HEADER SUGAR BINDING PROTEIN 01-FEB-19 6QLS
TITLE GALECTIN-3C IN COMPLEX WITH FLUOROARYLTRIAZOLE MONOTHIOGALACTOSIDE
TITLE 2 DERIVATIVE 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GALECTIN-3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GAL-3,35 KDA LECTIN,CARBOHYDRATE-BINDING PROTEIN 35,CBP 35,
COMPND 5 GALACTOSE-SPECIFIC LECTIN 3,GALACTOSIDE-BINDING PROTEIN,GALBP,IGE-
COMPND 6 BINDING PROTEIN,L-31,LAMININ-BINDING PROTEIN,LECTIN L-29,MAC-2
COMPND 7 ANTIGEN;
COMPND 8 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 BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS LECTIN, CARBOHYDRATE-BINDING PROTEIN, GALACTOSE-SPECIFIC LECTIN 3,
KEYWDS 2 GALACTOSIDE-BINDING PROTEIN, GALBP, IGE-6 BINDING PROTEIN, L-31,
KEYWDS 3 LAMININ-BINDING PROTEIN, LECTIN L-29, MAC-2, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.KUMAR,K.PETERSON,U.J.NILSSON,D.T.LOGAN
REVDAT 3 24-JAN-24 6QLS 1 REMARK
REVDAT 2 28-AUG-19 6QLS 1 JRNL
REVDAT 1 10-JUL-19 6QLS 0
JRNL AUTH R.KUMAR,M.M.IGNJATOVIC,K.PETERSON,M.OLSSON,H.LEFFLER,U.RYDE,
JRNL AUTH 2 U.J.NILSSON,D.T.LOGAN
JRNL TITL STRUCTURE AND ENERGETICS OF LIGAND-FLUORINE INTERACTIONS
JRNL TITL 2 WITH GALECTIN-3 BACKBONE AND SIDE-CHAIN AMIDES: INSIGHT INTO
JRNL TITL 3 SOLVATION EFFECTS AND MULTIPOLAR INTERACTIONS.
JRNL REF CHEMMEDCHEM V. 14 1528 2019
JRNL REFN ESSN 1860-7187
JRNL PMID 31246331
JRNL DOI 10.1002/CMDC.201900293
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3084: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 63982
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 3304
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 22.8497 - 3.0168 1.00 2760 127 0.1322 0.1279
REMARK 3 2 3.0168 - 2.3953 1.00 2660 119 0.1368 0.1555
REMARK 3 3 2.3953 - 2.0928 1.00 2571 154 0.1177 0.1467
REMARK 3 4 2.0928 - 1.9015 1.00 2597 132 0.1109 0.1371
REMARK 3 5 1.9015 - 1.7653 1.00 2550 141 0.1122 0.1353
REMARK 3 6 1.7653 - 1.6613 1.00 2551 139 0.1137 0.1589
REMARK 3 7 1.6613 - 1.5781 1.00 2553 152 0.1144 0.1461
REMARK 3 8 1.5781 - 1.5094 1.00 2546 125 0.1137 0.1681
REMARK 3 9 1.5094 - 1.4513 1.00 2553 131 0.1216 0.1681
REMARK 3 10 1.4513 - 1.4012 1.00 2526 131 0.1328 0.1590
REMARK 3 11 1.4012 - 1.3574 1.00 2516 156 0.1439 0.1740
REMARK 3 12 1.3574 - 1.3186 1.00 2516 154 0.1509 0.1844
REMARK 3 13 1.3186 - 1.2839 1.00 2494 155 0.1473 0.1784
REMARK 3 14 1.2839 - 1.2526 1.00 2514 127 0.1494 0.1738
REMARK 3 15 1.2526 - 1.2241 0.99 2531 149 0.1593 0.1907
REMARK 3 16 1.2241 - 1.1981 1.00 2505 139 0.1619 0.1892
REMARK 3 17 1.1981 - 1.1741 1.00 2527 120 0.1669 0.1837
REMARK 3 18 1.1741 - 1.1520 1.00 2500 146 0.1760 0.2160
REMARK 3 19 1.1520 - 1.1314 1.00 2521 137 0.1866 0.2137
REMARK 3 20 1.1314 - 1.1122 1.00 2519 127 0.1941 0.2182
REMARK 3 21 1.1122 - 1.0943 1.00 2498 156 0.2077 0.2204
REMARK 3 22 1.0943 - 1.0774 1.00 2464 154 0.2279 0.2496
REMARK 3 23 1.0774 - 1.0616 1.00 2493 130 0.2536 0.2845
REMARK 3 24 1.0616 - 1.0466 0.87 2213 103 0.2993 0.2950
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.012 1284
REMARK 3 ANGLE : 1.336 1765
REMARK 3 CHIRALITY : 0.106 200
REMARK 3 PLANARITY : 0.009 231
REMARK 3 DIHEDRAL : 12.450 502
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6QLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1200013016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.635784
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64101
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.047
REMARK 200 RESOLUTION RANGE LOW (A) : 22.844
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.09139
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.21800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3ZSL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1 M TRIS/HCL PH 7.5,
REMARK 280 0.1 M MGCL2, 0.4 M NASCN, 7.9 MM BETA-MERCAPTOETHANOL, VAPOR
