HEADER SIGNALING PROTEIN 07-JUL-06 2DSW
TITLE BINDING OF CHITIN-LIKE POLYSACCHARIDES TO PROTECTIVE SIGNALLING
TITLE 2 FACTOR: CRYSTAL STRUCTURE OF THE COMPLEX OF SIGNALLING PROTEIN FROM
TITLE 3 SHEEP (SPS-40) WITH A PENTASACCHARIDE AT 2.8 A RESOLUTION
CAVEAT 2DSW NAG B 2 HAS WRONG CHIRALITY AT ATOM C1 NAG C 2 HAS WRONG
CAVEAT 2 2DSW CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE-3-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPS-40, SIGNAL-PROCESSING PROTEIN, SECRETORY GLYOPROTEIN OF
COMPND 5 40 KDA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 3 ORGANISM_COMMON: SHEEP;
SOURCE 4 ORGANISM_TAXID: 9940;
SOURCE 5 SECRETION: MILK, MAMMARY GLAND
KEYWDS SPS-40, PENTASACCHARIDE, COMPLEX, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.B.SRIVASTAVA,A.S.ETHAYATHULLA,J.KUMAR,N.SINGH,S.SHARMA,P.KAUR,
AUTHOR 2 A.BHUSHAN,T.P.SINGH
REVDAT 6 25-OCT-23 2DSW 1 HETSYN
REVDAT 5 29-JUL-20 2DSW 1 CAVEAT COMPND REMARK HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 13-JUL-11 2DSW 1 VERSN
REVDAT 3 24-FEB-09 2DSW 1 VERSN
REVDAT 2 17-JUL-07 2DSW 1
REVDAT 1 01-AUG-06 2DSW 0
SPRSDE 01-AUG-06 2DSW 2B2P
JRNL AUTH D.B.SRIVASTAVA,A.S.ETHAYATHULLA,J.KUMAR,R.K.SOMVANSHI,
JRNL AUTH 2 S.SHARMA,S.DEY,T.P.SINGH
JRNL TITL CARBOHYDRATE BINDING PROPERTIES AND CARBOHYDRATE INDUCED
JRNL TITL 2 CONFORMATIONAL SWITCH IN SHEEP SECRETORY GLYCOPROTEIN
JRNL TITL 3 (SPS-40): CRYSTAL STRUCTURES OF FOUR COMPLEXES OF SPS-40
JRNL TITL 4 WITH CHITIN-LIKE OLIGOSACCHARIDES
JRNL REF J.STRUCT.BIOL. V. 158 255 2007
JRNL REFN ISSN 1047-8477
JRNL PMID 17188513
JRNL DOI 10.1016/J.JSB.2006.11.002
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1201776.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 11512
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) : 0.199
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.200
REMARK 3 FREE R VALUE TEST SET COUNT : 252
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1845
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 42
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 121
REMARK 3 SOLVENT ATOMS : 76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.10000
REMARK 3 B22 (A**2) : 0.59000
REMARK 3 B33 (A**2) : 0.50000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.39
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.030
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) : 1.890 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.580 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 23.23
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : CIS_PEPTIDE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DSW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000025805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.8
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11764
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 56.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 2DPE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS-HCL, 50MM NACL, 19% ETHANOL,
