longtext: 4W1R-pdb

content
HEADER    HYDROLASE                               14-AUG-14   4W1R
TITLE     KINETIC CRYSTALLOGRAPHY OF ALPHA_E7-CARBOXYLESTERSE FROM LUCILLA
TITLE    2 CUPRINA - ABSORBED X-RAY DOSE 9.24 MGY TEMP 150K
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: E3;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES;
COMPND   5 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE   3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE   4 ORGANISM_TAXID: 7375;
SOURCE   5 STRAIN: LS2;
SOURCE   6 GENE: LCAE7;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PETMCSIII
KEYWDS    ALPHA/BETA HYDROLASE FOLD, CARBOXYLESTERASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.J.JACKSON,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY
REVDAT   1   19-AUG-15 4W1R    0
JRNL        AUTH   C.J.JACKSON,P.D.CARR,M.WEIK,T.HUBER,T.MEIRELLES,G.CORREY
JRNL        TITL   MAPPING THE ACCESSIBLE CONFORMATIONAL LANDSCAPE OF AN
JRNL        TITL 2 ORGANOPHOSPHATE DETOXIFYING INSECT CARBOXYLESTERASE USING
JRNL        TITL 3 KINETIC CRYSTALLOGRAPHY AND CONFORMATIONAL ENSEMBLE ANALYSIS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1639)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.24
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 27944
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189
REMARK   3   R VALUE            (WORKING SET) : 0.186
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070
REMARK   3   FREE R VALUE TEST SET COUNT      : 1418
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 46.2521 -  4.8028    0.99     2789   162  0.1609 0.2172
REMARK   3     2  4.8028 -  3.8127    1.00     2661   158  0.1534 0.2098
REMARK   3     3  3.8127 -  3.3309    1.00     2670   124  0.1702 0.2327
REMARK   3     4  3.3309 -  3.0264    1.00     2663   146  0.1902 0.2376
REMARK   3     5  3.0264 -  2.8096    1.00     2618   144  0.2068 0.2891
REMARK   3     6  2.8096 -  2.6439    1.00     2657   145  0.2129 0.2720
REMARK   3     7  2.6439 -  2.5115    1.00     2629   137  0.2196 0.3178
REMARK   3     8  2.5115 -  2.4022    1.00     2613   131  0.2335 0.3412
REMARK   3     9  2.4022 -  2.3097    1.00     2617   133  0.2512 0.3483
REMARK   3    10  2.3097 -  2.2300    1.00     2609   138  0.2731 0.3286
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.760
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           4688
REMARK   3   ANGLE     :  1.062           6341
REMARK   3   CHIRALITY :  0.040            677
REMARK   3   PLANARITY :  0.005            817
REMARK   3   DIHEDRAL  : 13.982           1759
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4W1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-10
REMARK 200  TEMPERATURE           (KELVIN) : 150
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27995
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.240
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.900
REMARK 200  R MERGE                    (I) : 0.10800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.84900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4QWM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PEG2000, 0.1M MES, PH 4.6, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      111.82000
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      111.82000
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       24.68500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.78850
