longtext: 2J4F-pdb

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HEADER    HYDROLASE                               30-AUG-06   2J4F
TITLE     TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM DERIVATIVE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND   3 SYNONYM: ACHE;
COMPND   4 CHAIN: A;
COMPND   5 FRAGMENT: RESIDUES 22-564;
COMPND   6 EC: 3.1.1.7
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY
KEYWDS    NEUROTRANSMITTER DEGRADATION,
KEYWDS   2 NEUROTRANSMITTER CLEAVAGE,
KEYWDS   3 ALTERNATIVE SPLICING, ALPHA-BETA HYDROLASE,
KEYWDS   4 SERINE ESTERASE, SERINE HYDROLASE, CATALYTIC TRIAD,
KEYWDS   5 LIPOPROTEIN, GLYCOPROTEIN, CHOLINESTERASE,
KEYWDS   6 SYNAPSE, MEMBRANE, HYDROLASE, GPI-ANCHOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.I.KREIMER,E.A.DOLGINOVA,M.RAVES,J.L.SUSSMAN,I.SILMAN,
AUTHOR   2 L.WEINER
REVDAT   1   05-SEP-06 2J4F    0
JRNL        AUTH   D.I.KREIMER,E.A.DOLGINOVA,M.RAVES,J.L.SUSSMAN,
JRNL        AUTH 2 I.SILMAN,L.WEINER
JRNL        TITL   A METASTABLE STATE OF TORPEDO CALIFORNICA
JRNL        TITL 2 ACETYLCHOLINESTERASE GENERATED BY MODIFICATION
JRNL        TITL 3 WITH ORGANOMERCURIALS
JRNL        REF    BIOCHEMISTRY                  V.  33 14407 1994
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION. 2.8  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR NULL
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.8
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3966972
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.5
REMARK   3   NUMBER OF REFLECTIONS             : 19872
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) : 0.204
REMARK   3   FREE R VALUE                     : 0.262
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.7
REMARK   3   FREE R VALUE TEST SET COUNT      : 1935
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
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) : 2.8
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.8
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2312
REMARK   3   BIN R VALUE           (WORKING SET) : 0.292
REMARK   3   BIN FREE R VALUE                    : 0.391
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.7
REMARK   3   BIN FREE R VALUE SET COUNT          : 247
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4115
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 94
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 44.9
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.8
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) : 0.32
REMARK   3   ESD FROM SIGMAA              (A) : 0.44
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.0
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55
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) : 23.6
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.28
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) :  1.62 ;   1.5
REMARK   3   MAIN-CHAIN ANGLE             (A**2) :  2.57 ;   2.0
REMARK   3   SIDE-CHAIN BOND              (A**2) :   2.5 ;   2.0
REMARK   3   SIDE-CHAIN ANGLE             (A**2) :  3.65 ;   2.5
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   GROUP  2  POSITIONAL            (A) :  NULL ;  NULL
REMARK   3   GROUP  2  B-FACTOR           (A**2) :  NULL ;  NULL
REMARK   3   GROUP  3  POSITIONAL            (A) :  NULL ;  NULL
REMARK   3   GROUP  3  B-FACTOR           (A**2) :  NULL ;  NULL
REMARK   3   GROUP  4  POSITIONAL            (A) :  NULL ;  NULL
REMARK   3   GROUP  4  B-FACTOR           (A**2) :  NULL ;  NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO
REMARK   3  TOPOLOGY FILE   1  : TOPH19X.PRO
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2J4F COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 30-AUG-2006.
