HEADER SIGNALING PROTEIN 04-MAY-16 5JPV
TITLE EFFICIENT TARGETING OF THE ASIALOGLYCOPROTEIN RECEPTOR BY POLYVALENT
TITLE 2 DISPLAY OF A COMPACT GALACTOSEAMINE MIMIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASIALOGLYCOPROTEIN RECEPTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ASGPR 1,C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER H1,HEPATIC
COMPND 5 LECTIN H1,HL-1;
COMPND 6 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: ASGR1, CLEC4H1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 7 PPPARG4;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 1182032
KEYWDS ASIALOGLYCOPROTEIN RECEPTOR, CARBOHYDRATES, LIVER TARGETING,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LIU
REVDAT 3 27-SEP-23 5JPV 1 HETSYN
REVDAT 2 29-JUL-20 5JPV 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 FORMUL LINK SITE ATOM
REVDAT 1 14-JUN-17 5JPV 0
JRNL AUTH C.A.SANHUEZA,M.M.BAKSH,B.THUMA,M.D.ROY,S.DUTTA,C.PREVILLE,
JRNL AUTH 2 B.A.CHRUNYK,K.BEAUMONT,R.DULLEA,M.AMMIRATI,S.LIU,D.GEBHARD,
JRNL AUTH 3 J.E.FINLEY,C.T.SALATTO,A.KING-AHMAD,I.STOCK,K.ATKINSON,
JRNL AUTH 4 B.REIDICH,W.LIN,R.KUMAR,M.TU,E.MENHAJI-KLOTZ,D.A.PRICE,
JRNL AUTH 5 S.LIRAS,M.G.FINN,V.MASCITTI
JRNL TITL EFFICIENT LIVER TARGETING BY POLYVALENT DISPLAY OF A COMPACT
JRNL TITL 2 LIGAND FOR THE ASIALOGLYCOPROTEIN RECEPTOR.
JRNL REF J. AM. CHEM. SOC. V. 139 3528 2017
JRNL REFN ESSN 1520-5126
JRNL PMID 28230359
JRNL DOI 10.1021/JACS.6B12964
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 24043
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1251
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1736
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2142
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.06000
REMARK 3 B22 (A**2) : 1.32000
REMARK 3 B33 (A**2) : -0.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.957
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2284 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3132 ; 1.142 ; 1.903
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 254 ; 5.933 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;34.190 ;23.971
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 308 ;14.613 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;14.132 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 296 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1854 ; 0.004 ; 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): 1268 ; 0.585 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2034 ; 1.153 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1016 ; 1.631 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1098 ; 2.659 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-10
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 : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25588
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 96.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 1DV8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CACODYLATE, PH=6.8-7.4, 0.1
REMARK 280 -0.2M (NH4)2SO4,14-20% PEG 8000, 2% MPD, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.89250
REMARK 290 SMTRY3 2 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: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
