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HEADER HYDROLASE/TOXIN 08-MAR-10 2X8B
TITLE CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE INHIBITED
TITLE 2 BY AGED TABUN AND COMPLEXED WITH FASCICULIN-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETHYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: S203 IS PHOSPHORAMIDYLATED;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: FASCICULIN-2;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: FASCICULIN-II, ACETYLCHOLINESTERASE TOXIN F-VII,
COMPND 12 TOXIN TA1, FAS-2, FAS2, FAS-II
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CHO-K1;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 13 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 14 ORGANISM_TAXID: 8618
KEYWDS HYDROLASE-TOXIN COMPLEX, CELL JUNCTION, HYDROLASE,
KEYWDS 2 GPI-ANCHOR, NEUROTRANSMITTER DEGRADATION, TABUN, AGING,
KEYWDS 3 SERINE ESTERASE, BLOOD GROUP ANTIGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.CARLETTI,J.P.COLLETIER,F.NACHON
REVDAT 1 28-APR-10 2X8B 0
JRNL AUTH E.CARLETTI,J.P.COLLETIER,F.DUPEUX,M.TROVASLET,
JRNL AUTH 2 P.MASSON,F.NACHON
JRNL TITL STRUCTURAL EVIDENCE THAT HUMAN
JRNL TITL 2 ACETYLCHOLINESTERASE INHIBITED BY TABUN AGES
JRNL TITL 3 THROUGH O-DEALKYLATION
JRNL REF J.MED.CHEM. 2010
JRNL REFN ESSN 1520-4804
JRNL DOI 10.1021/JM901853B
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 2.950
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.264
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.82
REMARK 3 NUMBER OF REFLECTIONS : 22941
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) : 0.1867
REMARK 3 R VALUE (WORKING SET) : 0.1832
REMARK 3 FREE R VALUE : 0.2527
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1145
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4655
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.4
REMARK 3 B22 (A**2) : 17.4
REMARK 3 B33 (A**2) : -34.8
REMARK 3 B12 (A**2) : 0.00
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2X8B COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-09
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) : 0.933
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.95
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.51
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 7
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.2
REMARK 200 R MERGE FOR SHELL (I) : 0.06
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XDS
REMARK 200 STARTING MODEL: PDB ENTRY 1FSS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES BUFFER PH 7.4, 1.3
REMARK 280 M AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 75.65500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.67943
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.41333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 75.65500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.67943
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.41333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 75.65500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.67943
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.41333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 75.65500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.67943
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.41333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 75.65500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.67943
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 82.41333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 75.65500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.67943
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 82.41333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 87.35887
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 164.82667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 87.35887
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 164.82667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 87.35887
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 164.82667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 87.35887
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 164.82667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 87.35887
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 164.82667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 87.35887
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 164.82667
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: 4160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 GLU A 548
