HEADER ENTEROTOXIN 03-JUN-97 1CT1
TITLE CHOLERA TOXIN B-PENTAMER MUTANT G33R BOUND TO RECEPTOR PENTASACCHARIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLERA TOXIN;
COMPND 3 CHAIN: D, E, F, G, H;
COMPND 4 FRAGMENT: B-PENTAMER;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 STRAIN: OGAWA 41 (CLASSICAL BIOTYPE);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENTEROTOXIN, TOXIN-RECEPTOR COMPLEX, OLIGOSACCHARIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.MERRITT,W.G.J.HOL
REVDAT 6 09-AUG-23 1CT1 1 REMARK
REVDAT 5 03-NOV-21 1CT1 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 1CT1 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 04-AUG-09 1CT1 1 ATOM COMPND CONECT HET
REVDAT 3 2 1 HETATM HETNAM LINK SITE
REVDAT 2 24-FEB-09 1CT1 1 VERSN
REVDAT 1 15-OCT-97 1CT1 0
JRNL AUTH E.A.MERRITT,S.SARFATY,M.G.JOBLING,T.CHANG,R.K.HOLMES,
JRNL AUTH 2 T.R.HIRST,W.G.HOL
JRNL TITL STRUCTURAL STUDIES OF RECEPTOR BINDING BY CHOLERA TOXIN
JRNL TITL 2 MUTANTS.
JRNL REF PROTEIN SCI. V. 6 1516 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9232653
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 21343
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 SET) : 0.182
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 272
REMARK 3 BIN R VALUE (WORKING SET) : 0.2277
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 21
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4105
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 137
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20300
REMARK 3 B22 (A**2) : -3.33020
REMARK 3 B33 (A**2) : 3.53320
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.20290
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.570
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.000 ; 2.300
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.000 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; 2.300
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.000 ; 4.000
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM1.CHO (MODIFIED)
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH1.CHO (MODIFIED)
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BABINET BULK SOLVENT MODEL KSOL = 0.8
REMARK 3 BSOL = 50.0
REMARK 4
REMARK 4 1CT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-95
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 7.2-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MACRO, XENGEN
REMARK 200 DATA SCALING SOFTWARE : MACRO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22182
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1CHP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN, 20 MM TRIS, 1 MM GM1-OS, PH
REMARK 280 7.5 200 MM MGCL2, 100 MM CACODYLATE, 19% PEG 1000, 0.2% AGAROSE,
REMARK 280 PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.80500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.80500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, G, H, 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 400
REMARK 400 COMPOUND
REMARK 400 EACH CHAIN CONTAINS AN INTRODUCED MUTATION GLY->ARG AT
REMARK 400 RESIDUE 33 OF THE RECEPTOR BINDING SITE.
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 MET F 68 SD MET F 68 CE 0.398
REMARK 500 MET G 68 CG MET G 68 SD -0.319
REMARK 500 MET H 68 CG MET H 68 SD -0.169
REMARK 500 MET H 68 SD MET H 68 CE 0.409
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 LEU F 31 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 MET F 68 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 LEU G 31 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 LEU H 31 CA - CB - CG ANGL. DEV. = 15.2 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 LYS D 34 -2.04 75.38
REMARK 500 GLN E 16 139.23 -173.27
REMARK 500 LYS F 34 -1.42 78.52
REMARK 500 ARG G 35 30.31 -141.12
REMARK 500 GLN H 16 142.29 -173.64
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CT1 D 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1CT1 E 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1CT1 F 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1CT1 G 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1CT1 H 1 103 UNP P01556 CHTB_VIBCH 22 124
SEQADV 1CT1 HIS D 18 UNP P01556 TYR 39 CONFLICT
SEQADV 1CT1 ARG D 33 UNP P01556 GLY 54 ENGINEERED MUTATION
SEQADV 1CT1 THR D 47 UNP P01556 ILE 68 CONFLICT
SEQADV 1CT1 HIS E 18 UNP P01556 TYR 39 CONFLICT
SEQADV 1CT1 ARG E 33 UNP P01556 GLY 54 ENGINEERED MUTATION
SEQADV 1CT1 THR E 47 UNP P01556 ILE 68 CONFLICT
SEQADV 1CT1 HIS F 18 UNP P01556 TYR 39 CONFLICT
SEQADV 1CT1 ARG F 33 UNP P01556 GLY 54 ENGINEERED MUTATION
SEQADV 1CT1 THR F 47 UNP P01556 ILE 68 CONFLICT
SEQADV 1CT1 HIS G 18 UNP P01556 TYR 39 CONFLICT
SEQADV 1CT1 ARG G 33 UNP P01556 GLY 54 ENGINEERED MUTATION
SEQADV 1CT1 THR G 47 UNP P01556 ILE 68 CONFLICT
SEQADV 1CT1 HIS H 18 UNP P01556 TYR 39 CONFLICT
SEQADV 1CT1 ARG H 33 UNP P01556 GLY 54 ENGINEERED MUTATION
SEQADV 1CT1 THR H 47 UNP P01556 ILE 68 CONFLICT
SEQRES 1 D 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 D 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 D 103 TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE
SEQRES 4 D 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 D 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 D 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 D 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 D 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 E 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 E 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 E 103 TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE
SEQRES 4 E 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 E 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 E 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 E 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 E 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 F 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 F 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 F 103 TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE
SEQRES 4 F 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 F 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 F 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 F 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 F 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 G 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 G 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 G 103 TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE
SEQRES 4 G 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 G 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 G 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 G 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 G 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 H 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 H 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 H 103 TYR THR GLU SER LEU ALA ARG LYS ARG GLU MET ALA ILE
SEQRES 4 H 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 H 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 H 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 H 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 H 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
HET BGC A 1 12
HET GAL A 2 11
HET NGA A 3 14
HET GAL A 4 11
HET SIA A 5 20
HET BGC B 1 12
HET GAL B 2 11
HET NGA B 3 14
HET GAL B 4 11
HET SIA B 5 20
HET CL H 104 1
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM NGA 2-ACETAMIDO-2-DEOXY-BETA-D-GALACTOPYRANOSE
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
HETNAM CL CHLORIDE ION
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN NGA N-ACETYL-BETA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 NGA BETA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2-
HETSYN 3 NGA ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-D-GALACTOSAMINE
HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC
HETSYN 2 SIA ACID; O-SIALIC ACID
FORMUL 6 BGC 2(C6 H12 O6)
FORMUL 6 GAL 4(C6 H12 O6)
FORMUL 6 NGA 2(C8 H15 N O6)
FORMUL 6 SIA 2(C11 H19 N O9)
FORMUL 8 CL CL 1-
FORMUL 9 HOH *151(H2 O)
HELIX 1 DA1 ILE D 5 CYS D 9 1 5
HELIX 2 DA2 ASP D 59 THR D 78 1 20
HELIX 3 EA1 ILE E 5 CYS E 9 1 5
HELIX 4 EA2 LYS E 62 THR E 78 1 17
HELIX 5 FA1 ILE F 5 CYS F 9 1 5
HELIX 6 FA2 ASP F 59 THR F 78 1 20
HELIX 7 GA1 ILE G 5 CYS G 9 1 5
HELIX 8 GA2 GLN G 61 THR G 78 1 18
HELIX 9 HA1 ILE H 5 CYS H 9 1 5
HELIX 10 HA2 SER H 60 THR H 78 1 19
SHEET 1 BB1 6 THR D 15 ASP D 22 0
SHEET 2 BB1 6 VAL D 82 TRP D 88 -1
SHEET 3 BB1 6 HIS D 94 ALA D 102 -1
SHEET 4 BB1 6 SER E 26 SER E 30 -1
SHEET 5 BB1 6 MET E 37 THR E 41 -1
SHEET 6 BB1 6 THR E 47 VAL E 50 -1
SHEET 1 BB2 6 THR E 15 ASP E 22 0
SHEET 2 BB2 6 VAL E 82 TRP E 88 -1
SHEET 3 BB2 6 HIS E 94 ALA E 102 -1
SHEET 4 BB2 6 SER F 26 SER F 30 -1
SHEET 5 BB2 6 MET F 37 THR F 41 -1
SHEET 6 BB2 6 THR F 47 VAL F 50 -1
SHEET 1 BB3 6 THR F 15 ASP F 22 0
SHEET 2 BB3 6 VAL F 82 TRP F 88 -1
SHEET 3 BB3 6 HIS F 94 ALA F 102 -1
SHEET 4 BB3 6 SER G 26 SER G 30 -1
SHEET 5 BB3 6 MET G 37 THR G 41 -1
SHEET 6 BB3 6 THR G 47 VAL G 50 -1
SHEET 1 BB4 6 THR G 15 ASP G 22 0
SHEET 2 BB4 6 VAL G 82 TRP G 88 -1
SHEET 3 BB4 6 HIS G 94 ALA G 102 -1
SHEET 4 BB4 6 SER H 26 SER H 30 -1
SHEET 5 BB4 6 MET H 37 THR H 41 -1
SHEET 6 BB4 6 THR H 47 VAL H 50 -1
SHEET 1 BB5 6 THR H 15 ASP H 22 0
SHEET 2 BB5 6 VAL H 82 TRP H 88 -1
SHEET 3 BB5 6 HIS H 94 ALA H 102 -1
SHEET 4 BB5 6 SER D 26 SER D 30 -1
SHEET 5 BB5 6 MET D 37 THR D 41 -1
SHEET 6 BB5 6 THR D 47 VAL D 50 -1
SSBOND 1 CYS D 9 CYS D 86 1555 1555 2.03
SSBOND 2 CYS E 9 CYS E 86 1555 1555 2.03
SSBOND 3 CYS F 9 CYS F 86 1555 1555 2.03
SSBOND 4 CYS G 9 CYS G 86 1555 1555 2.04
SSBOND 5 CYS H 9 CYS H 86 1555 1555 2.01
LINK O4 BGC A 1 C1 GAL A 2 1555 1555 1.40
LINK O4 GAL A 2 C1 NGA A 3 1555 1555 1.43
LINK O3 GAL A 2 C2 SIA A 5 1555 1555 1.42
LINK O3 NGA A 3 C1 GAL A 4 1555 1555 1.40
LINK O4 BGC B 1 C1 GAL B 2 1555 1555 1.41
LINK O4 GAL B 2 C1 NGA B 3 1555 1555 1.43
LINK O3 GAL B 2 C2 SIA B 5 1555 1555 1.43
LINK O3 NGA B 3 C1 GAL B 4 1555 1555 1.43
CISPEP 1 THR D 92 PRO D 93 0 -0.29
CISPEP 2 THR E 92 PRO E 93 0 0.37
CISPEP 3 THR F 92 PRO F 93 0 -1.49
CISPEP 4 THR G 92 PRO G 93 0 -0.27
CISPEP 5 THR H 92 PRO H 93 0 1.13
CRYST1 103.400 67.610 101.700 90.00 131.66 90.00 C 1 2 1 20
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 0.009671 0.000000 0.008605 0.00000
SCALE2 0.000000 0.014791 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
