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PDBsum entry 2hox

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2hox
Jmol
Contents
Protein chains
425 a.a.
Ligands
NAG-FUC-NAG-BMA-
XYP-BMA
NAG ×8
P1T ×4
NAG-FUC
NAG-FUC-NAG-BMA
NAG-FUC-NAG
NAG-NAG
Metals
_CL ×4
Waters ×2669
HEADER    LYASE                                   17-JUL-06   2HOX
TITLE     ALLIINASE FROM ALLIUM SATIVUM (GARLIC)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALLIIN LYASE 1;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: ALLIIN LYASE 1;
COMPND   5 SYNONYM: ALLIINASE 1, CYSTEINE SULPHOXIDE LYASE 1;
COMPND   6 EC: 4.4.1.4
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ALLIUM SATIVUM;
SOURCE   3 ORGANISM_COMMON: GARLIC;
SOURCE   4 ORGANISM_TAXID: 4682;
SOURCE   5 TISSUE: BULBS
KEYWDS    CYSTEINE SULPHOXIDE LYASE, ALLIINASE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.J.W.SHIMON,A.RABINKOV,M.WILCHECK,D.MIRELMAN,F.FROLOW
REVDAT   5   16-APR-14 2HOX    1       REMARK
REVDAT   4   13-JUL-11 2HOX    1       VERSN
REVDAT   3   24-FEB-09 2HOX    1       VERSN
REVDAT   2   13-FEB-07 2HOX    1       JRNL
REVDAT   1   06-FEB-07 2HOX    0
JRNL        AUTH   L.J.SHIMON,A.RABINKOV,I.SHIN,T.MIRON,D.MIRELMAN,M.WILCHEK,
JRNL        AUTH 2 F.FROLOW
JRNL        TITL   TWO STRUCTURES OF ALLIINASE FROM ALLIIUM SATIVUM L.: APO
JRNL        TITL 2 FORM AND TERNARY COMPLEX WITH AMINOACRYLATE REACTION
JRNL        TITL 3 INTERMEDIATE COVALENTLY BOUND TO THE PLP COFACTOR.
JRNL        REF    J.MOL.BIOL.                   V. 366   611 2007
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   17174334
JRNL        DOI    10.1016/J.JMB.2006.11.041
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   L.J.W.SHIMON,A.RABINKOV,T.MIRON,D.MIRELMAN,M.WILCHECK,
REMARK   1  AUTH 2 F.FROLOW
REMARK   1  TITL   ALLIIN LYASE (ALLIINASE FROM GARLIC (ALLIUM SATIVUM)
REMARK   1  TITL 2 CRYSTALLIZATION AND PRELIMINARY X-RAY CHARACTERIZATION
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  58  1335 2002
REMARK   1  REFN                   ISSN 0907-4449
REMARK   2
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.10
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5
REMARK   3   NUMBER OF REFLECTIONS             : 310776
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169
REMARK   3   R VALUE            (WORKING SET) : 0.167
REMARK   3   FREE R VALUE                     : 0.205
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 16535
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.43
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17361
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.60
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090
REMARK   3   BIN FREE R VALUE SET COUNT          : 960
REMARK   3   BIN FREE R VALUE                    : 0.3260
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 13748
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 408
REMARK   3   SOLVENT ATOMS            : 2669
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.13
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.03000
REMARK   3    B22 (A**2) : -0.45000
REMARK   3    B33 (A**2) : 0.60000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.44000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.063
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.305
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14576 ; 0.018 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  9951 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19777 ; 1.728 ; 1.975
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24079 ; 0.991 ; 3.003
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1708 ; 6.113 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   679 ;29.808 ;24.168
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2444 ;12.538 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;15.317 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2123 ; 0.109 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15861 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  2981 ; 0.005 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2934 ; 0.221 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10920 ; 0.200 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7287 ; 0.189 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7220 ; 0.093 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1956 ; 0.211 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.241 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    88 ; 0.284 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    83 ; 0.227 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10909 ; 2.554 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3445 ; 0.529 ; 3.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13797 ; 2.860 ; 5.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7238 ; 4.542 ; 7.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5977 ; 5.987 ;10.000
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 30843 ; 6.646 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  2178 ;25.393 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 24090 ;10.818 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2HOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-06.