REMARK 280 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 18.24050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.56400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.56400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.24050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.30000
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 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO A 113 CG CD
REMARK 470 LYS A 139 NZ
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 O GLN A 187 O HOH A 401 2.16
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 A 183 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 183 NE - CZ - NH2 ANGL. DEV. = -4.2 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 ARG A 129 -2.16 87.79
REMARK 500 ASN A 164 68.24 -155.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 675 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 676 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 677 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 678 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 679 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A 680 DISTANCE = 7.40 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HRK A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
DBREF 6QLS A 113 250 UNP P17931 LEG3_HUMAN 113 250
SEQRES 1 A 138 PRO LEU ILE VAL PRO TYR ASN LEU PRO LEU PRO GLY GLY
SEQRES 2 A 138 VAL VAL PRO ARG MET LEU ILE THR ILE LEU GLY THR VAL
SEQRES 3 A 138 LYS PRO ASN ALA ASN ARG ILE ALA LEU ASP PHE GLN ARG
SEQRES 4 A 138 GLY ASN ASP VAL ALA PHE HIS PHE ASN PRO ARG PHE ASN
SEQRES 5 A 138 GLU ASN ASN ARG ARG VAL ILE VAL CYS ASN THR LYS LEU
SEQRES 6 A 138 ASP ASN ASN TRP GLY ARG GLU GLU ARG GLN SER VAL PHE
SEQRES 7 A 138 PRO PHE GLU SER GLY LYS PRO PHE LYS ILE GLN VAL LEU
SEQRES 8 A 138 VAL GLU PRO ASP HIS PHE LYS VAL ALA VAL ASN ASP ALA
SEQRES 9 A 138 HIS LEU LEU GLN TYR ASN HIS ARG VAL LYS LYS LEU ASN
SEQRES 10 A 138 GLU ILE SER LYS LEU GLY ILE SER GLY ASP ILE ASP LEU
SEQRES 11 A 138 THR SER ALA SER TYR THR MET ILE
HET HRK A 301 60
HET CL A 302 1
HETNAM HRK (2~{R},3~{S},4~{S},5~{R},6~{S})-2-(HYDROXYMETHYL)-6-
HETNAM 2 HRK [(2~{S},3~{R},4~{S},5~{R},6~{R})-6-(HYDROXYMETHYL)-3,
HETNAM 3 HRK 5-BIS(OXIDANYL)-4-(4-PHENYL-1,2,3-TRIAZOL-1-YL)OXAN-2-
HETNAM 4 HRK YL]SULFANYL-OXANE-3,4,5-TRIOL
HETNAM CL CHLORIDE ION
FORMUL 2 HRK C20 H27 N3 O9 S
FORMUL 3 CL CL 1-
FORMUL 4 HOH *280(H2 O)
HELIX 1 AA1 LYS A 227 ILE A 231 5 5
SHEET 1 AA1 6 TYR A 118 PRO A 121 0
SHEET 2 AA1 6 LYS A 233 GLY A 238 -1 O LEU A 234 N LEU A 120
SHEET 3 AA1 6 ILE A 145 ARG A 151 -1 N GLN A 150 O LYS A 233
SHEET 4 AA1 6 ASP A 154 GLU A 165 -1 O PHE A 157 N PHE A 149
SHEET 5 AA1 6 ARG A 168 LEU A 177 -1 O VAL A 170 N ARG A 162
SHEET 6 AA1 6 ASN A 180 TRP A 181 -1 O ASN A 180 N LEU A 177
SHEET 1 AA2 6 TYR A 118 PRO A 121 0
SHEET 2 AA2 6 LYS A 233 GLY A 238 -1 O LEU A 234 N LEU A 120
SHEET 3 AA2 6 ILE A 145 ARG A 151 -1 N GLN A 150 O LYS A 233
SHEET 4 AA2 6 ASP A 154 GLU A 165 -1 O PHE A 157 N PHE A 149
SHEET 5 AA2 6 ARG A 168 LEU A 177 -1 O VAL A 170 N ARG A 162
SHEET 6 AA2 6 GLU A 185 GLN A 187 -1 O GLU A 185 N CYS A 173
SHEET 1 AA3 5 ALA A 216 ASN A 222 0
SHEET 2 AA3 5 HIS A 208 VAL A 213 -1 N VAL A 211 O LEU A 218
SHEET 3 AA3 5 PRO A 197 VAL A 204 -1 N LEU A 203 O LYS A 210
SHEET 4 AA3 5 MET A 130 VAL A 138 -1 N ILE A 132 O VAL A 202
SHEET 5 AA3 5 ILE A 240 MET A 249 -1 O THR A 248 N LEU A 131
CISPEP 1 VAL A 116 PRO A 117 0 0.13
CISPEP 2 VAL A 116 PRO A 117 0 0.33
SITE 1 AC1 21 ARG A 144 ALA A 146 HIS A 158 ASN A 160
SITE 2 AC1 21 ARG A 162 ASN A 174 GLU A 184 ARG A 186
SITE 3 AC1 21 SER A 237 HOH A 419 HOH A 430 HOH A 444
SITE 4 AC1 21 HOH A 456 HOH A 473 HOH A 488 HOH A 504
SITE 5 AC1 21 HOH A 505 HOH A 521 HOH A 524 HOH A 544
SITE 6 AC1 21 HOH A 564
SITE 1 AC2 3 ASN A 160 ARG A 162 HOH A 466
CRYST1 36.481 58.600 63.128 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 0.027412 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
