longtext: 6bq0-pdb

content
HEADER    HYDROLASE/HYDROLASE INHIBITOR           27-NOV-17   6BQ0
TITLE     STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE BOUND TO A COVALENT
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: MGL,HU-K5,LYSOPHOSPHOLIPASE HOMOLOG,LYSOPHOSPHOLIPASE-LIKE,
COMPND   5 MONOACYLGLYCEROL LIPASE,MAGL;
COMPND   6 EC: 3.1.1.23;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: MGLL;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA
KEYWDS    MONOACYLGLYCEROL LIPASE, COVALENT INHIBITOR, SBDD, HYDROLASE-
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.PANDIT
REVDAT   1   14-MAR-18 6BQ0    0
JRNL        AUTH   L.A.MCALLISTER,C.R.BUTLER,S.MENTE,S.V.O'NEIL,K.R.FONSECA,
JRNL        AUTH 2 J.R.PIRO,J.A.CIANFROGNA,T.L.FOLEY,A.M.GILBERT,A.R.HARRIS,
JRNL        AUTH 3 C.J.HELAL,D.S.JOHNSON,J.I.MONTGOMERY,D.M.NASON,S.NOELL,
JRNL        AUTH 4 J.PANDIT,B.N.ROGERS,T.A.SAMAD,C.L.SHAFFER,R.G.DA SILVA,
JRNL        AUTH 5 D.P.UCCELLO,D.WEBB,M.A.BRODNEY
JRNL        TITL   DISCOVERY OF TRIFLUOROMETHYL GLYCOL CARBAMATES AS POTENT AND
JRNL        TITL 2 SELECTIVE COVALENT MONOACYLGLYCEROL LIPASE (MAGL) INHIBITORS
JRNL        TITL 3 FOR TREATMENT OF NEUROINFLAMMATION.
JRNL        REF    J. MED. CHEM.                              2018
JRNL        REFN                   ISSN 1520-4804
JRNL        PMID   29498843
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00070
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER 2.11.5
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 51177
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 + TEST SET)  : 0.180
REMARK   3   R VALUE            (WORKING SET)  : 0.179
REMARK   3   FREE R VALUE                      : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT       : 2610
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               : 20
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.05
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.62
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3629
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2138
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3433
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2104
REMARK   3   BIN FREE R VALUE                        : 0.2718
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 196
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4362
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 443
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 36.36
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.69
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.23630
REMARK   3    B22 (A**2) : 3.50150
REMARK   3    B33 (A**2) : -3.26530
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.211
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.146
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.134
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.140
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.132
REMARK   3
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK   3
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.
REMARK   3    BOND LENGTHS              : 4533   ; 2.000  ; HARMONIC
REMARK   3    BOND ANGLES               : 6156   ; 2.000  ; HARMONIC
REMARK   3    TORSION ANGLES            : 1551   ; 2.000  ; SINUSOIDAL
REMARK   3    TRIGONAL CARBON PLANES    : 90     ; 2.000  ; HARMONIC
REMARK   3    GENERAL PLANES            : 705    ; 5.000  ; HARMONIC
REMARK   3    ISOTROPIC THERMAL FACTORS : 4533   ; 20.000 ; HARMONIC
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL
REMARK   3    CHIRAL IMPROPER TORSION   : 569    ; 5.000  ; SEMIHARMONIC
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL
REMARK   3    IDEAL-DIST CONTACT TERM   : 5479   ; 4.000  ; SEMIHARMONIC
REMARK   3
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND LENGTHS                       (A) : 0.010
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.08
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.75