REMARK 100 THE RCSB ID CODE IS RCSB038593.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.60
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9333
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 327315
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.390
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7
REMARK 200  DATA REDUNDANCY                : 3.080
REMARK 200  R MERGE                    (I) : 0.04900
REMARK 200  R SYM                      (I) : 0.04900
REMARK 200   FOR THE DATA SET  : 40.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.41
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800
REMARK 200  R SYM FOR SHELL            (I) : 0.59800
REMARK 200   FOR SHELL         : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1LK9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE, TRI-
REMARK 280  SODIUM CITRATE, PH 5.6, PH 5.60, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
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       63.44600
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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     ARG A   426
REMARK 465     LYS A   427
REMARK 465     ARG C   426
REMARK 465     LYS C   427
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH A  6516     O    HOH A  6720              1.71
REMARK 500   O    HOH C  6008     O    HOH C  6677              1.75
REMARK 500   O    HOH A  6631     O    HOH A  6720              1.80
REMARK 500   O    HOH C  6135     O    HOH C  6744              1.84
REMARK 500   OH   TYR C   277     O    HOH C  6486              1.85
REMARK 500   O    HOH C  6435     O    HOH C  6486              1.88
REMARK 500   O    HOH C  6728     O    HOH C  6744              1.91
REMARK 500   SG   CYS D    41     O    HOH D  6250              1.94
REMARK 500   O    HOH A  6672     O    HOH A  6710              1.94
REMARK 500   CE2  TYR C   277     O    HOH C  6486              1.98
REMARK 500   O    HOH C  6007     O    HOH C  6662              2.00
REMARK 500   O3   NAG B  3500     O    HOH B  6270              2.01
REMARK 500   O    ASP D   123     O    HOH D  6449              2.01
REMARK 500   CZ   TYR C   277     O    HOH C  6486              2.02
REMARK 500   O    HOH C  6101     O    HOH C  6493              2.03
REMARK 500   O    HOH C  6231     O    HOH C  6718              2.03
REMARK 500   O    HOH A  6015     O    HOH A  6640              2.05
REMARK 500   O    HOH A  6672     O    HOH A  6718              2.05
REMARK 500   O    GLN B    55     O    HOH B  6653              2.05
REMARK 500   O    HOH D  6010     O    HOH D  6420              2.06
REMARK 500   O    HOH C  6040     O    HOH C  6740              2.06
REMARK 500   O    HOH B  6640     O    HOH B  6648              2.06
REMARK 500   O    HOH A  6682     O    HOH A  6709              2.07
REMARK 500   O    HOH A  6710     O    HOH B  6594              2.08
REMARK 500   O    HOH C  6441     O    HOH C  6477              2.09
REMARK 500   O    HOH C  6240     O    HOH C  6412              2.09
REMARK 500   O    HOH C  6660     O    HOH C  6677              2.11
REMARK 500   O    HOH A  6745     O    HOH D  6336              2.12
REMARK 500   O    HOH D  6412     O    HOH D  6430              2.12
REMARK 500   OE1  GLU C   343     O    HOH C  6286              2.12
REMARK 500   O    HOH A  6280     O    HOH A  6450              2.13
REMARK 500   OH   TYR D   277     O    HOH D  6442              2.14
REMARK 500   O    HOH D  6156     O    HOH D  6393              2.14
REMARK 500   OD2  ASP A    49     O    HOH A  6477              2.15
REMARK 500   O    HOH B  6419     O    HOH B  6497              2.16
REMARK 500   O2   BMA A   505     O    HOH A  6718              2.16
REMARK 500   O    HOH B  6497     O    HOH B  6643              2.17
REMARK 500   O    HOH B  6124     O    HOH B  6681              2.18
REMARK 500   OH   TYR B   377     O    HOH B  6343              2.18
REMARK 500   O    HOH D  6128     O    HOH D  6315              2.18
REMARK 500   O    HOH A  6641     O    HOH A  6713              2.18
REMARK 500   O    HOH C  6084     O    HOH C  6753              2.19
REMARK 500   NZ   LYS B    77     O    HOH B  6682              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH B  6436     O    HOH C  6361     1455     1.99
REMARK 500   O    HOH A  6664     O    HOH B  6132     2645     2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A 277   CE1   TYR A 277   CZ     -0.082
REMARK 500    TYR C 277   CE1   TYR C 277   CZ     -0.088
REMARK 500    TYR D 224   CZ    TYR D 224   CE2    -0.089
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG B  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG B 259   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG C  89   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
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    THR A   3      -90.88   -120.27
REMARK 500    SER A  21     -159.75     54.15
REMARK 500    ARG A  89       67.05     36.78
REMARK 500    SER A  98       36.20   -148.91
REMARK 500    THR A 282       -2.61   -143.16
REMARK 500    SER A 360       62.76   -156.45
REMARK 500    ARG A 384       34.25     72.06
REMARK 500    THR B   3      -90.44   -127.23
REMARK 500    GLU B  22       11.32     58.85
REMARK 500    ARG B  89       65.28     38.15
REMARK 500    SER B  98       42.98   -153.93
REMARK 500    THR B 282       -1.60   -142.54
REMARK 500    SER B 360       58.86   -151.06
REMARK 500    ARG B 384       32.65     75.82
REMARK 500    THR C   3      -92.12   -121.97
REMARK 500    SER C  21     -147.54     51.26
REMARK 500    ARG C  89       66.19     31.56
REMARK 500    SER C  98       38.61   -152.30
REMARK 500    THR C 282       -4.35   -141.48
REMARK 500    SER C 360       57.68   -152.52
REMARK 500    ARG C 384       35.59     71.38
REMARK 500    THR D   3      -97.06   -120.85
REMARK 500    GLU D  34       68.40     33.50
REMARK 500    ARG D  89       64.86     34.36
REMARK 500    SER D  98       38.56   -154.59
REMARK 500    THR D 282       -1.41   -140.73
REMARK 500    SER D 360       58.39   -154.67
REMARK 500    ARG D 384       30.80     77.60
REMARK 500    LYS D 406     -159.15    -87.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ALA C  424     LYS C  425                  149.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A6469        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH A6492        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH A6549        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH A6596        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A6622        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A6753        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH B6519        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH B6542        DISTANCE =  7.19 ANGSTROMS
REMARK 525    HOH B6571        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH B6572        DISTANCE =  8.30 ANGSTROMS
REMARK 525    HOH C6445        DISTANCE =  8.60 ANGSTROMS
REMARK 525    HOH C6569        DISTANCE =  7.73 ANGSTROMS
REMARK 525    HOH C6596        DISTANCE =  8.75 ANGSTROMS
REMARK 525    HOH C6622        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH C6650        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH D6310        DISTANCE =  7.88 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NAG A  507
REMARK 610     NAG B  502
REMARK 610     NAG B  503
REMARK 610     NAG C  505
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XYP A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 5004
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1T A 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1T B 6002
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1T C 6003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1T D 6004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HOR   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 THERE IS A VARIATION IN A SEQUENCE ASSIGNEMENT IN THE
REMARK 999 LITERATURE,ONE CONTAINS AN ASP IN POSITION 176 AND ONE
REMARK 999 CONTAINS ASN. THE AUTHORS HAVE BUILT AND REFINED THE
REMARK 999 STRUCTURE WITH AN ASP PRESENT IN THIS POSITION IN ACCORD
REMARK 999 WITH THE  RELATED STRUCTURE 1LK9.
