# MOLECULE_PROPERTIES

C1: T5369186
C22: MomanyRone
C23: True
C55: CONJUG> Minimization exiting with gradient tolerance ( 0.0100000) satisfied.
C30:
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<ffml version="1.0">
<forcefield name="CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
</parameters>
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C1: 2CKM
C18: 0:2CKM:A:PRO485:485:PRO:HSQE:4,
C22: MomanyRone
C23: True
C28: CHARMm
C29: CHARMm
C47: 1
C48: 9223372036858118157
C16:
HEADER    HYDROLASE                               20-APR-06   2CKM
TITLE     TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
TITLE    2 ALKYLENE-LINKED BIS-TACRINE DIMER (7 CARBON LINKER)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: ACHE;
COMPND   5 EC: 3.1.1.7
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE   4 ORGANISM_TAXID: 7787;
SOURCE   5 VARIANT: G2 FORM;
SOURCE   6 ORGAN: ELECTRIC ORGAN;
SOURCE   7 TISSUE: ELECTROPLAQUE
KEYWDS    SERINE ESTERASE, SERINE HYDROLASE, ALZHEIMER'S DISEASE,
KEYWDS   2 NERVE, MUSCLE, SYNAPSE, MEMBRANE, HYDROLASE, GPI-ANCHOR,
KEYWDS   3 LIPOPROTEIN, GLYCOPROTEIN, CHOLINESTERASE, ALTERNATIVE
KEYWDS   4 SPLICING, NEUROTRANSMITTER DEGRADATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.BRUMSHTEIN,E.H.RYDBERG,H.M.GREENBLATT,D.M.WONG,D.SHAYA,
AUTHOR   2 L.D.WILLIAMS,P.R.CARLIER,Y.P.PANG,I.SILMAN,J.L.SUSSMAN
REVDAT   2   24-FEB-09 2CKM    1       VERSN
REVDAT   1   04-SEP-06 2CKM    0
JRNL        AUTH   E.H.RYDBERG,B.BRUMSHTEIN,H.M.GREENBLATT,D.M.WONG,
JRNL        AUTH 2 D.SHAYA,L.D.WILLIAMS,P.R.CARLIER,Y.P.PANG,I.SILMAN,
JRNL        AUTH 3 J.L.SUSSMAN
JRNL        TITL   COMPLEXES OF ALKYLENE-LINKED TACRINE DIMERS WITH
JRNL        TITL 2 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE: BINDING
JRNL        TITL 3 OF BIS(5)-TACRINE PRODUCES A DRAMATIC
JRNL        TITL 4 REARRANGEMENT IN THE ACTIVE-SITE GORGE
JRNL        REF    J.MED.CHEM.                   V.  49 5491 2006
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   16942022
JRNL        DOI    10.1021/JM060164B
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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 : MLF
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.27
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2192213.75
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92
REMARK   3   NUMBER OF REFLECTIONS             : 50424
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) : 0.211
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 2517
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 50
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 716
REMARK   3   BIN R VALUE           (WORKING SET) : 0.42
REMARK   3   BIN FREE R VALUE                    : 0.38
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 35
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            : 4142
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 65
REMARK   3   SOLVENT ATOMS            : 206
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.1
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.05
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 8.34
REMARK   3    B22 (A**2) : 8.34
REMARK   3    B33 (A**2) : -16.69
REMARK   3    B12 (A**2) : 6.53
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) : 0.29
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) : 0.34
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.018
REMARK   3   BOND ANGLES            (DEGREES) : 1.9
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) : 1.12  ; 1.50
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.81  ; 2.00
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.55  ; 2.00
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.10  ; 2.50
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK   3   KSOL        : 0.338604
REMARK   3   BSOL        : 40.9311
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: THE BIOLOGICALLY ACTIVE FORM OF THIS
REMARK   3  MOLECULE IS A DIMER, FORMED BY ROTATING THE ASYMMETRIC UNIT
REMARK   3  ABOUT THE CRYSTALLOGRAPHIC TWO-FOLD AXIS
REMARK   4
REMARK   4 2CKM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-06.
REMARK 100 THE PDBE ID CODE IS EBI-28490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-00
REMARK 200  TEMPERATURE           (KELVIN) : 120.0
REMARK 200  PH                             : 5.80
REMARK 200  NUMBER OF CRYSTALS USED        : 2
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 RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC BLUE
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS4++)
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80692
