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PDBsum entry 4jf7

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Viral protein PDB id
4jf7
Jmol
Contents
Protein chains
492 a.a.
Ligands
NAG-MAN-NAG
NAG-NAG-MAN
SO4 ×4
NAG ×6
NAG-NAG ×4
Metals
_CA ×4
Waters ×688
HEADER    VIRAL PROTEIN                           27-FEB-13   4JF7
TITLE     STRUCTURE OF THE PARAINFLUENZA VIRUS 5 (PIV5) HEMAGGLUTININ-
TITLE    2 NEURAMINIDASE (HN) ECTODOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HEMAGGLUTININ-NEURAMINIDASE;
COMPND   3 CHAIN: D, A, B, C;
COMPND   4 FRAGMENT: ECTODOMAIN;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SIMIAN VIRUS 5;
SOURCE   3 ORGANISM_COMMON: SV5;
SOURCE   4 ORGANISM_TAXID: 11208;
SOURCE   5 STRAIN: W3;
SOURCE   6 GENE: HN;
SOURCE   7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBACGUS-11
KEYWDS    PARAMYXOVIRUS, PIV5, ATTACHMENT PROTEIN, HN, RECEPTOR BINDING
KEYWDS   2 PROTEIN, ECTODOMAIN, VIRAL PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.D.WELCH,P.YUAN,S.BOSE,C.A.KORS,R.A.LAMB,T.S.JARDETZKY
REVDAT   1   04-SEP-13 4JF7    0
JRNL        AUTH   B.D.WELCH,P.YUAN,S.BOSE,C.A.KORS,R.A.LAMB,T.S.JARDETZKY
JRNL        TITL   STRUCTURE OF THE PARAINFLUENZA VIRUS 5 (PIV5)
JRNL        TITL 2 HEMAGGLUTININ-NEURAMINIDASE (HN) ECTODOMAIN.
JRNL        REF    PLOS PATHOG.                  V.   9 03534 2013
JRNL        REFN                   ISSN 1553-7366
JRNL        PMID   23950713
JRNL        DOI    10.1371/JOURNAL.PPAT.1003534
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.36
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8
REMARK   3   NUMBER OF REFLECTIONS             : 116080
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166
REMARK   3   R VALUE            (WORKING SET) : 0.166
REMARK   3   FREE R VALUE                     : 0.207
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 1972
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 34.3668 -  6.0195    1.00     8429   155  0.1889 0.1946
REMARK   3     2  6.0195 -  4.7820    1.00     8354   134  0.1561 0.1872
REMARK   3     3  4.7820 -  4.1787    1.00     8360   148  0.1351 0.1734
REMARK   3     4  4.1787 -  3.7972    1.00     8336   136  0.1445 0.1703
REMARK   3     5  3.7972 -  3.5253    1.00     8273   140  0.1570 0.1957
REMARK   3     6  3.5253 -  3.3176    1.00     8308   146  0.1653 0.2304
REMARK   3     7  3.3176 -  3.1516    1.00     8328   139  0.1654 0.2389
REMARK   3     8  3.1516 -  3.0145    0.99     8214   148  0.1664 0.1994
REMARK   3     9  3.0145 -  2.8985    0.98     8194   131  0.1729 0.2282
REMARK   3    10  2.8985 -  2.7985    0.98     8100   142  0.1789 0.2405
REMARK   3    11  2.7985 -  2.7111    0.97     8033   131  0.1896 0.2475
REMARK   3    12  2.7111 -  2.6336    0.95     7894   157  0.1976 0.2579
REMARK   3    13  2.6336 -  2.5643    0.94     7802   135  0.2081 0.2721
REMARK   3    14  2.5643 -  2.5018    0.90     7483   130  0.2089 0.2783
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.00
REMARK   3   SHRINKAGE RADIUS   : 0.73
REMARK   3   K_SOL              : 0.34
REMARK   3   B_SOL              : 39.91
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.290
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.82
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.60020
REMARK   3    B22 (A**2) : 2.60020
REMARK   3    B33 (A**2) : -5.20030
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : 0.00000
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      :  0.011          16140
REMARK   3   ANGLE     :  1.180          21977
REMARK   3   CHIRALITY :  0.078           2521
REMARK   3   PLANARITY :  0.005           2792
REMARK   3   DIHEDRAL  : 14.692           5766
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 11
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain 'A' and (resseq 58:119)
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5845 190.3699 -55.3235
REMARK   3    T TENSOR
REMARK   3      T11:   0.9960 T22:   0.9352
REMARK   3      T33:   0.9835 T12:   0.3831
REMARK   3      T13:  -0.4053 T23:  -0.2486
REMARK   3    L TENSOR
REMARK   3      L11:   0.7669 L22:   2.1553
REMARK   3      L33:   0.7763 L12:   0.7582
REMARK   3      L13:  -0.2373 L23:   0.4039
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0528 S12:   0.4605 S13:   0.1628
REMARK   3      S21:  -1.0197 S22:  -0.0199 S23:   0.6192
REMARK   3      S31:  -0.3225 S32:  -0.5198 S33:   0.4382
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain 'A' and (resseq 120:565)
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6486 227.3966 -21.4826
REMARK   3    T TENSOR
REMARK   3      T11:   0.1193 T22:   0.1899
REMARK   3      T33:   0.2843 T12:   0.0416
REMARK   3      T13:   0.0331 T23:   0.0289
REMARK   3    L TENSOR
REMARK   3      L11:   1.1763 L22:   0.8902
REMARK   3      L33:   0.7870 L12:  -0.3730
REMARK   3      L13:   0.0529 L23:  -0.0867
REMARK   3    S TENSOR
REMARK   3      S11:   0.1318 S12:   0.2901 S13:   0.2304
REMARK   3      S21:  -0.1343 S22:  -0.0776 S23:  -0.4869
REMARK   3      S31:  -0.1392 S32:   0.1890 S33:  -0.0311
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain 'B' and (resseq 58:114)
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1766 201.0726 -48.4310
REMARK   3    T TENSOR
REMARK   3      T11:   1.0938 T22:   0.8044
REMARK   3      T33:   0.7439 T12:   0.2582
REMARK   3      T13:  -0.4310 T23:  -0.0841
REMARK   3    L TENSOR
REMARK   3      L11:   0.9943 L22:   0.3055
REMARK   3      L33:   0.2675 L12:   0.4880
REMARK   3      L13:  -0.2378 L23:  -0.0023
REMARK   3    S TENSOR
REMARK   3      S11:   0.1073 S12:   0.5788 S13:  -0.0955
REMARK   3      S21:  -0.6758 S22:   0.0661 S23:   0.4241
REMARK   3      S31:   0.3301 S32:  -0.1970 S33:   0.0720
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain 'B' and (resseq 115:565)
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9457 227.3966  10.8374
REMARK   3    T TENSOR
REMARK   3      T11:   0.2715 T22:   0.5573
REMARK   3      T33:  -0.3127 T12:   0.1802
REMARK   3      T13:   0.0307 T23:   0.2853
REMARK   3    L TENSOR
REMARK   3      L11:   0.4266 L22:   0.3497
REMARK   3      L33:   0.4986 L12:  -0.1272
REMARK   3      L13:   0.1724 L23:  -0.0414
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1043 S12:  -0.7615 S13:  -0.1290
REMARK   3      S21:   0.5315 S22:   0.1775 S23:   0.2105
