longtext: 6fqn-pdb

content
HEADER    HYDROLASE                               14-FEB-18   6FQN
TITLE     CARBAMYLATED T. CALIFORNICA ACETYLCHOLINETERASE BOUND TO UNCHARGED
TITLE    2 HYBRID REACTIVATOR 2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: ACHE;
COMPND   5 EC: 3.1.1.7;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE   4 ORGANISM_TAXID: 7787;
SOURCE   5 GENE: ACHE;
SOURCE   6 EXPRESSION_SYSTEM: TETRONARCE CALIFORNICA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7787
KEYWDS    ACETYLCHOLINESTERASE HYBRID REACTIVATORS ORGANOPHOSPHATE INHIBITION
KEYWDS   2 STRUCTURE-BASED OPTIMIZATION, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.DE LA MORA,G.SANTONI,J.DE SOUZA,J.SUSSMAN,I.SILMAN,R.BAATI,M.WEIK,
AUTHOR   2 F.NACHON
REVDAT   1   29-AUG-18 6FQN    0
JRNL        AUTH   G.SANTONI,J.DE SOUSA,E.DE LA MORA,J.DIAS,L.JEAN,J.L.SUSSMAN,
JRNL        AUTH 2 I.SILMAN,P.Y.RENARD,R.C.D.BROWN,M.WEIK,R.BAATI,F.NACHON
JRNL        TITL   STRUCTURE-BASED OPTIMIZATION OF NON-QUATERNARY REACTIVATORS
JRNL        TITL 2 OF ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHORUS NERVE
JRNL        TITL 3 AGENTS.
JRNL        REF    J. MED. CHEM.                              2018
JRNL        REFN                   ISSN 1520-4804
JRNL        PMID   30125110
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00592
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575
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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.97
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.351
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 45847
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.234
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.362
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
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)     : 0.336
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.774
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 41.15
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.74
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      :  0.007           4503
REMARK   3   ANGLE     :  1.032           6114
REMARK   3   CHIRALITY :  0.057            638
REMARK   3   PLANARITY :  0.007            791
REMARK   3   DIHEDRAL  : 23.604           1654
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 6FQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-15
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               : ESRF
REMARK 200  BEAMLINE                       : ID23-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45946
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.980
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 6.900
REMARK 200  R MERGE                    (I) : 0.10600
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) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.69100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.330
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100 MM PH 5.4 PEG 200 28%, VAPOR
REMARK 280  DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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       45.85667
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       91.71333
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       91.71333
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       45.85667
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: 6770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       45.85667
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   OE1  GLU A   260     O    HOH A   701              2.07
REMARK 500   ND2  ASN A    59     O5   NAG A   602              2.14
REMARK 500   O    PRO A   104     O    HOH A   702              2.15
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    VAL A  22      111.97   -165.26
REMARK 500    PHE A  45       -4.54     80.59
REMARK 500    SER A 108       88.17   -159.85
REMARK 500    PHE A 120       -2.97     67.72
REMARK 500    ALA A 164       73.20   -155.45
REMARK 500    PRO A 191        0.61    -67.24
REMARK 500    BXT A 200     -115.98     65.33
REMARK 500    PHE A 284       78.88    -65.89
REMARK 500    ASP A 285      -21.51   -172.32
REMARK 500    SER A 286     -119.16     99.57
REMARK 500    GLU A 299      -75.80    -85.27
REMARK 500    THR A 303     -163.61   -129.50
REMARK 500    THR A 317     -156.51   -155.76
REMARK 500    ASP A 380       43.82   -153.09
REMARK 500    VAL A 400      -64.37   -137.52
REMARK 500    ASN A 424       36.50   -143.03
REMARK 500    HIS A 440      123.69    -33.90
REMARK 500    PRO A 485      -72.10    -48.30
REMARK 500    ARG A 515       69.33     64.06
REMARK 500    ARG A 517       46.05     35.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASP A  285     SER A  286                  133.68
REMARK 500 SER A  286     ILE A  287                 -124.88
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 E2W A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800  to ASN A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800  to ASN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800  to ASN A 457
DBREF  6FQN A    4   535  UNP    P04058   ACES_TETCF      25    556
SEQRES   1 A  532  SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET
SEQRES   2 A  532  GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA
SEQRES   3 A  532  PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN
SEQRES   4 A  532  MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER
SEQRES   5 A  532  GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN
SEQRES   6 A  532  GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER
SEQRES   7 A  532  GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS
SEQRES   8 A  532  LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS
SEQRES   9 A  532  SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE
SEQRES  10 A  532  TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS
SEQRES  11 A  532  TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU
SEQRES  12 A  532  SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS
SEQRES  13 A  532  GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP
SEQRES  14 A  532  GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN
SEQRES  15 A  532  PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY
SEQRES  16 A  532  GLU BXT ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU
SEQRES  17 A  532  SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU
SEQRES  18 A  532  GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER
SEQRES  19 A  532  VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG
SEQRES  20 A  532  ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE
SEQRES  21 A  532  HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP
SEQRES  22 A  532  VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG
SEQRES  23 A  532  PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO
SEQRES  24 A  532  THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS
SEQRES  25 A  532  LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY
SEQRES  26 A  532  SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS
SEQRES  27 A  532  ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER
SEQRES  28 A  532  GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY
SEQRES  29 A  532  LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP
SEQRES  30 A  532  ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP
SEQRES  31 A  532  ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS
SEQRES  32 A  532  PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR
SEQRES  33 A  532  LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP
SEQRES  34 A  532  PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU
SEQRES  35 A  532  PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR
SEQRES  36 A  532  THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS
SEQRES  37 A  532  TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU
SEQRES  38 A  532  PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR
SEQRES  39 A  532  LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET
SEQRES  40 A  532  LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE
SEQRES  41 A  532  TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR
MODRES 6FQN BXT A  200  SER  MODIFIED RESIDUE
HET    BXT  A 200      12
HET    E2W  A 601      30
HET    NAG  A 602      14
HET    NAG  A 603      14
HET    NAG  A 604      14
HET    EDO  A 605       4
HET     CL  A 606       1
HET     CL  A 607       1
HET     CL  A 608       1
HET     CL  A 609       1
HET     CL  A 610       1
HET     CL  A 611       1
HET    P6G  A 612      19
HET    EDO  A 613       4
HETNAM     BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-
HETNAM   2 BXT  PROPANOIC ACID
HETNAM     E2W 6-[4-[(7-CHLORANYL-1,2,3,4-TETRAHYDROACRIDIN-9-YL)
HETNAM   2 E2W  AMINO]BUTYL]-2-[(OXIDANYLAMINO)METHYL]PYRIDIN-3-OL
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM      CL CHLORIDE ION
HETNAM     P6G HEXAETHYLENE GLYCOL
HETSYN     EDO ETHYLENE GLYCOL
HETSYN     P6G POLYETHYLENE GLYCOL PEG400
FORMUL   1  BXT    C7 H14 N2 O4
FORMUL   2  E2W    C23 H27 CL N4 O2
FORMUL   3  NAG    3(C8 H15 N O6)
FORMUL   6  EDO    2(C2 H6 O2)
FORMUL   7   CL    6(CL 1-)
FORMUL  13  P6G    C12 H26 O7
FORMUL  15  HOH   *163(H2 O)
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6
HELIX    3 AA3 LEU A  127  ASN A  131  5                                   5
HELIX    4 AA4 GLY A  132  GLU A  140  1                                   9
HELIX    5 AA5 VAL A  150  LEU A  156  1                                   7
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3
HELIX    8 AA8 BXT A  200  SER A  212  1                                  13
HELIX    9 AA9 SER A  212  ASP A  217  1                                   6
HELIX   10 AB1 SER A  237  LEU A  252  1                                  16
HELIX   11 AB2 SER A  258  LYS A  269  1                                  12
HELIX   12 AB3 LYS A  270  GLU A  278  1                                   9
HELIX   13 AB4 TRP A  279  LEU A  282  5                                   4
HELIX   14 AB5 SER A  304  GLY A  312  1                                   9
HELIX   15 AB6 GLY A  328  ALA A  336  1                                   9
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13
HELIX   17 AB8 ASN A  364  THR A  376  1                                  13
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18
HELIX   19 AC1 VAL A  400  LYS A  413  1                                  14
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6
HELIX   22 AC4 GLY A  449  ASN A  457  5                                   9
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10
HELIX   25 AC7 GLN A  526  ALA A  534  1                                   9
SHEET    1 AA1 3 LEU A   7  THR A  10  0
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16
SHEET    1 AA211 THR A  18  PRO A  21  0
SHEET    2 AA211 HIS A  26  PRO A  34 -1  O  ILE A  27   N  VAL A  20
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  LEU A  97   N  ILE A  33
SHEET    4 AA211 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100
SHEET    5 AA211 THR A 109  ILE A 115  1  N  MET A 112   O  VAL A 144
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  ASP A 190   N  THR A 109
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198
SHEET    8 AA211 ILE A 319  ASN A 324  1  O  LEU A 320   N  ALA A 222
SHEET    9 AA211 THR A 418  PHE A 423  1  O  PHE A 423   N  VAL A 323
SHEET   10 AA211 LYS A 501  LEU A 505  1  O  LEU A 505   N  PHE A 422
SHEET   11 AA211 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.04
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.04
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.04
LINK         ND2 ASN A  59                 C1  NAG A 602     1555   1555  1.44
LINK         C   GLU A 199                 N   BXT A 200     1555   1555  1.33
LINK         C   BXT A 200                 N   ALA A 201     1555   1555  1.33
LINK         ND2 ASN A 416                 C1  NAG A 603     1555   1555  1.45
LINK         ND2 ASN A 457                 C1  NAG A 604     1555   1555  1.45
CISPEP   1 SER A  103    PRO A  104          0         5.06
SITE     1 AC1 15 LYS A  11  TYR A  70  TYR A 121  HIS A 181
SITE     2 AC1 15 GLN A 185  PRO A 191  LYS A 192  TRP A 279
SITE     3 AC1 15 LEU A 282  ILE A 287  TYR A 334  GLY A 335
SITE     4 AC1 15 P6G A 612  HOH A 717  HOH A 809
SITE     1 AC2  4 ARG A 242  VAL A 246  LEU A 256  ASP A 259
SITE     1 AC3  1 HIS A 406
SITE     1 AC4  4 HIS A 425  ASN A 506  THR A 507  GLU A 508
SITE     1 AC5 10 TRP A  84  GLY A 117  GLY A 118  GLU A 199
SITE     2 AC5 10 BXT A 200  GLU A 327  PHE A 330  PHE A 331
SITE     3 AC5 10 HIS A 440  E2W A 601
SITE     1 AC6  5 SER A  79  MET A  83  ASN A 429  LEU A 430
SITE     2 AC6  5 VAL A 431
SITE     1 AC7  1 ASN A  59
SITE     1 AC8  1 ASN A 416
SITE     1 AC9  3 GLU A 455  ASN A 457  HOH A 766
CRYST1  113.430  113.430  137.570  90.00  90.00 120.00 P 31 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      0.008816  0.005090  0.000000        0.00000
SCALE2      0.000000  0.010180  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007269        0.00000
TER    4273      THR A 535
MASTER      304    0   14   25   14    0   15    6 4518    1  122   41
END