longtext: 6cqu-pdb

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HEADER    HYDROLASE                               16-MAR-18   6CQU
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE WITH
TITLE    2 REACTIVATOR HI-6
CAVEAT     6CQU    NAG A 603 HAS WRONG CHIRALITY AT ATOM C1
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,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT
REVDAT   1   05-DEC-18 6CQU    0
JRNL        AUTH   S.M.BESTER,M.A.GUELTA,J.CHEUNG,M.D.WINEMILLER,S.Y.BAE,
JRNL        AUTH 2 J.MYSLINSKI,S.D.PEGAN,J.J.HEIGHT
JRNL        TITL   STRUCTURAL INSIGHTS OF STEREOSPECIFIC INHIBITION OF HUMAN
JRNL        TITL 2 ACETYLCHOLINESTERASE BY VX AND SUBSEQUENT REACTIVATION BY
JRNL        TITL 3 HI-6.
JRNL        REF    CHEM. RES. TOXICOL.                        2018
JRNL        REFN                   ISSN 1520-5010
JRNL        PMID   30462502
JRNL        DOI    10.1021/ACS.CHEMRESTOX.8B00294
REMARK   2
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)
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) : 2.31
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.75
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6
REMARK   3   NUMBER OF REFLECTIONS             : 90115
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.170
REMARK   3   FREE R VALUE                     : 0.207
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020
REMARK   3   FREE R VALUE TEST SET COUNT      : 4524
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 34.7514 -  7.1518    0.93     2958   163  0.1643 0.2103
REMARK   3     2  7.1518 -  5.6846    0.99     2971   189  0.1703 0.1707
REMARK   3     3  5.6846 -  4.9684    0.99     2963   146  0.1497 0.1653
REMARK   3     4  4.9684 -  4.5152    0.98     2964   134  0.1247 0.1630
REMARK   3     5  4.5152 -  4.1922    0.98     2887   148  0.1276 0.1618
REMARK   3     6  4.1922 -  3.9454    0.98     2920   154  0.1367 0.1641
REMARK   3     7  3.9454 -  3.7480    0.98     2865   134  0.1445 0.2052
REMARK   3     8  3.7480 -  3.5850    0.98     2880   172  0.1566 0.1929
REMARK   3     9  3.5850 -  3.4471    0.98     2867   158  0.1634 0.1923
REMARK   3    10  3.4471 -  3.3283    0.98     2852   156  0.1668 0.1939
REMARK   3    11  3.3283 -  3.2243    0.98     2871   153  0.1713 0.2030
REMARK   3    12  3.2243 -  3.1322    0.98     2833   148  0.1783 0.2143
REMARK   3    13  3.1322 -  3.0498    0.98     2842   161  0.1811 0.2280
REMARK   3    14  3.0498 -  2.9754    0.98     2806   172  0.1809 0.2295
REMARK   3    15  2.9754 -  2.9078    0.97     2795   185  0.1846 0.2207
REMARK   3    16  2.9078 -  2.8460    0.98     2790   154  0.1835 0.2271
REMARK   3    17  2.8460 -  2.7891    0.98     2902   128  0.1908 0.2755
REMARK   3    18  2.7891 -  2.7364    0.98     2863   147  0.1940 0.2540
REMARK   3    19  2.7364 -  2.6876    0.97     2798   138  0.1994 0.2488
REMARK   3    20  2.6876 -  2.6421    0.98     2833   145  0.1972 0.2319
REMARK   3    21  2.6421 -  2.5994    0.98     2837   145  0.2096 0.2894
REMARK   3    22  2.5994 -  2.5595    0.97     2790   144  0.2123 0.2444
REMARK   3    23  2.5595 -  2.5218    0.98     2873   127  0.2109 0.2790
REMARK   3    24  2.5218 -  2.4863    0.97     2814   164  0.2175 0.2494
REMARK   3    25  2.4863 -  2.4527    0.97     2802   139  0.2157 0.2741
REMARK   3    26  2.4527 -  2.4209    0.98     2834   150  0.2194 0.2707
REMARK   3    27  2.4209 -  2.3906    0.98     2791   145  0.2357 0.2785
REMARK   3    28  2.3906 -  2.3618    0.98     2816   159  0.2413 0.2928
REMARK   3    29  2.3618 -  2.3344    0.97     2788   129  0.2480 0.2966
REMARK   3    30  2.3344 -  2.3082    0.95     2786   137  0.2596 0.3331
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)     : 0.250
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.090
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           8781
REMARK   3   ANGLE     :  0.656          12010
REMARK   3   CHIRALITY :  0.045           1300
REMARK   3   PLANARITY :  0.005           1570
REMARK   3   DIHEDRAL  : 14.251           5128
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 6CQU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-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-BM
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   : 90125