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.68500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.78850
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      111.82000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.68500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.78850
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.82000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.68500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.78850
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL
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     ASN A     2
REMARK 465     PHE A     3
REMARK 465     ASN A     4
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   OG   SER A   218     O4   DPF A   601              1.85
REMARK 500   OE2  GLU A   493     O    HOH A   861              2.16
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
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  73       -3.68     71.11
REMARK 500    ASP A 157       71.36   -100.51
REMARK 500    SER A 218     -121.62     65.98
REMARK 500    CYS A 372       19.13     59.86
REMARK 500    PHE A 421      -60.94   -131.03
REMARK 500    THR A 472       -8.63     78.19
REMARK 500    SER A 542     -140.31   -126.42
REMARK 500    HIS A 566       39.03   -147.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DPF A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QWM   RELATED DB: PDB
REMARK 900 4QWM CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 1.85 MGY AT 100K
REMARK 900 RELATED ID: 4UBI   RELATED DB: PDB
REMARK 900 4UBI CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 3.70 MGY AT 100K
REMARK 900 RELATED ID: 4UBJ   RELATED DB: PDB
REMARK 900 4UBJ CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 5.55 MGY AT 100K
REMARK 900 RELATED ID: 4UBK   RELATED DB: PDB
REMARK 900 4UBK CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 7.40 MGY AT 100K
REMARK 900 RELATED ID: 4UBL   RELATED DB: PDB
REMARK 900 4UBL CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 9.26 MGY AT 100K
REMARK 900 RELATED ID: 4UBM   RELATED DB: PDB
REMARK 900 4UBM CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 11.11 MGY AT 100K
REMARK 900 RELATED ID: 4UBN   RELATED DB: PDB
REMARK 900 4UBN CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 1.85 MGY AT 150K
REMARK 900 RELATED ID: 4UBO   RELATED DB: PDB
REMARK 900 4UBO CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 3.70 MGY AT 150K
REMARK 900 RELATED ID: 4W1P   RELATED DB: PDB
REMARK 900 4W1P CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 5.54 MGY AT 150K
REMARK 900 RELATED ID: 4W1Q   RELATED DB: PDB
REMARK 900 4W1Q CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 7.39 MGY AT 150K
REMARK 900 RELATED ID: 4W1S   RELATED DB: PDB
REMARK 900 4W1S CONTAINS THE SAME PROTEIN COLLECTED AT A TOTAL ABSORBED DOSE
REMARK 900 OF 11.09 MGY AT 150K
DBREF  4W1R A    1   570  UNP    Q25252   Q25252_LUCCU     1    570
SEQADV 4W1R LEU A  364  UNP  Q25252    MET   364 ENGINEERED MUTATION
SEQADV 4W1R PHE A  419  UNP  Q25252    ILE   419 ENGINEERED MUTATION
SEQADV 4W1R THR A  472  UNP  Q25252    ALA   472 ENGINEERED MUTATION
SEQADV 4W1R THR A  505  UNP  Q25252    ILE   505 ENGINEERED MUTATION
SEQADV 4W1R GLU A  530  UNP  Q25252    LYS   530 ENGINEERED MUTATION
SEQADV 4W1R GLY A  554  UNP  Q25252    ASP   554 ENGINEERED MUTATION
SEQRES   1 A  570  MET ASN PHE ASN VAL SER LEU MET GLU LYS LEU LYS TRP
SEQRES   2 A  570  LYS ILE LYS CYS ILE GLU ASN LYS PHE LEU ASN TYR ARG
SEQRES   3 A  570  LEU THR THR ASN GLU THR VAL VAL ALA GLU THR GLU TYR
