longtext: 6rtv-pdb

content
HEADER    HYDROLASE                               27-MAY-19   6RTV
TITLE     CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR
TITLE    2 INACTIVE S270A VARIANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;
COMPND   5 SYNONYM: GLUCURONOYL ESTERASE,GE;
COMPND   6 EC: 3.1.1.-;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CERRENA UNICOLOR;
SOURCE   3 ORGANISM_COMMON: CANKER ROT FUNGUS;
SOURCE   4 ORGANISM_TAXID: 90312;
SOURCE   5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: X-33;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA
KEYWDS    CE15, ESTERASE, ALPHA/BETA-HYDROLASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.A.ERNST,C.MOSBECH,A.LANGKILDE,P.WESTH,A.MEYER,J.W.AGGER,S.LARSEN
REVDAT   1   18-MAR-20 6RTV    0
JRNL        AUTH   H.A.ERNST,C.MOSBECH,A.E.LANGKILDE,P.WESTH,A.S.MEYER,
JRNL        AUTH 2 J.W.AGGER,S.LARSEN
JRNL        TITL   THE STRUCTURAL BASIS OF FUNGAL GLUCURONOYL ESTERASE ACTIVITY
JRNL        TITL 2 ON NATURAL SUBSTRATES.
JRNL        REF    NAT COMMUN                    V.  11  1026 2020
JRNL        REFN                   ESSN 2041-1723
JRNL        PMID   32094331
JRNL        DOI    10.1038/S41467-020-14833-9
REMARK   2
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX 1.13_2998
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) : 1.46
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.39
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 163459
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183
REMARK   3   R VALUE            (WORKING SET) : 0.182
REMARK   3   FREE R VALUE                     : 0.199
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010
REMARK   3   FREE R VALUE TEST SET COUNT      : 8194
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 44.4126 -  4.5350    1.00     5645   303  0.1570 0.1701
REMARK   3     2  4.5350 -  3.6001    1.00     5381   277  0.1421 0.1437
REMARK   3     3  3.6001 -  3.1452    1.00     5295   266  0.1632 0.1800
REMARK   3     4  3.1452 -  2.8577    1.00     5255   298  0.1763 0.1903
REMARK   3     5  2.8577 -  2.6529    1.00     5229   266  0.1728 0.1909
REMARK   3     6  2.6529 -  2.4965    1.00     5246   262  0.1704 0.1818
REMARK   3     7  2.4965 -  2.3715    1.00     5202   280  0.1722 0.1897
REMARK   3     8  2.3715 -  2.2682    1.00     5175   276  0.1760 0.1830
REMARK   3     9  2.2682 -  2.1809    1.00     5207   268  0.1796 0.2071
REMARK   3    10  2.1809 -  2.1057    1.00     5153   265  0.1657 0.1821
REMARK   3    11  2.1057 -  2.0398    1.00     5177   268  0.1888 0.2080
REMARK   3    12  2.0398 -  1.9815    1.00     5146   283  0.1805 0.2226
REMARK   3    13  1.9815 -  1.9293    1.00     5130   277  0.1868 0.2052
REMARK   3    14  1.9293 -  1.8823    1.00     5127   283  0.1831 0.2129
REMARK   3    15  1.8823 -  1.8395    1.00     5164   247  0.1841 0.1937
REMARK   3    16  1.8395 -  1.8003    1.00     5146   261  0.1890 0.2081
REMARK   3    17  1.8003 -  1.7643    1.00     5138   269  0.1972 0.2054
REMARK   3    18  1.7643 -  1.7310    1.00     5134   260  0.1960 0.2236
REMARK   3    19  1.7310 -  1.7001    1.00     5141   278  0.2014 0.2113
REMARK   3    20  1.7001 -  1.6713    1.00     5105   286  0.2137 0.2511
REMARK   3    21  1.6713 -  1.6443    1.00     5098   276  0.2184 0.2651
REMARK   3    22  1.6443 -  1.6190    1.00     5150   251  0.2077 0.2363
REMARK   3    23  1.6190 -  1.5952    1.00     5073   276  0.2107 0.2223
REMARK   3    24  1.5952 -  1.5727    1.00     5144   261  0.2207 0.2342
REMARK   3    25  1.5727 -  1.5515    1.00     5113   276  0.2277 0.2486
REMARK   3    26  1.5515 -  1.5313    1.00     5085   262  0.2387 0.2635
REMARK   3    27  1.5313 -  1.5122    1.00     5116   276  0.2505 0.2790
REMARK   3    28  1.5122 -  1.4940    1.00     5088   275  0.2615 0.2849
REMARK   3    29  1.4940 -  1.4766    1.00     5079   288  0.2719 0.3003
REMARK   3    30  1.4766 -  1.4600    1.00     5123   280  0.2887 0.2922
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)     : 0.150
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.790
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 11.52