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 6BQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-14
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CLSI
REMARK 200  BEAMLINE                       : 08ID-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51178
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.83900
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: 6AX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.07M SODIUM CACODYLATE PH 5.1-5.9 AND
REMARK 280  33-51% MPD, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
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       43.15500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.31000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.03000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.15500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.31000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.03000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.15500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.31000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.03000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.15500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       63.31000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       69.03000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   -23
REMARK 465     ALA A   -22
REMARK 465     SER A   -21
REMARK 465     ARG A   -20
REMARK 465     GLY A   -19
REMARK 465     SER A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     GLY A   -11
REMARK 465     ALA A   -10
REMARK 465     GLY A    -9
REMARK 465     ASP A    -8
REMARK 465     ARG A    -7
REMARK 465     GLY A    -6
REMARK 465     PRO A    -5
REMARK 465     GLU A    -4
REMARK 465     PHE A    -3
REMARK 465     PRO A    -2
REMARK 465     SER A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     PRO A     2
REMARK 465     GLU A     3
REMARK 465     GLU A     4
REMARK 465     SER A     5
REMARK 465     SER A     6
REMARK 465     PRO A     7
REMARK 465     ARG A     8
REMARK 465     ARG A     9
REMARK 465     THR A    10
REMARK 465     PRO A    11
REMARK 465     GLN A    12
REMARK 465     SER A    13
REMARK 465     ILE A    14
REMARK 465     PRO A    15
REMARK 465     TYR A    16
REMARK 465     GLN A    17
REMARK 465     GLY A   298
REMARK 465     THR A   299
REMARK 465     ALA A   300
REMARK 465     SER A   301
REMARK 465     PRO A   302
REMARK 465     PRO A   303
REMARK 465     LEU A   304
REMARK 465     GLU A   305
REMARK 465     VAL A   306
REMARK 465     ASP A   307
REMARK 465     LEU A   308
REMARK 465     GLN A   309
REMARK 465     GLY A   310
REMARK 465     ASP A   311
REMARK 465     HIS A   312
REMARK 465     GLY A   313
REMARK 465     LEU A   314
REMARK 465     SER A   315
REMARK 465     ALA A   316
REMARK 465     TRP A   317
REMARK 465     SER A   318
REMARK 465     HIS A   319
REMARK 465     PRO A   320
REMARK 465     GLN A   321
REMARK 465     PHE A   322
REMARK 465     GLU A   323
REMARK 465     LYS A   324
REMARK 465     MET B   -23
REMARK 465     ALA B   -22
REMARK 465     SER B   -21
REMARK 465     ARG B   -20
REMARK 465     GLY B   -19
REMARK 465     SER B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     GLY B   -11
REMARK 465     ALA B   -10
REMARK 465     GLY B    -9
REMARK 465     ASP B    -8
REMARK 465     ARG B    -7
REMARK 465     GLY B    -6
REMARK 465     PRO B    -5
REMARK 465     GLU B    -4
REMARK 465     PHE B    -3
REMARK 465     PRO B    -2
REMARK 465     SER B    -1
REMARK 465     SER B     0
REMARK 465     MET B     1
REMARK 465     PRO B     2
REMARK 465     GLU B     3
REMARK 465     GLU B     4
REMARK 465     SER B     5
REMARK 465     ASN B   152
REMARK 465     PRO B   153
REMARK 465     GLU B   154
REMARK 465     SER B   155
REMARK 465     ALA B   156
REMARK 465     THR B   157
REMARK 465     THR B   158
REMARK 465     PHE B   159
REMARK 465     ALA B   297
REMARK 465     GLY B   298
REMARK 465     THR B   299
REMARK 465     ALA B   300
REMARK 465     SER B   301
REMARK 465     PRO B   302
REMARK 465     PRO B   303
REMARK 465     LEU B   304