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0
REMARK 200  DATA REDUNDANCY                : 2.900
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-33% V/V PEG 200, 0.5M MES
REMARK 280  PH5.8, 4DEG CELCIUS, SEEDING
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       45.80433
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       91.60867
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       91.60867
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       45.80433
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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
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   BIOMT1   2 -0.500000  0.866025  0.000000      -55.94200
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       96.89439
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -45.79975
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A     1
REMARK 465     ASP A     2
REMARK 465     HIS A     3
REMARK 465     HIS A   486
REMARK 465     SER A   487
REMARK 465     GLN A   488
REMARK 465     GLU A   489
REMARK 465     ALA A   536
REMARK 465     CYS A   537
REMARK 465     ASP A   538
REMARK 465     GLY A   539
REMARK 465     GLU A   540
REMARK 465     LEU A   541
REMARK 465     SER A   542
REMARK 465     SER A   543
REMARK 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     LEU A   7    CD1  CD2
REMARK 470     ARG A  19    NE   CZ   NH1  NH2
REMARK 470     ASN A  42    CG   OD1  ND2
REMARK 470     LYS A  52    CD   CE   NZ
REMARK 470     GLU A  89    CG   CD   OE1  OE2
REMARK 470     LYS A 192    CD   CE   NZ
REMARK 470     ARG A 250    NH1  NH2
REMARK 470     GLU A 260    CD   OE1  OE2
REMARK 470     HIS A 264    ND1  CD2  CE1  NE2
REMARK 470     GLU A 268    OE1  OE2
REMARK 470     LYS A 270    CD   CE   NZ
REMARK 470     GLU A 299    CG   CD   OE1  OE2
REMARK 470     LYS A 346    CE   NZ
REMARK 470     GLU A 350    CG   CD   OE1  OE2
REMARK 470     ASP A 365    OD1  OD2
REMARK 470     LYS A 413    CD   CE   NZ
REMARK 470     GLU A 434    CD   OE1  OE2
REMARK 470     LYS A 454    CG   CD   CE   NZ
REMARK 470     LYS A 498    CG   CD   CE   NZ
REMARK 470     GLU A 508    OE1  OE2
REMARK 470     LYS A 511    CD   CE   NZ
REMARK 470     ARG A 515    NH1  NH2
REMARK 470     GLN A 526    OE1  NE2
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   NH1  ARG A   468  -  O    HOH A  2184              2.15
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500   O    HOH A  2149     O    HOH A  2149     4556      2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 344   CD    GLU A 344   OE1     0.075
REMARK 500    GLU A 344   CD    GLU A 344   OE2     0.091
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LYS A  14   CD  -  CE  -  NZ  ANGL. DEV. = -16.6 DEGREES
REMARK 500    ARG A  46   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A  46   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    LEU A 494   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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 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    PHE A  45      -10.66     80.53
REMARK 500    SER A 108       73.37   -158.70
REMARK 500    LEU A 158       76.85   -118.06
REMARK 500    ASN A 167       15.01     55.03
REMARK 500    SER A 200     -125.66     58.57
REMARK 500    GLU A 299      -73.77   -113.17
REMARK 500    THR A 317     -157.92   -161.20
REMARK 500    ASP A 380       50.00   -152.09
REMARK 500    VAL A 400      -62.72   -127.10
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         0.07    SIDE CHAIN
REMARK 500    TRP A 473         0.06    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LYS A 491        24.9      L          L   OUTSIDE RANGE
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 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AA7 A1536
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: 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: 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  2CKM A    1   543  UNP    P04058   ACES_TORCA      22    564
HET    NAG  A1537      14
HET    NAG  A1538      14
HET    AA7  A1536      37
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     AA7 N,N'-DI-1,2,3,4-TETRAHYDROACRIDIN-9-
HETNAM   2 AA7  YLHEPTANE-1,7-DIAMINE
HETSYN     NAG NAG
FORMUL   2  NAG    2(C8 H15 N O6)
FORMUL   4  AA7    C33 H40 N4
FORMUL   5  HOH   *206(H2 O1)
CRYST1  111.884  111.884  137.413  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      0.008938  0.005160  0.000000        0.00000
SCALE2      0.000000  0.010321  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007277        0.00000

