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HEADER HYDROLASE 26-JUL-99 1C2B
TITLE ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: A4 FORM;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ELECTROPHORUS ELECTRICUS;
SOURCE 3 ORGANISM_COMMON: ELECTRIC EEL;
SOURCE 4 OTHER_DETAILS: A4 FORM
KEYWDS SERINE HYDROLASE, ALPHA/BETA HYDROLASE, TETRAMER
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,P.MARCHOT
REVDAT 1 29-DEC-99 1C2B 0
JRNL AUTH Y.BOURNE,J.GRASSI,P.E.BOUGIS,P.MARCHOT
JRNL TITL CONFORMATIONAL FLEXIBILITY OF THE
JRNL TITL 2 ACETYLCHOLINESTERASE TETRAMER SUGGESTED BY X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY
JRNL REF J.BIOL.CHEM. V. 274 30370 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.369
REMARK 3 FREE R VALUE : 0.351
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C2B COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-1999.
REMARK 100 THE RCSB ID CODE IS RCSB009403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-1996
REMARK 200 TEMPERATURE (KELVIN) : 277.0
REMARK 200 PH : 8.00
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7742
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.500
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAKPO4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,1/2+Y,1/2+Z
REMARK 290 6555 -X,1/2-Y,1/2+Z
REMARK 290 7555 -X,1/2+Y,1/2-Z
REMARK 290 8555 X,1/2-Y,1/2-Z
REMARK 290 9555 1/2+X,Y,1/2+Z
REMARK 290 10555 1/2-X,-Y,1/2+Z
REMARK 290 11555 1/2-X,Y,1/2-Z
REMARK 290 12555 1/2+X,-Y,1/2-Z
REMARK 290 13555 1/2+X,1/2+Y,Z
REMARK 290 14555 1/2-X,1/2-Y,Z
REMARK 290 15555 1/2-X,1/2+Y,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 107.93500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 114.70500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 107.93500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 114.70500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 107.93500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 114.70500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 107.93500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 114.70500
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 114.70500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 114.70500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 114.70500
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 114.70500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 107.93500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 107.93500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 107.93500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 58.99000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 107.93500
REMARK 290 SMTRY3 16 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 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 58.99000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 107.93500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 58.99000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 114.70500
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 107.93500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 114.70500
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 4
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 491 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 SER A 495 OG
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 SER A 497 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N ALA A 262 C ALA A 262 11555 0.78
REMARK 500 CA ALA A 262 N ALA A 262 11555 0.79
REMARK 500 CA ALA A 262 CA ALA A 262 11555 0.83
REMARK 500 CA GLY A 261 N GLY A 263 11555 0.85
REMARK 500 CA GLY A 263 CA GLY A 261 11555 0.92
REMARK 500 N GLY A 263 C GLY A 261 11555 0.95
REMARK 500 CD ARG A 21 NH1 ARG A 21 4565 1.28
REMARK 500 CZ ARG A 21 NE ARG A 21 4565 1.30
REMARK 500 CZ ARG A 21 CZ ARG A 21 4565 1.35
REMARK 500 N GLY A 263 N GLY A 261 11555 1.55
REMARK 500 NH2 ARG A 21 NE ARG A 21 4565 1.59
REMARK 500 CB ALA A 262 CA ALA A 262 11555 1.65
REMARK 500 NH1 ARG A 21 NE ARG A 21 4565 1.67
REMARK 500 C GLY A 263 CA GLY A 261 11555 1.75
REMARK 500 CB ALA A 262 CB ALA A 262 11555 1.75
REMARK 500 CA GLY A 263 C GLY A 261 11555 1.78
REMARK 500 N ALA A 262 CB ALA A 262 11555 1.81
REMARK 500 O ALA A 262 N ALA A 262 11555 1.85
REMARK 500 O ALA A 262 O ALA A 262 11555 1.93
REMARK 500 CE2 TYR A 105 OH TYR A 105 4565 1.94
REMARK 500 O GLY A 261 N GLY A 263 11555 2.01
REMARK 500 C ALA A 262 CA ALA A 262 11555 2.02
REMARK 500 N ALA A 262 N ALA A 262 11555 2.03
REMARK 500 CB ALA A 109 CB ALA A 109 3555 2.03
REMARK 500 O GLY A 263 N GLY A 261 11555 2.07
REMARK 500 CZ ARG A 21 NH1 ARG A 21 4565 2.07
REMARK 500 CZ ARG A 21 CD ARG A 21 4565 2.12
REMARK 500 NH1 ARG A 21 NH1 ARG A 21 4565 2.14
REMARK 500 NH2 ARG A 21 CZ ARG A 21 4565 2.17
REMARK 500 O GLY A 261 CA GLY A 263 11555 2.19
REMARK 500 O GLY A 263 CA GLY A 261 11555 2.19
REMARK 500 CA GLY A 263 N GLY A 261 11555 2.19
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 THR A 543 CA - C - O ANGL. DEV. = 15.9 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 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
REMARK 500 LEU A 76 43.28 -74.69
REMARK 500 SER A 203 27.49 -120.87
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF
REMARK 999 MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO
REMARK 999 THE STRUCTURE) NOT OF ELECTROPHORUS ELECTRICUS.
