longtext: 7b8l-pdb

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HEADER    HYDROLASE                               13-DEC-20   7B8L
TITLE     NOTUM-FRAGMENT 174
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: HNOTUM;
COMPND   5 EC: 3.1.1.98;
COMPND   6 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: NOTUM, OK/SW-CL.30;
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS    NOTUM FRAGMENT, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.ZHAO,E.Y.JONEES
REVDAT   1   12-JAN-22 7B8L    0
JRNL        AUTH   Y.ZHAO,E.Y.JONES
JRNL        TITL   NOTUM FRAGMENT SCREEN
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   Y.ZHAO,E.Y.JONES
REMARK   1  TITL   NOTUM INHIBITOR
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874
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) : 1.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.39
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 61733
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217
REMARK   3   R VALUE            (WORKING SET) : 0.216
REMARK   3   FREE R VALUE                     : 0.247
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3088
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 53.3900 -  4.0600    1.00     2892   162  0.2005 0.2159
REMARK   3     2  4.0600 -  3.2300    1.00     2764   138  0.1916 0.2380
REMARK   3     3  3.2300 -  2.8200    1.00     2745   146  0.2072 0.2221
REMARK   3     4  2.8200 -  2.5600    1.00     2709   140  0.2047 0.2398
REMARK   3     5  2.5600 -  2.3800    1.00     2711   153  0.1991 0.2264
REMARK   3     6  2.3800 -  2.2400    1.00     2703   134  0.1956 0.2293
REMARK   3     7  2.2400 -  2.1200    1.00     2683   144  0.1933 0.2324
REMARK   3     8  2.1200 -  2.0300    1.00     2705   124  0.1958 0.2556
REMARK   3     9  2.0300 -  1.9500    1.00     2651   146  0.1971 0.2487
REMARK   3    10  1.9500 -  1.8900    1.00     2675   146  0.2067 0.2155
REMARK   3    11  1.8900 -  1.8300    0.99     2657   147  0.2176 0.2655
REMARK   3    12  1.8300 -  1.7800    1.00     2647   149  0.2283 0.2383
REMARK   3    13  1.7700 -  1.7300    0.99     2626   168  0.2428 0.2797
REMARK   3    14  1.7300 -  1.6900    0.99     2614   128  0.2617 0.3106
REMARK   3    15  1.6900 -  1.6500    0.99     2660   146  0.2740 0.3334
REMARK   3    16  1.6500 -  1.6100    0.99     2643   134  0.2888 0.3721
REMARK   3    17  1.6100 -  1.5800    0.99     2655   118  0.3085 0.3121
REMARK   3    18  1.5800 -  1.5500    0.99     2636   133  0.3147 0.3516
REMARK   3    19  1.5500 -  1.5200    0.99     2603   139  0.3283 0.3817
REMARK   3    20  1.5200 -  1.5000    0.98     2617   136  0.3424 0.3806
REMARK   3    21  1.5000 -  1.4700    0.97     2577   129  0.3735 0.3592
REMARK   3    22  1.4700 -  1.4500    0.93     2472   128  0.3758 0.3793
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)     : 0.220
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.820
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.03
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      :   NULL           NULL
REMARK   3   ANGLE     :   NULL           NULL
REMARK   3   CHIRALITY :   NULL           NULL
REMARK   3   PLANARITY :   NULL           NULL
REMARK   3   DIHEDRAL  :   NULL           NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: ALL
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7022  -1.0803  -2.3273
REMARK   3    T TENSOR
REMARK   3      T11:   0.1027 T22:   0.1293
REMARK   3      T33:   0.1025 T12:  -0.0009
REMARK   3      T13:  -0.0066 T23:   0.0162
REMARK   3    L TENSOR
REMARK   3      L11:   0.8846 L22:   1.4338
REMARK   3      L33:   0.7483 L12:   0.1019
REMARK   3      L13:  -0.1753 L23:   0.1105
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0205 S12:   0.0169 S13:   0.0058
REMARK   3      S21:   0.0318 S22:  -0.0100 S23:   0.0071
REMARK   3      S31:  -0.0465 S32:  -0.0057 S33:   0.0254
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 7B8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-17
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               : DIAMOND
REMARK 200  BEAMLINE                       : I04-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9282
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200  DATA SCALING SOFTWARE          : XIA2
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62349
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.350
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 6.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.7000