REMARK   3      S31:  -0.0355 S32:  -0.3196 S33:  -0.0285
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain 'C' and (resseq 58:124)
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7860 190.9568 -59.1540
REMARK   3    T TENSOR
REMARK   3      T11:   0.8612 T22:   0.6646
REMARK   3      T33:   0.8075 T12:   0.0693
REMARK   3      T13:  -0.0380 T23:   0.0423
REMARK   3    L TENSOR
REMARK   3      L11:   6.5927 L22:   3.8385
REMARK   3      L33:   4.4426 L12:   0.1206
REMARK   3      L13:   2.6674 L23:  -0.3043
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2663 S12:   0.5503 S13:   0.0724
REMARK   3      S21:  -0.8527 S22:   0.0441 S23:   0.4864
REMARK   3      S31:  -0.6242 S32:  -0.2319 S33:   0.0786
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: chain 'C' and (resseq 125:565)
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9307 167.3617 -52.4563
REMARK   3    T TENSOR
REMARK   3      T11:   0.1956 T22:   0.4182
REMARK   3      T33:  -0.4221 T12:  -0.1499
REMARK   3      T13:   0.2250 T23:   0.0761
REMARK   3    L TENSOR
REMARK   3      L11:   0.2622 L22:   0.3292
REMARK   3      L33:   1.1618 L12:  -0.0038
REMARK   3      L13:  -0.1468 L23:   0.1885
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0927 S12:   0.3265 S13:  -0.0290
REMARK   3      S21:  -0.3777 S22:   0.0926 S23:   0.0784
REMARK   3      S31:  -0.0281 S32:  -0.3756 S33:  -0.0289
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: chain 'D' and (resseq 58:98)
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1793 182.7761 -59.2565
REMARK   3    T TENSOR
REMARK   3      T11:   0.9352 T22:   0.7904
REMARK   3      T33:   0.7750 T12:   0.0606
REMARK   3      T13:  -0.2666 T23:  -0.0866
REMARK   3    L TENSOR
REMARK   3      L11:   4.4523 L22:   1.3024
REMARK   3      L33:   5.6952 L12:  -0.0502
REMARK   3      L13:   1.1296 L23:  -0.8536
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4649 S12:   0.2914 S13:  -0.2696
REMARK   3      S21:  -1.0651 S22:   0.0368 S23:   0.6324
REMARK   3      S31:  -1.2467 S32:  -1.3303 S33:   0.3366
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: chain 'D' and (resseq 99:165)
REMARK   3    ORIGIN FOR THE GROUP (A):  60.4049 167.9744 -20.5191
REMARK   3    T TENSOR
REMARK   3      T11:   0.1500 T22:   0.1003
REMARK   3      T33:   0.2439 T12:  -0.0294
REMARK   3      T13:  -0.0070 T23:  -0.0144
REMARK   3    L TENSOR
REMARK   3      L11:   1.3587 L22:   1.8714
REMARK   3      L33:   3.9952 L12:   0.8762
REMARK   3      L13:   0.0086 L23:  -0.6611
REMARK   3    S TENSOR
REMARK   3      S11:   0.1289 S12:  -0.0271 S13:  -0.1228
REMARK   3      S21:  -0.0076 S22:  -0.0151 S23:  -0.2342
REMARK   3      S31:   0.2315 S32:  -0.1087 S33:  -0.1282
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: chain 'D' and (resseq 166:241)
REMARK   3    ORIGIN FOR THE GROUP (A):  60.4863 180.8972 -26.4803
REMARK   3    T TENSOR
REMARK   3      T11:   0.1301 T22:   0.1920
REMARK   3      T33:   0.1978 T12:  -0.0176
REMARK   3      T13:   0.0622 T23:  -0.0520
REMARK   3    L TENSOR
REMARK   3      L11:   0.8255 L22:   1.6542
REMARK   3      L33:   1.6883 L12:  -0.2184
REMARK   3      L13:   1.0914 L23:   0.3367
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1104 S12:   0.0288 S13:   0.0458
REMARK   3      S21:  -0.1953 S22:   0.0037 S23:  -0.2898
REMARK   3      S31:   0.0788 S32:   0.0258 S33:   0.1326
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: chain 'D' and (resseq 242:366)
REMARK   3    ORIGIN FOR THE GROUP (A):  77.7292 188.8610 -14.7065
REMARK   3    T TENSOR
REMARK   3      T11:   0.0626 T22:   0.1913
REMARK   3      T33:   0.3972 T12:  -0.0119
REMARK   3      T13:  -0.0071 T23:  -0.0430
REMARK   3    L TENSOR
REMARK   3      L11:   1.3522 L22:   0.3925
REMARK   3      L33:   0.9136 L12:  -0.1455
REMARK   3      L13:   0.3559 L23:  -0.0738
REMARK   3    S TENSOR
REMARK   3      S11:   0.0309 S12:  -0.1549 S13:  -0.0711
REMARK   3      S21:   0.0227 S22:  -0.0528 S23:  -0.2712
REMARK   3      S31:   0.0049 S32:   0.1829 S33:  -0.0005
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION: chain 'D' and (resseq 367:565)
REMARK   3    ORIGIN FOR THE GROUP (A):  73.4508 172.4617 -15.5440
REMARK   3    T TENSOR
REMARK   3      T11:   0.1495 T22:   0.1820
REMARK   3      T33:   0.3812 T12:   0.0095
REMARK   3      T13:  -0.0291 T23:  -0.0000
REMARK   3    L TENSOR
REMARK   3      L11:   1.6591 L22:   0.6893
REMARK   3      L33:   0.9894 L12:   0.1139
REMARK   3      L13:   0.5161 L23:  -0.0698
REMARK   3    S TENSOR
REMARK   3      S11:   0.0621 S12:  -0.0672 S13:  -0.1770
REMARK   3      S21:   0.0611 S22:   0.0071 S23:  -0.4475
REMARK   3      S31:   0.1931 S32:   0.1343 S33:  -0.0436
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 4JF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-13.
REMARK 100 THE RCSB ID CODE IS RCSB077969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-11
REMARK 200  TEMPERATURE           (KELVIN) : 200
REMARK 200  PH                             : 6.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118507
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 6.300
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M MES
REMARK 280  MONOHYDRATE PH 6.5, 10% V/V 1,4-DIOXANE, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,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        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       97.19500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       97.19500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       92.98950
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       97.19500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       97.19500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       92.98950
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       97.19500
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       97.19500
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       92.98950
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       97.19500
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       97.19500
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       92.98950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     SER D    53
REMARK 465     PRO D    54
REMARK 465     SER D    55
