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HEADER HYDROLASE 21-APR-05 1ZGC
TITLE CRYSTAL STRUCTURE OF TORPEDO CALIFORNICA
TITLE 2 ACETYLCHOLINESTERASE IN COMPLEX WITH AN (RS)-TACRINE(10)-
TITLE 3 HUPYRIDONE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
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
KEYWDS SERINE-HYDROLASE, PROTEIN-INHIBITOR COMPLEX, ENANTIOMERIC
KEYWDS 2 SELECTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HAVIV,D.M.WONG,H.M.GREENBLATT,P.R.CARLIER,Y.P.PANG,
AUTHOR 2 I.SILMAN,J.L.SUSSMAN
REVDAT 1 16-AUG-05 1ZGC 0
JRNL AUTH H.HAVIV,D.M.WONG,H.M.GREENBLATT,P.R.CARLIER,
JRNL AUTH 2 Y.P.PANG,I.SILMAN,J.L.SUSSMAN
JRNL TITL CRYSTAL PACKING MEDIATES ENANTIOSELECTIVE LIGAND
JRNL TITL 2 RECOGNITION AT THE PERIPHERAL SITE OF
JRNL TITL 3 ACETYLCHOLINESTERASE
JRNL REF J.AM.CHEM.SOC. V. 127 11029 2005
JRNL REFN ASTM JACSAT US ISSN 0002-7863
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.CARLIER,D.-M.DU,Y.-F.HAN,J.LIU,Y.-P.PANG
REMARK 1 TITL POTENT, EASILY SYNTHESIZED HUPERZINE A-TACRINE
REMARK 1 TITL 2 HYBRID ACETYLCHOLINESTERASE INHIBITORS
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 9 2335 1999
REMARK 1 REFN ASTM BMCLE8 UK ISSN 0960-894X
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.M.WONG,H.M.GREENBLATT,H.DVIR,P.R.CARLIER,
REMARK 1 AUTH 2 Y.-F.HAN,Y.-P.PANG,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL ACETYLCHOLINESTERASE COMPLEXED WITH BIVALENT
REMARK 1 TITL 2 LIGANDS RELATED TO HUPERZINE A: EXPERIMENTAL
REMARK 1 TITL 3 EVIDENCE FOR SPECIES-DEPENDENT PROTEIN-LIGAND
REMARK 1 TITL 4 COMPLEMENTARITY
REMARK 1 REF J.AM.CHEM.SOC. V. 125 363 2003
REMARK 1 REFN ASTM JACSAT US ISSN 0002-7863
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.M.GREENBLATT,C.GUILLOU,D.GUENARD,A.ARGAMAN,
REMARK 1 AUTH 2 S.BOTTI,B.BADET,C.THAL,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL THE COMPLEX OF A BIVALENT DERIVATIVE OF
REMARK 1 TITL 2 GALANTHAMINE WITH TORPEDO ACETYLCHOLINESTERASE
REMARK 1 TITL 3 DISPLAYS DRASTIC DEFORMATION OF THE ACTIVE-SITE
REMARK 1 TITL 4 GORGE: IMPLICATIONS FOR STRUCTURE-BASED DRUG DESIGN
REMARK 1 REF J.AM.CHEM.SOC. V. 126 15405 2004
REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,
REMARK 1 AUTH 2 L.TOKER,I.SILMAN
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN
REMARK 1 REF SCIENCE V. 253 872 1991
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 80089
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4157
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5649
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 273
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 8854
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : 3.46000
REMARK 3 B33 (A**2) : -1.99000
REMARK 3 B12 (A**2) : 0.00000
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): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.485
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8774 ; 0.036 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 7701 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11922 ; 2.506 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17917 ; 1.246 ; 2.988
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1052 ; 7.574 ; 5.000
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): 1253 ; 0.199 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9755 ; 0.017 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1864 ; 0.019 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1831 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8837 ; 0.259 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 4848 ; 0.103 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 419 ; 0.140 ; 0.200
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): 12 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 20 ; 0.351 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.116 ; 0.200
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): 5252 ; 1.406 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8479 ; 2.292 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3522 ; 3.612 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3443 ; 5.237 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1ZGC COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-2005.
