 380 42.92 174.87
REMARK 500 VAL X 400 -58.57 -132.50
REMARK 500 ASN X 424 39.18 -140.47
REMARK 500 ASN X 457 37.69 86.16
REMARK 500 GLN X 526 -61.13 -105.04
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 600
REMARK 600 HETEROGEN
REMARK 600 5H (BMP): THE ELECTRON DENSITY FOR THE INHIBITOR WAS NOT
REMARK 600 COMPLETE SO ONLY PART OF IT WAS FIT TO THE DENSITY AND
REMARK 600 DEPOSITED. THE FORMULA OF THIS PART IS C23H40N2O
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 BM4 X 1536
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BM4 X1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X1540
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (R)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE
REMARK 900 COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-HUPRINE X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 2VQ6 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH 2-PAM
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 MONOCHROMATIC DATA
REMARK 900 RELATED ID: 2J3D RELATED DB: PDB
REMARK 900 NATIVE MONOCLINIC FORM OF TORPEDO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT F) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2CKM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH ALKYLENE-LINKED BIS-TACRINE DIMER (7
REMARK 900 CARBON LINKER)
REMARK 900 RELATED ID: 1DX6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-GALANTHAMINE AT 2.3A RESOLUTION
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT G) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT B) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1ODC RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH N-4'-QUINOLYL-N'-9
REMARK 900 "-(1",2",3",4"-TETRAHYDROACRIDINYL)-1,8-
REMARK 900 DIAMINOOCTANE AT 2.2A RESOLUTION
REMARK 900 RELATED ID: 2CMF RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH ALKYLENE-LINKED BIS-TACRINE DIMER (5
REMARK 900 CARBON LINKER)
REMARK 900 RELATED ID: 2J3Q RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 FLUOROPHORE THIOFLAVIN T
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH NAP
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH BW284C51
REMARK 900 RELATED ID: 2J4F RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF AGED DI-ISOPROPYL-
REMARK 900 PHOSPHORO-FLUORIDATE (DFP) BOUND TO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT H) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C5F RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-TRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7
REMARK 900 ) FROM TORPEDO CALIFORNICA AT 1.8A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 2VJC RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP
REMARK 900 - DATASET A AT 150K
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT C) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VJB RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP
REMARK 900 - DATASET D AT 100K
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT D) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT A) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ZGC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (RS)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 1JJB RELATED DB: PDB
REMARK 900 A NEUTRAL MOLECULE IN CATION-BINDING SITE:
REMARK 900 SPECIFIC BINDINGOF PEG-SH TO
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 900 RELATED ID: 2VJD RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP
REMARK 900 - DATASET C AT 150K
REMARK 900 RELATED ID: 1UT6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH N-9-(1',2',3',4
REMARK 900 '-TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT
REMARK 900 2.4 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 2VT6 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 COLLECTED WITH A CUMULATED DOSE OF 9400000
REMARK 900 GY
REMARK 900 RELATED ID: 2VT7 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 COLLECTED WITH A CUMULATED DOSE OF 800000
REMARK 900 GY
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL
REMARK 900 SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 REVEALED BY THE COMPLEX STRUCTURE WITH A
REMARK 900 BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT I) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH
REMARK 900 (+)-HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-
REMARK 900 HEPTYLENE-BIS-N,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH MF268
REMARK 900 RELATED ID: 1SOM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NERVE AGENT GD (SOMAN).
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 2VJA RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP
REMARK 900 - DATASET A AT 100K
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-
REMARK 900 ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)