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.308
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     (%) : 97.5
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.60500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.100
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   (%): 71.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-21% PEG 3350, 0.17-0.21M POTASSIUM
REMARK 280  NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, 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      108.04400
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      216.08800
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      216.08800
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      108.04400
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: 6400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 32.0 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  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -108.04400
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     PRO A   492
REMARK 465     ARG A   493
REMARK 465     ASP A   494
REMARK 465     PRO A   495
REMARK 465     LYS A   496
REMARK 465     ALA A   497
REMARK 465     THR A   543
REMARK 465     GLY B     2
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     PRO B   492
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   O    HOH B   701     O    HOH B   703              1.49
REMARK 500   ND2  ASN B   350     C1   NAG B   603              1.62
REMARK 500   OG   SER B   203     O    HOH B   701              1.83
REMARK 500   O    HOH B   703     O    HOH B   971              1.89
REMARK 500   O    HOH B   834     O    HOH B  1055              2.11
REMARK 500   O    HOH B   705     O    HOH B  1015              2.12
REMARK 500   O    HOH A   802     O    HOH A  1017              2.13
REMARK 500   ND2  ASN A   350     C2   NAG A   603              2.13
REMARK 500   O    HOH B   995     O    HOH B  1055              2.14
REMARK 500   O7   NAG B   603     O    HOH B   702              2.14
REMARK 500   O    HOH A   806     O    HOH A   891              2.14
REMARK 500   O    HOH A   757     O    HOH A  1018              2.15
REMARK 500   OD1  ASP B     5     OH   TYR B   105              2.15
REMARK 500   O    HOH B   993     O    HOH B  1100              2.15
REMARK 500   O    HOH A   944     O    HOH A  1041              2.16
REMARK 500   ND2  ASN A   464     O5   NAG A   605              2.17
REMARK 500   OE1  GLU A   285     O    HOH A   701              2.18
REMARK 500   OG   SER B   203     O    HOH B   703              2.18
REMARK 500   O    HOH A   805     O    HOH A  1017              2.19
REMARK 500   O    HOH B  1015     O    HOH B  1066              2.19
REMARK 500   O    HOH A  1004     O    HOH A  1016              2.19
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       -6.03     73.25
REMARK 500    ALA A 167       69.11   -151.47
REMARK 500    SER A 203     -120.01     59.35
REMARK 500    ASP A 306      -82.10    -93.76
REMARK 500    VAL A 407      -63.30   -127.84
REMARK 500    PHE B  47       -4.17     76.55
REMARK 500    PHE B 158       12.96   -143.15
REMARK 500    SER B 203     -119.48     57.78
REMARK 500    ASP B 306      -85.62    -91.30
REMARK 500    VAL B 407      -62.24   -129.17
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 A1073        DISTANCE =  6.17 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     NAG B  603
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PE A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800  607 through NAG A 609 bound to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A
REMARK 800  602 through NAG A 604 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800  to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B
REMARK 800  602 through NAG B 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6CQT   RELATED DB: PDB
REMARK 900 RELATED ID: 6CQV   RELATED DB: PDB
REMARK 900 RELATED ID: 6CQW   RELATED DB: PDB
REMARK 900 RELATED ID: 6CQX   RELATED DB: PDB
REMARK 900 RELATED ID: 6CQY   RELATED DB: PDB
REMARK 900 RELATED ID: 6CQZ   RELATED DB: PDB
DBREF  6CQU A    2   543  UNP    P22303   ACES_HUMAN      33    574
DBREF  6CQU 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    HI6  A 601      21
HET    FUC  A 602      10
HET    NAG  A 603      14