C17:
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

C20:
REMARK  99  MacroMolecule created from Mol2 file
REMARK  99  2CKM
REMARK  99  PROTEIN
REMARK  99  USER_CHARGES
REMARK  99
REMARK  99

C21:
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

C24:
A:LEU7 2.1039
A:ARG19 1.9805
A:ASN42 1.5649
A:LYS52 3.6886
A:GLU89 2.7101
A:LYS192 3.4547
A:ARG250 2.4595
A:GLU260 3.6035
A:HIS264 4.1611
A:GLU268 4.5504
A:LYS270 3.7896
A:GLU299 1.7130
A:LYS346 1.7204
A:GLU350 2.3071
A:ASP365 3.2711
A:LYS413 2.7664
A:GLU434 4.6470
A:LYS454 4.3134
A:LYS498 4.2012
A:GLU508 0.6438
A:LYS511 4.0839
A:ARG515 0.8584
A:GLN526 0.5099

C30:
<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE ffml SYSTEM "Ffml.dtd">
<ffml version="1.0">
<forcefield name="CHARMm" derivedFrom="CHARMm" base="CHARMm">
<atomTypes>
</atomTypes>
<parameters>
</parameters>
</forcefield>
</ffml>

C43:
0.00 0.20 0.40 0.60 0.80 1.00 1.20 1.40 1.60 1.80 2.00 2.20 2.40 2.60 2.80 3.00 3.20 3.40 3.60 3.80 4.00 4.20 4.40 4.60 4.80 5.00 5.20 5.40 5.60 5.80 6.00 6.20 6.40 6.60 6.80 7.00 7.20 7.40 7.60 7.80 8.00 8.20 8.40 8.60 8.80 9.00 9.20 9.40 9.60 9.80 10.00 10.20 10.40 10.60 10.80 11.00 11.20 11.40 11.60 11.80 12.00 12.20 12.40 12.60 12.80 13.00 13.20 13.40 13.60 13.80

C44:
62.97 62.96 62.93 62.89 62.82 62.72 62.56 62.32 61.96 61.42 60.65 59.58 58.12 56.28 54.09 51.51 48.62 45.37 42.03 38.61 35.19 31.84 28.64 25.62 22.90 20.36 18.12 16.10 14.36 12.78 11.31 9.89 8.50 7.11 5.72 4.35 2.99 1.68 0.44 -0.72 -1.76 -2.74 -3.64 -4.47 -5.27 -6.06 -6.87 -7.73 -8.67 -9.75 -11.01 -12.52 -14.24 -16.19 -18.31 -20.56 -22.85 -25.13 -27.35 -29.47 -31.46 -33.34 -35.11 -36.82 -38.48 -40.11 -41.70 -43.25 -44.75 -46.20

C45:
-332.12  -332.13  -332.14  -332.16  -332.19  -332.23  -332.31  -332.42  -332.59  -332.85  -333.23  -333.77  -334.52  -335.50  -336.70  -338.08  -339.52  -340.89  -341.97  -342.56  -342.52  -341.72  -340.22  -338.12  -335.57  -332.77  -329.89  -327.03  -324.25  -321.56  -318.92  -316.31  -313.67  -310.97  -308.22  -305.45  -302.72  -300.07  -297.56  -295.20  -292.98  -290.88  -288.87  -286.92  -284.96  -282.92  -280.69  -278.16  -275.15  -271.53  -267.18  -262.01  -256.03  -249.36  -242.11  -234.46  -226.52  -218.40  -210.08  -201.51  -192.68  -183.52  -174.11  -164.51  -154.86  -145.30  -135.91  -126.77  -117.93  -109.41