DBREF  2HOX A    1   427  UNP    Q01594   ALLN1_ALLSA     39    465
DBREF  2HOX B    1   427  UNP    Q01594   ALLN1_ALLSA     39    465
DBREF  2HOX C    1   427  UNP    Q01594   ALLN1_ALLSA     39    465
DBREF  2HOX D    1   427  UNP    Q01594   ALLN1_ALLSA     39    465
SEQADV 2HOX ASP A  176  UNP  Q01594    ASN   214 SEE REMARK 999
SEQADV 2HOX ASP B  176  UNP  Q01594    ASN   214 SEE REMARK 999
SEQADV 2HOX ASP C  176  UNP  Q01594    ASN   214 SEE REMARK 999
SEQADV 2HOX ASP D  176  UNP  Q01594    ASN   214 SEE REMARK 999
SEQRES   1 A  427  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU
SEQRES   2 A  427  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA
SEQRES   3 A  427  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS
SEQRES   4 A  427  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU
SEQRES   5 A  427  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP
SEQRES   6 A  427  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU
SEQRES   7 A  427  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER
SEQRES   8 A  427  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU
SEQRES   9 A  427  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY
SEQRES  10 A  427  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL
SEQRES  11 A  427  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU
SEQRES  12 A  427  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER
SEQRES  13 A  427  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG
SEQRES  14 A  427  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP
SEQRES  15 A  427  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO
SEQRES  16 A  427  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO
SEQRES  17 A  427  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS
SEQRES  18 A  427  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR
SEQRES  19 A  427  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE
SEQRES  20 A  427  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE
SEQRES  21 A  427  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN
SEQRES  22 A  427  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO
SEQRES  23 A  427  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU
SEQRES  24 A  427  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG
SEQRES  25 A  427  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG
SEQRES  26 A  427  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG
SEQRES  27 A  427  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN
SEQRES  28 A  427  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA
SEQRES  29 A  427  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR
SEQRES  30 A  427  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY
SEQRES  31 A  427  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER
SEQRES  32 A  427  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR
SEQRES  33 A  427  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS
SEQRES   1 B  427  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU
SEQRES   2 B  427  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA
SEQRES   3 B  427  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS
SEQRES   4 B  427  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU
SEQRES   5 B  427  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP
SEQRES   6 B  427  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU
SEQRES   7 B  427  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER
SEQRES   8 B  427  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU
SEQRES   9 B  427  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY
SEQRES  10 B  427  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL
SEQRES  11 B  427  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU
SEQRES  12 B  427  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER
SEQRES  13 B  427  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG
SEQRES  14 B  427  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP
SEQRES  15 B  427  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO
SEQRES  16 B  427  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO
SEQRES  17 B  427  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS
SEQRES  18 B  427  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR
SEQRES  19 B  427  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE
SEQRES  20 B  427  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE
SEQRES  21 B  427  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN
SEQRES  22 B  427  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO
SEQRES  23 B  427  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU
SEQRES  24 B  427  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG
SEQRES  25 B  427  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG
SEQRES  26 B  427  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG
SEQRES  27 B  427  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN
SEQRES  28 B  427  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA
SEQRES  29 B  427  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR
SEQRES  30 B  427  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY
SEQRES  31 B  427  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER
SEQRES  32 B  427  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR
SEQRES  33 B  427  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS
SEQRES   1 C  427  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU
SEQRES   2 C  427  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA
SEQRES   3 C  427  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS
SEQRES   4 C  427  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU
SEQRES   5 C  427  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP
SEQRES   6 C  427  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU
SEQRES   7 C  427  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER
SEQRES   8 C  427  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU
SEQRES   9 C  427  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY
SEQRES  10 C  427  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL
SEQRES  11 C  427  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU
SEQRES  12 C  427  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER
SEQRES  13 C  427  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG
SEQRES  14 C  427  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP
SEQRES  15 C  427  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO
SEQRES  16 C  427  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO
SEQRES  17 C  427  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS
SEQRES  18 C  427  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR
SEQRES  19 C  427  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE
SEQRES  20 C  427  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE
SEQRES  21 C  427  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN
SEQRES  22 C  427  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO
SEQRES  23 C  427  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU
SEQRES  24 C  427  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG
SEQRES  25 C  427  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG
SEQRES  26 C  427  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG
SEQRES  27 C  427  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN
SEQRES  28 C  427  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA
SEQRES  29 C  427  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR
SEQRES  30 C  427  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY
SEQRES  31 C  427  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER
SEQRES  32 C  427  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR
SEQRES  33 C  427  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS
SEQRES   1 D  427  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU
SEQRES   2 D  427  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA
SEQRES   3 D  427  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS
SEQRES   4 D  427  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU
SEQRES   5 D  427  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP
SEQRES   6 D  427  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU
SEQRES   7 D  427  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER
SEQRES   8 D  427  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU
SEQRES   9 D  427  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY
SEQRES  10 D  427  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL
SEQRES  11 D  427  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU
SEQRES  12 D  427  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER
SEQRES  13 D  427  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG
SEQRES  14 D  427  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP
SEQRES  15 D  427  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO
SEQRES  16 D  427  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO
SEQRES  17 D  427  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS
SEQRES  18 D  427  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR
SEQRES  19 D  427  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE
SEQRES  20 D  427  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE
SEQRES  21 D  427  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN
SEQRES  22 D  427  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO
SEQRES  23 D  427  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU
SEQRES  24 D  427  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG
SEQRES  25 D  427  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG
SEQRES  26 D  427  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG
SEQRES  27 D  427  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN
SEQRES  28 D  427  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA
SEQRES  29 D  427  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR
SEQRES  30 D  427  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY
SEQRES  31 D  427  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER
SEQRES  32 D  427  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR
SEQRES  33 D  427  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS
