HEADER SUGAR BINDING PROTEIN 09-FEB-15 4Y20
TITLE COMPLEX OF HUMAN GALECTIN-1 AND NEUACALPHA2-3GALBETA1-4GLC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALECTIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GAL-1,14 KDA LAMININ-BINDING PROTEIN,HLBP14,14 KDA LECTIN,
COMPND 5 BETA-GALACTOSIDE-BINDING LECTIN L-14-I,GALAPTIN,HBL,HPL,LACTOSE-
COMPND 6 BINDING LECTIN 1,LECTIN GALACTOSIDE-BINDING SOLUBLE 1,PUTATIVE MAPK-
COMPND 7 ACTIVATING PROTEIN PM12,S-LAC LECTIN 1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: GALECTIN-1;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: GAL-1,14 KDA LAMININ-BINDING PROTEIN,HLBP14,14 KDA LECTIN,
COMPND 13 BETA-GALACTOSIDE-BINDING LECTIN L-14-I,GALAPTIN,HBL,HPL,LACTOSE-
COMPND 14 BINDING LECTIN 1,LECTIN GALACTOSIDE-BINDING SOLUBLE 1,PUTATIVE MAPK-
COMPND 15 ACTIVATING PROTEIN PM12,S-LAC LECTIN 1;
COMPND 16 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: LGALS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: LGALS1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS COMPLEX, GALECTIN-1, LECTIN, NEUACALPHA2-3GALBETA1-4GLC, SUGAR
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.Y.LIN,T.J.HSIEH,C.H.LIN
REVDAT 2 29-JUL-20 4Y20 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 HETSYN FORMUL LINK SITE
REVDAT 2 3 1 ATOM
REVDAT 1 06-APR-16 4Y20 0
JRNL AUTH H.Y.LIN,T.J.HSIEH,Z.TU,B.S.HUANG,S.C.WU,C.T.CHIEN,S.T.HSU,
JRNL AUTH 2 C.H.LIN
JRNL TITL STRUCTURAL BASIS OF HUMAN GALECTIN-1 INHIBITION WITH KI
JRNL TITL 2 VALUES IN THE MICRO- TO NANOMOLAR RANGE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 14012
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1404
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 25.8726 - 4.7391 1.00 1430 158 0.1998 0.2112
REMARK 3 2 4.7391 - 3.7653 0.99 1357 150 0.1649 0.1941
REMARK 3 3 3.7653 - 3.2904 1.00 1318 148 0.1976 0.2439
REMARK 3 4 3.2904 - 2.9900 0.99 1335 147 0.2305 0.2792
REMARK 3 5 2.9900 - 2.7760 0.98 1287 141 0.2319 0.2813
REMARK 3 6 2.7760 - 2.6125 0.95 1258 141 0.2257 0.2756
REMARK 3 7 2.6125 - 2.4818 0.93 1230 136 0.2382 0.3280
REMARK 3 8 2.4818 - 2.3738 0.90 1169 131 0.2499 0.2888
REMARK 3 9 2.3738 - 2.2825 0.88 1144 129 0.2349 0.2737
REMARK 3 10 2.2825 - 2.2038 0.83 1080 123 0.2503 0.3039
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 2181
REMARK 3 ANGLE : 0.693 2963
REMARK 3 CHIRALITY : 0.032 306
REMARK 3 PLANARITY : 0.004 386
REMARK 3 DIHEDRAL : 17.566 909
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9706 -6.7375 -12.8160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0906 T22: 0.1792
REMARK 3 T33: 0.1350 T12: 0.0034
REMARK 3 T13: 0.0013 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.1752 L22: 3.9357
REMARK 3 L33: 1.3803 L12: -0.1271
REMARK 3 L13: 0.2799 L23: 0.5630
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: 0.0232 S13: -0.0249
REMARK 3 S21: 0.0048 S22: -0.0049 S23: -0.0717
REMARK 3 S31: 0.0680 S32: 0.0229 S33: -0.0128
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Y20 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97622
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14339
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.20300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS (PH 8.0), 0.2 M LI2SO4, 30%
REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 21.47100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.98450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.17250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.98450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.47100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.17250
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 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 ASN A 50 79.18 -161.32
REMARK 500 PRO A 78 33.88 -90.14
REMARK 500 ASN B 50 73.06 -158.85
REMARK 500 PRO B 78 40.37 -83.63
REMARK 500 ASP B 92 -166.17 -127.64
REMARK 500 ASP B 102 63.18 -118.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y1V RELATED DB: PDB
REMARK 900 RELATED ID: 4Y1U RELATED DB: PDB
REMARK 900 RELATED ID: 4Y1X RELATED DB: PDB
REMARK 900 RELATED ID: 4Y1Y RELATED DB: PDB
REMARK 900 RELATED ID: 4Y1Z RELATED DB: PDB
