HEADER SUGAR BINDING PROTEIN 20-JUN-13 4LBM
TITLE CRYSTAL STRUCTURE OF HUMAN GALECTIN-3 CRD IN COMPLEX WITH LNT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALECTIN-3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 112-250;
COMPND 5 SYNONYM: GAL-3, 35 KDA LECTIN, CARBOHYDRATE-BINDING PROTEIN 35, CBP
COMPND 6 35, GALACTOSE-SPECIFIC LECTIN 3, GALACTOSIDE-BINDING PROTEIN, GALBP,
COMPND 7 IGE-BINDING PROTEIN, L-31, LAMININ-BINDING PROTEIN, LECTIN L-29, MAC-
COMPND 8 2 ANTIGEN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LGALS3, MAC2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS GALECTIN, CARBOHYDRATE-RECOGNITION, LNT, GLYCOSPHINGOLIPID, BETA
KEYWDS 2 SANDWICH, CARBOHYDRATE BINDING PROTEIN, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.COLLINS,H.BLANCHARD
REVDAT 4 20-SEP-23 4LBM 1 HETSYN
REVDAT 3 29-JUL-20 4LBM 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 26-MAR-14 4LBM 1 JRNL
REVDAT 1 22-JAN-14 4LBM 0
JRNL AUTH P.M.COLLINS,K.BUM-ERDENE,X.YU,H.BLANCHARD
JRNL TITL GALECTIN-3 INTERACTIONS WITH GLYCOSPHINGOLIPIDS.
JRNL REF J.MOL.BIOL. V. 426 1439 2014
JRNL REFN ISSN 0022-2836
JRNL PMID 24326249
JRNL DOI 10.1016/J.JMB.2013.12.004
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 19365
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) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 978
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 883
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1112
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 112
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : -0.17000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.397
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1278 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1757 ; 1.427 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 161 ; 6.527 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 62 ;34.519 ;24.355
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 215 ;11.871 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;12.972 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 204 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 974 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 594 ; 1.862 ; 1.384
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 752 ; 2.868 ; 3.092
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 684 ; 4.048 ; 2.144
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 112 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7793 0.7919 6.8406
REMARK 3 T TENSOR
REMARK 3 T11: 0.0088 T22: 0.0177
REMARK 3 T33: 0.0171 T12: 0.0016
REMARK 3 T13: -0.0048 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.5074 L22: 0.9406
REMARK 3 L33: 1.4415 L12: 0.1557
REMARK 3 L13: -0.2218 L23: -0.5845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0340 S12: -0.0029 S13: -0.0401
REMARK 3 S21: -0.0042 S22: -0.0026 S23: 0.0523
REMARK 3 S31: 0.0700 S32: 0.0381 S33: -0.0314
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4LBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
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 : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54184
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SAINT, SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19413
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.496
REMARK 200 RESOLUTION RANGE LOW (A) : 42.912
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.12800
REMARK 200 R SYM FOR SHELL (I) : 0.12800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
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: PDB ENTRY 1A3K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 31% PEG 6000, 100MM MGCL2, 8MM BETA
REMARK 280 MERCEPTOETHANOL, 100MM TRIS HCL, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 18.33200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.80600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.06550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.80600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.33200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.06550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LBJ RELATED DB: PDB
REMARK 900 RELATED ID: 4LBK RELATED DB: PDB
REMARK 900 RELATED ID: 4LBL RELATED DB: PDB
REMARK 900 RELATED ID: 4LBN RELATED DB: PDB
REMARK 900 RELATED ID: 4LBO RELATED DB: PDB
DBREF 4LBM A 112 250 UNP P17931 LEG3_HUMAN 112 250
SEQRES 1 A 139 GLY PRO LEU ILE VAL PRO TYR ASN LEU PRO LEU PRO GLY
SEQRES 2 A 139 GLY VAL VAL PRO ARG MET LEU ILE THR ILE LEU GLY THR
SEQRES 3 A 139 VAL LYS PRO ASN ALA ASN ARG ILE ALA LEU ASP PHE GLN
SEQRES 4 A 139 ARG GLY ASN ASP VAL ALA PHE HIS PHE ASN PRO ARG PHE
SEQRES 5 A 139 ASN GLU ASN ASN ARG ARG VAL ILE VAL CYS ASN THR LYS
SEQRES 6 A 139 LEU ASP ASN ASN TRP GLY ARG GLU GLU ARG GLN SER VAL
SEQRES 7 A 139 PHE PRO PHE GLU SER GLY LYS PRO PHE LYS ILE GLN VAL
SEQRES 8 A 139 LEU VAL GLU PRO ASP HIS PHE LYS VAL ALA VAL ASN ASP
SEQRES 9 A 139 ALA HIS LEU LEU GLN TYR ASN HIS ARG VAL LYS LYS LEU
SEQRES 10 A 139 ASN GLU ILE SER LYS LEU GLY ILE SER GLY ASP ILE ASP
SEQRES 11 A 139 LEU THR SER ALA SER TYR THR MET ILE
HET BGC B 1 12
HET GAL B 2 11
HET NAG B 3 14
HET GAL B 4 11
HET CL A 305 1
HET CL A 306 1
HET CL A 307 1
HET CL A 308 1
HET CL A 309 1
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
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
FORMUL 2 BGC C6 H12 O6
FORMUL 2 GAL 2(C6 H12 O6)
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 CL 5(CL 1-)
FORMUL 8 HOH *112(H2 O)
HELIX 1 1 LYS A 227 ILE A 231 5 5
SHEET 1 A 6 TYR A 118 PRO A 121 0
SHEET 2 A 6 LYS A 233 GLY A 238 -1 O LEU A 234 N LEU A 120
SHEET 3 A 6 ILE A 145 ARG A 151 -1 N ASP A 148 O GLY A 235
SHEET 4 A 6 ASP A 154 GLU A 165 -1 O PHE A 157 N PHE A 149
SHEET 5 A 6 ARG A 168 LEU A 177 -1 O VAL A 170 N ARG A 162
SHEET 6 A 6 ASN A 180 TRP A 181 -1 O ASN A 180 N LEU A 177
SHEET 1 B 6 TYR A 118 PRO A 121 0
SHEET 2 B 6 LYS A 233 GLY A 238 -1 O LEU A 234 N LEU A 120
SHEET 3 B 6 ILE A 145 ARG A 151 -1 N ASP A 148 O GLY A 235
SHEET 4 B 6 ASP A 154 GLU A 165 -1 O PHE A 157 N PHE A 149
SHEET 5 B 6 ARG A 168 LEU A 177 -1 O VAL A 170 N ARG A 162
SHEET 6 B 6 GLU A 185 GLN A 187 -1 O GLU A 185 N CYS A 173
SHEET 1 C 5 ALA A 216 ASN A 222 0
SHEET 2 C 5 HIS A 208 VAL A 213 -1 N VAL A 211 O LEU A 219
SHEET 3 C 5 PRO A 197 VAL A 204 -1 N LEU A 203 O LYS A 210
SHEET 4 C 5 MET A 130 VAL A 138 -1 N ILE A 134 O ILE A 200
SHEET 5 C 5 ILE A 240 MET A 249 -1 O THR A 248 N LEU A 131
LINK O4 BGC B 1 C1 GAL B 2 1555 1555 1.43
LINK O3 GAL B 2 C1 NAG B 3 1555 1555 1.43
LINK O3 NAG B 3 C1 GAL B 4 1555 1555 1.44
CISPEP 1 VAL A 116 PRO A 117 0 1.84
CRYST1 36.664 58.131 63.612 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 0.027275 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017203 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015720 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
