| 2VQ6-pdb | HEADER HYDROLASE 11-MAR-08 2VQ6
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH 2-
TITLE 2 PAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 SYNONYM: ACHE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 22-464;
COMPND 6 EC: 3.1.1.7;
COMPND 7 OTHER_DETAILS: 2-FORMYL-1-METHYL-PYRIDINIUM CHLORIDE (
COMPND 8 PRALYDOXIME, 2-PAM) IN ACTIVE SITE GORGE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY
KEYWDS SERINE ESTERASE, ALTERNATIVE SPLICING,
KEYWDS 2 NEUROTRANSMITTER DEGRADATION,
KEYWDS 3 LIPOPROTEIN, GLYCOPROTEIN, TORPEDO ACHE, CELL JUNCTION,
KEYWDS 4 ANTICANCER PRODRUG CPT- 11,
KEYWDS 5 SYNAPSE, MEMBRANE, HYDROLASE, GPI-ANCHOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,I.SILMAN,J.L.SUSSMAN
REVDAT 1 13-MAY-08 2VQ6 0
SPRSDE 13-MAY-08 2VQ6 2VB4
JRNL AUTH M.HAREL,I.SILMAN,J.L.SUSSMAN
JRNL TITL THE STRUCTURE OF TORPEDO CALIFORNICA
JRNL TITL 2 ACETYLCHOLINESTERASE COMPLEXED WITH 2-PAM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 25095
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) : 0.17442
REMARK 3 R VALUE (WORKING SET) : 0.17122
REMARK 3 FREE R VALUE : 0.23399
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1340
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) : 2.712
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.781
REMARK 3 REFLECTION IN BIN (WORKING SET) : 708
REMARK 3 BIN R VALUE (WORKING SET) : 0.310
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.319
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.120
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16
REMARK 3 B22 (A**2) : 0.16
REMARK 3 B33 (A**2) : -0.24
REMARK 3 B12 (A**2) : 0.08
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.359
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.197
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.334
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4413 ; 0.030 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 5993 ; 2.651 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 533 ; 8.713 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;33.268 ;23.886
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 709 ;23.475 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.850 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 628 ; 0.166 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 3415 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 2056 ; 0.269 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 3050 ; 0.348 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 163 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 16 ; 0.288 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 2 ; 0.314 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2681 ; 1.256 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4268 ; 2.314 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1962 ; 3.417 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1722 ; 5.600 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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 2VQ6 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 11-MAR-2008.
REMARK 100 THE EBI ID CODE IS EBI-35651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-1991
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 15.66
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.4
REMARK 200 R MERGE (I) : 0.15
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PROTIN
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
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): 4.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 Y-X,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,Y-X,1/3-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 -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 46.01667
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 92.03333
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 92.03333
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 46.01667
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: PQS
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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 SER A 487
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
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 ND2 ASN A 59 - C2 NAG A 1539 2.14
REMARK 500 ND2 ASN A 59 - O5 NAG A 1539 2.11
REMARK 500 N SER A 108 - O HOH A 2026 2.19
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,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 114 C ILE A 115 N -0.142
REMARK 500 PHE A 219 CE1 PHE A 219 CZ 0.118
REMARK 500 SER A 228 CB SER A 228 OG -0.091
REMARK 500 ALA A 245 CA ALA A 245 CB -0.133
REMARK 500 PRO A 283 C PHE A 284 N 0.192
REMARK 500 ILE A 287 C PHE A 288 N -0.202
REMARK 500 PHE A 476 CE1 PHE A 476 CZ 0.144
REMARK 500 LYS A 478 CD LYS A 478 CE 0.188
REMARK 500 LYS A 530 CD LYS A 530 CE 0.154
REMARK 500 CYS A 254 CB CYS A 254 SG -0.103
REMARK 500 CYS A 231 CB CYS A 231 SG -0.115
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: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 31 CB - CG - CD1 ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PRO A 106 C - N - CA ANGL. DEV. = -10.6 DEGREES
REMARK 500 VAL A 129 CB - CA - C ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 244 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 285 C - N - CA ANGL. DEV. = -15.9 DEGREES
REMARK 500 SER A 286 O - C - N ANGL. DEV. = -10.8 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 LYS A 11 -28.09 -37.41
REMARK 500 LEU A 23 -121.23 52.98
REMARK 500 SER A 25 -148.91 -63.65
REMARK 500 PHE A 45 -3.25 73.92
REMARK 500 ALA A 60 50.03 -98.56
REMARK 500 GLN A 74 -55.86 -15.94
REMARK 500 PHE A 75 78.69 -115.62
REMARK 500 CYS A 94 23.52 -150.24
REMARK 500 PHE A 120 -15.90 69.68
REMARK 500 PHE A 155 -7.93 -141.75
REMARK 500 LEU A 158 78.96 -117.15
REMARK 500 HIS A 159 -66.21 -24.42
REMARK 500 ALA A 164 77.30 -153.62
REMARK 500 THR A 193 46.49 -146.80
REMARK 500 SER A 200 -112.87 38.82