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 146
REMARK 465 GLY A 147
REMARK 465 SER A 148
REMARK 465 GLU A 149
REMARK 465 ARG A 150
REMARK 465 THR A 151
REMARK 465 CYS A 152
REMARK 465 ASP A 281
REMARK 465 LYS A 282
REMARK 465 ALA A 283
REMARK 465 SER A 284
REMARK 465 GLN A 285
REMARK 465 GLU A 286
REMARK 465 PRO A 287
REMARK 465 PRO A 288
REMARK 465 LEU A 289
REMARK 465 LEU A 290
REMARK 465 MET B 146
REMARK 465 GLY B 147
REMARK 465 SER B 148
REMARK 465 GLU B 149
REMARK 465 ARG B 150
REMARK 465 THR B 151
REMARK 465 CYS B 152
REMARK 465 ASP B 281
REMARK 465 LYS B 282
REMARK 465 ALA B 283
REMARK 465 SER B 284
REMARK 465 GLN B 285
REMARK 465 GLU B 286
REMARK 465 PRO B 287
REMARK 465 PRO B 288
REMARK 465 LEU B 289
REMARK 465 LEU B 290
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 195 OD2 ASP B 185 2655 2.10
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 ASN A 234 46.30 -144.03
REMARK 500 ASN B 156 -3.13 81.59
REMARK 500 ALA B 186 -169.26 -126.46
REMARK 500 ASN B 234 45.22 -150.77
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 B 534 DISTANCE = 6.37 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 190 O
REMARK 620 2 GLU A 196 OE1 84.9
REMARK 620 3 GLU A 196 OE2 74.6 46.7
REMARK 620 4 GLU A 277 OE1 81.7 93.3 134.2
REMARK 620 5 GLU A 277 OE2 130.0 85.6 127.4 50.1
REMARK 620 6 HOH A 428 O 84.7 122.2 75.8 140.5 139.7
REMARK 620 7 HOH A 448 O 103.1 160.8 152.1 71.0 75.9 76.4
REMARK 620 8 HOH A 493 O 151.5 88.0 80.4 126.4 76.7 76.0 92.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 215 OD1
REMARK 620 2 ASP A 215 OD2 48.0
REMARK 620 3 ASP A 242 OD1 161.7 149.5
REMARK 620 4 GLU A 252 O 88.7 127.7 78.8
REMARK 620 5 ASP A 253 OD1 75.2 113.0 88.0 71.2
REMARK 620 6 HOH A 441 O 97.8 85.2 91.0 71.8 142.5
REMARK 620 7 HOH A 488 O 117.5 69.6 80.3 139.9 141.5 74.7
REMARK 620 8 HOH A 497 O 95.6 78.1 86.9 143.6 75.0 142.4 68.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 239 OE1
REMARK 620 2 ASP A 241 OD1 73.8
REMARK 620 3 GLU A 252 OE2 151.7 78.0
REMARK 620 4 ASN A 264 OD1 66.7 140.5 141.4
REMARK 620 5 ASP A 265 O 131.6 137.3 70.7 74.4
REMARK 620 6 ASP A 265 OD1 77.4 81.3 96.6 89.4 74.4
REMARK 620 7 GAL C 2 O3 122.2 127.6 77.3 77.1 72.9 146.9
REMARK 620 8 GAL C 2 O4 75.8 72.8 97.8 97.5 138.7 146.8 65.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 190 O
REMARK 620 2 GLU B 196 OE1 82.5
REMARK 620 3 GLU B 196 OE2 72.3 47.1
REMARK 620 4 GLU B 277 OE1 79.9 90.7 131.1
REMARK 620 5 GLU B 277 OE2 127.9 83.4 126.4 50.4
REMARK 620 6 HOH B 421 O 80.2 125.1 78.0 135.7 145.0
REMARK 620 7 HOH B 485 O 105.4 162.6 149.8 75.9 79.5 72.0
REMARK 620 8 HOH B 505 O 145.4 87.6 76.7 133.5 83.3 78.8 93.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 215 OD1
REMARK 620 2 ASP B 215 OD2 49.2
REMARK 620 3 ASP B 242 OD1 159.6 149.9
REMARK 620 4 GLU B 252 O 91.5 125.6 78.1
REMARK 620 5 ASP B 253 OD1 72.6 115.0 87.6 74.1
REMARK 620 6 HOH B 434 O 102.7 84.0 89.8 68.2 142.0
REMARK 620 7 HOH B 497 O 94.3 82.5 84.9 145.1 74.9 142.6
REMARK 620 8 HOH B 500 O 120.6 71.7 78.3 133.9 143.1 72.6 70.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 239 OE1
REMARK 620 2 ASP B 241 OD1 73.1
REMARK 620 3 GLU B 252 OE2 147.6 75.3