REMARK 100 THE EBI ID CODE IS EBI-29863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : MULTIWIRE
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23445
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8
REMARK 200  DATA REDUNDANCY                : 3.7
REMARK 200  R MERGE                    (I) : 0.11
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 69.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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   Y-X,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,2/3-Z
REMARK 290       6555   -X,Y-X,1/3-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.00000
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       90.00000
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       90.00000
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       45.00000
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 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 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     PRO A   485
REMARK 465     HIS A   486
REMARK 465     SER A   487
REMARK 465     GLN A   488
REMARK 465     GLU A   489
REMARK 465     ALA A   536
REMARK 465     CYS A   537
REMARK 465     ASP A   538
REMARK 465     GLY A   539
REMARK 465     GLU A   540
REMARK 465     LEU A   541
REMARK 465     SER A   542
REMARK 465     SER A   543
REMARK 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     LYS A  14    CE   NZ
REMARK 470     ARG A  19    CZ   NH1  NH2
REMARK 470     HIS A  26    CG   ND1  CD2  CE1  NE2
REMARK 470     ASN A  42    CG   OD1  ND2
REMARK 470     GLU A  89    CD   OE1  OE2
REMARK 470     GLN A 162    CG   CD   OE1  NE2
REMARK 470     ASN A 257    CG   OD1  ND2
REMARK 470     GLU A 260    CG   CD   OE1  OE2
REMARK 470     GLU A 261    CD   OE1  OE2
REMARK 470     LYS A 270    CD   CE   NZ
REMARK 470     PHE A 284    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     GLU A 299    CD   OE1  OE2
REMARK 470     GLU A 344    CD   OE1  OE2
REMARK 470     GLU A 350    CD   OE1  OE2
REMARK 470     MET A 353    SD   CE
REMARK 470     ASP A 365    CG   OD1  OD2
REMARK 470     ASN A 382    CG   OD1  ND2
REMARK 470     GLU A 461    CD   OE1  OE2
REMARK 470     GLU A 484    CD   OE1  OE2
REMARK 470     LYS A 498    CB   CG   CD   CE   NZ
REMARK 470     GLU A 499    CD   OE1  OE2
REMARK 470     GLU A 508    CB   CG   CD   OE1  OE2
REMARK 470     LYS A 511    CG   CD   CE   NZ
REMARK 470     ARG A 515    CZ   NH1  NH2
REMARK 470     GLN A 526    CD   OE1  NE2
REMARK 470     ASN A 533    CG   OD1  ND2
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    LEU A 158   N   -  CA  -  C   ANGL. DEV. = -10.4 DEGREES
REMARK 500    ASP A 297   N   -  CA  -  C   ANGL. DEV. =  11.0 DEGREES
REMARK 500    LEU A 320   N   -  CA  -  C   ANGL. DEV. =  -9.2 DEGREES
REMARK 500    ASN A 457   N   -  CA  -  C   ANGL. DEV. =  10.5 DEGREES
REMARK 500    TYR A 458   N   -  CA  -  C   ANGL. DEV. =  -9.3 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A   5      -76.00     63.15
REMARK 500    SER A 200     -119.95     55.96
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN
REMARK 525     A              Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM HG    HG A1536  THE COORDINATION ANGLES ARE:
REMARK 600  1 GLU    139A  OE1
REMARK 600  2 GLU    139A  OE2       50.6
REMARK 600  3 HIS    471A  ND1       75.5 113.3
REMARK 600                             1     2
REMARK 600
REMARK 600 FOR METAL ATOM HG    HG A1537  THE COORDINATION ANGLES ARE:
REMARK 600  1 SER    228A  O
REMARK 600  2 SER    228A  OG        73.4
REMARK 600  3 CYS    231A  SG       101.0  90.2
REMARK 600  4 SER    228A  N         69.0  75.8 164.5
REMARK 600                             1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: HG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: HG BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ACJ   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1ACL   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
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: 1AX9   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900  LAUE DATA
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: 1DX6   RELATED DB: PDB
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900   (-)-GALANTHAMINE AT 2.3A RESOLUTION
REMARK 900 RELATED ID: 1E3Q   RELATED DB: PDB
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900   WITH BW284C51
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: 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: 1EEA   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE
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: 1FSS   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-
REMARK 900  II
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: 1GPN   RELATED DB: PDB
REMARK 900  STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900   HUPERZINE B AT 2.35A RESOLUTION
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: 1GQS   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900  COMPLEXED WITH NAP
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: 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: 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: 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: 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: 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: 1OCE   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH MF268