REMARK 465     SER D    56
REMARK 465     GLY D    57
REMARK 465     LEU D    58
REMARK 465     GLY D    59
REMARK 465     SER D    60
REMARK 465     ILE D    61
REMARK 465     GLN D   102
REMARK 465     THR D   103
REMARK 465     SER D   104
REMARK 465     ASP D   105
REMARK 465     LYS D   106
REMARK 465     LEU D   107
REMARK 465     GLU D   108
REMARK 465     GLN D   109
REMARK 465     ASN D   110
REMARK 465     CYS D   111
REMARK 465     SER D   112
REMARK 465     TRP D   113
REMARK 465     SER A    53
REMARK 465     PRO A    54
REMARK 465     SER A    55
REMARK 465     SER A    56
REMARK 465     GLY A    57
REMARK 465     LEU A    58
REMARK 465     GLY A    59
REMARK 465     SER A    60
REMARK 465     THR A   103
REMARK 465     SER A   104
REMARK 465     ASP A   105
REMARK 465     LYS A   106
REMARK 465     SER B    53
REMARK 465     PRO B    54
REMARK 465     SER B    55
REMARK 465     SER B    56
REMARK 465     GLY B    57
REMARK 465     LEU B    58
REMARK 465     GLY B    59
REMARK 465     SER B    60
REMARK 465     ILE B    61
REMARK 465     THR B    62
REMARK 465     ASP B    63
REMARK 465     LEU B    64
REMARK 465     SER C    53
REMARK 465     PRO C    54
REMARK 465     SER C    55
REMARK 465     SER C    56
REMARK 465     GLY C    57
REMARK 465     LEU C    58
REMARK 465     GLY C    59
REMARK 465     SER C    60
REMARK 465     ILE C    61
REMARK 465     THR C    62
REMARK 465     ASP C    63
REMARK 465     GLN C   102
REMARK 465     THR C   103
REMARK 465     SER C   104
REMARK 465     ASP C   105
REMARK 465     LYS C   106
REMARK 465     LEU C   107
REMARK 465     GLU C   108
REMARK 465     GLN C   109
REMARK 465     ASN C   110
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     SER D 114    OG
REMARK 470     THR A  62    OG1  CG2
REMARK 470     ASN A  66    CG   OD1  ND2
REMARK 470     ASN B  67    CG   OD1  ND2
REMARK 470     THR B 339    OG1  CG2
REMARK 470     ASN C  66    CG   OD1  ND2
REMARK 470     LEU C  69    CG   CD1  CD2
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   ND2  ASN A   110     C2   NAG A   608              1.91
REMARK 500   O    GLN A   439     O    HOH A   808              2.06
REMARK 500   NH2  ARG C   442     O    CYS C   448              2.15
REMARK 500   NH2  ARG D   442     O    CYS D   448              2.18
REMARK 500   NH2  ARG A   442     O    CYS A   448              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    VAL D  81      -65.81   -125.83
REMARK 500    LEU D 117       54.44    -55.69
REMARK 500    ILE D 164       68.30     61.98
REMARK 500    ASN D 183       62.96   -112.63
REMARK 500    SER D 190      115.69     54.54
REMARK 500    THR D 291      -32.14     78.86
REMARK 500    ASN D 321       -2.90     78.62
REMARK 500    THR D 372      -73.39   -130.77
REMARK 500    SER D 408     -149.31   -114.72
REMARK 500    VAL D 440       94.10     61.63
REMARK 500    ALA D 464       84.12   -157.85
REMARK 500    ASN D 504     -168.07   -112.11
REMARK 500    ALA D 522     -113.00   -139.59
REMARK 500    LEU D 549      -83.31    -75.43
REMARK 500    LEU A  64       31.76    -90.65
REMARK 500    LEU A  65      -57.19   -124.20
REMARK 500    THR A  96       47.09    -93.41
REMARK 500    ALA A  97      -23.15   -163.34
REMARK 500    SER A 100       42.52    -68.98
REMARK 500    LEU A 117       48.01    -61.94
REMARK 500    ILE A 164       70.27     60.87
REMARK 500    ASN A 183       68.70   -117.97
REMARK 500    SER A 190      122.50     49.67
REMARK 500    ASP A 268       -1.17     83.05
REMARK 500    VAL A 283      -46.10   -131.09
REMARK 500    THR A 291      -25.61     75.71
REMARK 500    ASN A 321       -6.70     84.43
REMARK 500    SER A 334       59.82    -99.89
REMARK 500    PHE A 353       56.01    -96.41
REMARK 500    THR A 372      -75.63   -124.29
REMARK 500    SER A 408     -145.68   -109.17
REMARK 500    GLN A 438       30.82   -140.93
REMARK 500    VAL A 440       89.02     68.53
REMARK 500    ALA A 464       83.86   -152.56
REMARK 500    ASN A 504     -163.60   -102.42
REMARK 500    ALA A 522     -115.75   -142.17
REMARK 500    ILE B  68       45.18    -91.38
REMARK 500    LEU B  69      -26.95   -144.63
REMARK 500    ILE B 164       70.42     60.43
REMARK 500    ASP B 220       14.30   -143.90
REMARK 500    ASP B 268       -1.50     87.85
REMARK 500    VAL B 280      -61.83   -101.88
REMARK 500    VAL B 283      -50.33   -120.83
REMARK 500    THR B 291      -32.12     77.02
REMARK 500    PHE B 353       59.22    -94.71
REMARK 500    THR B 372      -70.81   -136.76
REMARK 500    SER B 408     -145.41   -108.62
REMARK 500    VAL B 440       92.54     73.47
REMARK 500    ARG B 495       76.16   -102.19
REMARK 500    ASN B 504     -169.80   -113.41
REMARK 500
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.
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                              CA C 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 250   O
REMARK 620 2 ALA C 255   O   164.1
REMARK 620 3 ALA C 285   O    90.6  75.4
REMARK 620 4 SER C 253   OG   96.3  98.7 170.1
REMARK 620 5 SER C 253   O    89.7  97.9  91.3  81.7
REMARK 620 6 HOH C 751   O   103.5  72.7 101.4  83.9 161.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA D 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 255   O
REMARK 620 2 ASP D 250   O   160.1
REMARK 620 3 SER D 253   OG  100.7  99.1
REMARK 620 4 HOH D 821   O    78.0  99.7  96.1
REMARK 620 5 ALA D 285   O    84.1  76.8 165.2  98.6
REMARK 620 6 SER D 253   O    99.6  83.2  82.4 176.9  83.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 255   O
REMARK 620 2 ASP B 250   O   133.6
REMARK 620 3 SER B 253   OG  109.8  86.7
REMARK 620 4 ALA B 285   O    71.8  66.7 135.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 285   O
REMARK 620 2 ALA A 255   O    83.6
REMARK 620 3 ASP A 250   O    76.9 160.4
REMARK 620 4 SER A 253   OG  159.4  95.6 103.5
REMARK 620 5 SER A 253   O    83.1  99.8  80.4  76.7
REMARK 620 6 HOH A 723   O   102.1  84.5  97.1  98.3 173.6
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 CA D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 606
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 The chain names represent the author's most probable connectivity
REMARK 999 despite the chain breaks
DBREF  4JF7 D   55   565  UNP    P04850   HN_SV5          55    565