REMARK 620 4 ASN B 264 OD1 70.5 143.5 141.1
REMARK 620 5 ASP B 265 O 130.8 136.0 71.1 73.7
REMARK 620 6 ASP B 265 OD1 75.0 81.1 93.4 92.0 73.6
REMARK 620 7 GAL D 2 O3 127.3 126.5 78.3 76.1 72.9 146.3
REMARK 620 8 GAL D 2 O4 79.1 71.8 97.6 98.5 139.4 146.9 66.7
REMARK 620 N 1 2 3 4 5 6 7
DBREF 5JPV A 147 290 UNP P07306 ASGR1_HUMAN 148 291
DBREF 5JPV B 147 290 UNP P07306 ASGR1_HUMAN 148 291
SEQADV 5JPV MET A 146 UNP P07306 EXPRESSION TAG
SEQADV 5JPV MET B 146 UNP P07306 EXPRESSION TAG
SEQRES 1 A 145 MET GLY SER GLU ARG THR CYS CYS PRO VAL ASN TRP VAL
SEQRES 2 A 145 GLU HIS GLU ARG SER CYS TYR TRP PHE SER ARG SER GLY
SEQRES 3 A 145 LYS ALA TRP ALA ASP ALA ASP ASN TYR CYS ARG LEU GLU
SEQRES 4 A 145 ASP ALA HIS LEU VAL VAL VAL THR SER TRP GLU GLU GLN
SEQRES 5 A 145 LYS PHE VAL GLN HIS HIS ILE GLY PRO VAL ASN THR TRP
SEQRES 6 A 145 MET GLY LEU HIS ASP GLN ASN GLY PRO TRP LYS TRP VAL
SEQRES 7 A 145 ASP GLY THR ASP TYR GLU THR GLY PHE LYS ASN TRP ARG
SEQRES 8 A 145 PRO GLU GLN PRO ASP ASP TRP TYR GLY HIS GLY LEU GLY
SEQRES 9 A 145 GLY GLY GLU ASP CYS ALA HIS PHE THR ASP ASP GLY ARG
SEQRES 10 A 145 TRP ASN ASP ASP VAL CYS GLN ARG PRO TYR ARG TRP VAL
SEQRES 11 A 145 CYS GLU THR GLU LEU ASP LYS ALA SER GLN GLU PRO PRO
SEQRES 12 A 145 LEU LEU
SEQRES 1 B 145 MET GLY SER GLU ARG THR CYS CYS PRO VAL ASN TRP VAL
SEQRES 2 B 145 GLU HIS GLU ARG SER CYS TYR TRP PHE SER ARG SER GLY
SEQRES 3 B 145 LYS ALA TRP ALA ASP ALA ASP ASN TYR CYS ARG LEU GLU
SEQRES 4 B 145 ASP ALA HIS LEU VAL VAL VAL THR SER TRP GLU GLU GLN
SEQRES 5 B 145 LYS PHE VAL GLN HIS HIS ILE GLY PRO VAL ASN THR TRP
SEQRES 6 B 145 MET GLY LEU HIS ASP GLN ASN GLY PRO TRP LYS TRP VAL
SEQRES 7 B 145 ASP GLY THR ASP TYR GLU THR GLY PHE LYS ASN TRP ARG
SEQRES 8 B 145 PRO GLU GLN PRO ASP ASP TRP TYR GLY HIS GLY LEU GLY
SEQRES 9 B 145 GLY GLY GLU ASP CYS ALA HIS PHE THR ASP ASP GLY ARG
SEQRES 10 B 145 TRP ASN ASP ASP VAL CYS GLN ARG PRO TYR ARG TRP VAL
SEQRES 11 B 145 CYS GLU THR GLU LEU ASP LYS ALA SER GLN GLU PRO PRO
SEQRES 12 B 145 LEU LEU
HET GLC C 1 12
HET GAL C 2 11
HET GLC D 1 12
HET GAL D 2 11
HET CA A 302 1
HET CA A 303 1
HET CA A 304 1
HET CL A 305 1
HET CA B 302 1
HET CA B 303 1
HET CA B 304 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 3 GLC 2(C6 H12 O6)
FORMUL 3 GAL 2(C6 H12 O6)
FORMUL 5 CA 6(CA 2+)
FORMUL 8 CL CL 1-
FORMUL 12 HOH *276(H2 O)
HELIX 1 AA1 ALA A 173 GLU A 184 1 12
HELIX 2 AA2 SER A 193 GLY A 205 1 13
HELIX 3 AA3 ALA B 173 GLU B 184 1 12
HELIX 4 AA4 SER B 193 GLY B 205 1 13
SHEET 1 AA1 5 VAL A 158 HIS A 160 0
SHEET 2 AA1 5 SER A 163 PHE A 167 -1 O TYR A 165 N VAL A 158
SHEET 3 AA1 5 ARG A 273 GLU A 279 -1 O THR A 278 N CYS A 164
SHEET 4 AA1 5 THR A 209 HIS A 214 1 N TRP A 210 O ARG A 273
SHEET 5 AA1 5 LYS A 221 TRP A 222 -1 O LYS A 221 N HIS A 214
SHEET 1 AA2 5 HIS A 187 LEU A 188 0
SHEET 2 AA2 5 ARG A 273 GLU A 279 -1 O GLU A 277 N HIS A 187
SHEET 3 AA2 5 THR A 209 HIS A 214 1 N TRP A 210 O ARG A 273
SHEET 4 AA2 5 CYS A 254 PHE A 257 -1 O ALA A 255 N LEU A 213
SHEET 5 AA2 5 TRP A 263 ASP A 266 -1 O ASP A 266 N CYS A 254
SHEET 1 AA3 5 VAL B 158 HIS B 160 0
SHEET 2 AA3 5 SER B 163 PHE B 167 -1 O TYR B 165 N VAL B 158
SHEET 3 AA3 5 ARG B 273 GLU B 279 -1 O THR B 278 N CYS B 164