REMARK 465     GLU B   305
REMARK 465     VAL B   306
REMARK 465     ASP B   307
REMARK 465     LEU B   308
REMARK 465     GLN B   309
REMARK 465     GLY B   310
REMARK 465     ASP B   311
REMARK 465     HIS B   312
REMARK 465     GLY B   313
REMARK 465     LEU B   314
REMARK 465     SER B   315
REMARK 465     ALA B   316
REMARK 465     TRP B   317
REMARK 465     SER B   318
REMARK 465     HIS B   319
REMARK 465     PRO B   320
REMARK 465     GLN B   321
REMARK 465     PHE B   322
REMARK 465     GLU B   323
REMARK 465     LYS B   324
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     SER B   6    OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A  53     -155.21   -100.83
REMARK 500    SER A 122     -118.63     55.14
REMARK 500    SER A 146       63.20     38.43
REMARK 500    TYR A 268     -150.71    -88.66
REMARK 500    LYS A 273       36.88   -140.02
REMARK 500    GLU B  53     -155.14   -100.44
REMARK 500    SER B 122     -118.55     55.72
REMARK 500    SER B 146       63.36     38.13
REMARK 500    TYR B 268     -150.98    -87.91
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 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 714        DISTANCE =  6.74 ANGSTROMS
REMARK 525    HOH A 715        DISTANCE =  7.86 ANGSTROMS
REMARK 525    HOH A 716        DISTANCE =  8.99 ANGSTROMS
REMARK 525    HOH B 721        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH B 722        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH B 723        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH B 724        DISTANCE =  6.95 ANGSTROMS
REMARK 525    HOH B 725        DISTANCE =  7.84 ANGSTROMS
REMARK 525    HOH B 726        DISTANCE =  8.40 ANGSTROMS
REMARK 525    HOH B 727        DISTANCE =  9.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E3A A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E3A B 401 and SER B
REMARK 800  122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide E3A B 401 and SER B
REMARK 800  122
DBREF  6BQ0 A    1   303  UNP    Q99685   MGLL_HUMAN       1    303
DBREF  6BQ0 B    1   303  UNP    Q99685   MGLL_HUMAN       1    303
SEQADV 6BQ0 MET A  -23  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA A  -22  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A  -21  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ARG A  -20  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A  -19  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A  -18  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -17  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -16  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -15  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -14  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -13  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  -12  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A  -11  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA A  -10  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A   -9  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP A   -8  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ARG A   -7  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A   -6  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO A   -5  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU A   -4  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PHE A   -3  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO A   -2  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A   -1  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A    0  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU A  304  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU A  305  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 VAL A  306  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP A  307  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU A  308  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLN A  309  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A  310  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP A  311  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  312  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY A  313  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU A  314  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A  315  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA A  316  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 TRP A  317  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER A  318  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS A  319  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO A  320  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLN A  321  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PHE A  322  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU A  323  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LYS A  324  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 MET B  -23  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA B  -22  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B  -21  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ARG B  -20  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B  -19  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B  -18  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -17  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -16  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -15  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -14  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -13  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  -12  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B  -11  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA B  -10  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B   -9  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP B   -8  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ARG B   -7  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B   -6  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO B   -5  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU B   -4  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PHE B   -3  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO B   -2  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B   -1  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B    0  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU B  304  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU B  305  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 VAL B  306  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP B  307  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU B  308  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLN B  309  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B  310  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ASP B  311  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  312  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLY B  313  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LEU B  314  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B  315  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 ALA B  316  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 TRP B  317  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 SER B  318  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 HIS B  319  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PRO B  320  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLN B  321  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 PHE B  322  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 GLU B  323  UNP  Q99685              EXPRESSION TAG
SEQADV 6BQ0 LYS B  324  UNP  Q99685              EXPRESSION TAG
SEQRES   1 A  348  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY
SEQRES   2 A  348  ALA GLY ASP ARG GLY PRO GLU PHE PRO SER SER MET PRO
SEQRES   3 A  348  GLU GLU SER SER PRO ARG ARG THR PRO GLN SER ILE PRO
SEQRES   4 A  348  TYR GLN ASP LEU PRO HIS LEU VAL ASN ALA ASP GLY GLN
SEQRES   5 A  348  TYR LEU PHE CYS ARG TYR TRP LYS PRO THR GLY THR PRO