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     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4UZQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM
REMARK 280  CITRATE, PH4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       30.34550
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.56250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.17050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.56250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.34550
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.17050
REMARK 290   SMTRY3   4  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: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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     GLU A    78
REMARK 465     THR A    79
REMARK 465     GLY A    80
REMARK 465     SER A    81
REMARK 465     ALA A    82
REMARK 465     GLN A    83
REMARK 465     GLN A    84
REMARK 465     LEU A    85
REMARK 465     ASN A    86
REMARK 465     GLU A    87
REMARK 465     THR A   277
REMARK 465     ASP A   278
REMARK 465     CYS A   279
REMARK 465     VAL A   280
REMARK 465     ILE A   283
REMARK 465     LEU A   351
REMARK 465     THR A   352
REMARK 465     GLY A   353
REMARK 465     GLN A   354
REMARK 465     PRO A   355
REMARK 465     ASP A   420
REMARK 465     SER A   421
REMARK 465     HIS A   422
REMARK 465     LYS A   423
REMARK 465     ALA A   424
REMARK 465     SER A   425
REMARK 465     LYS A   426
REMARK 465     THR A   427
REMARK 465     GLY A   452
REMARK 465     THR A   453
REMARK 465     LYS A   454
REMARK 465     HIS A   455
REMARK 465     HIS A   456
REMARK 465     HIS A   457
REMARK 465     HIS A   458
REMARK 465     HIS A   459
REMARK 465     HIS A   460
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     ARG A 115    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 154    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 196    CG   CD   OE1  OE2
REMARK 470     LYS A 197    CG   CD   CE   NZ
REMARK 470     LYS A 251    CG   CD   CE   NZ
REMARK 470     LYS A 272    CG   CD   CE   NZ
REMARK 470     HIS A 276    CG   ND1  CD2  CE1  NE2
REMARK 470     ASP A 281    CG   OD1  OD2
REMARK 470     ARG A 292    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 312    CG   CD   OE1  OE2
REMARK 470     LYS A 376    CG   CD   CE   NZ
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   OE1  GLU A   167     OG1  THR A   282     2554     2.05
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    TRP A 128     -141.63     60.67
REMARK 500    SER A 232     -122.02     61.26
REMARK 500    GLN A 311      178.78     68.62
REMARK 500    GLU A 390      160.76     69.17
REMARK 500    ILE A 391      -36.08   -159.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7B84   RELATED DB: PDB
DBREF  7B8L A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451
SEQADV 7B8L GLU A   78  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7B8L THR A   79  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7B8L GLY A   80  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7B8L SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION
SEQADV 7B8L GLY A  452  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L THR A  453  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L LYS A  454  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  455  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  456  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  457  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  458  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  459  UNP  Q6P988              EXPRESSION TAG
SEQADV 7B8L HIS A  460  UNP  Q6P988              EXPRESSION TAG
SEQRES   1 A  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES   2 A  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES   3 A  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES   4 A  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES   5 A  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES   6 A  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES   7 A  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES   8 A  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES   9 A  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES  10 A  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES  11 A  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES  12 A  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA
SEQRES  13 A  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES  14 A  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES  15 A  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES  16 A  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES  17 A  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES  18 A  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES  19 A  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES  20 A  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES  21 A  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES  22 A  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES  23 A  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES  24 A  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES  25 A  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES  26 A  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES  27 A  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES  28 A  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES  29 A  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS
SEQRES  30 A  383  HIS HIS HIS HIS HIS HIS
HET    SO4  A 501       5
HET    NAG  A 502      14
HET    SO4  A 503       5
HET    SO4  A 504       5
HET    SO4  A 505       5
HET    SO4  A 506       5
HET    SO4  A 507       5
HET    EDO  A 508       4
HET    EDO  A 509       4
HET    EDO  A 510       4
HET    AY4  A 511      14
HETNAM     SO4 SULFATE ION
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     AY4 2,4-BIS(FLUORANYL)-6-(1~{H}-PYRAZOL-3-YL)PHENOL
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   2  SO4    6(O4 S 2-)
FORMUL   3  NAG    C8 H15 N O6
FORMUL   9  EDO    3(C2 H6 O2)
FORMUL  12  AY4    C9 H6 F2 N2 O
FORMUL  13  HOH   *112(H2 O)
HELIX    1 AA1 ASN A  132  MET A  143  1                                  12
HELIX    2 AA2 ARG A  144  MET A  147  5                                   4
HELIX    3 AA3 THR A  159  SER A  163  5                                   5
HELIX    4 AA4 MET A  203  GLY A  217  1                                  15
HELIX    5 AA5 ARG A  218  ALA A  223  5                                   6
HELIX    6 AA6 SER A  232  LEU A  252  1                                  21
HELIX    7 AA7 ALA A  286  ASN A  299  1                                  14
HELIX    8 AA8 PRO A  303  GLN A  311  1                                   9
HELIX    9 AA9 GLU A  314  PHE A  319  5                                   6
HELIX   10 AB1 PHE A  320  TYR A  325  1                                   6
HELIX   11 AB2 PRO A  326  LEU A  328  5                                   3
HELIX   12 AB3 GLU A  341  ASP A  347  1                                   7
HELIX   13 AB4 GLN A  357  LEU A  375  1                                  19
HELIX   14 AB5 LEU A  407  LEU A  418  1                                  12
SHEET    1 AA110 THR A 155  ARG A 156  0
SHEET    2 AA110 LEU A  89  LEU A  93 -1  N  LEU A  89   O  ARG A 156
SHEET    3 AA110 GLY A 108  LYS A 112 -1  O  TYR A 109   N  HIS A  92
SHEET    4 AA110 ASN A 176  ILE A 180 -1  O  PHE A 179   N  TYR A 110
SHEET    5 AA110 ARG A 119  LEU A 124  1  N  PHE A 123   O  ILE A 180
SHEET    6 AA110 VAL A 225  SER A 231  1  O  ALA A 229   N  LEU A 124
SHEET    7 AA110 GLN A 258  ASP A 264  1  O  ARG A 260   N  LEU A 228
SHEET    8 AA110 VAL A 332  VAL A 335  1  O  PHE A 333   N  GLY A 261
SHEET    9 AA110 SER A 381  ALA A 383  1  O  PHE A 382   N  VAL A 334
SHEET   10 AA110 HIS A 435  VAL A 437  1  O  LEU A 436   N  ALA A 383
SHEET    1 AA2 2 PHE A 339  ASP A 340  0
SHEET    2 AA2 2 LEU A 387  SER A 388  1  O  SER A 388   N  PHE A 339
SHEET    1 AA3 2 GLN A 401  VAL A 402  0
SHEET    2 AA3 2 THR A 405  SER A 406 -1  O  THR A 405   N  VAL A 402
SSBOND   1 CYS A  101    CYS A  183                          1555   1555  2.05
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.03
SSBOND   3 CYS A  306    CYS A  318                          1555   1555  2.07
SSBOND   4 CYS A  386    CYS A  449                          1555   1555  2.02
SSBOND   5 CYS A  413    CYS A  432                          1555   1555  2.04
SSBOND   6 CYS A  440    CYS A  445                          1555   1555  2.02
LINK         ND2 ASN A  96                 C1  NAG A 502     1555   1555  1.44
CRYST1   60.691   72.341   79.125  90.00  90.00  90.00 P 21 21 21    4
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      0.016477  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013823  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012638        0.00000
TER    2760      THR A 451
MASTER      339    0   11   14   14    0    0    6 2911    1   83   30
END