REMARK 900 RELATED ID: 2V96 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF
REMARK 900 TCACHE WITH 1-(2-NITROPHENYL)-2,2,2-
REMARK 900 TRIFLUOROETHYL-ARSENOCHOLINE AT 100K
REMARK 900 RELATED ID: 1U65 RELATED DB: PDB
REMARK 900 ACHE W. CPT-11
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-
REMARK 900 ACTING GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 LAUE DATA
REMARK 900 RELATED ID: 1H22 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-
REMARK 900 ALZHEIMER DRUG, E2020 (ARICEPT), COMPLEXED
REMARK 900 WITH ITS TARGET ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C4H RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2VA9 RELATED DB: PDB
REMARK 900 STRUCTURE OF NATIVE TCACHE AFTER A 9
REMARK 900 SECONDS ANNEALING TO ROOM TEMPERATURE DURING
REMARK 900 THE FIRST 5 SECONDS OF WHICH LASER
REMARK 900 IRRADIATION AT 266NM TOOK PLACE
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH RIVASTIGMINE
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (S)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 2C58 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 1HBJ RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN
REMARK 900 TORPEDO CALIFORNICA ACHE AND A REVERSIBLE
REMARK 900 INHIBITOR, 4-AMINO-5-FLUORO-2-METHYL-3-(
REMARK 900 3-TRIFLUOROACETYLBENZYLTHIOMETHYL)QUINOLINE
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM THIOCHOLINE
REMARK 900 RELATED ID: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-
REMARK 900 PROPYLENE-BIS-N,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 2V98 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-
REMARK 900 ARSENOCHOLINE AFTER A 9 SECONDS ANNEALING TO
REMARK 900 ROOM TEMPERATURE, DURING HTE FIRST 5
REMARK 900 SECONDS OF WHICH LASER IRRADIATION AT 266NM
REMARK 900 TOOK PLACE
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 HUPERZINE B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT E) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900 II
REMARK 900 RELATED ID: 2V97 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF
REMARK 900 TCACHE WITH 1-(2-NITROPHENYL)-2,2,2-
REMARK 900 TRIFLUOROETHYL-ARSENOCHOLINE AFTER A 9 SECONDS
REMARK 900 ANNEALING TO ROOM TEMPERATURE
DBREF 2W6C X -20 565 UNP P04058 ACES_TORCA 1 586
SEQRES 1 X 586 MET ASN LEU LEU VAL THR SER SER LEU GLY VAL LEU LEU
SEQRES 2 X 586 HIS LEU VAL VAL LEU CYS GLN ALA ASP ASP HIS SER GLU
SEQRES 3 X 586 LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET GLY THR
SEQRES 4 X 586 ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA PHE LEU
SEQRES 5 X 586 GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN MET ARG
SEQRES 6 X 586 PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER GLY VAL
SEQRES 7 X 586 TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN GLN TYR
SEQRES 8 X 586 VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER GLU MET
SEQRES 9 X 586 TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS LEU TYR
SEQRES 10 X 586 LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS SER THR
SEQRES 11 X 586 THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE TYR SER
SEQRES 12 X 586 GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS TYR LEU
SEQRES 13 X 586 ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU SER TYR
SEQRES 14 X 586 ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS GLY SER
SEQRES 15 X 586 GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG
SEQRES 16 X 586 MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN PHE PHE
SEQRES 17 X 586 GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY GLU SER
SEQRES 18 X 586 ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU SER PRO
SEQRES 19 X 586 GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU GLN SER
SEQRES 20 X 586 GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER VAL ALA
SEQRES 21 X 586 GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG ASN LEU
SEQRES 22 X 586 ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE HIS CYS
SEQRES 23 X 586 LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP VAL GLU
SEQRES 24 X 586 TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG PHE SER
SEQRES 25 X 586 PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO THR SER
SEQRES 26 X 586 LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS LYS THR
SEQRES 27 X 586 GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY SER PHE
SEQRES 28 X 586 PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS ASP SER
SEQRES 29 X 586 GLU SER LYS ILE SER ARG GLU ASP PHE MET SER GLY VAL
SEQRES 30 X 586 LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY LEU ASP
SEQRES 31 X 586 ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP ASP ASN