MODRES 2HOX ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN A  328  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN B  146  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN C  146  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN C  328  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN D  146  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN D  328  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN A  191  ASN  GLYCOSYLATION SITE
MODRES 2HOX ASN B  191  ASN  GLYCOSYLATION SITE
HET    NAG  A 500      14
HET    FUC  A 501      10
HET    NAG  A 502      14
HET    BMA  A 503      11
HET    XYP  A 504       9
HET    BMA  A 505      11
HET    NAG  A 506      14
HET    NAG  A 507      14
HET    NAG  B 500      14
HET    FUC  B 501      10
HET    NAG  B 502      14
HET    NAG  B 503      14
HET    NAG  B3500      14
HET    NAG  A4500      14
HET    NAG  C 500      14
HET    FUC  C 501      10
HET    NAG  C 502      14
HET    BMA  C 503      11
HET    NAG  C 504      14
HET    NAG  C 505      14
HET    NAG  D 500      14
HET    FUC  D 501      10
HET    NAG  D 502      14
HET    NAG  D 503      14
HET    NAG  D 504      14
HET     CL  A5001       1
HET     CL  B5002       1
HET     CL  C5003       1
HET     CL  D5004       1
HET    P1T  A6001      21
HET    P1T  B6002      21
HET    P1T  C6003      21
HET    P1T  D6004      21
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     XYP BETA-D-XYLOPYRANOSE
HETNAM      CL CHLORIDE ION
HETNAM     P1T 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)
HETNAM   2 P1T  METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID
FORMUL   5  NAG    17(C8 H15 N O6)
FORMUL   5  FUC    4(C6 H12 O5)
FORMUL   5  BMA    3(C6 H12 O6)
FORMUL   5  XYP    C5 H10 O5
FORMUL  18   CL    4(CL 1-)
FORMUL  22  P1T    4(C11 H15 N2 O7 P)
FORMUL  26  HOH   *2669(H2 O)
HELIX    1   1 THR A    5  ASN A   17  1                                  13
HELIX    2   2 CYS A   20  GLU A   22  5                                   3
HELIX    3   3 GLY A   66  PHE A   68  5                                   3
HELIX    4   4 LEU A   69  LYS A   74  1                                   6
HELIX    5   5 HIS A   76  ALA A   81  1                                   6
HELIX    6   6 SER A  102  GLY A  117  1                                  16
HELIX    7   7 VAL A  130  SER A  144  1                                  15
HELIX    8   8 TYR A  165  PHE A  175  1                                  11
HELIX    9   9 ALA A  187  VAL A  190  5                                   4
HELIX   10  10 ASN A  194  GLU A  196  5                                   3
HELIX   11  11 MET A  249  THR A  253  1                                   5
HELIX   12  12 HIS A  255  ARG A  259  5                                   5
HELIX   13  13 ASP A  267  THR A  282  1                                  16
HELIX   14  14 PRO A  286  LYS A  308  1                                  23
HELIX   15  15 ASP A  313  ASP A  334  1                                  22
HELIX   16  16 TRP A  370  LYS A  374  5                                   5
HELIX   17  17 ASP A  375  GLY A  383  1                                   9
HELIX   18  18 VAL A  391  GLU A  394  5                                   4
HELIX   19  19 THR A  407  LYS A  423  1                                  17
HELIX   20  20 THR B    5  ASN B   17  1                                  13
HELIX   21  21 GLY B   66  PHE B   68  5                                   3
HELIX   22  22 LEU B   69  LYS B   74  1                                   6
HELIX   23  23 HIS B   76  ALA B   81  1                                   6
HELIX   24  24 SER B  102  GLY B  117  1                                  16
HELIX   25  25 VAL B  130  SER B  144  1                                  15
HELIX   26  26 TYR B  165  PHE B  175  1                                  11
HELIX   27  27 ALA B  187  VAL B  190  5                                   4
HELIX   28  28 ASN B  194  GLU B  196  5                                   3
HELIX   29  29 MET B  249  THR B  253  1                                   5
HELIX   30  30 HIS B  255  ARG B  259  5                                   5
HELIX   31  31 ASP B  267  THR B  282  1                                  16
HELIX   32  32 PRO B  286  LYS B  308  1                                  23
HELIX   33  33 ASP B  313  ASP B  334  1                                  22
HELIX   34  34 TRP B  370  LYS B  374  5                                   5
HELIX   35  35 ASP B  375  GLY B  383  1                                   9
HELIX   36  36 VAL B  391  GLU B  394  5                                   4
HELIX   37  37 THR B  407  LYS B  423  1                                  17
HELIX   38  38 THR C    5  ASN C   17  1                                  13
HELIX   39  39 GLY C   66  PHE C   68  5                                   3
HELIX   40  40 LEU C   69  LYS C   74  1                                   6
HELIX   41  41 HIS C   76  ALA C   81  1                                   6
HELIX   42  42 SER C  102  GLY C  117  1                                  16
HELIX   43  43 VAL C  130  SER C  144  1                                  15
HELIX   44  44 TYR C  165  PHE C  175  1                                  11