REMARK 100 THE RCSB ID CODE IS RCSB032687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-2003
REMARK 200 TEMPERATURE (KELVIN) : 120.0
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 RU-H3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC BLUE CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : STRATEGY
REMARK 200 DATA SCALING SOFTWARE : TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84805
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 34.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 0.610
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.830
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XTALVIEW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 200, PH 5.8, TEMPERATURE 277K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP. PROTEIN WAS CRYSTALLISED FROM
REMARK 280 28-30% V/V PEG 200 0.5 M MES PH 5.8 AT 277K, WITHOUT SEEDING
REMARK 280 WITH MICROCRYSTALS; THEN SOAKED IN MOTHER LIQUOR (40% V/V PEG
REMARK 280 200 IN 0.1 M MES BUFFER, PH 5.8) CONTAINING 4MM (RS)-(+/-)-
REMARK 280 TACRINE(10)-HUPYRIDONE ((5RS)-(+/-)-5-{[10-(1,2,3,4-
REMARK 280 TETRAHYDROACRIDIN-9-YLAMINO)DECYL]AMINO}5,6,7,8-TETRAHYDRO-
REMARK 280 QUINOLIN-2(1H)-ONE) BIS-OXALATE FOR 40 HOURS.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 -1.000000 0.000000 0.000000 45.49800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.22400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.77150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.22400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.49800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.77150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 2 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, 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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 486
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 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 486
REMARK 465 SER B 487
REMARK 465 GLN B 488
REMARK 465 GLU B 489
REMARK 465 ALA B 536
REMARK 465 CYS B 537
REMARK 465 ASP B 538
REMARK 465 GLY B 539
REMARK 465 GLU B 540
REMARK 465 LEU B 541
REMARK 465 SER B 542
REMARK 465 SER B 543
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 ARG A 46 CZ NH1 NH2
REMARK 470 GLU A 49 OE1
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 LYS A 270 CE NZ
REMARK 470 GLU A 299 CD OE1 OE2
REMARK 470 LYS A 357 NZ
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 LYS A 454 CG CD CE NZ
REMARK 470 GLU A 455 CG CD OE1 OE2
REMARK 470 LYS A 478 CD CE NZ
REMARK 470 THR A 497 CG2
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 ARG A 515 CZ NH1 NH2
REMARK 470 ARG B 46 CZ NH1 NH2
REMARK 470 GLU B 268 OE1 OE2
REMARK 470 LYS B 346 NZ
REMARK 470 MET B 379 CE
REMARK 470 LYS B 413 NZ
REMARK 470 LYS B 454 CD CE NZ
REMARK 470 GLU B 461 OE1 OE2
REMARK 470 LYS B 530 CE NZ
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 LYS A 11 CD LYS A 11 CE 0.217
REMARK 500 LYS A 11 CE LYS A 11 NZ 0.247
REMARK 500 MET A 16 SD MET A 16 CE -0.379
REMARK 500 MET A 175 SD MET A 175 CE -0.494
REMARK 500 MET A 353 SD MET A 353 CE 0.310
REMARK 500 MET A 379 SD MET A 379 CE 0.241
REMARK 500 PRO A 485 CB PRO A 485 CG 0.221
REMARK 500 MET B 16 SD MET B 16 CE 0.273
REMARK 500 LYS B 51 CE LYS B 51 NZ 0.384
REMARK 500 MET B 175 SD MET B 175 CE -0.621
REMARK 500 MET B 308 SD MET B 308 CE -0.232
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 LYS A 11 CD - CE - NZ ANGL. DEV. = 21.8 DEGREES
REMARK 500 ARG A 88 CG - CD - NE ANGL. DEV. =-17.0 DEGREES
REMARK 500 ARG A 243 CG - CD - NE ANGL. DEV. =-15.0 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 517 CG - CD - NE ANGL. DEV. =-14.9 DEGREES
REMARK 500 LEU A 531 CB - CG - CD1 ANGL. DEV. = 15.6 DEGREES
REMARK 500 LYS B 11 CD - CE - NZ ANGL. DEV. = 16.0 DEGREES
REMARK 500 LYS B 51 CG - CD - CE ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU B 494 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 200 -117.86 56.52
REMARK 500 SER B 200 -112.95 58.47
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 GLU A 484 PRO A 485 139.07