DBREF  4JF7 A   55   565  UNP    P04850   HN_SV5          55    565
DBREF  4JF7 B   55   565  UNP    P04850   HN_SV5          55    565
DBREF  4JF7 C   55   565  UNP    P04850   HN_SV5          55    565
SEQADV 4JF7 SER D   53  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 PRO D   54  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 SER D   55  UNP  P04850    ASN    55 CONFLICT
SEQADV 4JF7 SER A   53  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 PRO A   54  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 SER A   55  UNP  P04850    ASN    55 CONFLICT
SEQADV 4JF7 SER B   53  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 PRO B   54  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 SER B   55  UNP  P04850    ASN    55 CONFLICT
SEQADV 4JF7 SER C   53  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 PRO C   54  UNP  P04850              EXPRESSION TAG
SEQADV 4JF7 SER C   55  UNP  P04850    ASN    55 CONFLICT
SEQRES   1 D  513  SER PRO SER SER GLY LEU GLY SER ILE THR ASP LEU LEU
SEQRES   2 D  513  ASN ASN ILE LEU SER VAL ALA ASN GLN ILE ILE TYR ASN
SEQRES   3 D  513  SER ALA VAL ALA LEU PRO LEU GLN LEU ASP THR LEU GLU
SEQRES   4 D  513  SER THR LEU LEU THR ALA ILE LYS SER LEU GLN THR SER
SEQRES   5 D  513  ASP LYS LEU GLU GLN ASN CYS SER TRP SER ALA ALA LEU
SEQRES   6 D  513  ILE ASN ASP ASN ARG TYR ILE ASN GLY ILE ASN GLN PHE
SEQRES   7 D  513  TYR PHE SER ILE ALA GLU GLY ARG ASN LEU THR LEU GLY
SEQRES   8 D  513  PRO LEU LEU ASN MET PRO SER PHE ILE PRO THR ALA THR
SEQRES   9 D  513  THR PRO GLU GLY CYS THR ARG ILE PRO SER PHE SER LEU
SEQRES  10 D  513  THR LYS THR HIS TRP CYS TYR THR HIS ASN VAL ILE LEU
SEQRES  11 D  513  ASN GLY CYS GLN ASP HIS VAL SER SER ASN GLN PHE VAL
SEQRES  12 D  513  SER MET GLY ILE ILE GLU PRO THR SER ALA GLY PHE PRO
SEQRES  13 D  513  PHE PHE ARG THR LEU LYS THR LEU TYR LEU SER ASP GLY
SEQRES  14 D  513  VAL ASN ARG LYS SER CYS SER ILE SER THR VAL PRO GLY
SEQRES  15 D  513  GLY CYS MET MET TYR CYS PHE VAL SER THR GLN PRO GLU
SEQRES  16 D  513  ARG ASP ASP TYR PHE SER ALA ALA PRO PRO GLU GLN ARG
SEQRES  17 D  513  ILE ILE ILE MET TYR TYR ASN ASP THR ILE VAL GLU ARG
SEQRES  18 D  513  ILE ILE ASN PRO PRO GLY VAL LEU ASP VAL TRP ALA THR
SEQRES  19 D  513  LEU ASN PRO GLY THR GLY SER GLY VAL TYR TYR LEU GLY
SEQRES  20 D  513  TRP VAL LEU PHE PRO ILE TYR GLY GLY VAL ILE LYS GLY
SEQRES  21 D  513  THR SER LEU TRP ASN ASN GLN ALA ASN LYS TYR PHE ILE
SEQRES  22 D  513  PRO GLN MET VAL ALA ALA LEU CYS SER GLN ASN GLN ALA
SEQRES  23 D  513  THR GLN VAL GLN ASN ALA LYS SER SER TYR TYR SER SER
SEQRES  24 D  513  TRP PHE GLY ASN ARG MET ILE GLN SER GLY ILE LEU ALA
SEQRES  25 D  513  CYS PRO LEU ARG GLN ASP LEU THR ASN GLU CYS LEU VAL
SEQRES  26 D  513  LEU PRO PHE SER ASN ASP GLN VAL LEU MET GLY ALA GLU
SEQRES  27 D  513  GLY ARG LEU TYR MET TYR GLY ASP SER VAL TYR TYR TYR
SEQRES  28 D  513  GLN ARG SER ASN SER TRP TRP PRO MET THR MET LEU TYR
SEQRES  29 D  513  LYS VAL THR ILE THR PHE THR ASN GLY GLN PRO SER ALA
SEQRES  30 D  513  ILE SER ALA GLN ASN VAL PRO THR GLN GLN VAL PRO ARG
SEQRES  31 D  513  PRO GLY THR GLY ASP CYS SER ALA THR ASN ARG CYS PRO
SEQRES  32 D  513  GLY PHE CYS LEU THR GLY VAL TYR ALA ASP ALA TRP LEU
SEQRES  33 D  513  LEU THR ASN PRO SER SER THR SER THR PHE GLY SER GLU
SEQRES  34 D  513  ALA THR PHE THR GLY SER TYR LEU ASN THR ALA THR GLN
SEQRES  35 D  513  ARG ILE ASN PRO THR MET TYR ILE ALA ASN ASN THR GLN
SEQRES  36 D  513  ILE ILE SER SER GLN GLN PHE GLY SER SER GLY GLN GLU
SEQRES  37 D  513  ALA ALA TYR GLY HIS THR THR CYS PHE ARG ASP THR GLY
SEQRES  38 D  513  SER VAL MET VAL TYR CYS ILE TYR ILE ILE GLU LEU SER
SEQRES  39 D  513  SER SER LEU LEU GLY GLN PHE GLN ILE VAL PRO PHE ILE
SEQRES  40 D  513  ARG GLN VAL THR LEU SER
SEQRES   1 A  513  SER PRO SER SER GLY LEU GLY SER ILE THR ASP LEU LEU
SEQRES   2 A  513  ASN ASN ILE LEU SER VAL ALA ASN GLN ILE ILE TYR ASN
SEQRES   3 A  513  SER ALA VAL ALA LEU PRO LEU GLN LEU ASP THR LEU GLU
SEQRES   4 A  513  SER THR LEU LEU THR ALA ILE LYS SER LEU GLN THR SER
SEQRES   5 A  513  ASP LYS LEU GLU GLN ASN CYS SER TRP SER ALA ALA LEU
SEQRES   6 A  513  ILE ASN ASP ASN ARG TYR ILE ASN GLY ILE ASN GLN PHE
SEQRES   7 A  513  TYR PHE SER ILE ALA GLU GLY ARG ASN LEU THR LEU GLY
SEQRES   8 A  513  PRO LEU LEU ASN MET PRO SER PHE ILE PRO THR ALA THR
SEQRES   9 A  513  THR PRO GLU GLY CYS THR ARG ILE PRO SER PHE SER LEU
SEQRES  10 A  513  THR LYS THR HIS TRP CYS TYR THR HIS ASN VAL ILE LEU
SEQRES  11 A  513  ASN GLY CYS GLN ASP HIS VAL SER SER ASN GLN PHE VAL
SEQRES  12 A  513  SER MET GLY ILE ILE GLU PRO THR SER ALA GLY PHE PRO
SEQRES  13 A  513  PHE PHE ARG THR LEU LYS THR LEU TYR LEU SER ASP GLY
SEQRES  14 A  513  VAL ASN ARG LYS SER CYS SER ILE SER THR VAL PRO GLY
SEQRES  15 A  513  GLY CYS MET MET TYR CYS PHE VAL SER THR GLN PRO GLU
SEQRES  16 A  513  ARG ASP ASP TYR PHE SER ALA ALA PRO PRO GLU GLN ARG
SEQRES  17 A  513  ILE ILE ILE MET TYR TYR ASN ASP THR ILE VAL GLU ARG
SEQRES  18 A  513  ILE ILE ASN PRO PRO GLY VAL LEU ASP VAL TRP ALA THR
SEQRES  19 A  513  LEU ASN PRO GLY THR GLY SER GLY VAL TYR TYR LEU GLY
SEQRES  20 A  513  TRP VAL LEU PHE PRO ILE TYR GLY GLY VAL ILE LYS GLY
SEQRES  21 A  513  THR SER LEU TRP ASN ASN GLN ALA ASN LYS TYR PHE ILE
SEQRES  22 A  513  PRO GLN MET VAL ALA ALA LEU CYS SER GLN ASN GLN ALA
SEQRES  23 A  513  THR GLN VAL GLN ASN ALA LYS SER SER TYR TYR SER SER
SEQRES  24 A  513  TRP PHE GLY ASN ARG MET ILE GLN SER GLY ILE LEU ALA
SEQRES  25 A  513  CYS PRO LEU ARG GLN ASP LEU THR ASN GLU CYS LEU VAL
SEQRES  26 A  513  LEU PRO PHE SER ASN ASP GLN VAL LEU MET GLY ALA GLU
SEQRES  27 A  513  GLY ARG LEU TYR MET TYR GLY ASP SER VAL TYR TYR TYR
SEQRES  28 A  513  GLN ARG SER ASN SER TRP TRP PRO MET THR MET LEU TYR
SEQRES  29 A  513  LYS VAL THR ILE THR PHE THR ASN GLY GLN PRO SER ALA
SEQRES  30 A  513  ILE SER ALA GLN ASN VAL PRO THR GLN GLN VAL PRO ARG
SEQRES  31 A  513  PRO GLY THR GLY ASP CYS SER ALA THR ASN ARG CYS PRO
SEQRES  32 A  513  GLY PHE CYS LEU THR GLY VAL TYR ALA ASP ALA TRP LEU
SEQRES  33 A  513  LEU THR ASN PRO SER SER THR SER THR PHE GLY SER GLU
SEQRES  34 A  513  ALA THR PHE THR GLY SER TYR LEU ASN THR ALA THR GLN
SEQRES  35 A  513  ARG ILE ASN PRO THR MET TYR ILE ALA ASN ASN THR GLN
SEQRES  36 A  513  ILE ILE SER SER GLN GLN PHE GLY SER SER GLY GLN GLU