HELIX   45  45 ALA C  187  VAL C  190  5                                   4
HELIX   46  46 ASN C  194  GLU C  196  5                                   3
HELIX   47  47 MET C  249  THR C  253  1                                   5
HELIX   48  48 HIS C  255  ARG C  259  5                                   5
HELIX   49  49 ASP C  267  GLU C  283  1                                  17
HELIX   50  50 PRO C  286  LYS C  308  1                                  23
HELIX   51  51 ASP C  313  ASP C  334  1                                  22
HELIX   52  52 TRP C  370  LYS C  374  5                                   5
HELIX   53  53 ASP C  375  GLY C  383  1                                   9
HELIX   54  54 VAL C  391  GLU C  394  5                                   4
HELIX   55  55 THR C  407  ALA C  424  1                                  18
HELIX   56  56 THR D    5  ASN D   17  1                                  13
HELIX   57  57 GLY D   66  PHE D   68  5                                   3
HELIX   58  58 LEU D   69  GLN D   75  1                                   7
HELIX   59  59 HIS D   76  ALA D   81  1                                   6
HELIX   60  60 SER D  102  GLY D  117  1                                  16
HELIX   61  61 VAL D  130  SER D  144  1                                  15
HELIX   62  62 TYR D  165  PHE D  175  1                                  11
HELIX   63  63 ALA D  187  VAL D  190  5                                   4
HELIX   64  64 ASN D  194  GLU D  196  5                                   3
HELIX   65  65 MET D  249  THR D  253  1                                   5
HELIX   66  66 HIS D  255  ARG D  259  5                                   5
HELIX   67  67 ASP D  267  THR D  282  1                                  16
HELIX   68  68 PRO D  286  LYS D  308  1                                  23
HELIX   69  69 ASP D  313  ASP D  334  1                                  22
HELIX   70  70 TRP D  370  LYS D  374  5                                   5
HELIX   71  71 ASP D  375  GLY D  383  1                                   9
HELIX   72  72 VAL D  391  GLU D  394  5                                   4
HELIX   73  73 THR D  407  LYS D  423  1                                  17
SHEET    1   A 2 GLY A  24  ARG A  25  0
SHEET    2   A 2 GLU A  40  CYS A  41 -1  O  GLU A  40   N  ARG A  25
SHEET    1   B 2 ILE A  32  SER A  33  0
SHEET    2   B 2 SER A  36  PRO A  37 -1  O  SER A  36   N  SER A  33
SHEET    1   C 2 TYR A  45  THR A  46  0
SHEET    2   C 2 GLU A  52  LYS A  53 -1  O  GLU A  52   N  THR A  46
SHEET    1   D 2 ALA A  59  ASP A  60  0
SHEET    2   D 2 ILE A 385  ASN A 386  1  O  ASN A 386   N  ALA A  59
SHEET    1   E 2 VAL A  82  VAL A  84  0
SHEET    2   E 2 VAL B  82  VAL B  84 -1  O  VAL B  84   N  VAL A  82
SHEET    1   F 7 TYR A 125  GLY A 129  0
SHEET    2   F 7 GLY A 261  ILE A 265 -1  O  ILE A 265   N  TYR A 125
SHEET    3   F 7 ILE A 244  THR A 248 -1  N  LEU A 245   O  LEU A 264
SHEET    4   F 7 LYS A 221  ASP A 225  1  N  TYR A 224   O  LEU A 246
SHEET    5   F 7 TYR A 198  THR A 203  1  N  VAL A 202   O  ILE A 223
SHEET    6   F 7 SER A 156  ALA A 160  1  N  VAL A 159   O  MET A 201
SHEET    7   F 7 TYR A 180  ASN A 185  1  O  ALA A 183   N  VAL A 158
SHEET    1   G 4 PHE A 339  SER A 340  0
SHEET    2   G 4 TYR A 363  CYS A 368 -1  O  LYS A 367   N  SER A 340
SHEET    3   G 4 TYR A 399  SER A 403 -1  O  LEU A 402   N  ALA A 364
SHEET    4   G 4 GLN A 388  ASN A 389 -1  N  GLN A 388   O  ARG A 401
SHEET    1   H 2 GLU A 348  CYS A 350  0
SHEET    2   H 2 ARG A 355  ARG A 357 -1  O  ARG A 357   N  GLU A 348
SHEET    1   I 2 GLY B  24  ARG B  25  0
SHEET    2   I 2 GLU B  40  CYS B  41 -1  O  GLU B  40   N  ARG B  25
SHEET    1   J 2 ILE B  32  SER B  33  0
SHEET    2   J 2 SER B  36  PRO B  37 -1  O  SER B  36   N  SER B  33
SHEET    1   K 2 TYR B  45  THR B  46  0
SHEET    2   K 2 GLU B  52  LYS B  53 -1  O  GLU B  52   N  THR B  46
SHEET    1   L 2 ALA B  59  ASP B  60  0
SHEET    2   L 2 ILE B 385  ASN B 386  1  O  ASN B 386   N  ALA B  59
SHEET    1   M 7 TYR B 125  GLY B 129  0
SHEET    2   M 7 GLY B 261  ILE B 265 -1  O  ILE B 265   N  TYR B 125
SHEET    3   M 7 ILE B 244  THR B 248 -1  N  PHE B 247   O  TRP B 262
SHEET    4   M 7 LYS B 221  ASP B 225  1  N  TYR B 224   O  LEU B 246
SHEET    5   M 7 TYR B 198  THR B 203  1  N  VAL B 202   O  ASP B 225
SHEET    6   M 7 SER B 156  ALA B 160  1  N  VAL B 159   O  MET B 201
SHEET    7   M 7 TYR B 180  ASN B 185  1  O  ALA B 183   N  VAL B 158
SHEET    1   N 4 PHE B 339  TYR B 341  0
SHEET    2   N 4 TYR B 363  CYS B 368 -1  O  LYS B 367   N  SER B 340
SHEET    3   N 4 TYR B 399  SER B 403 -1  O  LEU B 402   N  ALA B 364
SHEET    4   N 4 GLN B 388  ASN B 389 -1  N  GLN B 388   O  ARG B 401
SHEET    1   O 2 GLU B 348  CYS B 350  0
SHEET    2   O 2 ARG B 355  ARG B 357 -1  O  ARG B 355   N  CYS B 350
SHEET    1   P 2 GLY C  24  ARG C  25  0
SHEET    2   P 2 GLU C  40  CYS C  41 -1  O  GLU C  40   N  ARG C  25
SHEET    1   Q 2 ILE C  32  SER C  33  0
SHEET    2   Q 2 SER C  36  PRO C  37 -1  O  SER C  36   N  SER C  33
SHEET    1   R 2 TYR C  45  THR C  46  0
SHEET    2   R 2 GLU C  52  LYS C  53 -1  O  GLU C  52   N  THR C  46