SEQRES   6 A  348  LYS ALA LEU ILE PHE VAL SER HIS GLY ALA GLY GLU HIS
SEQRES   7 A  348  SER GLY ARG TYR GLU GLU LEU ALA ARG MET LEU MET GLY
SEQRES   8 A  348  LEU ASP LEU LEU VAL PHE ALA HIS ASP HIS VAL GLY HIS
SEQRES   9 A  348  GLY GLN SER GLU GLY GLU ARG MET VAL VAL SER ASP PHE
SEQRES  10 A  348  HIS VAL PHE VAL ARG ASP VAL LEU GLN HIS VAL ASP SER
SEQRES  11 A  348  MET GLN LYS ASP TYR PRO GLY LEU PRO VAL PHE LEU LEU
SEQRES  12 A  348  GLY HIS SER MET GLY GLY ALA ILE ALA ILE LEU THR ALA
SEQRES  13 A  348  ALA GLU ARG PRO GLY HIS PHE ALA GLY MET VAL LEU ILE
SEQRES  14 A  348  SER PRO LEU VAL LEU ALA ASN PRO GLU SER ALA THR THR
SEQRES  15 A  348  PHE LYS VAL LEU ALA ALA LYS VAL LEU ASN LEU VAL LEU
SEQRES  16 A  348  PRO ASN LEU SER LEU GLY PRO ILE ASP SER SER VAL LEU
SEQRES  17 A  348  SER ARG ASN LYS THR GLU VAL ASP ILE TYR ASN SER ASP
SEQRES  18 A  348  PRO LEU ILE CYS ARG ALA GLY LEU LYS VAL CYS PHE GLY
SEQRES  19 A  348  ILE GLN LEU LEU ASN ALA VAL SER ARG VAL GLU ARG ALA
SEQRES  20 A  348  LEU PRO LYS LEU THR VAL PRO PHE LEU LEU LEU GLN GLY
SEQRES  21 A  348  SER ALA ASP ARG LEU CYS ASP SER LYS GLY ALA TYR LEU
SEQRES  22 A  348  LEU MET GLU LEU ALA LYS SER GLN ASP LYS THR LEU LYS
SEQRES  23 A  348  ILE TYR GLU GLY ALA TYR HIS VAL LEU HIS LYS GLU LEU
SEQRES  24 A  348  PRO GLU VAL THR ASN SER VAL PHE HIS GLU ILE ASN MET
SEQRES  25 A  348  TRP VAL SER GLN ARG THR ALA THR ALA GLY THR ALA SER
SEQRES  26 A  348  PRO PRO LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU
SEQRES  27 A  348  SER ALA TRP SER HIS PRO GLN PHE GLU LYS
SEQRES   1 B  348  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY
SEQRES   2 B  348  ALA GLY ASP ARG GLY PRO GLU PHE PRO SER SER MET PRO
SEQRES   3 B  348  GLU GLU SER SER PRO ARG ARG THR PRO GLN SER ILE PRO
SEQRES   4 B  348  TYR GLN ASP LEU PRO HIS LEU VAL ASN ALA ASP GLY GLN
SEQRES   5 B  348  TYR LEU PHE CYS ARG TYR TRP LYS PRO THR GLY THR PRO
SEQRES   6 B  348  LYS ALA LEU ILE PHE VAL SER HIS GLY ALA GLY GLU HIS
SEQRES   7 B  348  SER GLY ARG TYR GLU GLU LEU ALA ARG MET LEU MET GLY
SEQRES   8 B  348  LEU ASP LEU LEU VAL PHE ALA HIS ASP HIS VAL GLY HIS
SEQRES   9 B  348  GLY GLN SER GLU GLY GLU ARG MET VAL VAL SER ASP PHE
SEQRES  10 B  348  HIS VAL PHE VAL ARG ASP VAL LEU GLN HIS VAL ASP SER
SEQRES  11 B  348  MET GLN LYS ASP TYR PRO GLY LEU PRO VAL PHE LEU LEU
SEQRES  12 B  348  GLY HIS SER MET GLY GLY ALA ILE ALA ILE LEU THR ALA
SEQRES  13 B  348  ALA GLU ARG PRO GLY HIS PHE ALA GLY MET VAL LEU ILE
SEQRES  14 B  348  SER PRO LEU VAL LEU ALA ASN PRO GLU SER ALA THR THR
SEQRES  15 B  348  PHE LYS VAL LEU ALA ALA LYS VAL LEU ASN LEU VAL LEU
SEQRES  16 B  348  PRO ASN LEU SER LEU GLY PRO ILE ASP SER SER VAL LEU
SEQRES  17 B  348  SER ARG ASN LYS THR GLU VAL ASP ILE TYR ASN SER ASP
SEQRES  18 B  348  PRO LEU ILE CYS ARG ALA GLY LEU LYS VAL CYS PHE GLY
SEQRES  19 B  348  ILE GLN LEU LEU ASN ALA VAL SER ARG VAL GLU ARG ALA
SEQRES  20 B  348  LEU PRO LYS LEU THR VAL PRO PHE LEU LEU LEU GLN GLY
SEQRES  21 B  348  SER ALA ASP ARG LEU CYS ASP SER LYS GLY ALA TYR LEU
SEQRES  22 B  348  LEU MET GLU LEU ALA LYS SER GLN ASP LYS THR LEU LYS
SEQRES  23 B  348  ILE TYR GLU GLY ALA TYR HIS VAL LEU HIS LYS GLU LEU
SEQRES  24 B  348  PRO GLU VAL THR ASN SER VAL PHE HIS GLU ILE ASN MET
SEQRES  25 B  348  TRP VAL SER GLN ARG THR ALA THR ALA GLY THR ALA SER
SEQRES  26 B  348  PRO PRO LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU
SEQRES  27 B  348  SER ALA TRP SER HIS PRO GLN PHE GLU LYS
HET    E3A  A 401      20
HET    E3A  B 401      40
HETNAM     E3A 1-({(1R,5S,6R)-6-[1-(4-FLUOROPHENYL)-1H-PYRAZOL-3-YL]-
HETNAM   2 E3A  3-AZABICYCLO[3.1.0]HEXANE-3-CARBONYL}OXY)PYRROLIDINE-
HETNAM   3 E3A  2,5-DIONE
FORMUL   3  E3A    2(C19 H17 F N4 O4)
FORMUL   5  HOH   *443(H2 O)
HELIX    1 AA1 HIS A   54  ARG A   57  5                                   4
HELIX    2 AA2 TYR A   58  GLY A   67  1                                  10
HELIX    3 AA3 PHE A   93  TYR A  111  1                                  19
HELIX    4 AA4 MET A  123  ARG A  135  1                                  13