SEQRES 32 X 586 ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP ILE VAL
SEQRES 33 X 586 GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS PHE VAL
SEQRES 34 X 586 ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR LEU TYR
SEQRES 35 X 586 PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP PRO GLU
SEQRES 36 X 586 TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU PHE VAL
SEQRES 37 X 586 PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR THR ALA
SEQRES 38 X 586 GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS TYR TRP
SEQRES 39 X 586 ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU PRO HIS
SEQRES 40 X 586 SER GLN GLU SER LYS TRP PRO LEU PHE THR THR LYS GLU
SEQRES 41 X 586 GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET LYS VAL
SEQRES 42 X 586 HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE TRP ASN
SEQRES 43 X 586 GLN PHE LEU PRO LYS LEU LEU ASN ALA THR ALA CYS ASP
SEQRES 44 X 586 GLY GLU LEU SER SER SER GLY THR SER SER SER LYS GLY
SEQRES 45 X 586 ILE ILE PHE TYR VAL LEU PHE SER ILE LEU TYR LEU ILE
SEQRES 46 X 586 PHE
HET BM4 X1536 26
HET NAG X1537 14
HET NAG X1538 14
HET NAG X1539 14
HET NAG X1540 14
HETNAM BM4 3-[(3R)-3-ETHYL-1-{9-[(3S)-3-ETHYL-3-(3-
HETNAM 2 BM4 HYDROXYPHENYL)AZEPAN-1-YL]NONYL}AZEPAN-3-YL]
HETNAM 3 BM4 PHENOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 BM4 C37 H58 N2 O2
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 HOH *115(H2 O1)
HELIX 1 1 GLY X 41 MET X 43 5 3
HELIX 2 2 SER X 79 TRP X 84 1 6
HELIX 3 3 ASP X 128 TYR X 130 5 3
HELIX 4 4 LYS X 133 GLU X 139 1 7
HELIX 5 5 GLY X 151 PHE X 155 1 5
HELIX 6 6 VAL X 168 PHE X 187 1 20
HELIX 7 7 ALA X 201 LEU X 211 1 11
HELIX 8 8 PRO X 213 LEU X 218 1 6
HELIX 9 9 VAL X 238 LEU X 252 1 15
HELIX 10 10 ASP X 259 GLU X 268 1 10
HELIX 11 11 PRO X 271 VAL X 281 1 11
HELIX 12 12 LEU X 305 SER X 311 1 7
HELIX 13 13 SER X 329 GLY X 335 1 7
HELIX 14 14 ARG X 349 SER X 359 1 11
HELIX 15 15 ASP X 365 GLN X 374 1 10
HELIX 16 16 GLY X 384 ASN X 399 1 16
HELIX 17 17 ILE X 401 PHE X 414 1 14
HELIX 18 18 GLU X 434 MET X 436 5 3
HELIX 19 19 ILE X 444 VAL X 447 1 4
HELIX 20 20 LEU X 450 LEU X 452 5 3
HELIX 21 21 LYS X 454 LEU X 456 5 3
HELIX 22 22 ALA X 460 THR X 479 1 20
HELIX 23 23 VAL X 518 ASN X 525 1 8
HELIX 24 24 PHE X 527 ASN X 533 1 7
SHEET 1 A 3 LEU X 6 THR X 10 0
SHEET 2 A 3 GLY X 13 MET X 16 -1 N VAL X 15 O VAL X 8
SHEET 3 A 3 VAL X 57 ALA X 60 1 N TRP X 58 O LYS X 14
SHEET 1 B11 MET X 16 PRO X 21 0
SHEET 2 B11 HIS X 26 PRO X 34 -1 O ALA X 29 N THR X 18
SHEET 3 B11 TYR X 96 PRO X 102 -1 N ILE X 99 O PHE X 30
SHEET 4 B11 VAL X 142 SER X 147 -1 N LEU X 143 O TRP X 100
SHEET 5 B11 THR X 109 TYR X 116 1 N MET X 112 O VAL X 142
SHEET 6 B11 THR X 193 GLU X 199 1 O THR X 195 N VAL X 113
SHEET 7 B11 ARG X 220 SER X 226 1 N ILE X 223 O ILE X 196
SHEET 8 B11 GLN X 318 ASN X 324 1 N GLY X 322 O LEU X 224
SHEET 9 B11 GLY X 417 PHE X 423 1 N TYR X 421 O LEU X 321
SHEET 10 B11 PHE X 502 LEU X 505 1 N ILE X 503 O LEU X 420
SHEET 11 B11 MET X 510 GLN X 514 -1 N HIS X 513 O PHE X 502
SHEET 1 XA 3 LEU X 7 THR X 10 0
SHEET 2 XA 3 GLY X 13 MET X 16 -1 O GLY X 13 N THR X 10
SHEET 3 XA 3 VAL X 57 ASN X 59 1 O TRP X 58 N MET X 16
SHEET 1 XB11 THR X 18 PRO X 21 0
SHEET 2 XB11 HIS X 26 PRO X 34 -1 O ILE X 27 N VAL X 20
SHEET 3 XB11 TYR X 96 VAL X 101 -1 O LEU X 97 N ILE X 33
SHEET 4 XB11 VAL X 142 SER X 145 -1 O LEU X 143 N TRP X 100
SHEET 5 XB11 THR X 109 ILE X 115 1 O THR X 110 N VAL X 142
SHEET 6 XB11 GLY X 189 GLU X 199 1 N ASP X 190 O THR X 109
SHEET 7 XB11 ARG X 221 GLN X 225 1 O ARG X 221 N ILE X 196
SHEET 8 XB11 GLN X 318 ASN X 324 1 O GLN X 318 N ALA X 222
SHEET 9 XB11 GLY X 417 PHE X 423 1 O GLY X 417 N ILE X 319
SHEET 10 XB11 LYS X 501 LEU X 505 1 O ILE X 503 N PHE X 422
SHEET 11 XB11 VAL X 512 GLN X 514 -1 O HIS X 513 N PHE X 502
SSBOND 1 CYS X 67 CYS X 94 1555 1555 2.08
SSBOND 2 CYS X 254 CYS X 265 1555 1555 2.06
SSBOND 3 CYS X 402 CYS X 521 1555 1555 2.03
LINK ND2 ASN X 59 C1 NAG X1537 1555 1555 1.45
LINK ND2 ASN X 416 C1 NAG X1538 1555 1555 1.45
LINK ND2 ASN X 457 C1 NAG X1540 1555 1555 1.48
LINK O4 NAG X1538 C1 NAG X1539 1555 1555 1.47
CISPEP 1 SER X 103 PRO X 104 0 -0.50
SITE 1 AC1 12 TRP X 84 GLY X 117 GLY X 118 GLY X 119
SITE 2 AC1 12 TYR X 121 GLU X 199 SER X 200 PHE X 330
SITE 3 AC1 12 PHE X 331 TYR X 334 HIS X 440 HOH X2113
SITE 1 AC2 2 ASN X 59 SER X 61
SITE 1 AC3 3 ASN X 416 NAG X1539 HOH X2114
SITE 1 AC4 1 NAG X1538
SITE 1 AC5 3 GLU X 455 ASN X 457 HOH X2115
CRYST1 112.172 112.172 137.568 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 0.008915 0.005147 0.000000 0.00000
SCALE2 0.000000 0.010294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007269 0.00000
TER 4172 THR X 535
MASTER 748 0 5 24 28 0 7 6 4368 1 91 46
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