REMARK 900 RELATED ID: 4Y22 RELATED DB: PDB
REMARK 900 RELATED ID: 4Y24 RELATED DB: PDB
REMARK 900 RELATED ID: 4Y26 RELATED DB: PDB
DBREF 4Y20 A 2 134 UNP P09382 LEG1_HUMAN 3 135
DBREF 4Y20 B 2 134 UNP P09382 LEG1_HUMAN 3 135
SEQADV 4Y20 MET A -19 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY A -18 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER A -17 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER A -16 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -15 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -14 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -13 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -12 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -11 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A -10 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER A -9 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER A -8 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY A -7 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 LEU A -6 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 VAL A -5 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 PRO A -4 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 ARG A -3 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY A -2 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER A -1 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS A 0 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 MET A 1 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 MET B -19 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY B -18 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER B -17 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER B -16 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -15 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -14 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -13 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -12 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -11 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B -10 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER B -9 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER B -8 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY B -7 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 LEU B -6 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 VAL B -5 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 PRO B -4 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 ARG B -3 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 GLY B -2 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 SER B -1 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 HIS B 0 UNP P09382 EXPRESSION TAG
SEQADV 4Y20 MET B 1 UNP P09382 EXPRESSION TAG
SEQRES 1 A 154 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 154 LEU VAL PRO ARG GLY SER HIS MET CYS GLY LEU VAL ALA
SEQRES 3 A 154 SER ASN LEU ASN LEU LYS PRO GLY GLU CYS LEU ARG VAL
SEQRES 4 A 154 ARG GLY GLU VAL ALA PRO ASP ALA LYS SER PHE VAL LEU
SEQRES 5 A 154 ASN LEU GLY LYS ASP SER ASN ASN LEU CSO LEU HIS PHE
SEQRES 6 A 154 ASN PRO ARG PHE ASN ALA HIS GLY ASP ALA ASN THR ILE
SEQRES 7 A 154 VAL CSO ASN SER LYS ASP GLY GLY ALA TRP GLY THR GLU
SEQRES 8 A 154 GLN ARG GLU ALA VAL PHE PRO PHE GLN PRO GLY SER VAL
SEQRES 9 A 154 ALA GLU VAL CSO ILE THR PHE ASP GLN ALA ASN LEU THR
SEQRES 10 A 154 VAL LYS LEU PRO ASP GLY TYR GLU PHE LYS PHE PRO ASN
SEQRES 11 A 154 ARG LEU ASN LEU GLU ALA ILE ASN TYR MET ALA ALA ASP
SEQRES 12 A 154 GLY ASP PHE LYS ILE LYS CSO VAL ALA PHE ASP
SEQRES 1 B 154 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 154 LEU VAL PRO ARG GLY SER HIS MET CYS GLY LEU VAL ALA
SEQRES 3 B 154 SER ASN LEU ASN LEU LYS PRO GLY GLU CSO LEU ARG VAL
SEQRES 4 B 154 ARG GLY GLU VAL ALA PRO ASP ALA LYS SER PHE VAL LEU
SEQRES 5 B 154 ASN LEU GLY LYS ASP SER ASN ASN LEU CSO LEU HIS PHE
SEQRES 6 B 154 ASN PRO ARG PHE ASN ALA HIS GLY ASP ALA ASN THR ILE
SEQRES 7 B 154 VAL CSO ASN SER LYS ASP GLY GLY ALA TRP GLY THR GLU
SEQRES 8 B 154 GLN ARG GLU ALA VAL PHE PRO PHE GLN PRO GLY SER VAL
SEQRES 9 B 154 ALA GLU VAL CSO ILE THR PHE ASP GLN ALA ASN LEU THR