HELIX    5 AA5 THR A  157  LEU A  171  1                                  15
HELIX    6 AA6 ASP A  180  LEU A  184  5                                   5
HELIX    7 AA7 ASN A  187  ASP A  197  1                                  11
HELIX    8 AA8 LYS A  206  LEU A  224  1                                  19
HELIX    9 AA9 PRO A  225  LEU A  227  5                                   3
HELIX   10 AB1 ASP A  243  ALA A  254  1                                  12
HELIX   11 AB2 VAL A  270  GLU A  274  5                                   5
HELIX   12 AB3 LEU A  275  THR A  296  1                                  22
HELIX   13 AB4 PRO B   15  LEU B   19  5                                   5
HELIX   14 AB5 HIS B   54  ARG B   57  5                                   4
HELIX   15 AB6 TYR B   58  GLY B   67  1                                  10
HELIX   16 AB7 PHE B   93  TYR B  111  1                                  19
HELIX   17 AB8 MET B  123  ARG B  135  1                                  13
HELIX   18 AB9 VAL B  161  LEU B  167  1                                   7
HELIX   19 AC1 ASP B  180  LEU B  184  5                                   5
HELIX   20 AC2 ASN B  187  ASP B  197  1                                  11
HELIX   21 AC3 LYS B  206  LEU B  224  1                                  19
HELIX   22 AC4 PRO B  225  LEU B  227  5                                   3
HELIX   23 AC5 ASP B  243  ALA B  254  1                                  12
HELIX   24 AC6 VAL B  270  GLU B  274  5                                   5
HELIX   25 AC7 LEU B  275  THR B  296  1                                  22
SHEET    1 AA116 HIS A  21  VAL A  23  0
SHEET    2 AA116 TYR A  29  TRP A  35 -1  O  LEU A  30   N  LEU A  22
SHEET    3 AA116 LEU A  70  HIS A  75 -1  O  ALA A  74   N  ARG A  33
SHEET    4 AA116 ALA A  43  SER A  48  1  N  ALA A  43   O  LEU A  71
SHEET    5 AA116 VAL A 116  SER A 122  1  O  LEU A 119   N  SER A  48
SHEET    6 AA116 GLY A 141  PRO A 147  1  O  ILE A 145   N  GLY A 120
SHEET    7 AA116 PHE A 231  GLY A 236  1  O  LEU A 234   N  SER A 146
SHEET    8 AA116 LYS A 259  TYR A 264  1  O  THR A 260   N  LEU A 233
SHEET    9 AA116 LYS B 259  TYR B 264 -1  O  LEU B 261   N  LEU A 261
SHEET   10 AA116 PHE B 231  GLY B 236  1  N  LEU B 233   O  THR B 260
SHEET   11 AA116 GLY B 141  PRO B 147  1  N  SER B 146   O  LEU B 234
SHEET   12 AA116 VAL B 116  SER B 122  1  N  GLY B 120   O  ILE B 145
SHEET   13 AA116 ALA B  43  SER B  48  1  N  SER B  48   O  LEU B 119
SHEET   14 AA116 LEU B  70  HIS B  75  1  O  LEU B  71   N  ALA B  43
SHEET   15 AA116 TYR B  29  TRP B  35 -1  N  ARG B  33   O  ALA B  74
SHEET   16 AA116 HIS B  21  VAL B  23 -1  N  LEU B  22   O  LEU B  30
LINK         OG  SER A 122                 C15 E3A A 401     1555   1555  1.44
LINK         OG  SER B 122                 C15AE3A B 401     1555   1555  1.48
LINK         OG  SER B 122                 C15BE3A B 401     1555   1555  1.49
SITE     1 AC1  8 ALA A  51  SER A 122  MET A 123  LEU A 176
SITE     2 AC1  8 GLY A 177  LEU A 241  CYS A 242  HOH A 547
SITE     1 AC2 18 ALA B  51  HIS B 121  MET B 123  GLY B 124
SITE     2 AC2 18 GLY B 125  ALA B 126  ILE B 145  SER B 146
SITE     3 AC2 18 PRO B 147  LEU B 148  LEU B 176  GLY B 177
SITE     4 AC2 18 ILE B 179  LEU B 213  LEU B 214  LEU B 241
SITE     5 AC2 18 CYS B 242  HIS B 269
SITE     1 AC3 18 ALA B  51  HIS B 121  MET B 123  GLY B 124
SITE     2 AC3 18 GLY B 125  ALA B 126  ILE B 145  SER B 146
SITE     3 AC3 18 PRO B 147  LEU B 148  LEU B 176  GLY B 177
SITE     4 AC3 18 ILE B 179  LEU B 213  LEU B 214  LEU B 241
SITE     5 AC3 18 CYS B 242  HIS B 269
CRYST1   86.310  126.620  138.060  90.00  90.00  90.00 I 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      0.011586  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007898  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007243        0.00000
TER    2165      ALA A 297
TER    4364      THR B 296
MASTER      442    0    2   25   16    0   12    6 4845    2   62   54
END