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HEADER HYDROLASE 14-OCT-05 2BAG
TITLE 3D STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
TITLE 2 COMPLEXED WITH GANSTIGMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
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 VARIANT: G2 FORM;
SOURCE 5 ORGAN: ELETRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS SERINE HYDROLASE, CHOLINESTERASE, NEUROTRANSMITTER CLEAVAGE,
KEYWDS 2 ANTI-ALZHEIMER DRUG
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LAMBA,C.BARTOLUCCI,M.SIOTTO,M.RACCHI,G.VILLETTI,
AUTHOR 2 M.DELCANALE
REVDAT 1 29-AUG-06 2BAG 0
JRNL AUTH C.BARTOLUCCI,M.SIOTTO,E.GHIDINI,G.AMARI,
JRNL AUTH 2 P.T.BOLZONI,M.RACCHI,G.VILLETTI,M.DELCANALE,D.LAMBA
JRNL TITL STRUCTURAL DETERMINANTS OF TORPEDO CALIFORNICA
JRNL TITL 2 ACETYLCHOLINESTERASE INHIBITION BY THE NOVEL AND
JRNL TITL 3 ORALLY ACTIVE CARBAMATE BASED ANTI-ALZHEIMER DRUG
JRNL TITL 4 GANSTIGMINE (CHF-2819)
JRNL REF J.MED.CHEM. V. 49 5051 2006
JRNL REFN ASTM JMCMAR US ISSN 0022-2623
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.BARTOLUCCI,E.PEROLA,L.CELLAI,M.BRUFANI,D.LAMBA
REMARK 1 TITL BACK DOOR OPENING IMPLIED BY THE CRYSTAL STRUCTURE
REMARK 1 TITL 2 OF A CARBAMOYLATED ACETYLCHOLINESTERASE
REMARK 1 REF BIOCHEMISTRY V. 38 5714 1999
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.BAR-ON,C.B.MILLARD,M.HAREL,H.DVIR,A.ENZ,
REMARK 1 AUTH 2 J.L.SUSSMAN,I.SILMAN
REMARK 1 TITL KINETIC AND STRUCTURAL STUDIES ON THE INTERACTION
REMARK 1 TITL 2 OF CHOLINESTERASES WITH THE ANTI-ALZHEIMER DRUG
REMARK 1 TITL 3 RIVASTIGMINE
REMARK 1 REF BIOCHEMISTRY V. 41 3555 2002
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.PEROLA,L.CELLAI,D.LAMBA,L.FILOCAMO,M.BRUFANI
REMARK 1 TITL LONG CHAIN ANALOGS OF PHYSOSTIGMINE AS POTENTIAL
REMARK 1 TITL 2 DRUGS FOR ALZHEIMER'S DISEASE: NEW INSIGHTS INTO
REMARK 1 TITL 3 THE MECHANISM OF ACTION IN THE INHIBITION OF
REMARK 1 TITL 4 ACETYLCHOLINESTERASE
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1343 41 1997
REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1599796.360
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 37576
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3762
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 10.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5470
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 624
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 79
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.10000
REMARK 3 B22 (A**2) : 11.10000
REMARK 3 B33 (A**2) : -22.19000
REMARK 3 B12 (A**2) : 7.30000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.079 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.011 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.077 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.080 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 50.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BAG COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-OCT-2005.
REMARK 100 THE RCSB ID CODE IS RCSB034876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI111)
REMARK 200 OPTICS : THREE-SEGMENT PT-COATED
REMARK 200 TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37817
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 27.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.05700
REMARK 200 FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : 0.42200
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG200, 100MM MES, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,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 45.60800
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 91.21600
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 91.21600
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 45.60800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 136.82400
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 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: 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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 90 SD MET A 90 CE 0.062
REMARK 500 MET A 175 SD MET A 175 CE -0.162
REMARK 500 MET A 308 SD MET A 308 CE 0.095
REMARK 500 MET A 379 SD MET A 379 CE 0.073
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, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 93 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASN A 183 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. =-15.1 DEGREES
REMARK 500 ILE A 296 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLY A 328 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 504 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE STRUCTURE HAS BEEN DETERMINED BY SOAKING NATIVE
REMARK 600 ACHE CRYSTALS WITH THE COMPOUND GANSTIGMINE.
