HEADER SUGAR BINDING PROTEIN 19-AUG-04 1W6M
TITLE X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH
TITLE 2 GALACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALECTIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BETA-GALACTOSIDE-BINDING LECTIN L-14-I, HPL, LACTOSE-BINDING
COMPND 5 LECTIN 1, S-LAC LECTIN 1, GALAPTIN, HBL;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GALECTIN-1;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: BETA-GALACTOSIDE-BINDING LECTIN L-14-I, LACTOSE-BINDING
COMPND 12 LECTIN 1, S-LAC LECTIN 1, GALAPTIN, HPL, HBL;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SCS1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PUC540;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PH14GAL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: SCS1;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR: PUC540;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PH14GAL
KEYWDS SUGAR BINDING PROTEIN, LECTIN, CARBOHYDRATE-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.I.F.LOPEZ-LUCENDO,H.J.GABIUS,A.ROMERO
REVDAT 7 13-DEC-23 1W6M 1 HETSYN
REVDAT 6 29-JUL-20 1W6M 1 COMPND REMARK HETNAM SITE
REVDAT 5 08-MAY-19 1W6M 1 REMARK LINK
REVDAT 4 05-JUL-17 1W6M 1 REMARK
REVDAT 3 14-APR-10 1W6M 1 VERSN
REVDAT 2 24-FEB-09 1W6M 1 VERSN
REVDAT 1 20-OCT-04 1W6M 0
JRNL AUTH M.I.F.LOPEZ-LUCENDO,D.SOLIS,S.ANDRE,J.HIRABAYASHI,K.KASAI,
JRNL AUTH 2 H.KALTNER,H.J.GABIUS,A.ROMERO
JRNL TITL GROWTH-REGULATORY HUMAN GALECTIN-1: CRYSTALLOGRAPHIC
JRNL TITL 2 CHARACTERISATION OF THE STRUCTURAL CHANGES INDUCED BY
JRNL TITL 3 SINGLE-SITE MUTATIONS AND THEIR IMPACT ON THE THERMODYNAMICS
JRNL TITL 4 OF LIGAND BINDING.
JRNL REF J.MOL.BIOL. V. 343 957 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15476813
JRNL DOI 10.1016/J.JMB.2004.08.078
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1341364.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 13684
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) : 0.201
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 965
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2058
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2059
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.43000
REMARK 3 B22 (A**2) : -2.14000
REMARK 3 B33 (A**2) : -3.29000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : 1.260 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.110 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.920 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.860 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 33.62
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : GALACTOSA.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : GALACTOSA.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1W6M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1290020822.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13774
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 25.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08000
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) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1GZW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE OBTAINED IN SITTING
REMARK 280 DROPS BY MIXING EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML)
REMARK 280 AND THE PRECIPITATING BUFFER (2M AMMONIUM SULPHATE AND 1% BETA-
REMARK 280 MERCAPTO ETHANOL, PH 5.6). THE GALACTOSE COMPLEX WAS OBTAINED BY
REMARK 280 SOAKING C2S CRYSTALS FOR 72H IN THE MOTHER LIQUOR SUPPLEMENTED
REMARK 280 WITH 10 MM OF GALACTOSE, PH 5.60, VAPOR DIFFUSION, SITTING DROP
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 18.38800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.95650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.44900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.95650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.38800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.44900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 400
REMARK 400 COMPOUND
REMARK 400 MAY REGULATE CELL APOPTOSIS AND CELL DIFFERENTIATION.
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 2 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 65 TO ASP
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 2 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 65 TO ASP
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 O1 GAL B 4000 O HOH B 5079 2.17
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 B2048 NE - CZ - NH2 ANGL. DEV. = 3.5 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 SER A1002 -103.18 -64.03
REMARK 500 ALA A1024 151.17 -49.32
REMARK 500 SER A1029 161.42 171.81
REMARK 500 CYS A1130 147.15 -170.29
REMARK 500 SER B2029 177.42 176.31
REMARK 500 ASN B2050 84.78 -164.42
REMARK 500 PHE B2077 72.74 -153.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GZW RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HUMAN GALECTIN-1