SEQRES   4 A  570  GLY LYS VAL LYS GLY VAL LYS ARG LEU THR VAL TYR ASP
SEQRES   5 A  570  ASP SER TYR TYR SER PHE GLU GLY ILE PRO TYR ALA GLN
SEQRES   6 A  570  PRO PRO VAL GLY GLU LEU ARG PHE LYS ALA PRO GLN ARG
SEQRES   7 A  570  PRO THR PRO TRP ASP GLY VAL ARG ASP CYS CYS ASN HIS
SEQRES   8 A  570  LYS ASP LYS SER VAL GLN VAL ASP PHE ILE THR GLY LYS
SEQRES   9 A  570  VAL CYS GLY SER GLU ASP CYS LEU TYR LEU SER VAL TYR
SEQRES  10 A  570  THR ASN ASN LEU ASN PRO GLU THR LYS ARG PRO VAL LEU
SEQRES  11 A  570  VAL TYR ILE HIS GLY GLY GLY PHE ILE ILE GLY GLU ASN
SEQRES  12 A  570  HIS ARG ASP MET TYR GLY PRO ASP TYR PHE ILE LYS LYS
SEQRES  13 A  570  ASP VAL VAL LEU ILE ASN ILE GLN TYR ARG LEU GLY ALA
SEQRES  14 A  570  LEU GLY PHE LEU SER LEU ASN SER GLU ASP LEU ASN VAL
SEQRES  15 A  570  PRO GLY ASN ALA GLY LEU LYS ASP GLN VAL MET ALA LEU
SEQRES  16 A  570  ARG TRP ILE LYS ASN ASN CYS ALA ASN PHE GLY GLY ASN
SEQRES  17 A  570  PRO ASP ASN ILE THR VAL PHE GLY GLU SER ALA GLY ALA
SEQRES  18 A  570  ALA SER THR HIS TYR MET MET LEU THR GLU GLN THR ARG
SEQRES  19 A  570  GLY LEU PHE HIS ARG GLY ILE LEU MET SER GLY ASN ALA
SEQRES  20 A  570  ILE CYS PRO TRP ALA ASN THR GLN CYS GLN HIS ARG ALA
SEQRES  21 A  570  PHE THR LEU ALA LYS LEU ALA GLY TYR LYS GLY GLU ASP
SEQRES  22 A  570  ASN ASP LYS ASP VAL LEU GLU PHE LEU MET LYS ALA LYS
SEQRES  23 A  570  PRO GLN ASP LEU ILE LYS LEU GLU GLU LYS VAL LEU THR
SEQRES  24 A  570  LEU GLU GLU ARG THR ASN LYS VAL MET PHE PRO PHE GLY
SEQRES  25 A  570  PRO THR VAL GLU PRO TYR GLN THR ALA ASP CYS VAL LEU
SEQRES  26 A  570  PRO LYS HIS PRO ARG GLU MET VAL LYS THR ALA TRP GLY
SEQRES  27 A  570  ASN SER ILE PRO THR MET MET GLY ASN THR SER TYR GLU
SEQRES  28 A  570  GLY LEU PHE PHE THR SER ILE LEU LYS GLN MET PRO LEU
SEQRES  29 A  570  LEU VAL LYS GLU LEU GLU THR CYS VAL ASN PHE VAL PRO
SEQRES  30 A  570  SER GLU LEU ALA ASP ALA GLU ARG THR ALA PRO GLU THR
SEQRES  31 A  570  LEU GLU MET GLY ALA LYS ILE LYS LYS ALA HIS VAL THR
SEQRES  32 A  570  GLY GLU THR PRO THR ALA ASP ASN PHE MET ASP LEU CYS
SEQRES  33 A  570  SER HIS PHE TYR PHE TRP PHE PRO MET HIS ARG LEU LEU
SEQRES  34 A  570  GLN LEU ARG PHE ASN HIS THR SER GLY THR PRO VAL TYR
SEQRES  35 A  570  LEU TYR ARG PHE ASP PHE ASP SER GLU ASP LEU ILE ASN
SEQRES  36 A  570  PRO TYR ARG ILE MET ARG SER GLY ARG GLY VAL LYS GLY
SEQRES  37 A  570  VAL SER HIS THR ASP GLU LEU THR TYR PHE PHE TRP ASN
SEQRES  38 A  570  GLN LEU ALA LYS ARG MET PRO LYS GLU SER ARG GLU TYR
SEQRES  39 A  570  LYS THR ILE GLU ARG MET THR GLY ILE TRP THR GLN PHE
SEQRES  40 A  570  ALA THR THR GLY ASN PRO TYR SER ASN GLU ILE GLU GLY
SEQRES  41 A  570  MET GLU ASN VAL SER TRP ASP PRO ILE GLU LYS SER ASP
SEQRES  42 A  570  GLU VAL TYR LYS CYS LEU ASN ILE SER ASP GLU LEU LYS
SEQRES  43 A  570  MET ILE ASP VAL PRO GLU MET GLY LYS ILE LYS GLN TRP
SEQRES  44 A  570  GLU SER MET PHE GLU LYS HIS ARG ASP LEU PHE
HET    DPF  A 601       8
HETNAM     DPF DIETHYL HYDROGEN PHOSPHATE
FORMUL   2  DPF    C4 H11 O4 P
FORMUL   3  HOH   *203(H2 O)
HELIX    1 AA1 SER A    6  LEU A   27  1                                  22
HELIX    2 AA2 VAL A   68  ARG A   72  5                                   5
HELIX    3 AA3 TYR A  152  LYS A  156  5                                   5
HELIX    4 AA4 LEU A  167  LEU A  173  1                                   7
HELIX    5 AA5 SER A  177  ASN A  181  5                                   5
HELIX    6 AA6 ASN A  185  CYS A  202  1                                  18