REMARK 600 IN THE CRYSTAL, SER200 IS ACYLATED AND THE LEAVING
REMARK 600 GROUP OF THE REACTION, GENESEROLINE, NOT BEING RETAINED
REMARK 600 IN THE ENZYME ACTIVE SITE.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA COMPLEXED
REMARK 900 WITH MF268
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA COMPLEXED
REMARK 900 WITH RIVASTIGMINE
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA COMPLEXED
REMARK 900 WITH 3-[(1S)-1-(DIMETHYLAMINO)ETHYL]PHENOL
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA AT 1.8
DBREF 2BAG 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
MODRES 2BAG ASN A 59 ASN GLYCOSYLATION SITE
MODRES 2BAG ASN A 416 ASN GLYCOSYLATION SITE
HET NAG A1059 14
HET NAG A1416 14
HET 1PE 301 16
HET GSG A1200 11
HET MES 501 12
HET MES 502 12
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM GSG 1S,3AS,8AS-TRIMETHYL-1-OXIDO-1,2,3,3A,8,8A-
HETNAM 2 GSG HEXAHYDROPYRROLO[2,3-B]INDOL-5-YL 2-
HETNAM 3 GSG ETHYLPHENYLCARBAMATE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN NAG NAG
HETSYN 1PE PEG400
HETSYN GSG GANSTIGMINE; (-)-(3AS,8AS,1S)-1,2,3,3A,8A-HEXAHYDRO-1,
HETSYN 2 GSG 3A,8-TRIMETHYLPYRROLO[2,3-B]INDOL-5-OL-2'-
HETSYN 3 GSG ETHYLPHENYLCARBAMATE N-OXIDE HYDROCHLORIDE
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 4 1PE C10 H22 O6
FORMUL 5 GSG C22 H27 N3 O3
FORMUL 6 MES 2(C6 H13 N1 O4 S1)
FORMUL 8 HOH *274(H2 O1)
HELIX 1 1 VAL A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASN A 131 5 5
HELIX 4 4 GLY A 132 GLU A 140 1 9
HELIX 5 5 VAL A 150 LEU A 156 1 7
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 GLN A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 SER A 215 PHE A 219 5 5
HELIX 10 10 VAL A 238 LEU A 252 1 15
HELIX 11 11 SER A 258 LYS A 269 1 12
HELIX 12 12 LYS A 270 GLU A 278 1 9
HELIX 13 13 TRP A 279 LEU A 282 5 4
HELIX 14 14 SER A 304 GLY A 312 1 9
HELIX 15 15 GLY A 328 ALA A 336 1 9
HELIX 16 16 SER A 348 VAL A 360 1 13
HELIX 17 17 ASN A 364 THR A 376 1 13
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 LYS A 413 1 14
HELIX 20 20 PRO A 433 GLY A 437 5 5
HELIX 21 21 GLU A 443 PHE A 448 1 6
HELIX 22 22 GLY A 449 ASN A 457 5 9
HELIX 23 23 THR A 459 GLY A 480 1 22
HELIX 24 24 ARG A 517 GLN A 526 1 10
HELIX 25 25 GLN A 526 THR A 535 1 10
SHEET 1 A 3 LEU A 7 THR A 10 0
SHEET 2 A 3 GLY A 13 MET A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 A 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 B11 THR A 18 VAL A 22 0
SHEET 2 B11 SER A 25 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 B11 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 B11 VAL A 142 SER A 145 -1 O SER A 145 N ASN A 98
SHEET 5 B11 THR A 109 ILE A 115 1 N TRP A 114 O VAL A 144
SHEET 6 B11 GLY A 189 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 B11 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 B11 GLN A 318 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 B11 GLY A 417 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 B11 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 B11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 C 2 VAL A 236 SER A 237 0
SHEET 2 C 2 VAL A 295 ILE A 296 1 O ILE A 296 N VAL A 236
SSBOND 1 CYS A 67 CYS A 94
SSBOND 2 CYS A 254 CYS A 265
SSBOND 3 CYS A 402 CYS A 521
LINK ND2 ASN A 59 C1 NAG A1059
LINK ND2 ASN A 416 C1 NAG A1416
LINK OG SER A 200 C7 GSG A1200
CISPEP 1 SER A 103 PRO A 104 0 0.35
CRYST1 111.736 111.736 136.824 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 0.008950 0.005167 0.000000 0.00000
SCALE2 0.000000 0.010334 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007309 0.00000
TER 4245 THR A 535
MASTER 324 0 6 25 16 0 0 6 4597 1 88 42
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