SEQRES  37 A  513  ALA ALA TYR GLY HIS THR THR CYS PHE ARG ASP THR GLY
SEQRES  38 A  513  SER VAL MET VAL TYR CYS ILE TYR ILE ILE GLU LEU SER
SEQRES  39 A  513  SER SER LEU LEU GLY GLN PHE GLN ILE VAL PRO PHE ILE
SEQRES  40 A  513  ARG GLN VAL THR LEU SER
SEQRES   1 B  513  SER PRO SER SER GLY LEU GLY SER ILE THR ASP LEU LEU
SEQRES   2 B  513  ASN ASN ILE LEU SER VAL ALA ASN GLN ILE ILE TYR ASN
SEQRES   3 B  513  SER ALA VAL ALA LEU PRO LEU GLN LEU ASP THR LEU GLU
SEQRES   4 B  513  SER THR LEU LEU THR ALA ILE LYS SER LEU GLN THR SER
SEQRES   5 B  513  ASP LYS LEU GLU GLN ASN CYS SER TRP SER ALA ALA LEU
SEQRES   6 B  513  ILE ASN ASP ASN ARG TYR ILE ASN GLY ILE ASN GLN PHE
SEQRES   7 B  513  TYR PHE SER ILE ALA GLU GLY ARG ASN LEU THR LEU GLY
SEQRES   8 B  513  PRO LEU LEU ASN MET PRO SER PHE ILE PRO THR ALA THR
SEQRES   9 B  513  THR PRO GLU GLY CYS THR ARG ILE PRO SER PHE SER LEU
SEQRES  10 B  513  THR LYS THR HIS TRP CYS TYR THR HIS ASN VAL ILE LEU
SEQRES  11 B  513  ASN GLY CYS GLN ASP HIS VAL SER SER ASN GLN PHE VAL
SEQRES  12 B  513  SER MET GLY ILE ILE GLU PRO THR SER ALA GLY PHE PRO
SEQRES  13 B  513  PHE PHE ARG THR LEU LYS THR LEU TYR LEU SER ASP GLY
SEQRES  14 B  513  VAL ASN ARG LYS SER CYS SER ILE SER THR VAL PRO GLY
SEQRES  15 B  513  GLY CYS MET MET TYR CYS PHE VAL SER THR GLN PRO GLU
SEQRES  16 B  513  ARG ASP ASP TYR PHE SER ALA ALA PRO PRO GLU GLN ARG
SEQRES  17 B  513  ILE ILE ILE MET TYR TYR ASN ASP THR ILE VAL GLU ARG
SEQRES  18 B  513  ILE ILE ASN PRO PRO GLY VAL LEU ASP VAL TRP ALA THR
SEQRES  19 B  513  LEU ASN PRO GLY THR GLY SER GLY VAL TYR TYR LEU GLY
SEQRES  20 B  513  TRP VAL LEU PHE PRO ILE TYR GLY GLY VAL ILE LYS GLY
SEQRES  21 B  513  THR SER LEU TRP ASN ASN GLN ALA ASN LYS TYR PHE ILE
SEQRES  22 B  513  PRO GLN MET VAL ALA ALA LEU CYS SER GLN ASN GLN ALA
SEQRES  23 B  513  THR GLN VAL GLN ASN ALA LYS SER SER TYR TYR SER SER
SEQRES  24 B  513  TRP PHE GLY ASN ARG MET ILE GLN SER GLY ILE LEU ALA
SEQRES  25 B  513  CYS PRO LEU ARG GLN ASP LEU THR ASN GLU CYS LEU VAL
SEQRES  26 B  513  LEU PRO PHE SER ASN ASP GLN VAL LEU MET GLY ALA GLU
SEQRES  27 B  513  GLY ARG LEU TYR MET TYR GLY ASP SER VAL TYR TYR TYR
SEQRES  28 B  513  GLN ARG SER ASN SER TRP TRP PRO MET THR MET LEU TYR
SEQRES  29 B  513  LYS VAL THR ILE THR PHE THR ASN GLY GLN PRO SER ALA
SEQRES  30 B  513  ILE SER ALA GLN ASN VAL PRO THR GLN GLN VAL PRO ARG
SEQRES  31 B  513  PRO GLY THR GLY ASP CYS SER ALA THR ASN ARG CYS PRO
SEQRES  32 B  513  GLY PHE CYS LEU THR GLY VAL TYR ALA ASP ALA TRP LEU
SEQRES  33 B  513  LEU THR ASN PRO SER SER THR SER THR PHE GLY SER GLU
SEQRES  34 B  513  ALA THR PHE THR GLY SER TYR LEU ASN THR ALA THR GLN
SEQRES  35 B  513  ARG ILE ASN PRO THR MET TYR ILE ALA ASN ASN THR GLN
SEQRES  36 B  513  ILE ILE SER SER GLN GLN PHE GLY SER SER GLY GLN GLU
SEQRES  37 B  513  ALA ALA TYR GLY HIS THR THR CYS PHE ARG ASP THR GLY
SEQRES  38 B  513  SER VAL MET VAL TYR CYS ILE TYR ILE ILE GLU LEU SER
SEQRES  39 B  513  SER SER LEU LEU GLY GLN PHE GLN ILE VAL PRO PHE ILE
SEQRES  40 B  513  ARG GLN VAL THR LEU SER
SEQRES   1 C  513  SER PRO SER SER GLY LEU GLY SER ILE THR ASP LEU LEU
SEQRES   2 C  513  ASN ASN ILE LEU SER VAL ALA ASN GLN ILE ILE TYR ASN
SEQRES   3 C  513  SER ALA VAL ALA LEU PRO LEU GLN LEU ASP THR LEU GLU
SEQRES   4 C  513  SER THR LEU LEU THR ALA ILE LYS SER LEU GLN THR SER
SEQRES   5 C  513  ASP LYS LEU GLU GLN ASN CYS SER TRP SER ALA ALA LEU
SEQRES   6 C  513  ILE ASN ASP ASN ARG TYR ILE ASN GLY ILE ASN GLN PHE
SEQRES   7 C  513  TYR PHE SER ILE ALA GLU GLY ARG ASN LEU THR LEU GLY
SEQRES   8 C  513  PRO LEU LEU ASN MET PRO SER PHE ILE PRO THR ALA THR
SEQRES   9 C  513  THR PRO GLU GLY CYS THR ARG ILE PRO SER PHE SER LEU
SEQRES  10 C  513  THR LYS THR HIS TRP CYS TYR THR HIS ASN VAL ILE LEU
SEQRES  11 C  513  ASN GLY CYS GLN ASP HIS VAL SER SER ASN GLN PHE VAL
SEQRES  12 C  513  SER MET GLY ILE ILE GLU PRO THR SER ALA GLY PHE PRO
SEQRES  13 C  513  PHE PHE ARG THR LEU LYS THR LEU TYR LEU SER ASP GLY
SEQRES  14 C  513  VAL ASN ARG LYS SER CYS SER ILE SER THR VAL PRO GLY
SEQRES  15 C  513  GLY CYS MET MET TYR CYS PHE VAL SER THR GLN PRO GLU
SEQRES  16 C  513  ARG ASP ASP TYR PHE SER ALA ALA PRO PRO GLU GLN ARG
SEQRES  17 C  513  ILE ILE ILE MET TYR TYR ASN ASP THR ILE VAL GLU ARG
SEQRES  18 C  513  ILE ILE ASN PRO PRO GLY VAL LEU ASP VAL TRP ALA THR
SEQRES  19 C  513  LEU ASN PRO GLY THR GLY SER GLY VAL TYR TYR LEU GLY
SEQRES  20 C  513  TRP VAL LEU PHE PRO ILE TYR GLY GLY VAL ILE LYS GLY
SEQRES  21 C  513  THR SER LEU TRP ASN ASN GLN ALA ASN LYS TYR PHE ILE
SEQRES  22 C  513  PRO GLN MET VAL ALA ALA LEU CYS SER GLN ASN GLN ALA
SEQRES  23 C  513  THR GLN VAL GLN ASN ALA LYS SER SER TYR TYR SER SER
SEQRES  24 C  513  TRP PHE GLY ASN ARG MET ILE GLN SER GLY ILE LEU ALA
SEQRES  25 C  513  CYS PRO LEU ARG GLN ASP LEU THR ASN GLU CYS LEU VAL
SEQRES  26 C  513  LEU PRO PHE SER ASN ASP GLN VAL LEU MET GLY ALA GLU
SEQRES  27 C  513  GLY ARG LEU TYR MET TYR GLY ASP SER VAL TYR TYR TYR
SEQRES  28 C  513  GLN ARG SER ASN SER TRP TRP PRO MET THR MET LEU TYR
SEQRES  29 C  513  LYS VAL THR ILE THR PHE THR ASN GLY GLN PRO SER ALA
SEQRES  30 C  513  ILE SER ALA GLN ASN VAL PRO THR GLN GLN VAL PRO ARG
SEQRES  31 C  513  PRO GLY THR GLY ASP CYS SER ALA THR ASN ARG CYS PRO
SEQRES  32 C  513  GLY PHE CYS LEU THR GLY VAL TYR ALA ASP ALA TRP LEU
SEQRES  33 C  513  LEU THR ASN PRO SER SER THR SER THR PHE GLY SER GLU
SEQRES  34 C  513  ALA THR PHE THR GLY SER TYR LEU ASN THR ALA THR GLN
SEQRES  35 C  513  ARG ILE ASN PRO THR MET TYR ILE ALA ASN ASN THR GLN
SEQRES  36 C  513  ILE ILE SER SER GLN GLN PHE GLY SER SER GLY GLN GLU
SEQRES  37 C  513  ALA ALA TYR GLY HIS THR THR CYS PHE ARG ASP THR GLY
SEQRES  38 C  513  SER VAL MET VAL TYR CYS ILE TYR ILE ILE GLU LEU SER
SEQRES  39 C  513  SER SER LEU LEU GLY GLN PHE GLN ILE VAL PRO PHE ILE
SEQRES  40 C  513  ARG GLN VAL THR LEU SER
MODRES 4JF7 ASN C  504  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN B  267  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN D  504  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN D  267  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN A  504  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN C  267  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN C  139  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN A  267  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN B  504  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN A  139  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN D  139  ASN  GLYCOSYLATION SITE
