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HEADER HYDROLASE 24-JUL-11 3ZV7
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITION BY
TITLE 2 BISNORCYMSERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 22-564;
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 ORGANISM_TAXID: 7787;
SOURCE 5 VARIANT: G2 FORM;
SOURCE 6 ORGAN: PACIFIC ELECTRIC RAY;
SOURCE 7 TISSUE: ELECTROPLAQUE
KEYWDS HYDROLASE, NEUROTRANSMITTER CLEAVAGE, ANTI-ALZHEIMER DRUG
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BARTOLUCCI,J.STOJAN,N.H.GREIG,D.LAMBA
REVDAT 1 23-MAY-12 3ZV7 0
JRNL AUTH C.BARTOLUCCI,J.STOJAN,Q.S.YU,N.H.GREIG,D.LAMBA
JRNL TITL KINETICS OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
JRNL TITL 2 INHIBITION BY BISNORCYMSERINE AND CRYSTAL STRUCTURE OF THE
JRNL TITL 3 COMPLEX WITH ITS LEAVING GROUP.
JRNL REF BIOCHEM.J. V. 444 269 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22390827
JRNL DOI 10.1042/BJ20111675
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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 : MAXIMUM LIKELIHOOD TARGET USING
REMARK 3 AMPLITUDES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2226903.23
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.000000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 45736
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) : 0.206
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.1
REMARK 3 FREE R VALUE TEST SET COUNT : 4611
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.4
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5941
REMARK 3 BIN R VALUE (WORKING SET) : 0.410
REMARK 3 BIN FREE R VALUE : 0.439
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.8
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 642
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4263
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 106
REMARK 3 SOLVENT ATOMS : 300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.80
REMARK 3 B22 (A**2) : 11.80
REMARK 3 B33 (A**2) : -23.60
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.53
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) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.61
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
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) : 3.593 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.709 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.650 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.135 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 48.647
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : PROLIG.PAR
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NAG.TOP
REMARK 3 TOPOLOGY FILE 6 : PROLIG.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3ZV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-11.
REMARK 100 THE PDBE ID CODE IS EBI-49141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
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 : CCD
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 : 45813
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.26
REMARK 200 RESOLUTION RANGE LOW (A) : 29.21
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.8
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 30.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.39
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.10
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 1EA5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 44% PEG200,
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,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.79567
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 91.59133
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 91.59133
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 45.79567
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: 8860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.3 KCAL/MOL
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 137.38700
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 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 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 ALA A 536 CA C O CB
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 HIS A 3 -76.86 -94.60
REMARK 500 SER A 24 -9.53 77.25
REMARK 500 SER A 25 -162.23 -117.75
REMARK 500 PHE A 45 -8.41 81.03
REMARK 500 TYR A 63 155.17 -49.66
REMARK 500 SER A 108 83.02 -157.67
REMARK 500 ALA A 164 77.87 -154.08
REMARK 500 ASN A 167 10.66 58.70
REMARK 500 SER A 200 -122.76 62.91
REMARK 500 GLU A 299 -81.10 -113.26
REMARK 500 THR A 317 -155.88 -160.63
REMARK 500 ASP A 380 51.28 -163.85
REMARK 500 VAL A 400 -62.57 -128.47
REMARK 500 MET A 510 140.59 -39.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 442 0.08 SIDE CHAIN
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 1PE A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 59 RESIDUES 1544 TO 1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 416 RESIDUES 1539 TO 1543
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO CALIFORNICAACETYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH AN (R)-TACRINE(10)-HUPYRIDONE
REMARK 900 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 COMPLEXED WITH
REMARK 900 M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE
REMARK 900 X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 2VQ6 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH 2-
REMARK 900 PAM
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC
REMARK 900 DATA
REMARK 900 RELATED ID: 2J3D RELATED DB: PDB
REMARK 900 NATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2CKM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 ALKYLENE-LINKED BIS-TACRINE DIMER (7 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: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT B) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT G) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 1ODC RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH N-4'-QUINOLYL-N'-9"-(1",2",3",4"-
REMARK 900 TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT 2.2A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING GALANTHAMINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 2CMF RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 ALKYLENE-LINKED BIS-TACRINE DIMER (5 CARBON LINKER)
REMARK 900 RELATED ID: 2WG0 RELATED DB: PDB
REMARK 900 AGED CONJUGATE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 WITH SOMAN (OBTAINED BY IN CRYSTALLO AGING)
REMARK 900 RELATED ID: 2J3Q RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH FLUOROPHORE
REMARK 900 THIOFLAVIN T
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH
REMARK 900 NAP
REMARK 900 RELATED ID: 2J4F RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM DERIVATIVE
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 BW284C51
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT H) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF AGED DI-ISOPROPYL-PHOSPHORO-
REMARK 900 FLUORIDATE (DFP) BOUND TO ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C5F RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM
REMARK 900 TORPEDO CALIFORNICA AT 1.8A RESOLUTION
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT C) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VJC RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 A AT 150K
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VJB RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 D AT 100K
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT D) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT A) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ZGC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO CALIFORNICAACETYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH AN (RS)-TACRINE(10)-HUPYRIDONE
REMARK 900 INHIBITOR.
