longtext: 1LZK-pdb

content
HEADER    HYDROLASE                               10-JUN-02   1LZK
TITLE     BACTERIAL HEROIN ESTERASE COMPLEX WITH TRANSITION STATE
TITLE    2 ANALOG DIMETHYLARSENIC ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEROIN ESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE   3 ORGANISM_COMMON: BACTERIA;
SOURCE   4 STRAIN: H1;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834-(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS    ALPHA/BETA HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.ZHU,N.A.LARSEN,A.BASRAN,N.C.BRUCE,I.A.WILSON
REVDAT   1   28-JAN-03 1LZK    0
JRNL        AUTH   X.ZHU,N.A.LARSEN,A.BASRAN,N.C.BRUCE,I.A.WILSON
JRNL        TITL   OBSERVATION OF AN ARSENIC ADDUCT IN AN ACETYL
JRNL        TITL 2 ESTERASE CRYSTAL STRUCTURE
JRNL        REF    J.BIOL.CHEM.                  V. 278  2008 2003
JRNL        REFN   ASTM JBCHA3  US ISSN 0021-9258
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 1.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.40
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.157
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.223
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2725
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 55415
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.150
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.212
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2375
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 48433
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2386
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 4
REMARK   3   SOLVENT ATOMS      : 309
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 6
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.013
REMARK   3   ANGLE DISTANCES                      (A) : 0.027
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.027
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.053
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.056
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.014
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.003
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.052
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.075
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1LZK COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-2002
REMARK 200  TEMPERATURE           (KELVIN) : 92.7
REMARK 200  PH                             : 6.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : 11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.89471
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM Q315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56480
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.400
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 21.300
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 42.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.65300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CHLORIDE,
REMARK 280  CACODYLATE, PH 6.5, EVAPORATION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,2/3+Z
REMARK 290       3555   -X+Y,-X,1/3+Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,1/3-Z
REMARK 290       6555   -X,-X+Y,2/3-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       70.78000
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       35.39000
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       35.39000
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       70.78000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     1
REMARK 465     LEU A   319
REMARK 465     SER A   320
REMARK 465     PRO A   321
REMARK 465     VAL A   322
REMARK 465     SER A   323
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ARG A 272   NE    ARG A 272   CD    -0.064
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    ARG A 272   CD  -  NE  -  CZ  ANGL. DEV. = 28.6 DEGREES
REMARK 500    ARG A 313   CD  -  NE  -  CZ  ANGL. DEV. = 14.9 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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    LEU A 208      -53.96     72.41
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT GENBANK REFERENCE SEQUENCE
REMARK 999 IS INCORRECT FOR RESIDUES 159, 299, 301, 307-313
REMARK 999 AND 315-322. AUTHORS MAINTAIN THAT THEIR SEQUENCE
REMARK 999 IS CORRECT AND HAS AN ADDITIONAL RESIDUE 323. THIS
REMARK 999 SEQUENCE HAS NOT YET BEEN DEPOSITED IN ANY SEQUENCE
REMARK 999 REFERENCE DATABASE.
DBREF  1LZK A    1   323  GB     2088525  AAC45283         1    322
SEQADV 1LZK MSE A   17  GB   2088525   MET    17 MODIFIED RESIDUE
SEQADV 1LZK MSE A   40  GB   2088525   MET    40 MODIFIED RESIDUE
SEQADV 1LZK MSE A  200  GB   2088525   MET   200 MODIFIED RESIDUE
SEQADV 1LZK MSE A  257  GB   2088525   MET   257 MODIFIED RESIDUE
SEQADV 1LZK GLN A  159  GB   2088525   GLU   159 SEE REMARK 999
SEQADV 1LZK ALA A  299  GB   2088525   GLY   299 SEE REMARK 999
SEQADV 1LZK SER A  301  GB   2088525   ARG   301 SEE REMARK 999
SEQADV 1LZK GLU A  307  GB   2088525   LYS   307 SEE REMARK 999
SEQADV 1LZK ALA A  308  GB   2088525   PRO   308 SEE REMARK 999
