longtext: 6nea-pdb

content
HEADER    HYDROLASE                               17-DEC-18   6NEA
TITLE     HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH REACTIVATOR, HLO7
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: ACHE;
COMPND   5 EC: 3.1.1.7;
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: ACHE;
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS    HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.M.BESTER,J.MCGUIRE,J.J.HEIGHT,S.D.PEGAN
REVDAT   1   12-JUN-19 6NEA    0
JRNL        AUTH   F.L.HSU,S.Y.BAE,J.MCGUIRE,D.R.ANDERSON,S.M.BESTER,
JRNL        AUTH 2 J.J.HEIGHT,S.D.PEGAN,A.J.WALZ
JRNL        TITL   SYNTHESIS AND MOLECULAR PROPERTIES OF NERVE AGENT
JRNL        TITL 2 REACTIVATOR HLO-7 DIMETHANESULFONATE.
JRNL        REF    ACS MED.CHEM.LETT.            V.  10   761 2019
JRNL        REFN                   ISSN 1948-5875
JRNL        PMID   31097996
JRNL        DOI    10.1021/ACSMEDCHEMLETT.9B00021
REMARK   2
REMARK   2 RESOLUTION.    2.42 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (DEV_3311: ???)
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) : 2.42
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.25
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 79534
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : 0.205
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980
REMARK   3   FREE R VALUE TEST SET COUNT      : 3962
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 41.2585 -  7.3325    0.98     2916   150  0.1827 0.1940
REMARK   3     2  7.3325 -  5.8253    1.00     2791   154  0.1870 0.2216
REMARK   3     3  5.8253 -  5.0904    1.00     2802   129  0.1733 0.2061
REMARK   3     4  5.0904 -  4.6257    1.00     2748   156  0.1434 0.1641
REMARK   3     5  4.6257 -  4.2945    1.00     2731   145  0.1337 0.1312
REMARK   3     6  4.2945 -  4.0416    1.00     2691   151  0.1451 0.1742
REMARK   3     7  4.0416 -  3.8393    1.00     2721   141  0.1502 0.1843
REMARK   3     8  3.8393 -  3.6723    1.00     2719   151  0.1563 0.1877
REMARK   3     9  3.6723 -  3.5310    1.00     2684   141  0.1714 0.1970
REMARK   3    10  3.5310 -  3.4092    1.00     2708   121  0.1795 0.1898
REMARK   3    11  3.4092 -  3.3027    1.00     2715   127  0.1802 0.2283
REMARK   3    12  3.3027 -  3.2083    1.00     2686   172  0.1874 0.2012
REMARK   3    13  3.2083 -  3.1239    1.00     2703   129  0.1834 0.2199
REMARK   3    14  3.1239 -  3.0477    1.00     2677   141  0.1818 0.2152
REMARK   3    15  3.0477 -  2.9784    1.00     2660   142  0.1868 0.2261
REMARK   3    16  2.9784 -  2.9150    1.00     2706   107  0.2009 0.2823
REMARK   3    17  2.9150 -  2.8567    1.00     2681   157  0.1995 0.2508
REMARK   3    18  2.8567 -  2.8028    1.00     2700   136  0.2055 0.2677
REMARK   3    19  2.8028 -  2.7528    1.00     2634   147  0.2011 0.2443
REMARK   3    20  2.7528 -  2.7061    1.00     2711   137  0.2009 0.2587
REMARK   3    21  2.7061 -  2.6625    1.00     2680   126  0.2035 0.2740
REMARK   3    22  2.6625 -  2.6215    1.00     2632   152  0.1986 0.2261
REMARK   3    23  2.6215 -  2.5830    1.00     2713   148  0.1992 0.2488
REMARK   3    24  2.5830 -  2.5466    1.00     2634   158  0.2061 0.2518
REMARK   3    25  2.5466 -  2.5122    1.00     2661   152  0.2120 0.2741
REMARK   3    26  2.5122 -  2.4796    1.00     2666   133  0.2216 0.2740
REMARK   3    27  2.4796 -  2.4486    1.00     2673   135  0.2418 0.3038
REMARK   3    28  2.4486 -  2.4191    0.94     2529   124  0.2500 0.2918
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)     : 0.230
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.350
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      :  0.003           8742
REMARK   3   ANGLE     :  0.689          11965
REMARK   3   CHIRALITY :  0.047           1295
REMARK   3   PLANARITY :  0.005           1568
REMARK   3   DIHEDRAL  :  4.865           6948
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 6NEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000238635.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-OCT-16
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79654
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.419
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.11100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.8900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.62900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.550
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 TO 21% PEG 3350, 0.17 - 0.2M
REMARK 280  POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 295K