MODRES 4JF7 ASN A  110  ASN  GLYCOSYLATION SITE
HET     CA  D 601       1
HET    NAG  D 602      14
HET    MAN  D 603      11
HET    NAG  D 604      14
HET    NAG  D 605      14
HET    NAG  D 606      14
HET    MAN  D 607      11
HET    SO4  D 608       5
HET    NAG  D 609      14
HET     CA  A 601       1
HET    NAG  A 602      14
HET    NAG  A 603      14
HET    NAG  A 604      14
HET    NAG  A 605      14
HET    NAG  A 606      14
HET    SO4  A 607       5
HET    NAG  A 608      14
HET     CA  B 601       1
HET    SO4  B 602       5
HET    NAG  B 603      14
HET    NAG  B 604      14
HET    NAG  B 605      14
HET     CA  C 601       1
HET    SO4  C 602       5
HET    NAG  C 603      14
HET    NAG  C 604      14
HET    NAG  C 605      14
HET    NAG  C 606      14
HETNAM      CA CALCIUM ION
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     SO4 SULFATE ION
FORMUL   5   CA    4(CA 2+)
FORMUL   6  NAG    18(C8 H15 N O6)
FORMUL   6  MAN    2(C6 H12 O6)
FORMUL   9  SO4    4(O4 S 2-)
FORMUL  27  HOH   *688(H2 O)
HELIX    1   1 LEU D   65  SER D   70  1                                   6
HELIX    2   2 VAL D   71  VAL D   81  1                                  11
HELIX    3   3 VAL D   81  SER D  100  1                                  20
HELIX    4   4 SER D  133  ARG D  138  1                                   6
HELIX    5   5 PRO D  246  SER D  253  1                                   8
HELIX    6   6 THR D  313  ALA D  320  1                                   8
HELIX    7   7 MET D  328  CYS D  333  1                                   6
HELIX    8   8 ASN D  336  SER D  347  1                                  12
HELIX    9   9 THR D  445  SER D  449  5                                   5
HELIX   10  10 THR A   62  VAL A   81  1                                  20
HELIX   11  11 VAL A   81  LYS A   99  1                                  19
HELIX   12  12 ALA A  135  ARG A  138  5                                   4
HELIX   13  13 PRO A  246  SER A  253  1                                   8
HELIX   14  14 THR A  313  ALA A  320  1                                   8
HELIX   15  15 ASN A  336  SER A  347  1                                  12
HELIX   16  16 ASN A  471  THR A  475  5                                   5
HELIX   17  17 VAL B   71  VAL B   81  1                                  11
HELIX   18  18 VAL B   81  GLN B  109  1                                  29
HELIX   19  19 ALA B  115  LEU B  117  5                                   3
HELIX   20  20 ASP B  120  ASN B  125  1                                   6
HELIX   21  21 ALA B  135  ARG B  138  5                                   4
HELIX   22  22 PRO B  246  SER B  253  1                                   8
HELIX   23  23 THR B  313  ALA B  320  1                                   8
HELIX   24  24 VAL B  329  CYS B  333  5                                   5
HELIX   25  25 ASN B  336  SER B  347  1                                  12
HELIX   26  26 THR B  445  SER B  449  5                                   5
HELIX   27  27 ASN B  471  THR B  475  5                                   5
HELIX   28  28 LEU C   65  VAL C   81  1                                  17
HELIX   29  29 VAL C   81  LYS C   99  1                                  19
HELIX   30  30 TRP C  113  LEU C  117  5                                   5
HELIX   31  31 ASP C  120  ASN C  125  1                                   6
HELIX   32  32 SER C  133  ARG C  138  1                                   6
HELIX   33  33 PRO C  246  SER C  253  1                                   8
HELIX   34  34 THR C  313  ALA C  320  1                                   8
HELIX   35  35 ASN C  336  SER C  346  1                                  11
HELIX   36  36 THR C  445  SER C  449  5                                   5
HELIX   37  37 ASN C  471  THR C  475  5                                   5
SHEET    1   A 4 LEU D 140  LEU D 145  0
SHEET    2   A 4 PHE D 553  LEU D 564 -1  O  GLN D 561   N  GLY D 143
SHEET    3   A 4 MET D 536  SER D 546 -1  N  LEU D 545   O  GLN D 554
SHEET    4   A 4 ALA D 521  ASP D 531 -1  N  ASP D 531   O  MET D 536
SHEET    1   B 4 CYS D 161  LEU D 169  0
SHEET    2   B 4 TRP D 174  ILE D 181 -1  O  ILE D 181   N  CYS D 161
SHEET    3   B 4 ASN D 192  PRO D 202 -1  O  ASN D 192   N  VAL D 180
SHEET    4   B 4 PRO D 208  LEU D 218 -1  O  LEU D 216   N  VAL D 195
SHEET    1   C 4 ARG D 224  VAL D 232  0
SHEET    2   C 4 GLY D 235  VAL D 242 -1  O  PHE D 241   N  LYS D 225
SHEET    3   C 4 GLU D 258  TYR D 265 -1  O  ILE D 262   N  MET D 238
SHEET    4   C 4 ILE D 270  ILE D 275 -1  O  VAL D 271   N  ILE D 263
SHEET    1   D 4 TRP D 284  PRO D 289  0
SHEET    2   D 4 TRP D 300  VAL D 309 -1  O  GLY D 308   N  ALA D 285
SHEET    3   D 4 ARG D 356  PRO D 366 -1  O  CYS D 365   N  VAL D 301
SHEET    4   D 4 TYR D 349  SER D 350 -1  N  SER D 350   O  ARG D 356
SHEET    1   E 4 VAL D 295  TYR D 297  0
SHEET    2   E 4 TRP D 300  VAL D 309 -1  O  LEU D 302   N  VAL D 295
SHEET    3   E 4 ARG D 356  PRO D 366 -1  O  CYS D 365   N  VAL D 301
SHEET    4   E 4 LEU D 376  PRO D 379 -1  O  LEU D 378   N  ILE D 362
SHEET    1   F 4 GLY D 391  TYR D 396  0
SHEET    2   F 4 SER D 399  GLN D 404 -1  O  SER D 399   N  TYR D 396
SHEET    3   F 4 MET D 414  THR D 423 -1  O  VAL D 418   N  VAL D 400
SHEET    4   F 4 GLN D 426  ASN D 434 -1  O  SER D 428   N  THR D 421
SHEET    1   G 4 ALA D 466  LEU D 468  0
SHEET    2   G 4 PHE D 484  LEU D 489 -1  O  THR D 485   N  TRP D 467
SHEET    3   G 4 PRO D 498  ALA D 503 -1  O  ALA D 503   N  PHE D 484
SHEET    4   G 4 ILE D 508  GLN D 513 -1  O  SER D 510   N  ILE D 502
SHEET    1   H 2 CYS A 111  TRP A 113  0
SHEET    2   H 2 CYS B 111  TRP B 113 -1  O  SER B 112   N  SER A 112
SHEET    1   I 4 LEU A 140  LEU A 145  0
SHEET    2   I 4 PHE A 553  LEU A 564 -1  O  GLN A 561   N  GLY A 143
SHEET    3   I 4 MET A 536  SER A 546 -1  N  TYR A 541   O  PHE A 558
SHEET    4   I 4 ALA A 521  ASP A 531 -1  N  HIS A 525   O  ILE A 542
SHEET    1   J 4 CYS A 161  LEU A 169  0
SHEET    2   J 4 TRP A 174  ILE A 181 -1  O  CYS A 175   N  SER A 168
