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HEADER HYDROLASE 09-DEC-07 2VJB
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
TITLE 2 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
TITLE 3 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP -
TITLE 4 DATASET D AT 100K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 22-558;
COMPND 5 SYNONYM: ACHE;
COMPND 6 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: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS SERINE ESTERASE, ALTERNATIVE SPLICING, NEUROTRANSMITTER
KEYWDS 2 DEGRADATION, KINETIC CRYSTALLOGRAPHY, STRUCTURAL DYNAMICS,
KEYWDS 3 XRAY DAMAGE, SUBSTRATE ANALOGUE, LIPOPROTEIN,
KEYWDS 4 GLYCOPROTEIN, CELL JUNCTION, SYNAPSE, MEMBRANE, HYDROLASE,
KEYWDS 5 GPI-ANCHOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-P.COLLETIER,D.BOURGEOIS,D.FOURNIER,I.SILMAN,J.L.SUSSMAN,
AUTHOR 2 M.WEIK
REVDAT 1 22-JUL-08 2VJB 0
JRNL AUTH J.-P.COLLETIER,D.BOURGEOIS,
JRNL AUTH 2 D.FOURNIER,I.SILMAN,J.L.SUSSMAN,
JRNL AUTH 3 M.WEIK
JRNL TITL SHOOT TO SNAP : SPECIFIC X-RAY DAMAGE AS A METHOD
JRNL TITL 2 TO STUDY STRUCTURAL DYNAMICS IN CRYSTALLINE
JRNL TITL 3 PROTEINS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 3716067.50
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 59257
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 : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2963
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 30.3
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3196
REMARK 3 BIN R VALUE (WORKING SET) : 0.318
REMARK 3 BIN FREE R VALUE : 0.354
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 BIN FREE R VALUE SET COUNT : 168
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 130
REMARK 3 SOLVENT ATOMS : 1601
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.13
REMARK 3 B22 (A**2) : 20.37
REMARK 3 B33 (A**2) : -13.24
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.35
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.25 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.05 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.02 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.02 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 57.1714
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 PARAMETER FILE 5 : AS.PARAM
REMARK 3 TOPOLOGY FILE 5 : AS.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2VJB COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 10-DEC-2007.
REMARK 100 THE EBI ID CODE IS EBI-34719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-2006
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.932240
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 : 59627
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.2
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.80
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) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1W75
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG200, 150MM MES, PH6, 4
REMARK 280 DEG. C. 2 HOURS SOAKING IN MOTHER LIQUOR SOLUTION
REMARK 280 CONTAINING 0.5 MM OTMA
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 46.03500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.74500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.64500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.74500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.03500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.64500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 O HOH B 2584 - O HOH B 2663 2.15
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 SER A 25 -165.75 179.83
REMARK 500 PHE A 45 -8.07 75.57
REMARK 500 SER A 108 58.61 38.52
REMARK 500 HIS A 159 137.52 -39.47
REMARK 500 ALA A 164 65.51 -155.06
REMARK 500 SER A 200 -112.21 55.55
REMARK 500 THR A 317 -154.25 -155.28
REMARK 500 ASN A 364 -168.40 -78.94
REMARK 500 ASP A 380 54.19 -172.10
REMARK 500 VAL A 400 -71.33 -126.07
REMARK 500 LYS A 498 -71.32 -66.01
REMARK 500 GLN A 526 -54.31 -121.69