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      108.08233
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      216.16467
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      216.16467
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      108.08233
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: 5740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 22.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000      -52.36500
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       90.69884
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      648.49400
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     GLY A     2
REMARK 465     GLY A   260
REMARK 465     GLY A   261
REMARK 465     THR A   262
REMARK 465     ARG A   493
REMARK 465     ASP A   494
REMARK 465     PRO A   495
REMARK 465     LYS A   496
REMARK 465     THR A   543
REMARK 465     GLY B     2
REMARK 465     ARG B     3
REMARK 465     GLU B     4
REMARK 465     PRO B   259
REMARK 465     GLY B   260
REMARK 465     GLY B   261
REMARK 465     THR B   262
REMARK 465     GLY B   263
REMARK 465     GLY B   264
REMARK 465     ARG B   493
REMARK 465     ASP B   494
REMARK 465     PRO B   495
REMARK 465     LYS B   496
REMARK 465     THR B   543
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 B   203     O    HOH B   701              2.13
REMARK 500   OE1  GLU B   313     O    HOH B   702              2.17
REMARK 500   O    HOH B   705     O    HOH B  1001              2.17
REMARK 500   OG   SER A   309     O    HOH A   701              2.18
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  47       -0.43     67.41
REMARK 500    PHE A 158       10.48   -142.66
REMARK 500    SER A 203     -122.73     58.10
REMARK 500    ASP A 306      -84.71    -98.16
REMARK 500    VAL A 407      -62.85   -127.18
REMARK 500    ALA B  62       52.73   -114.37
REMARK 500    PHE B 158       12.62   -142.96
REMARK 500    SER B 203     -121.67     56.32
REMARK 500    ASP B 306      -84.32    -99.36
REMARK 500    VAL B 407      -60.72   -126.21
REMARK 500    SER B 462        3.56    -69.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B1047        DISTANCE =  6.36 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     FUC A  606
REMARK 610     NAG A  607
REMARK 610     NAG A  608
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HLO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUC A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HLO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800  601 through NAG A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800  to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800  601 through NAG B 603 bound to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800  to ASN B 464
DBREF  6NEA A    2   543  UNP    P22303   ACES_HUMAN      33    574
DBREF  6NEA B    2   543  UNP    P22303   ACES_HUMAN      33    574
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR
HET    FUC  A 601      10
HET    NAG  A 602      14
HET    NAG  A 603      14
HET    NAG  A 604      14
HET    HLO  A 605      24
HET    FUC  A 606      10
HET    NAG  A 607      14
HET    NAG  A 608      14
HET    FUC  B 601      10
HET    NAG  B 602      14
HET    NAG  B 603      14
HET    NAG  B 604      14
HET    HLO  B 605      24
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     HLO 1-[({2,4-BIS[(E)-(HYDROXYIMINO)METHYL]PYRIDINIUM-1-
HETNAM   2 HLO  YL}METHOXY)METHYL]-4-CARBAMOYLPYRIDINIUM
FORMUL   3  FUC    3(C6 H12 O5)
FORMUL   3  NAG    8(C8 H15 N O6)
FORMUL   5  HLO    2(C15 H17 N5 O4 2+)
FORMUL  12  HOH   *633(H2 O)
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3
HELIX    2 AA2 MET A   42  ARG A   46  5                                   5
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5
HELIX    5 AA5 GLY A  135  ARG A  143  1                                   9
HELIX    6 AA6 GLY A  154  LEU A  159  1                                   6
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3
HELIX    9 AA9 SER A  203  SER A  215  1                                  13
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6
HELIX   11 AB2 MET A  241  VAL A  255  1                                  15
HELIX   12 AB3 ASN A  265  THR A  275  1                                  11
HELIX   13 AB4 PRO A  277  GLU A  285  1                                   9
HELIX   14 AB5 TRP A  286  LEU A  289  5                                   4
HELIX   15 AB6 THR A  311  ALA A  318  1                                   8
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13