REMARK 280 PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.33000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.76300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.24000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.76300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.33000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.24000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 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 A 320 CA - CB - CG ANGL. DEV. = 19.1 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 TRP A 48 -59.10 -124.37
REMARK 500 ALA A 117 64.58 -116.92
REMARK 500 HIS A 188 -143.87 -119.30
REMARK 500 ALA A 190 56.26 33.76
REMARK 500 TRP A 191 74.08 39.90
REMARK 500 ASN A 205 -7.85 -33.61
REMARK 500 SER A 209 -35.74 159.86
REMARK 500 SER A 210 55.93 -117.85
REMARK 500 ARG A 212 -13.02 -39.95
REMARK 500 LYS A 300 112.89 -168.79
REMARK 500 GLN A 345 115.81 -33.30
REMARK 500 ASN A 346 83.90 -61.49
REMARK 500 PHE A 349 62.72 64.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DPE RELATED DB: PDB
REMARK 900 RELATED ID: 2ESC RELATED DB: PDB
REMARK 900 RELATED ID: 2DSU RELATED DB: PDB
REMARK 900 RELATED ID: 2DSV RELATED DB: PDB
DBREF 2DSW A 1 362 UNP Q6TMG6 CH3L1_SHEEP 1 361
SEQRES 1 A 361 TYR LYS LEU ILE CYS TYR TYR THR SER TRP SER GLN TYR
SEQRES 2 A 361 ARG GLU GLY ASP GLY SER CYS PHE PRO ASP ALA ILE ASP
SEQRES 3 A 361 PRO PHE LEU CYS THR HIS VAL ILE TYR SER PHE ALA ASN
SEQRES 4 A 361 ILE SER ASN ASN GLU ILE ASP THR TRP GLU TRP ASN ASP
SEQRES 5 A 361 VAL THR LEU TYR ASP THR LEU ASN THR LEU LYS ASN ARG
SEQRES 6 A 361 ASN PRO LYS LEU LYS THR LEU LEU SER VAL GLY GLY TRP
SEQRES 7 A 361 ASN PHE GLY PRO GLU ARG PHE SER ALA ILE ALA SER LYS
SEQRES 8 A 361 THR GLN SER ARG ARG THR PHE ILE LYS SER VAL PRO PRO
SEQRES 9 A 361 PHE LEU ARG THR HIS GLY PHE ASP GLY LEU ASP LEU ALA
SEQRES 10 A 361 TRP LEU TYR PRO GLY ARG ARG ASP LYS ARG HIS LEU THR
SEQRES 11 A 361 THR LEU VAL LYS GLU MET LYS ALA GLU PHE ILE ARG GLU
SEQRES 12 A 361 ALA GLN ALA GLY THR GLU GLN LEU LEU LEU SER ALA ALA
SEQRES 13 A 361 VAL SER ALA GLY LYS ILE ALA ILE ASP ARG GLY TYR ASP
SEQRES 14 A 361 ILE ALA GLN ILE SER ARG HIS LEU ASP PHE ILE SER LEU
SEQRES 15 A 361 LEU THR TYR ASP PHE HIS GLY ALA TRP ARG GLN THR VAL
SEQRES 16 A 361 GLY HIS HIS SER PRO LEU PHE ALA GLY ASN GLU ASP ALA
SEQRES 17 A 361 SER SER ARG PHE SER ASN ALA ASP TYR ALA VAL SER TYR
SEQRES 18 A 361 MET LEU ARG LEU GLY ALA PRO ALA ASN LYS LEU VAL MET
SEQRES 19 A 361 GLY ILE PRO THR PHE GLY ARG SER PHE THR LEU ALA SER
SEQRES 20 A 361 SER LYS THR ASP VAL GLY ALA PRO VAL SER GLY PRO GLY
SEQRES 21 A 361 VAL PRO GLY ARG PHE THR LYS GLU LYS GLY ILE LEU ALA
SEQRES 22 A 361 TYR TYR GLU ILE CYS ASP PHE LEU HIS GLY ALA THR THR
SEQRES 23 A 361 HIS ARG PHE ARG ASP GLN GLN VAL PRO TYR ALA THR LYS