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.23
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  : 10
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 128 )
REMARK   3    ORIGIN FOR THE GROUP (A):  65.5103  47.9833  31.2723
REMARK   3    T TENSOR
REMARK   3      T11:   0.1052 T22:   0.0881
REMARK   3      T33:   0.0822 T12:  -0.0068
REMARK   3      T13:  -0.0192 T23:  -0.0203
REMARK   3    L TENSOR
REMARK   3      L11:   2.1446 L22:   1.9418
REMARK   3      L33:   2.1578 L12:   0.3345
REMARK   3      L13:  -0.0257 L23:  -0.6157
REMARK   3    S TENSOR
REMARK   3      S11:   0.0242 S12:  -0.2381 S13:   0.0449
REMARK   3      S21:   0.2125 S22:  -0.0127 S23:   0.0376
REMARK   3      S31:  -0.0617 S32:  -0.0737 S33:  -0.0415
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3937  48.5009  15.4202
REMARK   3    T TENSOR
REMARK   3      T11:   0.1131 T22:   0.0757
REMARK   3      T33:   0.0972 T12:   0.0052
REMARK   3      T13:  -0.0042 T23:  -0.0017
REMARK   3    L TENSOR
REMARK   3      L11:   0.3367 L22:   0.3925
REMARK   3      L33:   0.2945 L12:  -0.1024
REMARK   3      L13:  -0.0492 L23:   0.0248
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0016 S12:   0.0141 S13:  -0.0148
REMARK   3      S21:   0.0072 S22:  -0.0020 S23:   0.0684
REMARK   3      S31:  -0.0049 S32:  -0.0192 S33:   0.0045
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 422 )
REMARK   3    ORIGIN FOR THE GROUP (A):  59.5236  40.6632  13.0068
REMARK   3    T TENSOR
REMARK   3      T11:   0.1021 T22:   0.0833
REMARK   3      T33:   0.0930 T12:   0.0123
REMARK   3      T13:  -0.0064 T23:  -0.0053
REMARK   3    L TENSOR
REMARK   3      L11:   0.3212 L22:   0.5525
REMARK   3      L33:   0.4872 L12:   0.0966
REMARK   3      L13:  -0.0263 L23:  -0.1864
REMARK   3    S TENSOR
REMARK   3      S11:   0.0165 S12:   0.0178 S13:  -0.0267
REMARK   3      S21:  -0.0171 S22:  -0.0347 S23:   0.0057
REMARK   3      S31:   0.0137 S32:   0.0115 S33:   0.0200
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )
REMARK   3    ORIGIN FOR THE GROUP (A):  64.8628  31.9426  15.7426
REMARK   3    T TENSOR
REMARK   3      T11:   0.1241 T22:   0.0858
REMARK   3      T33:   0.1117 T12:   0.0225
REMARK   3      T13:  -0.0032 T23:   0.0100
REMARK   3    L TENSOR
REMARK   3      L11:   0.7151 L22:   0.5870
REMARK   3      L33:   0.5110 L12:   0.3948
REMARK   3      L13:  -0.0609 L23:  -0.0168
REMARK   3    S TENSOR
REMARK   3      S11:   0.0151 S12:  -0.0112 S13:  -0.1143
REMARK   3      S21:   0.0123 S22:  -0.0175 S23:  -0.0323
REMARK   3      S31:   0.0230 S32:   0.0689 S33:   0.0151
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 110 )
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1591   7.5557  36.0393
REMARK   3    T TENSOR
REMARK   3      T11:   0.1184 T22:   0.0991
REMARK   3      T33:   0.1290 T12:   0.0003
REMARK   3      T13:  -0.0301 T23:  -0.0236
REMARK   3    L TENSOR
REMARK   3      L11:   2.5847 L22:   1.7404
REMARK   3      L33:   3.6083 L12:   0.2419
REMARK   3      L13:  -0.8158 L23:   0.0574
REMARK   3    S TENSOR
REMARK   3      S11:   0.0610 S12:  -0.2439 S13:   0.2313
REMARK   3      S21:   0.2055 S22:  -0.0226 S23:   0.0212
REMARK   3      S31:  -0.2143 S32:  -0.0849 S33:  -0.0398
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 149 )
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4640  10.2799  27.9169
REMARK   3    T TENSOR
REMARK   3      T11:   0.0884 T22:   0.0703
REMARK   3      T33:   0.1053 T12:   0.0032
REMARK   3      T13:   0.0160 T23:  -0.0151
REMARK   3    L TENSOR
REMARK   3      L11:   1.2706 L22:   0.5556
REMARK   3      L33:   0.6194 L12:  -0.4196
REMARK   3      L13:   0.3056 L23:  -0.0351
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0067 S12:  -0.0484 S13:  -0.0193
REMARK   3      S21:   0.0627 S22:  -0.0069 S23:   0.0805
REMARK   3      S31:  -0.0222 S32:  -0.0726 S33:   0.0130
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 172 )
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9294  17.0291  19.2578
REMARK   3    T TENSOR
REMARK   3      T11:   0.0856 T22:   0.1139