REMARK 900 RELATED ID: 1W6N RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1
REMARK 900 RELATED ID: 1W6O RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH
REMARK 900 LACTOSE
REMARK 900 RELATED ID: 1W6P RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1 COMPLEXED WITH N-
REMARK 900 ACETYL- LACTOSAMINE
REMARK 900 RELATED ID: 1W6Q RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF R111H HUMAN GALECTIN-1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CYS 2 ENGINEERED TO SER GLY 65 ADDITIONAL MUTATION TO ASP
DBREF 1W6M A 1001 1134 UNP P09382 LEG1_HUMAN 1 134
DBREF 1W6M B 2001 2134 UNP P09382 LEG1_HUMAN 1 134
SEQADV 1W6M SER A 1002 UNP P09382 CYS 2 ENGINEERED MUTATION
SEQADV 1W6M ASP A 1065 UNP P09382 GLY 65 ENGINEERED MUTATION
SEQADV 1W6M SER B 2002 UNP P09382 CYS 2 ENGINEERED MUTATION
SEQADV 1W6M ASP B 2065 UNP P09382 GLY 65 ENGINEERED MUTATION
SEQRES 1 A 134 ALA SER GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO
SEQRES 2 A 134 GLY GLU CSO LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP
SEQRES 3 A 134 ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN
SEQRES 4 A 134 ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS
SEQRES 5 A 134 GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP ASP
SEQRES 6 A 134 GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO
SEQRES 7 A 134 PHE GLN PRO GLY SER VAL ALA GLU VAL CYS ILE THR PHE
SEQRES 8 A 134 ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR
SEQRES 9 A 134 GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE
SEQRES 10 A 134 ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CYS
SEQRES 11 A 134 VAL ALA PHE ASP
SEQRES 1 B 134 ALA SER GLY LEU VAL ALA SER ASN LEU ASN LEU LYS PRO
SEQRES 2 B 134 GLY GLU CYS LEU ARG VAL ARG GLY GLU VAL ALA PRO ASP
SEQRES 3 B 134 ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP SER ASN
SEQRES 4 B 134 ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN ALA HIS
SEQRES 5 B 134 GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS ASP ASP
SEQRES 6 B 134 GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL PHE PRO
SEQRES 7 B 134 PHE GLN PRO GLY SER VAL ALA GLU VAL CYS ILE THR PHE
SEQRES 8 B 134 ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP GLY TYR
SEQRES 9 B 134 GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU ALA ILE
SEQRES 10 B 134 ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE LYS CYS
SEQRES 11 B 134 VAL ALA PHE ASP
MODRES 1W6M CSO A 1016 CYS S-HYDROXYCYSTEINE
HET CSO A1016 7
HET BME A2135 4
HET BME A2136 4
HET SO4 A2137 5
HET SO4 A2138 5
HET GAL A4000 12
HET BME B3135 4
HET BME B3136 4
HET BME B3137 4
HET GAL B4000 12
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM SO4 SULFATE ION
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 3 BME 5(C2 H6 O S)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 GAL 2(C6 H12 O6)
FORMUL 12 HOH *131(H2 O)
SHEET 1 AA11 ALA A1067 TRP A1068 0
SHEET 2 AA11 ASP A1054 ASP A1064 -1 O ASP A1064 N ALA A1067
SHEET 3 AA11 ASN A1040 ALA A1051 -1 O LEU A1041 N LYS A1063
SHEET 4 AA11 PHE A1030 ASP A1037 -1 N PHE A1030 O PRO A1047
SHEET 5 AA11 ILE A1117 GLY A1124 -1 N ASN A1118 O GLY A1035
SHEET 6 AA11 VAL A1005 LEU A1011 -1 O ALA A1006 N MET A1120
SHEET 7 AA11 VAL B2005 SER B2007 -1 O VAL B2005 N SER A1007
SHEET 8 AA11 TYR B2119 ALA B2122 -1 O MET B2120 N ALA B2006
SHEET 9 AA11 LEU B2032 ASP B2037 -1 O ASN B2033 N ALA B2121
SHEET 10 AA11 ASN B2040 ALA B2051 -1 O ASN B2040 N LYS B2036
SHEET 11 AA11 ASP B2054 ASP B2064 -1 O ASP B2054 N ALA B2051
SHEET 1 AB 3 ALA A1067 TRP A1068 0
SHEET 2 AB 3 ASP A1054 ASP A1064 -1 O ASP A1064 N ALA A1067
SHEET 3 AB 3 GLN A1072 ARG A1073 -1 O GLN A1072 N CYS A1060
SHEET 1 AC10 GLU A1105 PRO A1109 0
SHEET 2 AC10 ASN A1095 LYS A1099 -1 O LEU A1096 N PHE A1108
SHEET 3 AC10 SER A1083 PHE A1091 -1 O CYS A1088 N LYS A1099
SHEET 4 AC10 CSO A1016 VAL A1023 -1 O LEU A1017 N ILE A1089
SHEET 5 AC10 PHE A1126 PHE A1133 -1 O LYS A1127 N GLU A1022
SHEET 6 AC10 PHE B2126 PHE B2133 -1 O LYS B2129 N PHE A1133
SHEET 7 AC10 LEU B2017 VAL B2023 -1 O ARG B2018 N ALA B2132
SHEET 8 AC10 SER B2083 PHE B2091 -1 O SER B2083 N VAL B2023
SHEET 9 AC10 ASN B2095 LYS B2099 -1 O THR B2097 N THR B2090
SHEET 10 AC10 GLU B2105 PRO B2109 -1 O PHE B2106 N VAL B2098
LINK C GLU A1015 N CSO A1016 1555 1555 1.33
LINK C CSO A1016 N LEU A1017 1555 1555 1.33
LINK SG CYS A1088 S2 BME A2135 1555 1555 1.92
LINK SG CYS A1130 S2 BME A2136 1555 1555 1.92
LINK SG CYS B2016 S2 BME B3135 1555 1555 1.92
LINK SG CYS B2088 S2 BME B3136 1555 1555 1.92
LINK SG CYS B2130 S2 BME B3137 1555 1555 1.92
CRYST1 36.776 88.898 93.913 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 0.027192 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010648 0.00000
MTRIX1 1 -0.371500 -0.359860 -0.855860 66.52913 1
MTRIX2 1 -0.375820 -0.784640 0.493050 68.79607 1
MTRIX3 1 -0.848970 0.504820 0.156250 19.14160 1
(ATOM LINES ARE NOT SHOWN.)
END