REMARK 500 PHE B 45 -12.60 80.98
REMARK 500 ALA B 60 55.26 -116.42
REMARK 500 SER B 108 70.12 -157.02
REMARK 500 PHE B 155 12.10 -142.80
REMARK 500 SER B 200 -116.52 55.03
REMARK 500 GLU B 299 -79.55 -116.62
REMARK 500 THR B 317 -158.87 -148.67
REMARK 500 ASP B 342 40.04 -103.65
REMARK 500 VAL B 360 70.25 -119.76
REMARK 500 ASP B 380 53.06 -165.22
REMARK 500 VAL B 400 -66.60 -125.50
REMARK 500 PRO B 485 150.90 -48.59
REMARK 500 HIS B 486 36.38 36.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 4-OXO-N,N,N- TRIMETHYLPENTANAMINIUM (CCD): ALREADY PRESENT
REMARK 600 IN PDB ENTRY 2C5F - IT IS COVALENTLY BOUND TO CATALYTIC
REMARK 600 SERINE 200
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCD A 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCD A 1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCD B 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CCD B 1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 1541
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: 2VQ6 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH 2-PAM
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: 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: 2VT6 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 COLLECTED WITH A CUMULATED DOSE OF 9400000
REMARK 900 GY
REMARK 900 RELATED ID: 2VT7 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 COLLECTED WITH A CUMULATED DOSE OF 800000
REMARK 900 GY
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL
REMARK 900 SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 REVEALED BY THE COMPLEX STRUCTURE WITH A
REMARK 900 BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT I) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH
REMARK 900 (+)-HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-
REMARK 900 HEPTYLENE-BIS-N,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 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: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-
REMARK 900 PROPYLENE-BIS-N,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 2V98 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-
REMARK 900 ARSENOCHOLINE AFTER A 9 SECONDS ANNEALING TO
REMARK 900 ROOM TEMPERATURE, DURING HTE FIRST 5
REMARK 900 SECONDS OF WHICH LASER IRRADIATION AT 266NM
REMARK 900 TOOK PLACE
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 HUPERZINE B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT E) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900 II
REMARK 900 RELATED ID: 2V97 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF
REMARK 900 TCACHE WITH 1-(2-NITROPHENYL)-2,2,2-
REMARK 900 TRIFLUOROETHYL-ARSENOCHOLINE AFTER A 9 SECONDS
REMARK 900 ANNEALING TO ROOM TEMPERATURE
DBREF 2VJB A 1 537 UNP P04058 ACES_TORCA 22 558
DBREF 2VJB B 1 537 UNP P04058 ACES_TORCA 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
SEQRES 1 B 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 537 ALA THR ALA CYS
HET NAG A1536 14
HET NAG A1537 14
HET NAG B1536 14
HET NAG B1537 14
HET CL A1538 1
HET CL A1543 1
HET CL B1538 1
HET CL A1544 1
HET CCD A1539 10
HET CCD A1540 10
HET CCD B1539 10
HET CCD B1540 10
HET PGE A1541 10
HET PGE A1542 10
HET PGE B1541 10
HETNAM CCD (4R)-4-HYDROXY-N,N,N-TRIMETHYLPENTAN-1-
HETNAM 2 CCD AMINIUM
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 CCD 4(C8 H20 N O 1+)
FORMUL 4 CL 4(CL 1-)
FORMUL 5 PGE 3(C6 H14 O4)
FORMUL 6 NAG 4(C8 H15 N O6)
FORMUL 7 HOH *1601(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 SER A 212 ASP A 217 1 6
HELIX 10 10 VAL A 238 LEU A 252 1 15
HELIX 11 11 SER A 258 ARG A 267 1 10
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 TYR A 375 1 12
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 VAL A 453 5 5
HELIX 23 23 VAL A 453 ASN A 457 5 5
HELIX 24 24 THR A 459 GLY A 480 1 22
HELIX 25 25 ARG A 517 GLN A 526 1 10
HELIX 26 26 GLN A 526 THR A 535 1 10
HELIX 27 27 VAL B 40 ARG B 44 5 5
HELIX 28 28 PHE B 78 MET B 83 1 6
HELIX 29 29 LEU B 127 ASN B 131 5 5