REMARK   3      T33:   0.1252 T12:   0.0254
REMARK   3      T13:   0.0096 T23:  -0.0002
REMARK   3    L TENSOR
REMARK   3      L11:   1.0896 L22:   7.1958
REMARK   3      L33:   3.9062 L12:   0.3609
REMARK   3      L13:   0.3965 L23:   3.9945
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0030 S12:  -0.0072 S13:   0.0410
REMARK   3      S21:  -0.3147 S22:   0.0853 S23:   0.0040
REMARK   3      S31:  -0.2545 S32:  -0.0958 S33:  -0.0478
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 205 )
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0833  -1.9609  18.6389
REMARK   3    T TENSOR
REMARK   3      T11:   0.0966 T22:   0.1147
REMARK   3      T33:   0.1561 T12:  -0.0248
REMARK   3      T13:   0.0043 T23:  -0.0284
REMARK   3    L TENSOR
REMARK   3      L11:   1.2970 L22:   0.8872
REMARK   3      L33:   2.4116 L12:  -0.2930
REMARK   3      L13:  -0.6243 L23:  -0.0459
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0599 S12:   0.0351 S13:  -0.1305
REMARK   3      S21:   0.0277 S22:  -0.0510 S23:   0.2383
REMARK   3      S31:   0.2038 S32:  -0.2733 S33:   0.0578
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 370 )
REMARK   3    ORIGIN FOR THE GROUP (A):  31.1226   6.6785  17.0615
REMARK   3    T TENSOR
REMARK   3      T11:   0.0962 T22:   0.0802
REMARK   3      T33:   0.0892 T12:   0.0028
REMARK   3      T13:  -0.0019 T23:  -0.0012
REMARK   3    L TENSOR
REMARK   3      L11:   0.5235 L22:   0.5420
REMARK   3      L33:   0.3815 L12:   0.0084
REMARK   3      L13:  -0.0785 L23:  -0.0173
REMARK   3    S TENSOR
REMARK   3      S11:   0.0065 S12:   0.0466 S13:   0.0377
REMARK   3      S21:  -0.0084 S22:  -0.0123 S23:   0.0354
REMARK   3      S31:  -0.0225 S32:  -0.0229 S33:   0.0061
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 371 THROUGH 458 )
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0833 -10.2075  21.0011
REMARK   3    T TENSOR
REMARK   3      T11:   0.1097 T22:   0.0573
REMARK   3      T33:   0.1065 T12:   0.0019
REMARK   3      T13:   0.0005 T23:  -0.0005
REMARK   3    L TENSOR
REMARK   3      L11:   1.0166 L22:   0.5836
REMARK   3      L33:   0.9517 L12:   0.1419
REMARK   3      L13:  -0.1898 L23:   0.1056
REMARK   3    S TENSOR
REMARK   3      S11:   0.0028 S12:   0.0018 S13:  -0.0845
REMARK   3      S21:   0.0196 S22:  -0.0197 S23:   0.0471
REMARK   3      S31:   0.0906 S32:  -0.0108 S33:   0.0197
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 6RTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-18
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                       : MASSIF-3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.3
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 163708
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.170
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 9.700
REMARK 200  R MERGE                    (I) : 0.15800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.86400
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: PHASER
REMARK 200 STARTING MODEL: 3PIC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7, 0.1 M KCL, 25% W/V
REMARK 280  SOKALAN CP7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      130.56350
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       42.13650
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       42.13650
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       65.28175
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       42.13650
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       42.13650
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      195.84525
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       42.13650
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.13650
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       65.28175
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       42.13650
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.13650
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      195.84525
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      130.56350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 898  LIES ON A SPECIAL POSITION.