SEQRES 24 A 361 GLY ASN GLN TRP VAL ALA TYR ASP ASP GLN GLU SER VAL
SEQRES 25 A 361 LYS ASN LYS ALA ARG TYR LEU LYS ASN ARG GLN LEU ALA
SEQRES 26 A 361 GLY ALA MET VAL TRP ALA LEU ASP LEU ASP ASP PHE ARG
SEQRES 27 A 361 GLY THR PHE CYS GLY GLN ASN LEU THR PHE PRO LEU THR
SEQRES 28 A 361 SER ALA VAL LYS ASP VAL LEU ALA GLU VAL
MODRES 2DSW ASN A 39 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET MAN B 3 11
HET MAN B 4 11
HET NAG C 1 15
HET NAG C 2 14
HET NAG C 3 14
HET NAG C 4 14
HET NAG C 5 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 7(C8 H15 N O6)
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 4 HOH *76(H2 O)
HELIX 1 1 TRP A 10 ARG A 14 5 5
HELIX 2 2 GLU A 15 SER A 19 5 5
HELIX 3 3 PHE A 21 ILE A 25 5 5
HELIX 4 4 ASN A 51 THR A 61 1 11
HELIX 5 5 LEU A 62 ARG A 65 5 4
HELIX 6 6 GLY A 81 SER A 90 1 10
HELIX 7 7 LYS A 91 GLY A 110 1 20
HELIX 8 8 ASP A 125 ALA A 144 1 20
HELIX 9 9 GLN A 145 GLY A 147 5 3
HELIX 10 10 GLY A 160 TYR A 168 1 9
HELIX 11 11 ASP A 169 LEU A 177 1 9
HELIX 12 12 ASN A 215 GLY A 227 1 13
HELIX 13 13 PRO A 229 ASN A 231 5 3
HELIX 14 14 TYR A 275 HIS A 283 1 9
HELIX 15 15 ASP A 309 ARG A 323 1 15
HELIX 16 16 ALA A 332 ASP A 336 5 5
HELIX 17 17 PHE A 349 GLU A 361 1 13
SHEET 1 A10 GLU A 44 ASP A 46 0
SHEET 2 A10 HIS A 32 SER A 41 -1 N ASN A 39 O ASP A 46
SHEET 3 A10 LYS A 70 GLY A 76 1 O SER A 74 N ALA A 38
SHEET 4 A10 GLY A 113 ALA A 117 1 O ASP A 115 N LEU A 73
SHEET 5 A10 LEU A 152 VAL A 157 1 O SER A 154 N LEU A 116
SHEET 6 A10 PHE A 179 LEU A 182 1 O SER A 181 N VAL A 157
SHEET 7 A10 LEU A 233 PRO A 238 1 O VAL A 234 N LEU A 182
SHEET 8 A10 GLY A 327 TRP A 331 1 O MET A 329 N ILE A 237
SHEET 9 A10 LYS A 2 THR A 8 1 N ILE A 4 O VAL A 330
SHEET 10 A10 HIS A 32 SER A 41 1 O ILE A 34 N CYS A 5
SHEET 1 B 3 VAL A 257 PRO A 260 0
SHEET 2 B 3 PHE A 240 LEU A 246 -1 N THR A 245 O SER A 258
SHEET 3 B 3 ILE A 272 ALA A 274 -1 O LEU A 273 N GLY A 241
SHEET 1 C 5 VAL A 257 PRO A 260 0
SHEET 2 C 5 PHE A 240 LEU A 246 -1 N THR A 245 O SER A 258
SHEET 3 C 5 GLN A 303 ALA A 306 -1 O TRP A 304 N PHE A 244
SHEET 4 C 5 VAL A 295 LYS A 300 -1 N ALA A 298 O VAL A 305
SHEET 5 C 5 THR A 286 PHE A 290 -1 N HIS A 288 O TYR A 297
SSBOND 1 CYS A 5 CYS A 30 1555 1555 2.03
SSBOND 2 CYS A 279 CYS A 343 1555 1555 2.03
LINK ND2 ASN A 39 C1 NAG B 1 1555 1555 1.47
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.41
LINK O4 NAG B 2 C1 MAN B 3 1555 1555 1.41
LINK O4 MAN B 3 C1 MAN B 4 1555 1555 1.39
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.41
LINK O4 NAG C 2 C1 NAG C 3 1555 1555 1.39
LINK O4 NAG C 3 C1 NAG C 4 1555 1555 1.40
LINK O4 NAG C 4 C1 NAG C 5 1555 1555 1.57
CISPEP 1 SER A 36 PHE A 37 0 -0.23
CISPEP 2 LEU A 119 TYR A 120 0 0.11
CISPEP 3 TRP A 331 ALA A 332 0 -0.06
CRYST1 62.660 66.480 107.526 90.00 90.00 90.00 P 21 21 21 4
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 0.015959 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