HELIX 30 30 GLY B 132 GLU B 140 1 9
HELIX 31 31 VAL B 150 LEU B 156 1 7
HELIX 32 32 ASN B 167 ILE B 184 1 18
HELIX 33 33 GLN B 185 PHE B 187 5 3
HELIX 34 34 SER B 200 SER B 212 1 13
HELIX 35 35 SER B 215 PHE B 219 5 5
HELIX 36 36 SER B 237 ASN B 251 1 15
HELIX 37 37 SER B 258 LYS B 269 1 12
HELIX 38 38 LYS B 270 GLU B 278 1 9
HELIX 39 39 TRP B 279 LEU B 282 5 4
HELIX 40 40 SER B 304 SER B 311 1 8
HELIX 41 41 GLY B 328 ALA B 336 1 9
HELIX 42 42 SER B 348 VAL B 360 1 13
HELIX 43 43 ASN B 364 TYR B 375 1 12
HELIX 44 44 ASN B 383 VAL B 400 1 18
HELIX 45 45 VAL B 400 THR B 412 1 13
HELIX 46 46 PRO B 433 GLY B 437 5 5
HELIX 47 47 GLU B 443 PHE B 448 1 6
HELIX 48 48 GLY B 449 VAL B 453 5 5
HELIX 49 49 VAL B 453 ASN B 457 5 5
HELIX 50 50 THR B 459 GLY B 480 1 22
HELIX 51 51 ARG B 517 GLN B 526 1 10
HELIX 52 52 GLN B 526 ALA B 534 1 9
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 PRO A 102 -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
SHEET 1 AC 2 VAL A 236 SER A 237 0
SHEET 2 AC 2 VAL A 295 ILE A 296 1 N ILE A 296 O VAL A 236
SHEET 1 BA 3 LEU B 7 THR B 10 0
SHEET 2 BA 3 GLY B 13 MET B 16 -1 O GLY B 13 N THR B 10
SHEET 3 BA 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 BB11 THR B 18 VAL B 22 0
SHEET 2 BB11 SER B 25 PRO B 34 -1 O SER B 25 N VAL B 22
SHEET 3 BB11 TYR B 96 VAL B 101 -1 O LEU B 97 N ILE B 33
SHEET 4 BB11 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 BB11 THR B 109 ILE B 115 1 O THR B 110 N VAL B 142
SHEET 6 BB11 GLY B 189 GLU B 199 1 N ASP B 190 O THR B 109
SHEET 7 BB11 ARG B 221 GLN B 225 1 O ARG B 221 N ILE B 196
SHEET 8 BB11 ILE B 319 ASN B 324 1 O LEU B 320 N LEU B 224
SHEET 9 BB11 THR B 418 PHE B 423 1 O TYR B 419 N LEU B 321
SHEET 10 BB11 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 BB11 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.04
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.04
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.05
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.04
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.04
LINK ND2 ASN A 59 C1 NAG A1536 1555 1555 1.45
LINK OG SER A 200 C5 CCD A1539 1555 1555 1.43
LINK ND2 ASN A 416 C1 NAG A1537 1555 1555 1.45
LINK ND2 ASN B 59 C1 NAG B1536 1555 1555 1.45
LINK OG SER B 200 C5 CCD B1539 1555 1555 1.43
LINK ND2 ASN B 416 C1 NAG B1537 1555 1555 1.45
CISPEP 1 SER A 103 PRO A 104 0 0.20
CISPEP 2 SER B 103 PRO B 104 0 0.18
SITE 1 AC1 11 ASN A 59 SER A 61 HOH A2836 HOH A2837
SITE 2 AC1 11 HOH A2838 HOH A2839 HOH A2840 HOH A2841
SITE 3 AC1 11 HOH A2842 HOH A2843 HOH A2844
SITE 1 AC2 9 ASN A 416 HOH A2687 HOH A2845 HOH A2846
SITE 2 AC2 9 HOH A2847 HOH A2848 HOH A2849 HOH A2850
SITE 3 AC2 9 HOH A2851
SITE 1 AC3 8 ASN B 59 SER B 61 HOH B2722 HOH B2723
SITE 2 AC3 8 HOH B2724 HOH B2726 HOH B2728 HOH B2729
SITE 1 AC4 8 ASN B 416 HOH B2731 HOH B2732 HOH B2733
SITE 2 AC4 8 HOH B2734 HOH B2735 HOH B2736 HOH B2737
SITE 1 AC5 3 LYS A 133 TYR A 134 HOH A2063
SITE 1 AC6 4 HOH A2229 HOH A2232 HOH A2233 HOH A2245
SITE 1 AC7 4 ASN B 525 HOH B2571 HOH B2572 HOH B2703
SITE 1 AC8 10 GLY A 117 GLY A 118 GLY A 119 GLU A 199
SITE 2 AC8 10 SER A 200 ALA A 201 HIS A 440 HOH A2127
SITE 3 AC8 10 HOH A2310 HOH A2447
SITE 1 AC9 6 TYR A 70 TRP A 279 TYR A 334 HOH A2286
SITE 2 AC9 6 HOH A2309 HOH A2311
SITE 1 BC1 8 TRP B 84 GLY B 118 GLY B 119 GLU B 199
SITE 2 BC1 8 SER B 200 ALA B 201 HIS B 440 HOH B2603
SITE 1 BC2 7 HOH A2418 TRP B 279 TYR B 334 HOH B2411
SITE 2 BC2 7 HOH B2414 HOH B2740 HOH B2741
SITE 1 BC3 7 ASP A 297 GLY A 298 HOH A2164 HOH A2553
SITE 2 BC3 7 HOH A2558 HOH A2853 HOH A2855
SITE 1 BC4 9 HOH A2856 HOH A2857 HIS B 159 ILE B 296
SITE 2 BC4 9 ASP B 297 GLY B 298 HOH B2100 HOH B2423
SITE 3 BC4 9 HOH B2428
SITE 1 BC5 3 SER B 55 HOH B2742 HOH B2744
CRYST1 92.070 107.290 151.490 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 0.010861 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006601 0.00000
TER 4211 THR A 535
TER 8456 THR B 535
MASTER 638 0 15 52 30 0 28 610185 2 144 84
END |