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   459
REMARK 465     ASN A   460
REMARK 465     LEU A   461
REMARK 465     TYR A   462
REMARK 465     PHE A   463
REMARK 465     GLN A   464
REMARK 465     GLY A   465
REMARK 465     VAL A   466
REMARK 465     ASP A   467
REMARK 465     HIS A   468
REMARK 465     HIS A   469
REMARK 465     HIS A   470
REMARK 465     HIS A   471
REMARK 465     HIS A   472
REMARK 465     HIS A   473
REMARK 465     GLU B   459
REMARK 465     ASN B   460
REMARK 465     LEU B   461
REMARK 465     TYR B   462
REMARK 465     PHE B   463
REMARK 465     GLN B   464
REMARK 465     GLY B   465
REMARK 465     VAL B   466
REMARK 465     ASP B   467
REMARK 465     HIS B   468
REMARK 465     HIS B   469
REMARK 465     HIS B   470
REMARK 465     HIS B   471
REMARK 465     HIS B   472
REMARK 465     HIS B   473
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    ASN A  92       97.81   -162.24
REMARK 500    ARG A 109      -34.00   -131.78
REMARK 500    GLU A 129      -18.51   -141.17
REMARK 500    SER A 162      -12.66     89.40
REMARK 500    GLN A 213       44.77   -150.82
REMARK 500    SER A 215     -170.37   -175.33
REMARK 500    ALA A 270     -129.89     62.99
REMARK 500    ASN A 325     -166.86   -161.32
REMARK 500    PRO A 343       35.32    -80.29
REMARK 500    SER A 370       66.14     63.85
REMARK 500    TRP A 449      -31.74   -134.88
REMARK 500    ASN B  92       96.06   -161.73
REMARK 500    GLN B 213       46.89   -144.53
REMARK 500    SER B 215     -173.49   -171.52
REMARK 500    ALA B 270     -131.17     62.53
REMARK 500    ASN B 325     -166.83   -160.06
REMARK 500    PRO B 343       35.03    -82.05
REMARK 500    SER B 370       65.79     66.92
REMARK 500    TRP B 449      -31.30   -137.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 507  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 259   O
REMARK 620 2 GOL B 505   O2  102.1
REMARK 620 3 GOL B 505   O3  169.9  68.8
REMARK 620 4 HOH B 812   O    97.2 160.8  92.0
REMARK 620 5 HOH B 800   O    91.4  93.4  93.4  87.2
REMARK 620 6 HOH B 798   O    85.5  91.2  90.4  89.3 174.9
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound
REMARK 800  to ASN A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound
REMARK 800  to ASN B 104
DBREF1 6RTV A   79   458  UNP                  GCE_CERUI
DBREF2 6RTV A     A0A0A7EQR3                         95         474
DBREF1 6RTV B   79   458  UNP                  GCE_CERUI
DBREF2 6RTV B     A0A0A7EQR3                         95         474
SEQADV 6RTV GLU A   73  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA A   74  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLU A   75  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA A   76  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLU A   77  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV PHE A   78  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA A  270  UNP  A0A0A7EQR SER   286 ENGINEERED MUTATION
SEQADV 6RTV GLU A  459  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ASN A  460  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV LEU A  461  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV TYR A  462  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV PHE A  463  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLN A  464  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLY A  465  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV VAL A  466  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ASP A  467  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  468  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  469  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  470  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  471  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  472  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS A  473  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLU B   73  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA B   74  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLU B   75  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA B   76  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLU B   77  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV PHE B   78  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ALA B  270  UNP  A0A0A7EQR SER   286 ENGINEERED MUTATION