REMARK 465 ALA A 549
REMARK 465 GLU A 550
REMARK 465 ARG A 551
REMARK 465 GLN A 552
REMARK 465 TRP A 553
REMARK 465 LYS A 554
REMARK 465 ALA A 555
REMARK 465 GLU A 556
REMARK 465 PHE A 557
REMARK 465 HIS A 558
REMARK 465 ARG A 559
REMARK 465 TRP A 560
REMARK 465 SER A 561
REMARK 465 SER A 562
REMARK 465 TYR A 563
REMARK 465 MET A 564
REMARK 465 VAL A 565
REMARK 465 HIS A 566
REMARK 465 TRP A 567
REMARK 465 LYS A 568
REMARK 465 ASN A 569
REMARK 465 GLN A 570
REMARK 465 PHE A 571
REMARK 465 ASP A 572
REMARK 465 HIS A 573
REMARK 465 TYR A 574
REMARK 465 SER A 575
REMARK 465 LYS A 576
REMARK 465 GLN A 577
REMARK 465 ASP A 578
REMARK 465 ARG A 579
REMARK 465 CYS A 580
REMARK 465 SER A 581
REMARK 465 ASP A 582
REMARK 465 LEU A 583
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 ASP A 494 CG OD1 OD2
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 ALA A 6 -64.01 66.40
REMARK 500 PHE A 47 -8.05 75.81
REMARK 500 ASP A 95 84.80 -62.38
REMARK 500 ARG A 107 126.05 -36.02
REMARK 500 THR A 109 -88.09 -84.74
REMARK 500 ARG A 143 79.35 23.79
REMARK 500 PRO A 162 133.72 -39.21
REMARK 500 SEN A 203 -115.23 65.24
REMARK 500 PRO A 217 -9.60 -52.54
REMARK 500 ALA A 231 140.07 -178.25
REMARK 500 GLN A 291 171.69 94.63
REMARK 500 GLU A 292 70.85 47.67
REMARK 500 ASP A 306 -89.23 -88.40
REMARK 500 GLN A 369 93.50 18.02
REMARK 500 HIS A 387 59.47 -143.74
REMARK 500 VAL A 407 -69.80 -131.00
REMARK 500 ASN A 464 49.60 -105.64
REMARK 500 GLU A 491 128.46 -32.44
REMARK 500 PRO A 492 -40.92 -27.44
REMARK 500 ARG A 493 93.05 -161.69
REMARK 500 LYS A 496 44.37 -88.62
REMARK 500 THR A 545 41.08 -80.27
REMARK 500 HIS B 6 -179.56 -178.32
REMARK 500 THR B 7 -165.97 -124.97
REMARK 500 ASN B 20 -156.83 101.87
REMARK 500 ASP B 45 -166.88 -172.28
REMARK 500 THR B 54 -42.51 -132.41
REMARK 500 ASP B 57 116.90 82.04
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 CL A1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1559
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FSC RELATED DB: PDB
REMARK 900 FASCICULIN 2 (SYNCHROTRON X-RAY DIFFRACTION)
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2CLJ RELATED DB: PDB
REMARK 900 HOMOLOGY-BUILT MODEL OF HUMAN
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 FASCICULIN-II,GLYCOSYLATED PROTEIN
REMARK 900 RELATED ID: 1PUV 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: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900 II
REMARK 900 RELATED ID: 1PUW 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: 1VZJ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE TETRAMERIZATION DOMAIN OF
REMARK 900 ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF
REMARK 900 A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE
REMARK 900 HELIX
REMARK 900 RELATED ID: 1F8U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT E202Q OF
REMARK 900 HUMANACETYLCHOLINESTERASE COMPLEXED WITH GREEN
REMARK 900 MAMBA VENOMPEPTIDE FASCICULIN-II
DBREF 2X8B A 1 583 UNP P22303 ACES_HUMAN 32 614
DBREF 2X8B B 1 61 UNP P0C1Z0 TXFA2_DENAN 1 61
SEQRES 1 A 583 GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG
SEQRES 2 A 583 GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY
SEQRES 3 A 583 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 583 PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO
SEQRES 5 A 583 LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE
SEQRES 6 A 583 GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 583 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 583 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 583 TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP
SEQRES 10 A 583 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU
SEQRES 11 A 583 ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG
SEQRES 12 A 583 THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE
SEQRES 13 A 583 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 583 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 583 VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR
SEQRES 16 A 583 SER VAL THR LEU PHE GLY GLU SEN ALA GLY ALA ALA SER
SEQRES 17 A 583 VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU
SEQRES 18 A 583 PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY
SEQRES 19 A 583 PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG
SEQRES 20 A 583 ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 583 GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU
SEQRES 22 A 583 ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP
SEQRES 23 A 583 HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE
SEQRES 24 A 583 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 583 GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN
SEQRES 26 A 583 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 583 LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 583 SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG
SEQRES 29 A 583 VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 583 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 583 PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY
SEQRES 32 A 583 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 583 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL
SEQRES 34 A 583 PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP
SEQRES 35 A 583 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 583 GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU
SEQRES 37 A 583 GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA
SEQRES 38 A 583 ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP
SEQRES 39 A 583 PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA
SEQRES 40 A 583 GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL
SEQRES 41 A 583 ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN
SEQRES 42 A 583 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 A 583 ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU PHE HIS ARG
SEQRES 44 A 583 TRP SER SER TYR MET VAL HIS TRP LYS ASN GLN PHE ASP
SEQRES 45 A 583 HIS TYR SER LYS GLN ASP ARG CYS SER ASP LEU
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
MODRES 2X8B ASN A 350 ASN GLYCOSYLATION SITE
MODRES 2X8B SEN A 203 SER O-[N,N-DIMETHYLPHOSPHORAMIDATE]-L-SERINE
HET SEN A 203 12
HET CL A1549 1
HET CL A1550 1
HET CL A1551 1
HET CL A1552 1
HET CL A1553 1
HET CL A1554 1
HET SO4 A1555 5
HET UNX A1556 1
HET UNX A1557 1
HET NAG A1558 14
HET NAG A1559 14
HET CL A1560 1
HET CL A1561 1
HET CL A1562 1
HET CL A1563 1
HET CL A1564 1
HET UNX A1565 1
HETNAM SEN O-[N,N-DIMETHYLPHOSPHORAMIDATE]-L-SERINE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 1 SEN C5 H13 N2 O5 P
FORMUL 2 CL 11(CL 1-)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 UNX 3(X)
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 6 HOH *236(H2 O)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ARG A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 VAL A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SEN A 203 LEU A 213 1 11
HELIX 9 9 SER A 215 GLY A 220 1 6
HELIX 10 10 GLY A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 HIS A 284 1 8
HELIX 13 13 GLU A 285 LEU A 289 5 5
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 GLY A 342 5 8
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 THR A 466 GLY A 487 1 22
HELIX 24 24 ARG A 525 ARG A 534 1 10
HELIX 25 25 PHE A 535 THR A 545 1 11
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 LEU A 22 0
SHEET 2 AB11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 11 AB11 VAL A 520 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AC 2 ALA A 38 GLU A 39 0
SHEET 2 AC 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 AD 2 VAL A 68 CYS A 69 0
SHEET 2 AD 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 2 MET B 2 SER B 5 0
SHEET 2 BA 2 ILE B 13 ASN B 16 -1 O ILE B 13 N SER B 5
SHEET 1 BB 3 VAL B 34 CYS B 39 0
SHEET 2 BB 3 CYS B 22 ARG B 27 -1 O TYR B 23 N GLY B 38
SHEET 3 BB 3 LEU B 48 CYS B 53 -1 O GLU B 49 N SER B 26
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 3 CYS B 22 1555 1555 2.03
SSBOND 5 CYS B 17 CYS B 39 1555 1555 2.04
SSBOND 6 CYS B 41 CYS B 52 1555 1555 2.04
SSBOND 7 CYS B 53 CYS B 59 1555 1555 2.03
LINK C GLU A 202 N SEN A 203 1555 1555 1.33
LINK C SEN A 203 N ALA A 204 1555 1555 1.33
LINK ND2 ASN A 350 C1 NAG A1558 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 1.28
CISPEP 2 CYS A 257 PRO A 258 0 -5.78
CISPEP 3 PRO A 495 LYS A 496 0 -4.88
CISPEP 4 PRO B 30 PRO B 31 0 1.79
SITE 1 AC1 1 ARG A 478
SITE 1 AC2 2 ARG A 296 GLN A 369
SITE 1 AC3 1 ARG B 11
SITE 1 AC4 2 GLY A 242 HOH A2098
SITE 1 AC5 1 ARG A 417
SITE 1 AC6 1 ARG A 356
SITE 1 AC7 2 ARG A 16 GLY A 58
SITE 1 AC8 1 ARG A 136
SITE 1 AC9 1 ARG A 224
SITE 1 BC1 3 ARG A 525 GLN A 527 ALA A 528
SITE 1 BC2 3 THR A 504 GLY A 506 ALA A 507
SITE 1 BC3 4 SER A 347 ASN A 350 NAG A1559 HOH A2210
SITE 1 BC4 5 GLY A 345 NAG A1558 HOH A2211 HOH A2212
SITE 2 BC4 5 HOH A2214
CRYST1 151.310 151.310 247.240 90.00 90.00 120.00 H 3 2 18
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 0.006609 0.003816 0.000000 0.00000
SCALE2 0.000000 0.007631 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004045 0.00000
END |