SHEET    1   S 2 ALA C  59  ASP C  60  0
SHEET    2   S 2 ILE C 385  ASN C 386  1  O  ASN C 386   N  ALA C  59
SHEET    1   T 2 VAL C  82  VAL C  84  0
SHEET    2   T 2 VAL D  82  VAL D  84 -1  O  VAL D  82   N  VAL C  84
SHEET    1   U 7 TYR C 125  GLY C 129  0
SHEET    2   U 7 GLY C 261  ILE C 265 -1  O  ILE C 265   N  TYR C 125
SHEET    3   U 7 ILE C 244  THR C 248 -1  N  PHE C 247   O  TRP C 262
SHEET    4   U 7 LYS C 221  ASP C 225  1  N  TYR C 224   O  LEU C 246
SHEET    5   U 7 TYR C 198  THR C 203  1  N  VAL C 202   O  ILE C 223
SHEET    6   U 7 SER C 156  ALA C 160  1  N  VAL C 159   O  MET C 201
SHEET    7   U 7 TYR C 180  ASN C 185  1  O  ALA C 183   N  VAL C 158
SHEET    1   V 4 PHE C 339  TYR C 341  0
SHEET    2   V 4 TYR C 363  CYS C 368 -1  O  LYS C 367   N  SER C 340
SHEET    3   V 4 TYR C 399  SER C 403 -1  O  LEU C 402   N  ALA C 364
SHEET    4   V 4 GLN C 388  ASN C 389 -1  N  GLN C 388   O  ARG C 401
SHEET    1   W 2 GLU C 348  CYS C 350  0
SHEET    2   W 2 ARG C 355  ARG C 357 -1  O  ARG C 357   N  GLU C 348
SHEET    1   X 2 GLY D  24  ARG D  25  0
SHEET    2   X 2 GLU D  40  CYS D  41 -1  O  GLU D  40   N  ARG D  25
SHEET    1   Y 2 ILE D  32  SER D  33  0
SHEET    2   Y 2 SER D  36  PRO D  37 -1  O  SER D  36   N  SER D  33
SHEET    1   Z 2 TYR D  45  THR D  46  0
SHEET    2   Z 2 GLU D  52  LYS D  53 -1  O  GLU D  52   N  THR D  46
SHEET    1  AA 2 ALA D  59  ASP D  60  0
SHEET    2  AA 2 ILE D 385  ASN D 386  1  O  ASN D 386   N  ALA D  59
SHEET    1  AB 7 TYR D 125  GLY D 129  0
SHEET    2  AB 7 GLY D 261  ILE D 265 -1  O  ILE D 265   N  TYR D 125
SHEET    3  AB 7 ILE D 244  THR D 248 -1  N  PHE D 247   O  TRP D 262
SHEET    4  AB 7 LYS D 221  ASP D 225  1  N  TYR D 224   O  LEU D 246
SHEET    5  AB 7 TYR D 198  THR D 203  1  N  VAL D 202   O  ASP D 225
SHEET    6  AB 7 SER D 156  ALA D 160  1  N  VAL D 159   O  MET D 201
SHEET    7  AB 7 TYR D 180  ASN D 185  1  O  ALA D 183   N  VAL D 158
SHEET    1  AC 4 PHE D 339  TYR D 341  0
SHEET    2  AC 4 TYR D 363  CYS D 368 -1  O  LYS D 367   N  SER D 340
SHEET    3  AC 4 TYR D 399  SER D 403 -1  O  LEU D 402   N  ALA D 364
SHEET    4  AC 4 GLN D 388  ASN D 389 -1  N  GLN D 388   O  ARG D 401
SHEET    1  AD 2 GLU D 348  CYS D 350  0
SHEET    2  AD 2 ARG D 355  ARG D 357 -1  O  ARG D 357   N  GLU D 348
SSBOND   1 CYS A   39    CYS A   20                          1555   1555  2.06
SSBOND   2 CYS A   50    CYS A   41                          1555   1555  2.09
SSBOND   3 CYS A   57    CYS A   44                          1555   1555  2.07
SSBOND   4 CYS A  376    CYS A  368                          1555   1555  2.12
SSBOND   5 CYS B   39    CYS B   20                          1555   1555  2.09
SSBOND   6 CYS B   50    CYS B   41                          1555   1555  2.14
SSBOND   7 CYS B   57    CYS B   44                          1555   1555  2.07
SSBOND   8 CYS B  376    CYS B  368                          1555   1555  2.11
SSBOND   9 CYS C   39    CYS C   20                          1555   1555  2.07
SSBOND  10 CYS C   50    CYS C   41                          1555   1555  2.07
SSBOND  11 CYS C   57    CYS C   44                          1555   1555  2.06
SSBOND  12 CYS C  376    CYS C  368                          1555   1555  2.12
SSBOND  13 CYS D   39    CYS D   20                          1555   1555  2.07
SSBOND  14 CYS D   50    CYS D   41                          1555   1555  2.07
SSBOND  15 CYS D   57    CYS D   44                          1555   1555  2.07
SSBOND  16 CYS D  376    CYS D  368                          1555   1555  2.13
LINK         ND2 ASN A 146                 C1  NAG A 500     1555   1555  1.47
LINK         ND2 ASN A 328                 C1  NAG A 506     1555   1555  1.44
LINK         ND2 ASN B 146                 C1  NAG B 500     1555   1555  1.46
LINK         ND2 ASN C 146                 C1  NAG C 500     1555   1555  1.44
LINK         ND2 ASN C 328                 C1  NAG C 504     1555   1555  1.44
LINK         ND2 ASN D 146                 C1  NAG D 500     1555   1555  1.46
LINK         ND2 ASN D 328                 C1  NAG D 503     1555   1555  1.44
LINK         O4  NAG A 500                 C1  NAG A 502     1555   1555  1.42
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.43
LINK         O2  BMA A 503                 C1B XYP A 504     1555   1555  1.44
LINK         O3  BMA A 503                 C1  BMA A 505     1555   1555  1.40
LINK         O4  NAG C 500                 C1  NAG C 502     1555   1555  1.44
LINK         O4  NAG C 502                 C1  BMA C 503     1555   1555  1.46
LINK         O4  NAG D 500                 C1  NAG D 502     1555   1555  1.44
LINK         O4  NAG D 503                 C1  NAG D 504     1555   1555  1.45
LINK         ND2 ASN A 191                 C1  NAG A4500     1555   1555  1.45
LINK         ND2 ASN B 191                 C1  NAG B3500     1555   1555  1.45
LINK         O3  NAG A 500                 C1  FUC A 501     1555   1555  1.44
LINK         O3  NAG B 500                 C1  FUC B 501     1555   1555  1.45
LINK         O3  NAG C 500                 C1  FUC C 501     1555   1555  1.46
LINK         O3  NAG D 500                 C1  FUC D 501     1555   1555  1.44