SEQADV 6RTV GLU B  459  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ASN B  460  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV LEU B  461  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV TYR B  462  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV PHE B  463  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLN B  464  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV GLY B  465  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV VAL B  466  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV ASP B  467  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  468  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  469  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  470  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  471  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  472  UNP  A0A0A7EQR           EXPRESSION TAG
SEQADV 6RTV HIS B  473  UNP  A0A0A7EQR           EXPRESSION TAG
SEQRES   1 A  401  GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA
SEQRES   2 A  401  SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP
SEQRES   3 A  401  PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS
SEQRES   4 A  401  ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU
SEQRES   5 A  401  ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO
SEQRES   6 A  401  PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR
SEQRES   7 A  401  GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN
SEQRES   8 A  401  THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY
SEQRES   9 A  401  THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR
SEQRES  10 A  401  GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR
SEQRES  11 A  401  LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER
SEQRES  12 A  401  ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR
SEQRES  13 A  401  GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL
SEQRES  14 A  401  TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR
SEQRES  15 A  401  PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR
SEQRES  16 A  401  GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY
SEQRES  17 A  401  ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU
SEQRES  18 A  401  SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS
SEQRES  19 A  401  TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL
SEQRES  20 A  401  GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE
SEQRES  21 A  401  ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP
SEQRES  22 A  401  HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET
SEQRES  23 A  401  ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO
SEQRES  24 A  401  MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL
SEQRES  25 A  401  TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA
SEQRES  26 A  401  GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER
SEQRES  27 A  401  LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU
SEQRES  28 A  401  LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN
SEQRES  29 A  401  ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP
SEQRES  30 A  401  ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR
SEQRES  31 A  401  PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES   1 B  401  GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA
SEQRES   2 B  401  SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP
SEQRES   3 B  401  PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS
SEQRES   4 B  401  ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU
SEQRES   5 B  401  ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO
SEQRES   6 B  401  PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR
SEQRES   7 B  401  GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN
SEQRES   8 B  401  THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY
SEQRES   9 B  401  THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR
SEQRES  10 B  401  GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR
SEQRES  11 B  401  LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER
SEQRES  12 B  401  ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR
SEQRES  13 B  401  GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL
SEQRES  14 B  401  TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR
SEQRES  15 B  401  PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR
SEQRES  16 B  401  GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY
SEQRES  17 B  401  ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU
SEQRES  18 B  401  SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS
SEQRES  19 B  401  TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL
SEQRES  20 B  401  GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE
SEQRES  21 B  401  ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP
SEQRES  22 B  401  HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET
SEQRES  23 B  401  ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO
SEQRES  24 B  401  MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL
SEQRES  25 B  401  TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA
SEQRES  26 B  401  GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER
SEQRES  27 B  401  LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU
SEQRES  28 B  401  LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN
SEQRES  29 B  401  ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP
SEQRES  30 B  401  ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR
SEQRES  31 B  401  PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS
HET    NAG  A 501      14
HET    EDO  A 502      10
HET    GOL  A 503      14
HET    GOL  A 504      14
HET    GOL  A 505      14
HET    NAG  B 501      14
HET    EDO  B 502      10
HET    GOL  B 503      14
HET    GOL  B 504      14
HET    GOL  B 505      14
HET    GOL  B 506      14
HET     NA  B 507       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     GOL GLYCEROL
HETNAM      NA SODIUM ION
HETSYN     EDO ETHYLENE GLYCOL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  NAG    2(C8 H15 N O6)
FORMUL   4  EDO    2(C2 H6 O2)
FORMUL   5  GOL    7(C3 H8 O3)
FORMUL  14   NA    NA 1+
FORMUL  15  HOH   *757(H2 O)
HELIX    1 AA1 ALA A   74  GLY A   79  1                                   6
HELIX    2 AA2 THR A  110  GLU A  129  1                                  20
HELIX    3 AA3 SER A  206  ALA A  211  1                                   6
HELIX    4 AA4 SER A  215  ARG A  219  5                                   5
HELIX    5 AA5 GLY A  222  GLY A  229  1                                   8
HELIX    6 AA6 SER A  235  MET A  253  1                                  19
HELIX    7 AA7 THR A  254  ALA A  257  5                                   4
HELIX    8 AA8 ALA A  270  GLU A  283  1                                  14
HELIX    9 AA9 CYS A  301  ASN A  311  1                                  11
HELIX   10 AB1 ASP A  317  ASN A  325  1                                   9
HELIX   11 AB2 SER A  329  TYR A  335  5                                   7
HELIX   12 AB3 LYS A  338  VAL A  342  5                                   5
HELIX   13 AB4 ASP A  345  MET A  352  1                                   8
HELIX   14 AB5 TYR A  366  LEU A  369  5                                   4
HELIX   15 AB6 SER A  370  LEU A  388  1                                  19
HELIX   16 AB7 ILE A  390  ASP A  392  5                                   3
HELIX   17 AB8 PRO A  408  SER A  410  5                                   3
HELIX   18 AB9 LEU A  411  LEU A  423  1                                  13
HELIX   19 AC1 ASN A  445  TRP A  449  5                                   5
HELIX   20 AC2 ALA B   74  GLY B   79  1                                   6
HELIX   21 AC3 THR B  110  GLU B  129  1                                  20
HELIX   22 AC4 SER B  206  ALA B  211  1                                   6
HELIX   23 AC5 SER B  215  ARG B  219  5                                   5
HELIX   24 AC6 GLY B  222  GLY B  229  1                                   8
HELIX   25 AC7 SER B  235  MET B  253  1                                  19
HELIX   26 AC8 THR B  254  ALA B  257  5                                   4
HELIX   27 AC9 ALA B  270  GLU B  283  1                                  14
HELIX   28 AD1 CYS B  301  ASN B  311  1                                  11
HELIX   29 AD2 ASP B  317  ASN B  325  1                                   9
HELIX   30 AD3 SER B  329  TYR B  335  5                                   7
HELIX   31 AD4 LYS B  338  VAL B  342  5                                   5
HELIX   32 AD5 ASP B  345  MET B  352  1                                   8
HELIX   33 AD6 TYR B  366  LEU B  369  5                                   4
HELIX   34 AD7 SER B  370  LEU B  388  1                                  19
HELIX   35 AD8 ILE B  390  ASP B  392  5                                   3
HELIX   36 AD9 PRO B  408  SER B  410  5                                   3
HELIX   37 AE1 LEU B  411  LEU B  423  1                                  13
HELIX   38 AE2 ASN B  445  TRP B  449  5                                   5
SHEET    1 AA1 3 VAL A 139  SER A 147  0
SHEET    2 AA1 3 THR A 150  GLY A 158 -1  O  THR A 152   N  SER A 145
SHEET    3 AA1 3 THR A 164  PHE A 167 -1  O  PHE A 167   N  ILE A 155
SHEET    1 AA210 VAL A 139  SER A 147  0