SHEET    3   J 4 ASN A 192  PRO A 202 -1  O  ASN A 192   N  VAL A 180
SHEET    4   J 4 PRO A 208  LEU A 218 -1  O  LEU A 218   N  GLN A 193
SHEET    1   K 4 ARG A 224  VAL A 232  0
SHEET    2   K 4 GLY A 235  VAL A 242 -1  O  TYR A 239   N  SER A 228
SHEET    3   K 4 GLN A 259  TYR A 265 -1  O  ILE A 262   N  MET A 238
SHEET    4   K 4 ILE A 270  ILE A 275 -1  O  ARG A 273   N  ILE A 261
SHEET    1   L 4 TRP A 284  PRO A 289  0
SHEET    2   L 4 TRP A 300  VAL A 309 -1  O  TYR A 306   N  ASN A 288
SHEET    3   L 4 ARG A 356  PRO A 366 -1  O  MET A 357   N  VAL A 309
SHEET    4   L 4 TYR A 349  SER A 350 -1  N  SER A 350   O  ARG A 356
SHEET    1   M 4 VAL A 295  TYR A 297  0
SHEET    2   M 4 TRP A 300  VAL A 309 -1  O  TRP A 300   N  TYR A 297
SHEET    3   M 4 ARG A 356  PRO A 366 -1  O  MET A 357   N  VAL A 309
SHEET    4   M 4 LEU A 376  PRO A 379 -1  O  LEU A 376   N  ALA A 364
SHEET    1   N 4 GLY A 391  TYR A 396  0
SHEET    2   N 4 SER A 399  GLN A 404 -1  O  SER A 399   N  TYR A 396
SHEET    3   N 4 MET A 414  THR A 423 -1  O  VAL A 418   N  VAL A 400
SHEET    4   N 4 GLN A 426  ASN A 434 -1  O  SER A 431   N  THR A 419
SHEET    1   O 4 ALA A 466  LEU A 468  0
SHEET    2   O 4 PHE A 484  LEU A 489 -1  O  THR A 485   N  TRP A 467
SHEET    3   O 4 PRO A 498  ALA A 503 -1  O  THR A 499   N  TYR A 488
SHEET    4   O 4 ILE A 508  GLN A 513 -1  O  GLN A 512   N  MET A 500
SHEET    1   P 4 LEU B 140  LEU B 146  0
SHEET    2   P 4 PHE B 553  LEU B 564 -1  O  ILE B 559   N  LEU B 146
SHEET    3   P 4 MET B 536  SER B 546 -1  N  TYR B 541   O  PHE B 558
SHEET    4   P 4 ALA B 521  ASP B 531 -1  N  THR B 527   O  ILE B 540
SHEET    1   Q 4 CYS B 161  LEU B 169  0
SHEET    2   Q 4 TRP B 174  ILE B 181 -1  O  ASN B 179   N  ARG B 163
SHEET    3   Q 4 ASN B 192  PRO B 202 -1  O  ASN B 192   N  VAL B 180
SHEET    4   Q 4 PRO B 208  LEU B 218 -1  O  PHE B 209   N  GLU B 201
SHEET    1   R 4 ARG B 224  VAL B 232  0
SHEET    2   R 4 GLY B 235  VAL B 242 -1  O  PHE B 241   N  LYS B 225
SHEET    3   R 4 GLN B 259  TYR B 265 -1  O  MET B 264   N  CYS B 236
SHEET    4   R 4 ILE B 270  ILE B 274 -1  O  VAL B 271   N  ILE B 263
SHEET    1   S 4 TRP B 284  PRO B 289  0
SHEET    2   S 4 TRP B 300  VAL B 309 -1  O  TYR B 306   N  ASN B 288
SHEET    3   S 4 ARG B 356  PRO B 366 -1  O  CYS B 365   N  VAL B 301
SHEET    4   S 4 TYR B 349  SER B 350 -1  N  SER B 350   O  ARG B 356
SHEET    1   T 4 VAL B 295  TYR B 297  0
SHEET    2   T 4 TRP B 300  VAL B 309 -1  O  TRP B 300   N  TYR B 297
SHEET    3   T 4 ARG B 356  PRO B 366 -1  O  CYS B 365   N  VAL B 301
SHEET    4   T 4 LEU B 376  PRO B 379 -1  O  LEU B 376   N  ALA B 364
SHEET    1   U 4 GLY B 391  TYR B 396  0
SHEET    2   U 4 SER B 399  GLN B 404 -1  O  SER B 399   N  TYR B 396
SHEET    3   U 4 MET B 414  THR B 423 -1  O  VAL B 418   N  VAL B 400
SHEET    4   U 4 GLN B 426  ASN B 434 -1  O  GLN B 426   N  THR B 423
SHEET    1   V 4 ALA B 466  LEU B 468  0
SHEET    2   V 4 PHE B 484  LEU B 489 -1  O  THR B 485   N  TRP B 467
SHEET    3   V 4 PRO B 498  ALA B 503 -1  O  ALA B 503   N  PHE B 484
SHEET    4   V 4 ILE B 508  GLN B 513 -1  O  GLN B 512   N  MET B 500
SHEET    1   W 4 LEU C 140  LEU C 146  0
SHEET    2   W 4 PHE C 553  LEU C 564 -1  O  GLN C 561   N  GLY C 143
SHEET    3   W 4 MET C 536  SER C 546 -1  N  TYR C 541   O  PHE C 558
SHEET    4   W 4 ALA C 521  ASP C 531 -1  N  THR C 527   O  ILE C 540
SHEET    1   X 4 CYS C 161  LEU C 169  0
SHEET    2   X 4 TRP C 174  ILE C 181 -1  O  ILE C 181   N  CYS C 161
SHEET    3   X 4 ASN C 192  PRO C 202 -1  O  ASN C 192   N  VAL C 180
SHEET    4   X 4 PRO C 208  LEU C 218 -1  O  LEU C 213   N  MET C 197
SHEET    1   Y 4 ARG C 224  VAL C 232  0
SHEET    2   Y 4 GLY C 235  VAL C 242 -1  O  PHE C 241   N  LYS C 225
SHEET    3   Y 4 GLN C 259  TYR C 265 -1  O  MET C 264   N  CYS C 236
SHEET    4   Y 4 ILE C 270  ILE C 274 -1  O  VAL C 271   N  ILE C 263
SHEET    1   Z 4 TRP C 284  PRO C 289  0
SHEET    2   Z 4 TRP C 300  VAL C 309 -1  O  TYR C 306   N  ASN C 288
SHEET    3   Z 4 ARG C 356  PRO C 366 -1  O  CYS C 365   N  VAL C 301
SHEET    4   Z 4 TYR C 349  SER C 350 -1  N  SER C 350   O  ARG C 356
SHEET    1  AA 4 VAL C 295  TYR C 297  0
SHEET    2  AA 4 TRP C 300  VAL C 309 -1  O  TRP C 300   N  TYR C 297
SHEET    3  AA 4 ARG C 356  PRO C 366 -1  O  CYS C 365   N  VAL C 301
SHEET    4  AA 4 LEU C 376  PRO C 379 -1  O  LEU C 376   N  ALA C 364
SHEET    1  AB 4 GLY C 391  TYR C 396  0
SHEET    2  AB 4 SER C 399  GLN C 404 -1  O  TYR C 401   N  TYR C 394
SHEET    3  AB 4 MET C 414  PHE C 422 -1  O  VAL C 418   N  VAL C 400
SHEET    4  AB 4 PRO C 427  ASN C 434 -1  O  GLN C 433   N  LYS C 417
SHEET    1  AC 4 ALA C 466  LEU C 468  0
SHEET    2  AC 4 THR C 483  LEU C 489 -1  O  THR C 485   N  TRP C 467
SHEET    3  AC 4 PRO C 498  ASN C 504 -1  O  ALA C 503   N  PHE C 484
SHEET    4  AC 4 ILE C 508  GLN C 513 -1  O  SER C 510   N  ILE C 502
SSBOND   1 CYS D  161    CYS D  185                          1555   1555  2.04
SSBOND   2 CYS D  175    CYS D  236                          1555   1555  2.05
SSBOND   3 CYS D  227    CYS D  240                          1555   1555  2.05
SSBOND   4 CYS D  333    CYS D  454                          1555   1555  2.04
SSBOND   5 CYS D  365    CYS D  375                          1555   1555  2.08
SSBOND   6 CYS D  448    CYS D  458                          1555   1555  2.03
SSBOND   7 CYS D  528    CYS D  539                          1555   1555  2.04
SSBOND   8 CYS A  111    CYS B  111                          1555   1555  2.03
SSBOND   9 CYS A  161    CYS A  185                          1555   1555  2.06
SSBOND  10 CYS A  175    CYS A  236                          1555   1555  2.04
SSBOND  11 CYS A  227    CYS A  240                          1555   1555  2.05
SSBOND  12 CYS A  333    CYS A  454                          1555   1555  2.04
SSBOND  13 CYS A  365    CYS A  375                          1555   1555  2.09
SSBOND  14 CYS A  448    CYS A  458                          1555   1555  2.03
SSBOND  15 CYS A  528    CYS A  539                          1555   1555  2.03
SSBOND  16 CYS B  161    CYS B  185                          1555   1555  2.05
SSBOND  17 CYS B  175    CYS B  236                          1555   1555  2.04
SSBOND  18 CYS B  227    CYS B  240                          1555   1555  2.04
