HEADER SUGAR BINDING PROTEIN 05-MAR-04 1SL6
TITLE CRYSTAL STRUCTURE OF A FRAGMENT OF DC-SIGNR (CONTAING THE CARBOHYDRATE
TITLE 2 RECOGNITION DOMAIN AND TWO REPEATS OF THE NECK) COMPLEXED WITH LEWIS-
TITLE 3 X.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-TYPE LECTIN DC-SIGNR;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: A FRAGMENT CONTAINING THE CRD DOMAIN AND TWO REPEATS
COMPND 6 FROM THE NECK DOMAIN
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_CELL_LINE: BL21/DE3
KEYWDS DC-SIGNR, C-TYPE LECTIN, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GUO,H.FEINBERG,E.CONROY,D.A.MITCHELL,R.ALVAREZ,O.BLIXT,M.E.TAYLOR,
AUTHOR 2 W.I.WEIS,K.DRICKAMER
REVDAT 4 29-JUL-20 1SL6 1 COMPND REMARK HETNAM SSBOND
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 24-FEB-09 1SL6 1 VERSN
REVDAT 2 14-SEP-04 1SL6 1 REMARK
REVDAT 1 15-JUN-04 1SL6 0
JRNL AUTH Y.GUO,H.FEINBERG,E.CONROY,D.A.MITCHELL,R.ALVAREZ,O.BLIXT,
JRNL AUTH 2 M.E.TAYLOR,W.I.WEIS,K.DRICKAMER
JRNL TITL STRUCTURAL BASIS FOR DISTINCT LIGAND-BINDING AND TARGETING
JRNL TITL 2 PROPERTIES OF THE RECEPTORS DC-SIGN AND DC-SIGNR
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 591 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15195147
JRNL DOI 10.1038/NSMB784
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3723247.210
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 73013
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) : 0.219
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.400
REMARK 3 FREE R VALUE TEST SET COUNT : 6102
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8666
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 790
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 240
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.33000
REMARK 3 B22 (A**2) : -13.33000
REMARK 3 B33 (A**2) : 26.65000
REMARK 3 B12 (A**2) : -4.11000
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) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.31
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.290 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 38.86
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM_N
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN_BREAK.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-03
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 : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07810
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80306
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
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) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32200
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: CNS, COMO
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 300, 0.2M NACL, 0.1 HEPES
REMARK 280 PH=7.5. PROTEIN SOLUTION: 10 MG/ML PROTEIN, 5MM CACL2, 10 MM
REMARK 280 OLIGOSACCHARIDE., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.80133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.90067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.90067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 85.80133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 APPLY THE FOLLOWING TO CHAINS: A, G
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
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 216
REMARK 465 GLU A 217
REMARK 465 LEU A 218
REMARK 465 LYS A 235
REMARK 465 ALA A 236
REMARK 465 ALA A 237
REMARK 465 VAL A 238
REMARK 465 GLY A 239
REMARK 465 GLU A 240
REMARK 465 LEU A 241
REMARK 465 PRO A 242
REMARK 465 ASP A 243
REMARK 465 GLN A 244
REMARK 465 SER A 245
REMARK 465 ASP A 398
REMARK 465 GLU A 399
REMARK 465 GLY B 216
REMARK 465 GLU B 217
REMARK 465 LEU B 218
REMARK 465 LYS B 235
REMARK 465 ALA B 236
REMARK 465 ALA B 237
REMARK 465 VAL B 238
REMARK 465 GLY B 239
REMARK 465 GLU B 240
REMARK 465 LEU B 241
REMARK 465 PRO B 242
REMARK 465 ASP B 243
REMARK 465 GLN B 244
REMARK 465 SER B 245
REMARK 465 ASP B 398
REMARK 465 GLU B 399
REMARK 465 GLY C 216
REMARK 465 GLU C 217
REMARK 465 LEU C 218
REMARK 465 LYS C 235
REMARK 465 ALA C 236
REMARK 465 ALA C 237
REMARK 465 VAL C 238
REMARK 465 GLY C 239
REMARK 465 GLU C 240
REMARK 465 LEU C 241
REMARK 465 PRO C 242
REMARK 465 ASP C 243
REMARK 465 GLN C 244
REMARK 465 SER C 245
REMARK 465 ASP C 398
REMARK 465 GLU C 399
REMARK 465 GLY D 216
REMARK 465 GLU D 217
REMARK 465 LEU D 218
REMARK 465 VAL D 238
REMARK 465 GLY D 239