REMARK 900 RELATED ID: 2WFZ RELATED DB: PDB
REMARK 900 NON-AGED CONJUGATE OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE WITH SOMAN
REMARK 900 RELATED ID: 2VJD RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 C AT 150K
REMARK 900 RELATED ID: 1JJB RELATED DB: PDB
REMARK 900 A NEUTRAL MOLECULE IN CATION-BINDING SITE: SPECIFIC
REMARK 900 BINDINGOF PEG-SH TO ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2WG1 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF THE AGED CONJUGATE OF TORPEDO
REMARK 900 CALIFORNICA ACEYLCHOLINESTERASE WITH SOMAN AND 2-PAM
REMARK 900 RELATED ID: 1UT6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH N-9-(1',2',3',4'-TETRAHYDROACRIDINYL)-
REMARK 900 1,8- DIAMINOOCTANE AT 2.4 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 2VT6 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COLLECTED
REMARK 900 WITH A CUMULATED DOSE OF 9400000 GY
REMARK 900 RELATED ID: 2WG2 RELATED DB: PDB
REMARK 900 NON-AGED CONJUGATE OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE WITH SOMAN (ALTERNATIVE REFINEMENT)
REMARK 900 RELATED ID: 2W9I RELATED DB: PDB
REMARK 900 ACHE IN COMPLEX WITH METHYLENE BLUE
REMARK 900 RELATED ID: 2VT7 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COLLECTED
REMARK 900 WITH A CUMULATED DOSE OF 800000 GY
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE
REMARK 900 COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT I) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-HEPTYLENE-BIS-N
REMARK 900 ,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH (+)-
REMARK 900 HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND ACETYLCHOLINESTERASE
REMARK 900 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 BY NERVE
REMARK 900 AGENT GD (SOMAN).
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY
REMARK 900 REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL) AMINO
REMARK 900 ]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 2VJA RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 A AT 100K
REMARK 900 RELATED ID: 2W6C RELATED DB: PDB
REMARK 900 ACHE IN COMPLEX WITH A BIS-(-)-NOR-MEPTAZINOL
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY
REMARK 900 REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB,
REMARK 900 SARIN)
REMARK 900 RELATED ID: 2V96 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE AT
REMARK 900 100K
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1U65 RELATED DB: PDB
REMARK 900 ACHE W. CPT-11
REMARK 900 RELATED ID: 1H22 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPERZINE A-LIKE
REMARK 900 INHIBITOR AT 2.15A RESOLUTION
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG
REMARK 900 , E2020 (ARICEPT), COMPLEXED WITH ITS TARGET
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C4H RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH
REMARK 900 RIVASTIGMINE
REMARK 900 RELATED ID: 2VA9 RELATED DB: PDB
REMARK 900 STRUCTURE OF NATIVE TCACHE AFTER A 9 SECONDS ANNEALING
REMARK 900 TO ROOM TEMPERATURE DURING THE FIRST 5 SECONDS OF
REMARK 900 WHICH LASER IRRADIATION AT 266NM TOOK PLACE
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE OBTAINED BY
REMARK 900 REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL) AMINO
REMARK 900 ]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (S)-E2020 BOUND ACETYLCHOLINESTERASE
REMARK 900 COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 2C58 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 20MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 1HBJ RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN TORPEDO
REMARK 900 CALIFORNICA ACHE AND A REVERSIBLE INHIBITOR, 4-AMINO-5
REMARK 900 -FLUORO-2-METHYL-3-(3-TRIFLUOROACETYLBENZYLTHIOMETHYL)
REMARK 900 QUINOLINE
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 20MM THIOCHOLINE
REMARK 900 RELATED ID: 2V98 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX OF TCACHE WITH 1-(2-
REMARK 900 NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE AFTER A
REMARK 900 9 SECONDS ANNEALING TO ROOM TEMPERATURE, DURING HTE
