longtext: 7bcc-pdb

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HEADER    HYDROLASE                               19-DEC-20   7BCC
TITLE     NOTUM FRAGMENT 705
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_TAXID: 9606
KEYWDS    NOTUM INHIBITOR, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.ZHAO,E.Y.JONES
REVDAT   1   12-JAN-22 7BCC    0
JRNL        AUTH   Y.ZHAO,E.Y.JONES
JRNL        TITL   NOTUM FRAGMENT SCREEN
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.58 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) : 1.58
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.38
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 47718
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219
REMARK   3   R VALUE            (WORKING SET) : 0.218
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870
REMARK   3   FREE R VALUE TEST SET COUNT      : 2326
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 53.3800 -  4.0600    1.00     2870   173  0.2007 0.2048
REMARK   3     2  4.0600 -  3.2300    1.00     2753   141  0.1985 0.2191
REMARK   3     3  3.2200 -  2.8200    1.00     2706   155  0.2127 0.2126
REMARK   3     4  2.8200 -  2.5600    1.00     2705   134  0.2146 0.2122
REMARK   3     5  2.5600 -  2.3800    0.99     2689   138  0.2069 0.2282
REMARK   3     6  2.3800 -  2.2400    1.00     2682   141  0.2015 0.2382
REMARK   3     7  2.2400 -  2.1200    1.00     2678   135  0.1977 0.2067
REMARK   3     8  2.1200 -  2.0300    1.00     2675   138  0.2102 0.2182
REMARK   3     9  2.0300 -  1.9500    0.99     2656   109  0.2156 0.2681
REMARK   3    10  1.9500 -  1.8900    0.99     2677   117  0.2311 0.2774
REMARK   3    11  1.8900 -  1.8300    0.98     2626   128  0.2489 0.3003
REMARK   3    12  1.8300 -  1.7700    0.99     2636   140  0.2594 0.3175
REMARK   3    13  1.7700 -  1.7300    0.98     2620   137  0.2754 0.3413
REMARK   3    14  1.7300 -  1.6900    0.99     2582   143  0.2997 0.3742
REMARK   3    15  1.6900 -  1.6500    0.99     2651   134  0.3107 0.3161
REMARK   3    16  1.6500 -  1.6100    0.98     2615   137  0.3231 0.3625
REMARK   3    17  1.6100 -  1.5800    0.97     2571   126  0.3513 0.3963
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)     : 0.240
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.130
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.04
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: ( CHAIN A AND ( RESID 88:451 OR RESID 501:502 OR
REMARK   3               RESID 604:692 OR RESID 601:603 OR RESID 507:507 OR
REMARK   3               RESID 503:506 ) )
REMARK   3    ORIGIN FOR THE GROUP (A):    4.460   -1.241   -1.948
REMARK   3    T TENSOR
REMARK   3      T11:   0.1435 T22:   0.1720
REMARK   3      T33:   0.1606 T12:  -0.0004
REMARK   3      T13:  -0.0128 T23:   0.0201
REMARK   3    L TENSOR
REMARK   3      L11:   0.8229 L22:   1.2779
REMARK   3      L33:   0.9805 L12:   0.1440
REMARK   3      L13:  -0.2931 L23:   0.1021
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0195 S12:   0.0281 S13:   0.0256
REMARK   3      S21:   0.0053 S22:   0.0037 S23:  -0.0122
REMARK   3      S31:  -0.0822 S32:   0.0178 S33:   0.0123
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 7BCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292113126.
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   : 48153
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.870
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 6.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61
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   (%): 38.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
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       30.23500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.43700
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.25250
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.43700
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.23500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.25250
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: 1180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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     LEU A   351
REMARK 465     THR A   352
REMARK 465     GLY A   353
REMARK 465     GLN A   354
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     LYS A 197    CG   CD   CE   NZ
REMARK 470     VAL A 280    CG1  CG2
REMARK 470     ASP A 281    CG   OD1  OD2
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 369    CG   CD   NE   CZ   NH1  NH2
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    CYS A 101     -179.57    -69.02
REMARK 500    TRP A 128     -147.93     63.70
REMARK 500    ALA A 191       57.92   -146.39
REMARK 500    ALA A 191       56.48   -146.39
REMARK 500    SER A 232     -127.53     64.92
REMARK 500    GLN A 311     -177.05     67.79
REMARK 500    GLU A 390      154.05     74.47
REMARK 500    ILE A 391      -36.55   -153.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7B84   RELATED DB: PDB
DBREF  7BCC A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451
SEQADV 7BCC GLU A   78  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7BCC THR A   79  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7BCC GLY A   80  UNP  Q6P988              CLONING ARTIFACT
SEQADV 7BCC SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION
SEQADV 7BCC GLY A  452  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC THR A  453  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC LYS A  454  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC HIS A  455  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC HIS A  456  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC HIS A  457  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC HIS A  458  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC HIS A  459  UNP  Q6P988              EXPRESSION TAG
SEQADV 7BCC 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    TB5  A 507      17
HETNAM     SO4 SULFATE ION
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM     TB5 4-(4-PYRROL-1-YLPHENYL)MORPHOLINE
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     TB5 4-[4-(1H-PYRROL-1-YL)PHENYL]MORPHOLINE
FORMUL   2  SO4    5(O4 S 2-)
FORMUL   3  NAG    C8 H15 N O6
FORMUL   8  TB5    C14 H16 N2 O
FORMUL   9  HOH   *92(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  LEU A  216  1                                  14
HELIX    5 AA5 GLY A  217  ALA A  223  5                                   7
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  LEU A 227   N  TRP A 120
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  VAL A 335   N  ALA A 263
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  2.04
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.02
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.04
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.06
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.01
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.01
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.03
LINK         ND2 ASN A  96                 C1  NAG A 502     1555   1555  1.44
CRYST1   60.470   72.505   78.874  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      0.016537  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013792  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012678        0.00000
TER    2835      THR A 451
MASTER      302    0    7   14   14    0    0    6 2949    1   72   30
END