SEQADV 1LZK LEU A  309  GB   2088525   HIS   309 SEE REMARK 999
SEQADV 1LZK THR A  310  GB   2088525   CYS   310 SEE REMARK 999
SEQADV 1LZK ALA A  311  GB   2088525   ASP   311 SEE REMARK 999
SEQADV 1LZK ILE A  312  GB   2088525   PRO   312 SEE REMARK 999
SEQADV 1LZK ARG A  313  GB   2088525   GLU   313 SEE REMARK 999
SEQADV 1LZK GLY A  315  GB   2088525   VAL   315 SEE REMARK 999
SEQADV 1LZK LEU A  316  GB   2088525   ALA   316 SEE REMARK 999
SEQADV 1LZK ARG A  317  GB   2088525   PHE   317 SEE REMARK 999
SEQADV 1LZK SER A  318  GB   2088525   ALA   318 SEE REMARK 999
SEQADV 1LZK LEU A  319  GB   2088525   VAL   319 SEE REMARK 999
SEQADV 1LZK SER A  320  GB   2088525   ALA   320 SEE REMARK 999
SEQADV 1LZK PRO A  321  GB   2088525   VAL   321 SEE REMARK 999
SEQADV 1LZK VAL A  322  GB   2088525   SER   322 SEE REMARK 999
SEQADV 1LZK SER A  323  GB   2088525         323 SEE REMARK 999
SEQRES   1 A  323  MET THR THR PHE PRO THR LEU ASP PRO GLU LEU ALA ALA
SEQRES   2 A  323  ALA LEU THR MSE LEU PRO LYS VAL ASP PHE ALA ASP LEU
SEQRES   3 A  323  PRO ASN ALA ARG ALA THR TYR ASP ALA LEU ILE GLY ALA
SEQRES   4 A  323  MSE LEU ALA ASP LEU SER PHE ASP GLY VAL SER LEU ARG
SEQRES   5 A  323  GLU LEU SER ALA PRO GLY LEU ASP GLY ASP PRO GLU VAL
SEQRES   6 A  323  LYS ILE ARG PHE VAL THR PRO ASP ASN THR ALA GLY PRO
SEQRES   7 A  323  VAL PRO VAL LEU LEU TRP ILE HIS GLY GLY GLY PHE ALA
SEQRES   8 A  323  ILE GLY THR ALA GLU SER SER ASP PRO PHE CYS VAL GLU
SEQRES   9 A  323  VAL ALA ARG GLU LEU GLY PHE ALA VAL ALA ASN VAL GLU
SEQRES  10 A  323  TYR ARG LEU ALA PRO GLU THR THR PHE PRO GLY PRO VAL
SEQRES  11 A  323  ASN ASP CYS TYR ALA ALA LEU LEU TYR ILE HIS ALA HIS
SEQRES  12 A  323  ALA GLU GLU LEU GLY ILE ASP PRO SER ARG ILE ALA VAL
SEQRES  13 A  323  GLY GLY GLN SER ALA GLY GLY GLY LEU ALA ALA GLY THR
SEQRES  14 A  323  VAL LEU LYS ALA ARG ASP GLU GLY VAL VAL PRO VAL ALA
SEQRES  15 A  323  PHE GLN PHE LEU GLU ILE PRO GLU LEU ASP ASP ARG LEU
SEQRES  16 A  323  GLU THR VAL SER MSE THR ASN PHE VAL ASP THR PRO LEU
SEQRES  17 A  323  TRP HIS ARG PRO ASN ALA ILE LEU SER TRP LYS TYR TYR
SEQRES  18 A  323  LEU GLY GLU SER TYR SER GLY PRO GLU ASP PRO ASP VAL
SEQRES  19 A  323  SER ILE TYR ALA ALA PRO SER ARG ALA THR ASP LEU THR
SEQRES  20 A  323  GLY LEU PRO PRO THR TYR LEU SER THR MSE GLU LEU ASP
SEQRES  21 A  323  PRO LEU ARG ASP GLU GLY ILE GLU TYR ALA LEU ARG LEU
SEQRES  22 A  323  LEU GLN ALA GLY VAL SER VAL GLU LEU HIS SER PHE PRO
SEQRES  23 A  323  GLY THR PHE HIS GLY SER ALA LEU VAL ALA THR ALA ALA
SEQRES  24 A  323  VAL SER GLU ARG GLY ALA ALA GLU ALA LEU THR ALA ILE
SEQRES  25 A  323  ARG ARG GLY LEU ARG SER LEU SER PRO VAL SER
MODRES 1LZK MSE A   17  MET  SELENOMETHIONINE
MODRES 1LZK MSE A   40  MET  SELENOMETHIONINE
MODRES 1LZK MSE A  200  MET  SELENOMETHIONINE
MODRES 1LZK MSE A  257  MET  SELENOMETHIONINE
HET    MSE  A  17       8
HET    MSE  A  40       8
HET    MSE  A 200       8
HET    MSE  A 257       8
HET    CAC  A 500       4
HETNAM     MSE SELENOMETHIONINE
HETNAM     CAC CACODYLATE ION
FORMUL   1  MSE    4(C5 H11 N1 O2 SE1)
FORMUL   2  CAC    C2 H6 O2 AS1 1-
FORMUL   3  HOH   *309(H2 O1)
HELIX    1   1 ASP A    8  ALA A   14  1                                   7
HELIX    2   2 ASP A   25  ALA A   42  1                                  18
HELIX    3   3 THR A   94  SER A   97  5                                   4
HELIX    4   4 SER A   98  GLY A  110  1                                  13
HELIX    5   5 PRO A  127  HIS A  143  1                                  17
HELIX    6   6 HIS A  143  GLY A  148  1                                   6
HELIX    7   7 SER A  160  GLY A  177  1                                  18
HELIX    8   8 THR A  197  PHE A  203  1                                   7
HELIX    9   9 HIS A  210  GLY A  223  1                                  14
HELIX   10  10 ALA A  239  ALA A  243  5                                   5
HELIX   11  11 LEU A  262  ALA A  276  1                                  15
HELIX   12  12 GLY A  291  VAL A  295  5                                   5
HELIX   13  13 ALA A  298  LEU A  316  1                                  19
SHEET    1   A 8 VAL A  49  ALA A  56  0
SHEET    2   A 8 VAL A  65  PRO A  72 -1  O  VAL A  65   N  ALA A  56
SHEET    3   A 8 ALA A 112  VAL A 116 -1  O  ASN A 115   N  ARG A  68
SHEET    4   A 8 VAL A  79  ILE A  85  1  N  LEU A  82   O  ALA A 114
SHEET    5   A 8 PHE A 183  GLU A 187  1  O  GLU A 187   N  GLY A 158
SHEET    6   A 8 THR A 252  MSE A 257  1  O  TYR A 253   N  LEU A 186
SHEET    7   A 8 VAL A 280  PHE A 285  1  O  GLU A 281   N  LEU A 254
LINK         OG  SER A 160                AS   CAC A 500
CISPEP   1 GLY A   77    PRO A   78          0         1.01
CISPEP   2 ALA A  121    PRO A  122          0        -2.02
CISPEP   3 PHE A  126    PRO A  127          0         5.92
CRYST1   71.584   71.584  106.170  90.00  90.00 120.00 P 32 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      0.013970  0.008065  0.000000        0.00000
SCALE2      0.000000  0.016131  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009419        0.00000
END