HET    NAG  A 604      14
HET    NAG  A 605      14
HET    7PE  A 606      21
HET    FUC  A 607      10
HET    NAG  A 608      14
HET    NAG  A 609      14
HET    HI6  B 601      21
HET    FUC  B 602      10
HET    NAG  B 603      14
HET    NAG  B 604      14
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     7PE 2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)
HETNAM   2 7PE  ETHOXY)ETHANOL
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER
HETSYN     7PE POLYETHYLENE GLYCOL FRAGMENT
FORMUL   3  HI6    2(C14 H16 N4 O3 2+)
FORMUL   4  FUC    3(C6 H12 O5)
FORMUL   4  NAG    7(C8 H15 N O6)
FORMUL   6  7PE    C14 H30 O7
FORMUL  10  HOH   *807(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  LEU A  214  1                                  12
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6
HELIX   11 AB2 GLY A  240  VAL A  255  1                                  16
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  GLY A  319  1                                   9
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  SER A  541  1                                   8
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 MET B  241  VAL B  255  1                                  15
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  VAL B  340  1                                   6
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  ALA B  542  1                                   9
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  LEU A  22  0
SHEET    2 AA211 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35
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  GLN A 228   N  GLY A 201
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 3 LEU B   9  VAL B  12  0
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16
SHEET    1 AA511 ILE B  20  LEU B  22  0
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  SER B 196   N  VAL B 114
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510
SHEET    1 AA6 2 VAL B  68  CYS B  69  0
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68
SHEET    1 AA7 2 VAL B 239  GLY B 240  0
SHEET    2 AA7 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  VAL B 239
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  2.03
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.04
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04
LINK         ND2 ASN A 265                 C1  NAG A 608     1555   1555  1.56
LINK         ND2 ASN A 350                 C1  NAG A 603     1555   1555  1.29
LINK         ND2 ASN A 464                 C1  NAG A 605     1555   1555  1.35
LINK         C1  FUC A 602                 O6  NAG A 603     1555   1555  1.53
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.44
LINK         C1  FUC A 607                 O6  NAG A 608     1555   1555  1.44
LINK         O4  NAG A 608                 C1  NAG A 609     1555   1555  1.44
LINK         C1  FUC B 602                 O6  NAG B 603     1555   1555  1.44
LINK         O4  NAG B 603                 C1  NAG B 604     1555   1555  1.44
CISPEP   1 TYR A  105    PRO A  106          0         2.28
CISPEP   2 CYS A  257    PRO A  258          0        -4.21
CISPEP   3 TYR B  105    PRO B  106          0        -1.21
CISPEP   4 CYS B  257    PRO B  258          0        -1.85
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  TYR A 341
SITE     3 AC1 11 HOH A 719  HOH A 728  HOH A 851
SITE     1 AC2  6 GLY A 163  ASP A 304  GLY A 305  ASP A 306
SITE     2 AC2  6 SER A 309  ASN B 283
SITE     1 AC3 12 TRP B  86  GLY B 121  TYR B 124  GLU B 202
SITE     2 AC3 12 PHE B 295  TYR B 337  TYR B 341  HIS B 447
SITE     3 AC3 12 GLY B 448  HOH B 824  HOH B 994  HOH B1039
SITE     1 AC4  4 ASN A 265  THR A 267  GLU A 268  HOH A 960
SITE     1 AC5  4 GLY A 345  ASN A 350  HOH A 892  HOH A 894
SITE     1 AC6  2 SER A 462  ASN A 464
SITE     1 AC7  5 PRO B 344  GLY B 345  SER B 347  ASN B 350
SITE     2 AC7  5 HOH B 702
CRYST1  105.141  105.141  324.132  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      0.009511  0.005491  0.000000        0.00000
SCALE2      0.000000  0.010982  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003085        0.00000
TER    4154      ALA A 542
TER    8298      ALA B 542
MASTER      380    0   13   52   34    0   13    6 9262    2  206   84
END