HEADER SUGAR BINDING PROTEIN 13-MAR-17 5NF9
TITLE STRUCTURE OF GALECTIN-3 CRD IN COMPLEX WITH COMPOUND 2
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GALECTIN-3 CRD, CATION-PI INTERACTIONS, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.RONIN,C.ATMANENE,F.M.GAUTIER,F.DJEDAINI PILARD,S.TELETCHEA,
AUTHOR 2 F.CIESIELSKI,V.VIVAT HANNAH,C.GRANDJEAN
REVDAT 2 17-JAN-24 5NF9 1 REMARK
REVDAT 1 21-JUN-17 5NF9 0
JRNL AUTH C.ATMANENE,C.RONIN,S.TELETCHEA,F.M.GAUTIER,
JRNL AUTH 2 F.DJEDAINI-PILARD,F.CIESIELSKI,V.VIVAT,C.GRANDJEAN
JRNL TITL BIOPHYSICAL AND STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 MONO/DI-ARYLATED LACTOSAMINE DERIVATIVES INTERACTION WITH
JRNL TITL 3 HUMAN GALECTIN-3.
JRNL REF BIOCHEM. BIOPHYS. RES. V. 489 281 2017
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 28554839
JRNL DOI 10.1016/J.BBRC.2017.05.150
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 11078
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) : 0.145
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 584
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) : 1.87
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 780
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.1490
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.69000
REMARK 3 B22 (A**2) : -1.07000
REMARK 3 B33 (A**2) : -0.62000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.582
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1217 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1177 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1662 ; 1.959 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2705 ; 0.872 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 7.392 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ;36.360 ;23.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 200 ;13.188 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.517 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 187 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1382 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 300 ; 0.003 ; 0.020
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): 568 ; 1.756 ; 1.790
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 567 ; 1.731 ; 1.787
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 712 ; 2.470 ; 2.669
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 713 ; 2.477 ; 2.672
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 649 ; 3.246 ; 2.253
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 649 ; 3.246 ; 2.253
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 947 ; 4.944 ; 3.235
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1245 ; 6.318 ;15.463
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1216 ; 6.242 ;15.139
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5NF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11662
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14400
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
REMARK 200 STARTING MODEL: 3ZSL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS HCL PH7.5; 30-34% PEG4000;
REMARK 280 100MM MGCL2; 400MM NASCN; 8MM BETA-MERCAPTOETHANOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 18.43500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.49000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.49000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.43500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.97500
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: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 GLY A 104
REMARK 465 SER A 105
REMARK 465 PRO A 106
REMARK 465 TYR A 107
REMARK 465 GLY A 108
REMARK 465 ALA A 109
REMARK 465 PRO A 110
REMARK 465 ALA A 111
REMARK 465 GLY A 112
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 -1.91 90.73
REMARK 500 ASN A 141 51.10 -115.44
REMARK 500 ASN A 164 74.67 -153.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VW A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5NF7 RELATED DB: PDB
REMARK 900 SAME PROJECT : SAME PROTEIN WITH ANOTHER COMPOUND OF THE SAME SERIES
DBREF 5NF9 A 106 250 UNP P17931 LEG3_HUMAN 106 250
SEQADV 5NF9 GLY A 104 UNP P17931 EXPRESSION TAG
SEQADV 5NF9 SER A 105 UNP P17931 EXPRESSION TAG
SEQRES 1 A 147 GLY SER PRO TYR GLY ALA PRO ALA GLY PRO LEU ILE VAL
SEQRES 2 A 147 PRO TYR ASN LEU PRO LEU PRO GLY GLY VAL VAL PRO ARG
SEQRES 3 A 147 MET LEU ILE THR ILE LEU GLY THR VAL LYS PRO ASN ALA
SEQRES 4 A 147 ASN ARG ILE ALA LEU ASP PHE GLN ARG GLY ASN ASP VAL
SEQRES 5 A 147 ALA PHE HIS PHE ASN PRO ARG PHE ASN GLU ASN ASN ARG
SEQRES 6 A 147 ARG VAL ILE VAL CYS ASN THR LYS LEU ASP ASN ASN TRP
SEQRES 7 A 147 GLY ARG GLU GLU ARG GLN SER VAL PHE PRO PHE GLU SER
SEQRES 8 A 147 GLY LYS PRO PHE LYS ILE GLN VAL LEU VAL GLU PRO ASP
SEQRES 9 A 147 HIS PHE LYS VAL ALA VAL ASN ASP ALA HIS LEU LEU GLN
SEQRES 10 A 147 TYR ASN HIS ARG VAL LYS LYS LEU ASN GLU ILE SER LYS
SEQRES 11 A 147 LEU GLY ILE SER GLY ASP ILE ASP LEU THR SER ALA SER
SEQRES 12 A 147 TYR THR MET ILE
HET 8VW A 301 36
HETNAM 8VW ~{N}-[(2~{R},3~{R},4~{R},5~{S},6~{R})-2-ACETAMIDO-6-
HETNAM 2 8VW (HYDROXYMETHYL)-5-[(2~{S},3~{R},4~{S},5~{R},6~{R})-6-
HETNAM 3 8VW (HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]OXY-4-
HETNAM 4 8VW OXIDANYL-OXAN-3-YL]-3-METHOXY-BENZAMIDE
FORMUL 2 8VW C22 H32 N2 O12
FORMUL 3 HOH *102(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 GLN A 201 O ALA A 212
SHEET 4 AA3 5 MET A 130 VAL A 138 -1 N GLY A 136 O PHE A 198
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 3.60
SITE 1 AC1 10 ILE A 115 HIS A 158 ASN A 160 ARG A 162
SITE 2 AC1 10 GLU A 165 ASN A 174 GLU A 184 ARG A 186
SITE 3 AC1 10 HOH A 441 HOH A 477
CRYST1 36.870 57.950 62.980 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 0.027122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015878 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