HELIX    7 AA7 ALA A  203  PHE A  205  5                                   3
HELIX    8 AA8 SER A  218  THR A  230  1                                  13
HELIX    9 AA9 GLU A  231  ARG A  234  5                                   4
HELIX   10 AB1 CYS A  249  ASN A  253  5                                   5
HELIX   11 AB2 HIS A  258  ALA A  267  1                                  10
HELIX   12 AB3 ASN A  274  ALA A  285  1                                  12
HELIX   13 AB4 LYS A  286  GLU A  294  1                                   9
HELIX   14 AB5 GLU A  295  VAL A  297  5                                   3
HELIX   15 AB6 THR A  299  ASN A  305  1                                   7
HELIX   16 AB7 HIS A  328  LYS A  334  1                                   7
HELIX   17 AB8 THR A  335  ILE A  341  5                                   7
HELIX   18 AB9 TYR A  350  PHE A  354  5                                   5
HELIX   19 AC1 PHE A  355  MET A  362  1                                   8
HELIX   20 AC2 PRO A  363  THR A  371  5                                   9
HELIX   21 AC3 CYS A  372  VAL A  376  5                                   5
HELIX   22 AC4 ALA A  387  VAL A  402  1                                  16
HELIX   23 AC5 THR A  408  PHE A  421  1                                  14
HELIX   24 AC6 PHE A  421  ASN A  434  1                                  14
HELIX   25 AC7 PRO A  456  ARG A  461  1                                   6
HELIX   26 AC8 GLU A  474  PHE A  478  5                                   5
HELIX   27 AC9 SER A  491  GLY A  511  1                                  21
HELIX   28 AD1 GLU A  552  SER A  561  1                                  10
HELIX   29 AD2 MET A  562  PHE A  570  5                                   9
SHEET    1 AA1 3 THR A  28  ALA A  35  0
SHEET    2 AA1 3 LYS A  41  LEU A  48 -1  O  VAL A  42   N  ALA A  35
SHEET    3 AA1 3 VAL A  85  ASP A  87  1  O  ARG A  86   N  LYS A  43
SHEET    1 AA212 THR A  28  ALA A  35  0
SHEET    2 AA212 LYS A  41  LEU A  48 -1  O  VAL A  42   N  ALA A  35
SHEET    3 AA212 SER A  54  PRO A  62 -1  O  SER A  57   N  VAL A  45
SHEET    4 AA212 TYR A 113  THR A 118 -1  O  THR A 118   N  TYR A  56
SHEET    5 AA212 VAL A 159  ILE A 163 -1  O  LEU A 160   N  TYR A 117
SHEET    6 AA212 ARG A 127  ILE A 133  1  N  TYR A 132   O  ILE A 161
SHEET    7 AA212 GLY A 207  GLU A 217  1  O  ASN A 208   N  ARG A 127
SHEET    8 AA212 ARG A 239  MET A 243  1  O  MET A 243   N  GLY A 216
SHEET    9 AA212 THR A 343  THR A 348  1  O  MET A 344   N  LEU A 242
SHEET   10 AA212 VAL A 441  PHE A 446  1  O  TYR A 442   N  MET A 345
SHEET   11 AA212 LYS A 537  ILE A 541  1  O  ILE A 541   N  ARG A 445
SHEET   12 AA212 LEU A 545  ASP A 549 -1  O  LYS A 546   N  ASN A 540
SHEET    1 AA3 2 GLN A  97  VAL A  98  0
SHEET    2 AA3 2 VAL A 105  CYS A 106 -1  O  CYS A 106   N  GLN A  97
LINK         OG  SER A 218                 P1  DPF A 601     1555   1555  1.51
SITE     1 AC1  9 GLY A 136  GLY A 137  SER A 218  ALA A 219
SITE     2 AC1  9 TRP A 251  PHE A 354  TYR A 457  HIS A 471
SITE     3 AC1  9 THR A 472
CRYST1   49.370  101.577  223.640  90.00  90.00  90.00 C 2 2 21      8
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      0.020255  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009845  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004471        0.00000
TER    4565      PHE A 570
MASTER      304    0    1   29   17    0    3    6 4770    1    9   44
END