REMARK 500 SER A 490 LYS A 491 -141.18
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN COMPLEX WITH (R)-
REMARK 900 TACRINE(10)-HUPYRIDONE INHIBITOR
DBREF 1ZGC A 1 543 SWS P04058 ACES_TORCA 22 564
DBREF 1ZGC B 1 543 SWS 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
SEQRES 1 B 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
MODRES 1ZGC ASN A 59 ASN GLYCOSYLATION SITE
MODRES 1ZGC ASN A 416 ASN GLYCOSYLATION SITE
MODRES 1ZGC ASN A 457 ASN GLYCOSYLATION SITE
MODRES 1ZGC ASN B 59 ASN GLYCOSYLATION SITE
MODRES 1ZGC ASN B 416 ASN GLYCOSYLATION SITE
HET NAG A1059 14
HET NAG A1416 14
HET NAG A1457 14
HET NAG B1592 14
HET NAG B4162 14
HET A2E 1001 37
HET A2E 1002 37
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM A2E (5S)-5-{[10-(1,2,3,4-TETRAHYDROACRIDIN-9-YLAMINO)
HETNAM 2 A2E DECYL]AMINO}-5,6,7,8-TETRAHYDROQUINOLIN-2(1H)-ONE
HETSYN NAG NAG
HETSYN A2E (S)-N-9 -(1 ,2 ,3 ,4 -TETRAHYDROACRIDINYL)-N'-5 -[5 ,
HETSYN 2 A2E 6 ,7 ,8 -TETRAHYDRO-2'(1'H)-QUINOLINONYL]-1,10-
HETSYN 3 A2E DIAMINODECANE; (S)-TACRINE(10)-HUPYRIDONE
FORMUL 3 NAG 5(C8 H15 N1 O6)
FORMUL 8 A2E 2(C32 H44 N4 O1)
FORMUL 10 HOH *341(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 GLY A 151 LEU A 156 1 6
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 PRO A 213 PHE A 219 5 7
HELIX 10 10 VAL A 238 LEU A 252 1 15
HELIX 11 11 SER A 258 GLU A 268 1 11
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
HELIX 26 26 VAL B 40 ARG B 44 5 5
HELIX 27 27 PHE B 78 MET B 83 1 6
HELIX 28 28 LEU B 127 ASN B 131 5 5
HELIX 29 29 GLY B 132 GLU B 140 1 9
HELIX 30 30 GLY B 151 LEU B 156 1 6
HELIX 31 31 ASN B 167 ILE B 184 1 18
HELIX 32 32 GLN B 185 PHE B 187 5 3
HELIX 33 33 SER B 200 SER B 212 1 13
HELIX 34 34 SER B 212 ASP B 217 1 6
HELIX 35 35 VAL B 238 LEU B 252 1 15
HELIX 36 36 SER B 258 ARG B 267 1 10
HELIX 37 37 LYS B 270 GLU B 278 1 9
HELIX 38 38 TRP B 279 LEU B 282 5 4
HELIX 39 39 SER B 304 GLY B 312 1 9
HELIX 40 40 GLY B 328 ALA B 336 1 9
HELIX 41 41 SER B 348 VAL B 360 1 13
HELIX 42 42 ASN B 364 THR B 376 1 13
HELIX 43 43 ASN B 383 VAL B 400 1 18
HELIX 44 44 VAL B 400 GLY B 415 1 16
HELIX 45 45 PRO B 433 GLY B 437 5 5
HELIX 46 46 GLU B 443 PHE B 448 1 6
HELIX 47 47 GLY B 449 ASN B 457 5 9
HELIX 48 48 THR B 459 GLY B 480 1 22
HELIX 49 49 ARG B 517 GLN B 526 1 10
HELIX 50 50 GLN B 526 THR B 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 LYS A 14
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 ILE A 503 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
SHEET 1 D 3 LEU B 7 THR B 10 0
SHEET 2 D 3 GLY B 13 MET B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 D 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 E11 THR B 18 VAL B 22 0
SHEET 2 E11 SER B 25 PRO B 34 -1 O ILE B 27 N VAL B 20
SHEET 3 E11 TYR B 96 VAL B 101 -1 O ILE B 99 N PHE B 30
SHEET 4 E11 VAL B 142 SER B 145 -1 O SER B 145 N ASN B 98
SHEET 5 E11 THR B 109 ILE B 115 1 N TRP B 114 O VAL B 144
SHEET 6 E11 GLY B 189 GLU B 199 1 O THR B 195 N VAL B 113
SHEET 7 E11 ARG B 221 GLN B 225 1 O ILE B 223 N ILE B 196
SHEET 8 E11 ILE B 319 ASN B 324 1 O LEU B 320 N LEU B 224
SHEET 9 E11 THR B 418 PHE B 423 1 O PHE B 423 N VAL B 323
SHEET 10 E11 LYS B 501 LEU B 505 1 O LEU B 505 N PHE B 422
SHEET 11 E11 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 F 2 VAL B 236 SER B 237 0
SHEET 2 F 2 VAL B 295 ILE B 296 1 O ILE B 296 N VAL B 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
SSBOND 4 CYS B 67 CYS B 94
SSBOND 5 CYS B 254 CYS B 265
SSBOND 6 CYS B 402 CYS B 521
LINK ND2 ASN A 59 C1 NAG A1059
LINK ND2 ASN A 416 C1 NAG A1416
LINK ND2 ASN A 457 C1 NAG A1457
LINK ND2 ASN B 59 C1 NAG B1592
LINK ND2 ASN B 416 C1 NAG B4162
CISPEP 1 SER A 103 PRO A 104 0 3.05
CISPEP 2 SER B 103 PRO B 104 0 3.17
CRYST1 90.996 105.543 150.448 90.00 90.00 90.00 P 21 21 21 8
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 0.010989 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006647 0.00000
TER 4175 THR A 535
TER 8371 THR B 535
MASTER 407 0 7 50 32 0 0 6 8854 2 161 84
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