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: 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: 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: 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: 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: 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: 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: 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: 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: 1QTI   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE
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: 1U65   RELATED DB: PDB
REMARK 900  ACHE W. CPT-11
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: 1VOT   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
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: 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: 1W4L   RELATED DB: PDB
REMARK 900  COMPLEX OF TCACHE WITH BIS-ACTING
REMARK 900  GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W6R   RELATED DB: PDB
REMARK 900  COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W75   RELATED DB: PDB
REMARK 900  NATIVE ORTHORHOMBIC FORM OF TORPEDO
REMARK 900  CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
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: 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: 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: 2ACE   RELATED DB: PDB
REMARK 900  NATIVE ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900  CALIFORNICA
REMARK 900 RELATED ID: 2ACK   RELATED DB: PDB
REMARK 900  ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900  MONOCHROMATIC DATA
REMARK 900 RELATED ID: 2C4H   RELATED DB: PDB
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900  COMPLEX WITH 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2C58   RELATED DB: PDB
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900  COMPLEX WITH 20MM ACETYLTHIOCHOLINE
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: 2C5G   RELATED DB: PDB
REMARK 900  TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900  COMPLEX WITH 20MM THIOCHOLINE
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: 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: 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: 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: 2J3D   RELATED DB: PDB
REMARK 900  NATIVE MONOCLINIC FORM OF TORPEDO
REMARK 900  ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2J3Q   RELATED DB: PDB
REMARK 900  TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900  FLUOROPHORE THIOFLAVIN T
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: 4ACE   RELATED DB: PDB
REMARK 900  THEORETICAL MODEL OF (S)-E2020 BOUND
REMARK 900  ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
DBREF  2J4F 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     HG  A1536       1
HET     HG  A1537       1
HETNAM      HG MERCURY (II) ION
FORMUL   2   HG    2(HG1 2+)
FORMUL   3  HOH   *94(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  139  1                                   8
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 CYS A  231  SER A  235  5                                   5
HELIX   10  10 VAL A  238  LEU A  252  1                                  15
HELIX   11  11 SER A  258  LYS A  269  1                                  12
HELIX   12  12 LYS A  270  GLU A  278  1                                   9
HELIX   13  13 SER A  304  GLY A  312  1                                   9
HELIX   14  14 GLY A  328  ALA A  336  1                                   9
HELIX   15  15 SER A  348  VAL A  360  1                                  13
HELIX   16  16 ASN A  364  THR A  376  1                                  13
HELIX   17  17 ASN A  383  VAL A  400  1                                  18
HELIX   18  18 VAL A  400  LYS A  413  1                                  14
HELIX   19  19 PRO A  433  GLY A  437  5                                   5
HELIX   20  20 GLU A  443  PHE A  448  1                                   6
HELIX   21  21 GLY A  449  VAL A  453  5                                   5
HELIX   22  22 VAL A  453  ASN A  457  5                                   5
HELIX   23  23 THR A  459  GLY A  480  1                                  22
HELIX   24  24 ARG A  517  GLN A  526  1                                  10
HELIX   25  25 GLN A  526  THR A  535  1                                  10
SHEET    1  AA 3 LEU A   7  ASN A   9  0
SHEET    2  AA 3 LYS A  14  MET A  16 -1  O  VAL A  15   N  VAL A   8
SHEET    3  AA 3 TRP A  58  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  ASP A 504  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
LINK        HG    HG A1536                 OE1 GLU A 139     1555   1555
LINK        HG    HG A1536                 OE2 GLU A 139     1555   1555
LINK        HG    HG A1536                 ND1 HIS A 471     1555   1555
LINK        HG    HG A1537                 OG  SER A 228     1555   1555
LINK        HG    HG A1537                 SG  CYS A 231     1555   1555
LINK        HG    HG A1537                 N   SER A 228     1555   1555
LINK        HG    HG A1537                 O   SER A 228     1555   1555
CISPEP   1 SER A  103    PRO A  104          0         0.10
SITE     1 AC1  2 GLU A 139  HIS A 471
SITE     1 AC2  3 GLY A 227  SER A 228  CYS A 231
CRYST1  110.700  110.700  135.000  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      0.009033  0.005215  0.000000        0.00000
SCALE2      0.000000  0.010431  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007407        0.00000
TER    4116      THR A 535
MASTER      555    0    2   25   16    0    2    6 4211    1    9   42
END