SSBOND  19 CYS B  333    CYS B  454                          1555   1555  2.04
SSBOND  20 CYS B  365    CYS B  375                          1555   1555  2.06
SSBOND  21 CYS B  448    CYS B  458                          1555   1555  2.03
SSBOND  22 CYS B  528    CYS B  539                          1555   1555  2.02
SSBOND  23 CYS C  161    CYS C  185                          1555   1555  2.06
SSBOND  24 CYS C  175    CYS C  236                          1555   1555  2.05
SSBOND  25 CYS C  227    CYS C  240                          1555   1555  2.04
SSBOND  26 CYS C  333    CYS C  454                          1555   1555  2.09
SSBOND  27 CYS C  365    CYS C  375                          1555   1555  2.05
SSBOND  28 CYS C  448    CYS C  458                          1555   1555  2.04
SSBOND  29 CYS C  528    CYS C  539                          1555   1555  2.03
LINK         ND2 ASN C 504                 C1  NAG C 605     1555   1555  1.29
LINK         ND2 ASN B 267                 C1  NAG B 603     1555   1555  1.34
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.34
LINK         ND2 ASN D 504                 C1  NAG D 606     1555   1555  1.38
LINK         C1  NAG D 602                 O4  NAG D 604     1555   1555  1.48
LINK         ND2 ASN D 267                 C1  NAG D 604     1555   1555  1.51
LINK         O4  NAG B 603                 C1  NAG B 604     1555   1555  1.51
LINK         ND2 ASN A 504                 C1  NAG A 605     1555   1555  1.54
LINK         C1  NAG D 605                 O4  NAG D 606     1555   1555  1.55
LINK         ND2 ASN C 267                 C1  NAG C 604     1555   1555  1.57
LINK         ND2 ASN C 139                 C1  NAG C 603     1555   1555  1.58
LINK         ND2 ASN A 267                 C1  NAG A 603     1555   1555  1.59
LINK         O4  NAG A 605                 C1  NAG A 606     1555   1555  1.56
LINK         ND2 ASN B 504                 C1  NAG B 605     1555   1555  1.62
LINK         O4  NAG D 602                 C1  MAN D 603     1555   1555  1.63
LINK         O4  NAG D 605                 C1  MAN D 607     1555   1555  1.67
LINK         ND2 ASN A 139                 C1  NAG A 602     1555   1555  1.69
LINK         ND2 ASN D 139                 C1  NAG D 609     1555   1555  1.80
LINK         ND2 ASN A 110                 C1  NAG A 608     1555   1555  1.97
LINK         O4  NAG C 605                 C1  NAG C 606     1555   1555  1.71
LINK         O   ASP C 250                CA    CA C 601     1555   1555  2.66
LINK         O   ALA C 255                CA    CA C 601     1555   1555  2.68
LINK         O   ALA D 255                CA    CA D 601     1555   1555  2.69
LINK         O   ASP D 250                CA    CA D 601     1555   1555  2.71
LINK         O   ALA B 255                CA    CA B 601     1555   1555  2.71
LINK         O   ALA A 285                CA    CA A 601     1555   1555  2.72
LINK         O   ALA A 255                CA    CA A 601     1555   1555  2.73
LINK         O   ASP A 250                CA    CA A 601     1555   1555  2.76
LINK         OG  SER A 253                CA    CA A 601     1555   1555  2.76
LINK         O   ASP B 250                CA    CA B 601     1555   1555  2.77
LINK         O   ALA C 285                CA    CA C 601     1555   1555  2.79
LINK         OG  SER D 253                CA    CA D 601     1555   1555  2.81
LINK        CA    CA D 601                 O   HOH D 821     1555   1555  2.81
LINK         OG  SER C 253                CA    CA C 601     1555   1555  2.82
LINK         O   ALA D 285                CA    CA D 601     1555   1555  2.83
LINK         O   SER A 253                CA    CA A 601     1555   1555  2.83
LINK        CA    CA A 601                 O   HOH A 723     1555   1555  2.85
LINK         O   SER C 253                CA    CA C 601     1555   1555  2.86
LINK         O   SER D 253                CA    CA D 601     1555   1555  2.91
LINK         OG  SER B 253                CA    CA B 601     1555   1555  3.00
LINK        CA    CA C 601                 O   HOH C 751     1555   1555  3.03
LINK         O   ALA B 285                CA    CA B 601     1555   1555  3.04
SITE     1 AC1  5 ASP D 250  SER D 253  ALA D 255  ALA D 285
SITE     2 AC1  5 HOH D 821
SITE     1 AC2  6 PRO D 233  TYR D 265  GLN D 369  MAN D 603
SITE     2 AC2  6 NAG D 604  HOH D 854
SITE     1 AC3  1 NAG D 602
SITE     1 AC4  5 GLY D 234  ASN D 267  THR D 269  GLN D 369
SITE     2 AC4  5 NAG D 602
SITE     1 AC5  4 GLN D 507  NAG D 606  MAN D 607  HOH D 881
SITE     1 AC6  6 ASN D 504  ASN D 505  THR D 506  GLN D 507
SITE     2 AC6  6 ILE D 509  NAG D 605
SITE     1 AC7  2 NAG D 605  HOH D 913
SITE     1 AC8  2 ARG D 405  ARG D 495
SITE     1 AC9  1 ASN D 139
SITE     1 BC1  5 ASP A 250  SER A 253  ALA A 255  ALA A 285
SITE     2 BC1  5 HOH A 723
SITE     1 BC2  1 ASN A 139
SITE     1 BC3  6 ASN A 267  THR A 269  GLN A 369  NAG A 604
SITE     2 BC3  6 HOH A 768  GLN B 109
SITE     1 BC4  2 GLN A 369  NAG A 603
SITE     1 BC5  7 GLU A 481  ASN A 504  THR A 506  GLN A 507
SITE     2 BC5  7 ILE A 509  NAG A 606  HOH A 820
SITE     1 BC6  2 GLN A 507  NAG A 605
SITE     1 BC7  5 ARG A 405  ARG A 495  TYR A 523  HOH A 848
SITE     2 BC7  5 HOH A 857
SITE     1 BC8  2 LEU A 107  ASN A 110
SITE     1 BC9  4 ASP B 250  SER B 253  ALA B 255  ALA B 285
SITE     1 CC1  4 ARG B 163  ARG B 405  ARG B 495  TYR B 523
SITE     1 CC2  6 GLU A 108  GLN A 109  ASN B 267  THR B 269
SITE     2 CC2  6 GLN B 369  NAG B 604
SITE     1 CC3  4 TYR B 265  GLN B 369  NAG B 603  HOH B 790
SITE     1 CC4  5 GLU B 481  ASN B 504  THR B 506  GLN B 507
SITE     2 CC4  5 HOH B 715
SITE     1 CC5  5 ASP C 250  SER C 253  ALA C 255  ALA C 285
SITE     2 CC5  5 HOH C 751
SITE     1 CC6  4 ARG C 163  ARG C 405  ARG C 495  TYR C 523
SITE     1 CC7  2 ASN C 139  HOH C 824
SITE     1 CC8  3 ASN C 267  THR C 269  GLN C 369
SITE     1 CC9  6 GLU C 481  ASN C 504  THR C 506  GLN C 507
SITE     2 CC9  6 ILE C 509  NAG C 606
SITE     1 DC1  2 GLN C 507  NAG C 605
CRYST1  194.390  194.390  185.979  90.00  90.00  90.00 I 4          32
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      0.005144  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005144  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005377        0.00000
      
PROCHECK
Go to PROCHECK summary
 References