CISPEP   1 ASN A   95    PRO A   96          0         1.30
CISPEP   2 ALA A  162    PRO A  163          0         5.28
CISPEP   3 SER A  204    PRO A  205          0        -6.66
CISPEP   4 ASN A  207    PRO A  208          0        22.73
CISPEP   5 ASN B   95    PRO B   96          0         4.46
CISPEP   6 ALA B  162    PRO B  163          0         2.76
CISPEP   7 SER B  204    PRO B  205          0        -6.43
CISPEP   8 ASN B  207    PRO B  208          0        20.99
CISPEP   9 ASN C   95    PRO C   96          0         2.19
CISPEP  10 ALA C  162    PRO C  163          0         1.05
CISPEP  11 SER C  204    PRO C  205          0        -7.58
CISPEP  12 ASN C  207    PRO C  208          0        21.00
CISPEP  13 ASN D   95    PRO D   96          0         2.63
CISPEP  14 ALA D  162    PRO D  163          0         2.97
CISPEP  15 SER D  204    PRO D  205          0        -5.99
CISPEP  16 ASN D  207    PRO D  208          0        22.00
SITE     1 AC1  6 ASN A 146  ALA A 149  FUC A 501  NAG A 502
SITE     2 AC1  6 HOH A6696  HOH A6723
SITE     1 AC2  6 NAG A 500  NAG A 502  HOH A6280  HOH A6416
SITE     2 AC2  6 HOH A6450  HOH A6715
SITE     1 AC3  8 NAG A 500  FUC A 501  BMA A 503  XYP A 504
SITE     2 AC3  8 HOH A6362  HOH A6386  HOH A6484  ASP C 123
SITE     1 AC4  8 NAG A 502  XYP A 504  BMA A 505  HOH A6119
SITE     2 AC4  8 HOH A6228  HOH A6332  HOH A6336  HOH A6684
SITE     1 AC5 10 NAG A 502  BMA A 503  BMA A 505  HOH A6228
SITE     2 AC5 10 HOH A6665  ASP C 123  ARG C 124  TYR C 125
SITE     3 AC5 10 LYS C 266  HOH C6384
SITE     1 AC6 11 BMA A 503  XYP A 504  HOH A6215  HOH A6294
SITE     2 AC6 11 HOH A6466  HOH A6672  HOH A6697  HOH A6710
SITE     3 AC6 11 HOH A6718  HOH A6725  LYS C 266
SITE     1 AC7  6 ASN A 328  GLN A 408  PHE A 411  NAG A 507
SITE     2 AC7  6 HOH A6235  HOH A6308
SITE     1 AC8  2 NAG A 506  HOH A6404
SITE     1 AC9  6 ASN B 146  THR B 148  ALA B 149  FUC B 501
SITE     2 AC9  6 HOH B6006  HOH B6613
SITE     1 BC1  2 NAG B 500  HOH B6277
SITE     1 BC2  7 GLU B 324  ASN B 328  GLN B 408  NAG B 503
SITE     2 BC2  7 HOH B6179  HOH B6272  HOH B6650
SITE     1 BC3  4 NAG B 502  HOH B6455  HOH B6488  HOH B6663
SITE     1 BC4  6 ASN A  17  ASN B 191  HOH B6270  HOH B6279
SITE     2 BC4  6 HOH B6296  HOH B6309
SITE     1 BC5  6 ASN A 191  HOH A6248  HOH A6269  HOH A6301
SITE     2 BC5  6 HOH A6704  HOH A6728
SITE     1 BC6  5 ASN C 146  FUC C 501  NAG C 502  HOH C6272
SITE     2 BC6  5 TYR D 174
SITE     1 BC7  6 ASN C 276  LYS C 280  NAG C 500  NAG C 502
SITE     2 BC7  6 HOH C6694  GLU D 170
SITE     1 BC8  4 NAG C 500  FUC C 501  BMA C 503  LYS D 173
SITE     1 BC9  2 HOH A6573  NAG C 502
SITE     1 CC1  9 ASN C 328  GLN C 408  PHE C 411  NAG C 505
SITE     2 CC1  9 HOH C6328  HOH C6343  HOH C6457  HOH C6515
SITE     3 CC1  9 HOH C6739
SITE     1 CC2  4 NAG C 504  HOH C6370  HOH C6676  ASP D 152
SITE     1 CC3  7 ASN D 146  THR D 148  ALA D 149  FUC D 501
SITE     2 CC3  7 NAG D 502  HOH D6154  HOH D6213
SITE     1 CC4  5 NAG D 500  NAG D 502  HOH D6209  HOH D6415
SITE     2 CC4  5 HOH D6432
SITE     1 CC5  4 NAG D 500  FUC D 501  HOH D6204  HOH D6400
SITE     1 CC6  6 ASN D 328  GLN D 408  PHE D 411  NAG D 504
SITE     2 CC6  6 HOH D6259  HOH D6304
SITE     1 CC7  3 NAG D 503  HOH D6238  HOH D6382
SITE     1 CC8  5 PHE A  93  PHE A  94  SER A  98  ASN A  99
SITE     2 CC8  5 PHE A 100
SITE     1 CC9  5 PHE B  93  PHE B  94  SER B  98  ASN B  99
SITE     2 CC9  5 PHE B 100
SITE     1 DC1  5 PHE C  93  PHE C  94  SER C  98  ASN C  99
SITE     2 DC1  5 PHE C 100
SITE     1 DC2  5 PHE D  93  PHE D  94  SER D  98  ASN D  99
SITE     2 DC2  5 PHE D 100
SITE     1 DC3 19 GLY A  64  GLY A 131  VAL A 132  THR A 133
SITE     2 DC3 19 TYR A 165  THR A 203  ASN A 207  ASP A 225
SITE     3 DC3 19 VAL A 227  TYR A 228  THR A 248  SER A 250
SITE     4 DC3 19 LYS A 251  ARG A 259  TYR A 363  ARG A 401
SITE     5 DC3 19 HOH A6130  HOH A6641  TYR B  92
SITE     1 DC4 19 TYR A  92  GLY B  64  GLY B 131  VAL B 132
SITE     2 DC4 19 THR B 133  TYR B 165  THR B 203  ASN B 207
SITE     3 DC4 19 ASP B 225  VAL B 227  TYR B 228  THR B 248
SITE     4 DC4 19 SER B 250  LYS B 251  ARG B 259  TYR B 363
SITE     5 DC4 19 ARG B 401  HOH B6166  HOH B6428
SITE     1 DC5 19 GLY C  64  GLY C 131  VAL C 132  THR C 133
SITE     2 DC5 19 TYR C 165  THR C 203  ASN C 207  ASP C 225
SITE     3 DC5 19 VAL C 227  TYR C 228  THR C 248  SER C 250
SITE     4 DC5 19 LYS C 251  ARG C 259  TYR C 363  ARG C 401
SITE     5 DC5 19 HOH C6017  HOH C6211  TYR D  92
SITE     1 DC6 20 TYR C  92  GLY D  64  GLY D 131  VAL D 132
SITE     2 DC6 20 THR D 133  TYR D 165  THR D 203  ASN D 207
SITE     3 DC6 20 ASP D 225  VAL D 227  TYR D 228  THR D 248
SITE     4 DC6 20 SER D 250  LYS D 251  ARG D 259  TYR D 363
SITE     5 DC6 20 ARG D 401  HOH D6118  HOH D6265  HOH D6412
CRYST1   67.665  126.892  102.664  90.00  97.30  90.00 P 1 21 1      8
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      0.014779  0.000000  0.001893        0.00000
SCALE2      0.000000  0.007881  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009820        0.00000
      
PROCHECK
Go to PROCHECK summary
 References