SEQRES 10 B 154 VAL LYS LEU PRO ASP GLY TYR GLU PHE LYS PHE PRO ASN
SEQRES 11 B 154 ARG LEU ASN LEU GLU ALA ILE ASN TYR MET ALA ALA ASP
SEQRES 12 B 154 GLY ASP PHE LYS ILE LYS CSO VAL ALA PHE ASP
MODRES 4Y20 CSO A 42 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO A 60 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO A 88 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO A 130 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO B 16 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO B 42 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO B 60 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO B 88 CYS MODIFIED RESIDUE
MODRES 4Y20 CSO B 130 CYS MODIFIED RESIDUE
HET CSO A 42 7
HET CSO A 60 7
HET CSO A 88 7
HET CSO A 130 7
HET CSO B 16 7
HET CSO B 42 7
HET CSO B 60 7
HET CSO B 88 7
HET CSO B 130 7
HET GLC C 1 12
HET GAL C 2 11
HET SIA C 3 20
HET GLC D 1 12
HET GAL D 2 11
HET SIA D 3 20
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
FORMUL 1 CSO 9(C3 H7 N O3 S)
FORMUL 3 GLC 2(C6 H12 O6)
FORMUL 3 GAL 2(C6 H12 O6)
FORMUL 3 SIA 2(C11 H19 N O9)
FORMUL 5 HOH *49(H2 O)
SHEET 1 AA112 ALA A 67 TRP A 68 0
SHEET 2 AA112 ASP A 54 ASP A 64 -1 N ASP A 64 O ALA A 67
SHEET 3 AA112 ASN A 40 ALA A 51 -1 N ARG A 48 O THR A 57
SHEET 4 AA112 PHE A 30 ASP A 37 -1 N LEU A 34 O LEU A 43
SHEET 5 AA112 ILE A 117 GLY A 124 -1 O ALA A 121 N ASN A 33
SHEET 6 AA112 VAL A 5 LEU A 11 -1 N ALA A 6 O MET A 120
SHEET 7 AA112 VAL B 5 LEU B 11 -1 O SER B 7 N VAL A 5
SHEET 8 AA112 ILE B 117 GLY B 124 -1 O MET B 120 N ALA B 6
SHEET 9 AA112 PHE B 30 ASP B 37 -1 N ASN B 33 O ALA B 121
SHEET 10 AA112 ASN B 40 ALA B 51 -1 O ASN B 40 N LYS B 36
SHEET 11 AA112 ASP B 54 ASP B 64 -1 O THR B 57 N ARG B 48
SHEET 12 AA112 ALA B 67 TRP B 68 -1 O ALA B 67 N ASP B 64
SHEET 1 AA212 GLN A 72 GLU A 74 0
SHEET 2 AA212 ASP A 54 ASP A 64 -1 N CSO A 60 O GLN A 72
SHEET 3 AA212 ASN A 40 ALA A 51 -1 N ARG A 48 O THR A 57
SHEET 4 AA212 PHE A 30 ASP A 37 -1 N LEU A 34 O LEU A 43
SHEET 5 AA212 ILE A 117 GLY A 124 -1 O ALA A 121 N ASN A 33
SHEET 6 AA212 VAL A 5 LEU A 11 -1 N ALA A 6 O MET A 120
SHEET 7 AA212 VAL B 5 LEU B 11 -1 O SER B 7 N VAL A 5
SHEET 8 AA212 ILE B 117 GLY B 124 -1 O MET B 120 N ALA B 6
SHEET 9 AA212 PHE B 30 ASP B 37 -1 N ASN B 33 O ALA B 121
SHEET 10 AA212 ASN B 40 ALA B 51 -1 O ASN B 40 N LYS B 36
SHEET 11 AA212 ASP B 54 ASP B 64 -1 O THR B 57 N ARG B 48
SHEET 12 AA212 GLN B 72 GLU B 74 -1 O GLN B 72 N CSO B 60
SHEET 1 AA310 GLU A 105 PRO A 109 0
SHEET 2 AA310 ASN A 95 LYS A 99 -1 N LEU A 96 O PHE A 108
SHEET 3 AA310 SER A 83 PHE A 91 -1 N CSO A 88 O LYS A 99
SHEET 4 AA310 CYS A 16 VAL A 23 -1 N VAL A 23 O SER A 83
SHEET 5 AA310 PHE A 126 ASP A 134 -1 O ASP A 134 N CYS A 16
SHEET 6 AA310 PHE B 126 PHE B 133 -1 O LYS B 129 N PHE A 133
SHEET 7 AA310 LEU B 17 VAL B 23 -1 N ARG B 20 O LYS B 129
SHEET 8 AA310 VAL B 84 PHE B 91 -1 O VAL B 87 N VAL B 19
SHEET 9 AA310 ASN B 95 LYS B 99 -1 O LYS B 99 N CSO B 88
SHEET 10 AA310 GLU B 105 PRO B 109 -1 O PHE B 108 N LEU B 96
LINK C LEU A 41 N CSO A 42 1555 1555 1.33
LINK C CSO A 42 N LEU A 43 1555 1555 1.33
LINK C VAL A 59 N CSO A 60 1555 1555 1.33
LINK C CSO A 60 N ASN A 61 1555 1555 1.33
LINK C VAL A 87 N CSO A 88 1555 1555 1.33
LINK C CSO A 88 N ILE A 89 1555 1555 1.33
LINK C LYS A 129 N CSO A 130 1555 1555 1.33
LINK C CSO A 130 N VAL A 131 1555 1555 1.33
LINK C GLU B 15 N CSO B 16 1555 1555 1.33
LINK C CSO B 16 N LEU B 17 1555 1555 1.33
LINK C LEU B 41 N CSO B 42 1555 1555 1.33
LINK C CSO B 42 N LEU B 43 1555 1555 1.33
LINK C VAL B 59 N CSO B 60 1555 1555 1.33
LINK C CSO B 60 N ASN B 61 1555 1555 1.33
LINK C VAL B 87 N CSO B 88 1555 1555 1.33
LINK C CSO B 88 N ILE B 89 1555 1555 1.33
LINK C LYS B 129 N CSO B 130 1555 1555 1.33
LINK C CSO B 130 N VAL B 131 1555 1555 1.33
LINK O4 GLC C 1 C1 GAL C 2 1555 1555 1.44
LINK O3 GAL C 2 C2 SIA C 3 1555 1555 1.46
LINK O4 GLC D 1 C1 GAL D 2 1555 1555 1.41
LINK O3 GAL D 2 C2 SIA D 3 1555 1555 1.42
CRYST1 42.942 58.345 111.969 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 0.023287 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008931 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