SHEET 4 AA3 5 THR B 209 HIS B 214 1 N TRP B 210 O ARG B 273
SHEET 5 AA3 5 LYS B 221 TRP B 222 -1 O LYS B 221 N HIS B 214
SHEET 1 AA4 5 HIS B 187 LEU B 188 0
SHEET 2 AA4 5 ARG B 273 GLU B 279 -1 O GLU B 277 N HIS B 187
SHEET 3 AA4 5 THR B 209 HIS B 214 1 N TRP B 210 O ARG B 273
SHEET 4 AA4 5 CYS B 254 PHE B 257 -1 O ALA B 255 N LEU B 213
SHEET 5 AA4 5 TRP B 263 ASP B 266 -1 O ASP B 266 N CYS B 254
SSBOND 1 CYS A 153 CYS A 164 1555 1555 2.03
SSBOND 2 CYS A 181 CYS A 276 1555 1555 2.06
SSBOND 3 CYS A 254 CYS A 268 1555 1555 2.04
SSBOND 4 CYS B 153 CYS B 164 1555 1555 2.04
SSBOND 5 CYS B 181 CYS B 276 1555 1555 2.06
SSBOND 6 CYS B 254 CYS B 268 1555 1555 2.03
LINK O4 GLC C 1 C1 GAL C 2 1555 1555 1.43
LINK O4 GLC D 1 C1 GAL D 2 1555 1555 1.43
LINK O VAL A 190 CA CA A 304 1555 1555 2.36
LINK OE1 GLU A 196 CA CA A 304 1555 1555 2.33
LINK OE2 GLU A 196 CA CA A 304 1555 1555 3.01
LINK OD1 ASP A 215 CA CA A 302 1555 1555 2.72
LINK OD2 ASP A 215 CA CA A 302 1555 1555 2.62
LINK OE1 GLN A 239 CA CA A 303 1555 1555 2.59
LINK OD1 ASP A 241 CA CA A 303 1555 1555 2.46
LINK OD1 ASP A 242 CA CA A 302 1555 1555 2.43
LINK O GLU A 252 CA CA A 302 1555 1555 2.43
LINK OE2 GLU A 252 CA CA A 303 1555 1555 2.34
LINK OD1 ASP A 253 CA CA A 302 1555 1555 2.59
LINK OD1 ASN A 264 CA CA A 303 1555 1555 2.50
LINK O ASP A 265 CA CA A 303 1555 1555 2.54
LINK OD1 ASP A 265 CA CA A 303 1555 1555 2.44
LINK OE1 GLU A 277 CA CA A 304 1555 1555 2.70
LINK OE2 GLU A 277 CA CA A 304 1555 1555 2.48
LINK CA CA A 302 O HOH A 441 1555 1555 2.48
LINK CA CA A 302 O HOH A 488 1555 1555 2.61
LINK CA CA A 302 O HOH A 497 1555 1555 2.45
LINK CA CA A 303 O3 GAL C 2 1555 1555 2.57
LINK CA CA A 303 O4 GAL C 2 1555 1555 2.51
LINK CA CA A 304 O HOH A 428 1555 1555 2.33
LINK CA CA A 304 O HOH A 448 1555 1555 2.47
LINK CA CA A 304 O HOH A 493 1555 1555 2.38
LINK O VAL B 190 CA CA B 304 1555 1555 2.34
LINK OE1 GLU B 196 CA CA B 304 1555 1555 2.26
LINK OE2 GLU B 196 CA CA B 304 1555 1555 2.98
LINK OD1 ASP B 215 CA CA B 302 1555 1555 2.67
LINK OD2 ASP B 215 CA CA B 302 1555 1555 2.55
LINK OE1 GLN B 239 CA CA B 303 1555 1555 2.56
LINK OD1 ASP B 241 CA CA B 303 1555 1555 2.50
LINK OD1 ASP B 242 CA CA B 302 1555 1555 2.53
LINK O GLU B 252 CA CA B 302 1555 1555 2.48
LINK OE2 GLU B 252 CA CA B 303 1555 1555 2.36
LINK OD1 ASP B 253 CA CA B 302 1555 1555 2.57
LINK OD1 ASN B 264 CA CA B 303 1555 1555 2.45
LINK O ASP B 265 CA CA B 303 1555 1555 2.51
LINK OD1 ASP B 265 CA CA B 303 1555 1555 2.35
LINK OE1 GLU B 277 CA CA B 304 1555 1555 2.71
LINK OE2 GLU B 277 CA CA B 304 1555 1555 2.37
LINK CA CA B 302 O HOH B 434 1555 1555 2.32
LINK CA CA B 302 O HOH B 497 1555 1555 2.39
LINK CA CA B 302 O HOH B 500 1555 1555 2.67
LINK CA CA B 303 O3 GAL D 2 1555 1555 2.49
LINK CA CA B 303 O4 GAL D 2 1555 1555 2.55
LINK CA CA B 304 O HOH B 421 1555 1555 2.40
LINK CA CA B 304 O HOH B 485 1555 1555 2.32
LINK CA CA B 304 O HOH B 505 1555 1555 2.38
CISPEP 1 GLN A 239 PRO A 240 0 -6.58
CISPEP 2 GLN B 239 PRO B 240 0 -3.45
CRYST1 41.100 59.785 68.818 90.00 93.27 90.00 P 1 21 1 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 0.024331 0.000000 0.001390 0.00000
SCALE2 0.000000 0.016727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