HELIX   18 AB9 SER A  371  THR A  383  1                                  13
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10
HELIX   26 AC8 ARG A  534  ALA A  542  1                                   9
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3
HELIX   28 AD1 MET B   42  ARG B   46  5                                   5
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5
HELIX   31 AD4 GLY B  135  ARG B  143  1                                   9
HELIX   32 AD5 GLY B  154  LEU B  159  1                                   6
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6
HELIX   37 AE1 GLY B  240  VAL B  255  1                                  16
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10
HELIX   39 AE3 PRO B  277  GLU B  285  1                                   9
HELIX   40 AE4 TRP B  286  LEU B  289  5                                   4
HELIX   41 AE5 THR B  311  ALA B  318  1                                   8
HELIX   42 AE6 GLY B  335  GLY B  342  5                                   8
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13
HELIX   44 AE8 SER B  371  THR B  383  1                                  13
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10
HELIX   52 AF7 ARG B  534  SER B  541  1                                   8
SHEET    1 AA1 3 LEU A   9  VAL A  12  0
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16
SHEET    1 AA211 ILE A  20  LYS A  23  0
SHEET    2 AA211 PRO A  28  PRO A  36 -1  O  VAL A  29   N  LEU A  22
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  THR A 103   N  SER A  30
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100
SHEET    5 AA211 THR A 112  ILE A 118  1  N  TRP A 117   O  VAL A 147
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  ASP A 193   N  THR A 112
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510
SHEET    1 AA3 2 VAL A  68  CYS A  69  0
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68
SHEET    1 AA4 2 VAL A 239  GLY A 240  0
SHEET    2 AA4 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239
SHEET    1 AA5 3 LEU B   9  VAL B  12  0
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16
SHEET    1 AA611 ILE B  20  THR B  24  0
SHEET    2 AA611 GLY B  27  PRO B  36 -1  O  VAL B  29   N  LEU B  22
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100
SHEET    5 AA611 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510
SHEET    1 AA7 2 VAL B  68  CYS B  69  0
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.04
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.00
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.03
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05
LINK         ND2 ASN A 350                 C1  NAG A 602     1555   1555  1.45
LINK         ND2 ASN A 464                 C1  NAG A 604     1555   1555  1.43
LINK         ND2 ASN B 350                 C1  NAG B 602     1555   1555  1.44
LINK         ND2 ASN B 464                 C1  NAG B 604     1555   1555  1.45
LINK         C1  FUC A 601                 O6  NAG A 602     1555   1555  1.44
LINK         O4  NAG A 602                 C1  NAG A 603     1555   1555  1.46
LINK         C1  FUC B 601                 O6  NAG B 602     1555   1555  1.45
LINK         O4  NAG B 602                 C1  NAG B 603     1555   1555  1.44
CISPEP   1 TYR A  105    PRO A  106          0         0.87
CISPEP   2 CYS A  257    PRO A  258          0        -2.36
CISPEP   3 TYR B  105    PRO B  106          0        -1.74
CISPEP   4 ALA B  497    PRO B  498          0         0.95
SITE     1 AC1 11 TYR A  72  ASP A  74  TYR A 124  VAL A 282
SITE     2 AC1 11 GLU A 285  TRP A 286  TYR A 337  PHE A 338
SITE     3 AC1 11 TYR A 341  HOH A 745  HOH A 797
SITE     1 AC2  1 NAG A 607
SITE     1 AC3  4 ASN A 265  THR A 267  FUC A 606  NAG A 608
SITE     1 AC4  1 NAG A 607
SITE     1 AC5  9 TYR B  72  TYR B 124  VAL B 282  GLU B 285
SITE     2 AC5  9 TRP B 286  PHE B 295  TYR B 337  PHE B 338
SITE     3 AC5  9 TYR B 341
SITE     1 AC6  4 GLY A 345  SER A 347  ASP A 349  ASN A 350
SITE     1 AC7  2 SER A 462  ASN A 464
SITE     1 AC8  4 PRO B 344  GLY B 345  SER B 347  ASN B 350
SITE     1 AC9  1 ASN B 464
CRYST1  104.730  104.730  324.247  90.00  90.00 120.00 P 31 2 1     12
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      0.009548  0.005513  0.000000        0.00000
SCALE2      0.000000  0.011025  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003084        0.00000
TER    4151      ALA A 542
TER    8282      ALA B 542
MASTER      366    0   13   52   34    0   13    6 9072    2  206   84
END