REMARK 500 LEU A 256 53.66 -115.23
REMARK 500 GLU A 299 -63.11 -106.57
REMARK 500 THR A 317 -148.18 -132.78
REMARK 500 ASP A 326 75.54 -119.49
REMARK 500 MET A 379 41.18 -106.95
REMARK 500 ASP A 380 35.88 145.53
REMARK 500 VAL A 400 -56.10 -136.65
REMARK 500 VAL A 438 95.84 -66.17
REMARK 500 PRO A 451 -9.80 -55.13
REMARK 500 ASN A 457 47.57 86.25
REMARK 500 MET A 470 -35.33 -34.95
REMARK 500 TYR A 472 -56.00 -20.38
REMARK 500 GLN A 500 48.57 87.80
REMARK 500 THR A 507 3.89 -62.35
REMARK 500 ARG A 517 51.69 28.59
REMARK 500 GLN A 519 -72.70 -11.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 42 MET A 43 0 140.61
REMARK 500 PHE A 292 VAL A 293 0 -147.81
REMARK 500 SER A 490 LYS A 491 0 -146.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 0 PHE A 284 15.52
REMARK 500 0 ILE A 287 -15.74
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FP1 A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1539
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: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
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: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-HUPRINE X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 2J3D RELATED DB: PDB
REMARK 900 NATIVE MONOCLINIC FORM OF TORPEDO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 MONOCHROMATIC DATA
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: 2J4F RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH BW284C51
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: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
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: 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: 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: 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: 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: 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: 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: 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: 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: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH
REMARK 900 (+)-HUPERZINE A AT 2.1A RESOLUTION
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: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH MF268
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
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: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 LAUE DATA
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: 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: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH RIVASTIGMINE
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: 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: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM THIOCHOLINE
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: 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: 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: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900 II
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
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 2VQ6 A 1 543 UNP P04058 ACES_TORCA 22 564
SEQRES 1 A 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
HET FP1 A1536 10
HET SO4 A1537 5
HET NAG A1538 14
HET NAG A1539 14
HETNAM SO4 SULFATE ION
HETNAM FP1 N-HYDROXY-1-(1-METHYLPYRIDIN-2(1H)-YLIDENE)
HETNAM 2 FP1 METHANAMINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 FP1 C7 H10 N2 O
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 HOH *93(H2 O1)
HELIX 1 1 PHE A 78 MET A 83 1 6
HELIX 2 2 LEU A 127 ASN A 131 5 5
HELIX 3 3 GLY A 132 GLU A 140 1 9
HELIX 4 4 VAL A 150 LEU A 156 1 7
HELIX 5 5 ASN A 167 ILE A 184 1 18
HELIX 6 6 GLN A 185 PHE A 187 5 3
HELIX 7 7 SER A 200 SER A 212 1 13
HELIX 8 8 SER A 215 PHE A 219 5 5
HELIX 9 9 SER A 237 ASN A 251 1 15
HELIX 10 10 SER A 258 LYS A 269 1 12
HELIX 11 11 LYS A 270 GLU A 278 1 9
HELIX 12 12 TRP A 279 LEU A 282 5 4
HELIX 13 13 SER A 304 SER A 311 1 8
HELIX 14 14 GLY A 328 ALA A 336 1 9
HELIX 15 15 SER A 348 VAL A 360 1 13
HELIX 16 16 ASN A 364 THR A 376 1 13
HELIX 17 17 ASN A 383 VAL A 400 1 18
HELIX 18 18 VAL A 400 GLY A 415 1 16
HELIX 19 19 PRO A 433 GLY A 437 5 5
HELIX 20 20 GLU A 443 PHE A 448 1 6
HELIX 21 21 GLY A 449 VAL A 453 5 5
HELIX 22 22 VAL A 453 ASN A 457 5 5
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 AA 3 LEU A 7 THR A 10 0
SHEET 2 AA 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AB11 THR A 18 PRO A 21 0
SHEET 2 AB11 HIS A 26 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 AB11 TYR A 96 VAL A 101 -1 O LEU A 97 N ILE A 33
SHEET 4 AB11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AB11 THR A 109 ILE A 115 1 O THR A 110 N VAL A 142
SHEET 6 AB11 GLY A 189 GLU A 199 1 N ASP A 190 O THR A 109
SHEET 7 AB11 ARG A 221 GLN A 225 1 O ARG A 221 N ILE A 196
SHEET 8 AB11 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AB11 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AB11 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AB11 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 2.08
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.00
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.14
LINK ND2 ASN A 59 C1 NAG A1539 1555 1555 1.48
LINK ND2 ASN A 416 C1 NAG A1538 1555 1555 1.46
CISPEP 1 SER A 103 PRO A 104 0 4.06
SITE 1 AC1 5 GLY A 117 GLY A 118 PHE A 330 HIS A 440
SITE 2 AC1 5 HOH A2030
SITE 1 AC2 6 GLY A 118 GLY A 119 TYR A 121 PHE A 330
SITE 2 AC2 6 PHE A 331 HOH A2091
SITE 1 AC3 4 ASN A 416 GLY A 417 HOH A2092 HOH A2093
SITE 1 AC4 4 MET A 16 ASN A 59 SER A 61 THR A 62
CRYST1 113.950 113.950 138.050 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 0.008776 0.005067 0.000000 0.00000
SCALE2 0.000000 0.010133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007244 0.00000
TER 4242 THR A 535
MASTER 687 0 4 25 14 0 6 6 4377 1 51 42
END
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