REMARK 999 AT THE RESOLUTION OF THE EXPERIMENTAL DATA (4.5A)
REMARK 999 NO SEQUENCE DISCREPANCIES CAN BE SEEN.
DBREF 1C2B A 4 543 SWS P21836 ACES_MOUSE 35 574
SEQRES 1 A 540 GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN
SEQRES 2 A 540 LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL
SEQRES 3 A 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 A 540 GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO
SEQRES 5 A 540 TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL
SEQRES 6 A 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 A 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 A 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 A 540 PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 A 540 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 A 540 ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU
SEQRES 12 A 540 VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU
SEQRES 13 A 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 A 540 ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR
SEQRES 16 A 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 540 HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG
SEQRES 18 A 540 ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA
SEQRES 19 A 540 THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU
SEQRES 20 A 540 LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY
SEQRES 21 A 540 GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG
SEQRES 22 A 540 PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU
SEQRES 23 A 540 PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 A 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 A 540 ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL
SEQRES 26 A 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 A 540 GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 A 540 SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL
SEQRES 29 A 540 PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 A 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS
SEQRES 31 A 540 LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN
SEQRES 32 A 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 A 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS
SEQRES 34 A 540 ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL
SEQRES 35 A 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO
SEQRES 36 A 540 LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE
SEQRES 37 A 540 PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA
SEQRES 38 A 540 ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER
SEQRES 39 A 540 PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR
SEQRES 40 A 540 VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 A 540 LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 A 540 PRO LYS LEU LEU SER ALA THR
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 VAL A 141 1 7
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 218 PHE A 222 5 5
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 VAL A 288 5 3
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 TYR A 341 1 7
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 GLY A 456 1 7
HELIX 22 22 LEU A 457 ASP A 460 5 4
HELIX 23 23 THR A 466 THR A 486 1 21
HELIX 24 24 ARG A 525 ARG A 534 1 10
HELIX 25 25 ARG A 534 SER A 541 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 N LEU A 60 O GLN A 16
SHEET 1 B15 ILE A 20 ALA A 24 0
SHEET 2 B15 GLY A 27 ALA A 31 -1 N GLY A 27 O ALA A 24
SHEET 3 B15 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 B15 ILE A 35 PRO A 36 -1 N ILE A 35 O LEU A 99
SHEET 5 B15 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 6 B15 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 7 B15 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 8 B15 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 9 B15 ARG A 224 GLN A 228 1 N ARG A 224 O VAL A 197
SHEET 10 B15 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 11 B15 ARG A 424 TYR A 426 1 O ARG A 424 N VAL A 326
SHEET 12 B15 GLN A 325 VAL A 331 1 N VAL A 326 O ARG A 424
SHEET 13 B15 TYR A 428 PHE A 430 1 O TYR A 428 N VAL A 330
SHEET 14 B15 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 15 B15 ARG A 521 ARG A 522 -1 N ARG A 521 O TYR A 510
SHEET 1 C 2 ALA A 38 GLU A 39 0
SHEET 2 C 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
CISPEP 1 TYR A 105 PRO A 106 0 5.73
CISPEP 2 CYS A 257 PRO A 258 0 -9.78
CRYST1 117.980 215.870 229.410 90.00 90.00 90.00 F 2 2 2 16
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 0.008476 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004359 0.00000 |