REMARK 900 FIRST 5 SECONDS OF WHICH LASER IRRADIATION AT 266NM
REMARK 900 TOOK PLACE
REMARK 900 RELATED ID: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-PROPYLENE-BIS-N
REMARK 900 ,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 2XI4 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AFLATOXIN B1 (ORTHORHOMBIC SPACE GROUP)
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE
REMARK 900 B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT E) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH (S,S)-(-)-BIS(12)-HUPERZINE A-LIKE
REMARK 900 INHIBITOR AT 2.15A RESOLUTION
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 2V97 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE
REMARK 900 AFTER A 9 SECONDS ANNEALING TO ROOM TEMPERATURE
DBREF 3ZV7 A 1 543 UNP P04058 ACES_TORCA 22 564
SEQRES 1 A 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
HET 1PE A1537 16
HET PEG A1538 7
HET NAG A1539 14
HET EDO A1540 4
HET NHG A1541 14
HET MES A1542 12
HET NAG A1543 14
HET NAG A1544 14
HET CL A1545 1
HET CL A1546 1
HET CL A1547 1
HET CL A1548 1
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 CL A1555 1
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NHG BIS-NORESEROLINE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM CL CHLORIDE ION
HETSYN 1PE PEG400
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 1PE C10 H22 O6
FORMUL 3 PEG C4 H10 O3
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 NHG C11 H14 N2 O
FORMUL 7 MES C6 H13 N O4 S
FORMUL 8 CL 11(CL 1-)
FORMUL 9 HOH *300(H2 O)
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 ASP A 276 1 7
HELIX 13 13 VAL A 277 LEU A 282 5 6
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 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
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 VAL A 22 0
SHEET 2 AB11 SER A 25 PRO A 34 -1 O SER A 25 N VAL A 22
SHEET 3 AB11 TYR A 96 VAL A 101 -1 O LEU A 97 N ILE A 33
SHEET 4 AB11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AB11 THR A 109 ILE A 115 1 O THR A 110 N VAL A 142
SHEET 6 AB11 GLY A 189 GLU A 199 1 N ASP A 190 O THR A 109
SHEET 7 AB11 ARG A 221 GLN A 225 1 O ARG A 221 N ILE A 196
SHEET 8 AB11 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AB11 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AB11 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AB11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AC 2 ASN A 66 CYS A 67 0
SHEET 2 AC 2 MET A 90 SER A 91 1 N SER A 91 O ASN A 66
SHEET 1 AD 2 VAL A 236 SER A 237 0
SHEET 2 AD 2 VAL A 295 ILE A 296 1 N ILE A 296 O VAL A 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.04
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.03
LINK ND2 ASN A 59 C1 NAG A1544 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A1543 1555 1555 1.45
LINK C1 NAG A1539 O4 NAG A1543 1555 1555 1.39
CISPEP 1 SER A 103 PRO A 104 0 0.19
SITE 1 AC1 7 TYR A 70 TYR A 121 GLN A 185 PRO A 191
SITE 2 AC1 7 TRP A 279 PHE A 330 HOH A2133
SITE 1 AC2 3 ASN A 230 SER A 235 HOH A2194
SITE 1 AC3 2 HIS A 406 CL A1548
SITE 1 AC4 2 TYR A 458 HOH A2064
SITE 1 AC5 3 HOH A2007 HOH A2083 HOH A2207
SITE 1 AC6 4 MET A 405 ASN A 409 CL A1546 CL A1551
SITE 1 AC7 2 LEU A 256 ASP A 259
SITE 1 AC8 2 CYS A 521 CL A1548
SITE 1 AC9 5 ARG A 243 ASN A 280 VAL A 281 LEU A 282
SITE 2 AC9 5 MES A1542
SITE 1 BC1 3 LEU A 430 VAL A 431 HOH A2256
SITE 1 BC2 2 ASN A 59 SER A 61
SITE 1 BC3 27 ASP A 2 ASN A 9 THR A 10 LYS A 11
SITE 2 BC3 27 TRP A 84 GLY A 119 TYR A 121 GLU A 199
SITE 3 BC3 27 SER A 200 GLU A 247 LEU A 282 PHE A 284
SITE 4 BC3 27 ASP A 285 PHE A 331 ASN A 416 TRP A 435
SITE 5 BC3 27 HIS A 440 CL A1552 HOH A2099 HOH A2169
SITE 6 BC3 27 HOH A2182 HOH A2242 HOH A2243 HOH A2296
SITE 7 BC3 27 HOH A2297 HOH A2298 HOH A2300
CRYST1 111.008 111.008 137.387 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 0.009008 0.005201 0.000000 0.00000
SCALE2 0.000000 0.010402 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007279 0.00000
TER 4264 ALA A 536
MASTER 623 0 19 26 18 0 20 6 4669 1 103 42
END |