SHEET    2 AA210 THR A 150  GLY A 158 -1  O  THR A 152   N  SER A 145
SHEET    3 AA210 THR A 170  SER A 172 -1  O  ILE A 171   N  GLY A 151
SHEET    4 AA210 ALA A 201  TYR A 205 -1  O  THR A 202   N  SER A 172
SHEET    5 AA210 TRP A 183  TYR A 189  1  N  ALA A 188   O  LEU A 203
SHEET    6 AA210 ILE A 259  CYS A 269  1  O  GLY A 265   N  ILE A 187
SHEET    7 AA210 LEU A 288  GLN A 292  1  O  ILE A 290   N  VAL A 266
SHEET    8 AA210 ALA A 357  ASN A 363  1  O  ILE A 359   N  THR A 289
SHEET    9 AA210 HIS A 394  VAL A 399  1  O  GLY A 395   N  MET A 358
SHEET   10 AA210 PHE A 433  THR A 434  1  O  THR A 434   N  PHE A 396
SHEET    1 AA3 3 VAL B 139  SER B 147  0
SHEET    2 AA3 3 THR B 150  SER B 160 -1  O  THR B 152   N  SER B 145
SHEET    3 AA3 3 GLN B 163  PHE B 167 -1  O  PHE B 167   N  ILE B 155
SHEET    1 AA410 VAL B 139  SER B 147  0
SHEET    2 AA410 THR B 150  SER B 160 -1  O  THR B 152   N  SER B 145
SHEET    3 AA410 THR B 170  SER B 172 -1  O  ILE B 171   N  GLY B 151
SHEET    4 AA410 ALA B 201  TYR B 205 -1  O  THR B 202   N  SER B 172
SHEET    5 AA410 TRP B 183  TYR B 189  1  N  ALA B 188   O  LEU B 203
SHEET    6 AA410 ILE B 259  CYS B 269  1  O  GLY B 265   N  ILE B 187
SHEET    7 AA410 LEU B 288  GLN B 292  1  O  ILE B 290   N  VAL B 266
SHEET    8 AA410 ALA B 357  ASN B 363  1  O  PHE B 361   N  PRO B 291
SHEET    9 AA410 HIS B 394  VAL B 399  1  O  GLY B 395   N  MET B 358
SHEET   10 AA410 PHE B 433  THR B 434  1  O  THR B 434   N  PHE B 396
SSBOND   1 CYS A   81    CYS A  116                          1555   1555  2.04
SSBOND   2 CYS A  269    CYS A  405                          1555   1555  2.06
SSBOND   3 CYS A  301    CYS A  377                          1555   1555  2.10
SSBOND   4 CYS B   81    CYS B  116                          1555   1555  2.04
SSBOND   5 CYS B  269    CYS B  405                          1555   1555  2.05
SSBOND   6 CYS B  301    CYS B  377                          1555   1555  2.10
LINK         ND2 ASN A 104                 C1  NAG A 501     1555   1555  1.44
LINK         ND2 ASN B 104                 C1  NAG B 501     1555   1555  1.44
LINK         O   ILE B 259                NA    NA B 507     1555   1555  2.30
LINK         O2  GOL B 505                NA    NA B 507     1555   1555  2.48
LINK         O3  GOL B 505                NA    NA B 507     1555   1555  2.46
LINK        NA    NA B 507                 O   HOH B 812     1555   1555  2.41
LINK        NA    NA B 507                 O   HOH B 800     1555   1555  2.48
LINK        NA    NA B 507                 O   HOH B 798     1555   1555  2.52
CISPEP   1 ALA A  354    PRO A  355          0         8.41
CISPEP   2 ALA B  354    PRO B  355          0         7.14
SITE     1 AC1  4 LYS A 274  GLN A 316  GLU A 324  TRP A 368
SITE     1 AC2  7 PHE A 282  GLU A 283  GLU A 284  ARG A 285
SITE     2 AC2  7 HOH A 749  HOH A 765  HOH A 775
SITE     1 AC3  7 TYR A  91  THR A 101  PHE A 102  ALA A 103
SITE     2 AC3  7 ARG A 117  PRO A 343  HOH A 892
SITE     1 AC4  8 LYS A 136  PRO A 138  VAL A 139  VAL A 140
SITE     2 AC4  8 MET A 253  HOH A 766  HOH A 881  MET B 253
SITE     1 AC5  4 LYS B 274  GLN B 316  GLU B 324  TRP B 368
SITE     1 AC6  8 PHE B 282  GLU B 283  GLU B 284  ARG B 285
SITE     2 AC6  8 HOH B 679  HOH B 753  HOH B 763  HOH B 815
SITE     1 AC7  6 TYR B  91  THR B 101  PHE B 102  ALA B 103
SITE     2 AC7  6 ARG B 117  PRO B 343
SITE     1 AC8  9 GLU A 252  GLU B 252  PRO B 255  THR B 261
SITE     2 AC8  9  NA B 507  HOH B 622  HOH B 767  HOH B 781
SITE     3 AC8  9 HOH B 846
SITE     1 AC9  6 PRO B 413  GLN B 414  THR B 429  THR B 430
SITE     2 AC9  6 ASN B 431  HOH B 683
SITE     1 AD1  5 ILE B 259  GOL B 505  HOH B 798  HOH B 800
SITE     2 AD1  5 HOH B 812
SITE     1 AD2 14 GLU A  73  GLU A  75  CYS A  81  ALA A  83
SITE     2 AD2 14 ILE A  84  PHE A 102  ASN A 104  THR A 106
SITE     3 AD2 14 HOH A 611  HOH A 626  HOH A 763  HOH A 782
SITE     4 AD2 14 HOH A 800  ASN B  92
SITE     1 AD3 14 ASN A  92  GLU B  73  GLU B  75  CYS B  81
SITE     2 AD3 14 ILE B  84  PHE B 102  ASN B 104  THR B 106
SITE     3 AD3 14 HOH B 629  HOH B 634  HOH B 759  HOH B 772
SITE     4 AD3 14 HOH B 773  HOH B 803
CRYST1   84.273   84.273  261.127  90.00  90.00  90.00 P 41 21 2    16
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      0.011866  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011866  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003830        0.00000
TER    2976      THR A 458
TER    5938      THR B 458
MASTER      536    0   12   38   26    0   27    6 6654    2  166   62
END