REMARK 465 GLU D 240
REMARK 465 LEU D 241
REMARK 465 PRO D 242
REMARK 465 ASP D 243
REMARK 465 GLN D 244
REMARK 465 SER D 245
REMARK 465 LYS D 246
REMARK 465 GLN D 247
REMARK 465 GLN D 248
REMARK 465 ASP D 398
REMARK 465 GLU D 399
REMARK 465 GLY E 216
REMARK 465 GLU E 217
REMARK 465 LEU E 218
REMARK 465 VAL E 238
REMARK 465 GLY E 239
REMARK 465 GLU E 240
REMARK 465 LEU E 241
REMARK 465 PRO E 242
REMARK 465 ASP E 243
REMARK 465 GLN E 244
REMARK 465 SER E 245
REMARK 465 LYS E 246
REMARK 465 GLN E 247
REMARK 465 GLN E 248
REMARK 465 ASP E 398
REMARK 465 GLU E 399
REMARK 465 GLY F 216
REMARK 465 GLU F 217
REMARK 465 LEU F 218
REMARK 465 VAL F 238
REMARK 465 GLY F 239
REMARK 465 GLU F 240
REMARK 465 LEU F 241
REMARK 465 PRO F 242
REMARK 465 ASP F 243
REMARK 465 GLN F 244
REMARK 465 SER F 245
REMARK 465 LYS F 246
REMARK 465 GLN F 247
REMARK 465 GLN F 248
REMARK 465 ASP F 398
REMARK 465 GLU F 399
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 LYS A 246 CG CD CE NZ
REMARK 470 GLN A 248 CG CD OE1 NE2
REMARK 470 ARG A 397 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 GLN B 248 CG CD OE1 NE2
REMARK 470 LYS C 246 CG CD CE NZ
REMARK 470 GLN C 248 CG CD OE1 NE2
REMARK 470 ARG D 397 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 397 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 397 CG CD NE CZ NH1 NH2
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 GLN A 233 22.80 -76.18
REMARK 500 ASP A 271 -2.96 78.24
REMARK 500 VAL A 304 115.79 -36.59
REMARK 500 VAL A 342 -5.10 -59.97
REMARK 500 SER A 363 106.38 -57.63
REMARK 500 ASN A 365 83.15 62.67
REMARK 500 GLN B 233 16.14 -69.69
REMARK 500 ASP B 271 6.72 84.36
REMARK 500 ALA B 301 -165.88 -127.64
REMARK 500 VAL B 304 116.47 -36.93
REMARK 500 SER B 363 103.25 -55.89
REMARK 500 ASN B 365 86.59 71.25
REMARK 500 GLN C 233 22.74 -65.87
REMARK 500 ARG C 266 46.52 -146.06
REMARK 500 ASP C 271 -7.58 77.17
REMARK 500 ALA C 301 -155.99 -123.43
REMARK 500 VAL C 304 118.62 -30.95
REMARK 500 ASN C 365 99.97 62.80
REMARK 500 LYS D 223 -126.22 -111.66
REMARK 500 LYS D 235 -70.93 -52.93
REMARK 500 ALA D 236 34.68 -65.98
REMARK 500 ARG D 266 37.67 -143.90
REMARK 500 ASP D 271 -5.29 80.37
REMARK 500 PHE D 275 116.21 -160.57
REMARK 500 ALA D 301 -165.30 -121.12
REMARK 500 VAL D 304 119.45 -38.67
REMARK 500 ASN D 365 75.76 71.32
REMARK 500 LYS E 223 -141.00 -106.89
REMARK 500 TYR E 251 -19.25 -47.68
REMARK 500 GLN E 252 -73.80 -67.86
REMARK 500 ARG E 266 33.49 -146.66
REMARK 500 ASP E 271 6.28 84.33
REMARK 500 VAL E 304 121.87 -34.41
REMARK 500 ASN E 365 81.98 66.04
REMARK 500 LYS F 223 -126.46 -116.76
REMARK 500 ASP F 271 -6.48 86.27
REMARK 500 GLN F 276 53.81 39.22
REMARK 500 ALA F 301 -168.37 -128.70
REMARK 500 ASN F 365 78.72 75.26
REMARK 500
REMARK 500 REMARK: NULL
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 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 332 OD1
REMARK 620 2 ASP A 332 OD2 50.4
REMARK 620 3 GLU A 336 OE2 120.0 70.4
REMARK 620 4 GLU A 336 OE1 103.7 82.1 53.5
REMARK 620 5 ASN A 362 OD1 161.8 147.8 78.0 84.6
REMARK 620 6 GLU A 366 O 89.5 131.4 145.7 140.9 74.3
REMARK 620 7 ASP A 367 OD1 72.8 107.1 123.3 69.9 95.6 79.6
REMARK 620 8 HOH A 400 O 103.6 90.1 83.6 136.6 79.7 71.9 151.4
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 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 359 OE1
REMARK 620 2 ASN A 361 OD1 72.2
REMARK 620 3 GLU A 366 OE1 139.4 69.7
REMARK 620 4 ASN A 377 OD1 72.3 144.1 145.9
REMARK 620 5 ASP A 378 O 130.3 134.0 72.3 75.7
REMARK 620 6 ASP A 378 OD1 74.0 86.8 90.2 88.7 68.2
REMARK 620 7 FUC G 2 O3 134.5 120.9 78.9 81.7 74.9 143.1
REMARK 620 8 FUC G 2 O4 72.6 79.7 113.0 84.8 140.4 146.4 68.3
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 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 336 OE1
REMARK 620 2 ASN A 365 OD1 101.5
REMARK 620 3 ASP A 367 OD1 70.4 88.6
REMARK 620 4 ASP A 367 OD2 120.8 90.3 51.9
REMARK 620 5 HOH A 401 O 87.7 168.8 100.5 90.4
REMARK 620 6 HOH A 402 O 155.6 88.4 132.7 81.0 80.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 253 OE1
REMARK 620 2 ASP A 256 OD2 114.4
REMARK 620 3 HOH E 422 O 147.1 94.0
REMARK 620 4 GLU F 230 OE1 74.5 89.3 124.3
REMARK 620 5 GLU F 230 OE2 114.9 94.3 76.8 47.5
REMARK 620 6 GLN F 233 OE1 73.9 164.5 82.7 80.3 70.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 230 OE1
REMARK 620 2 GLN A 233 OE1 116.6
REMARK 620 3 GLU F 253 OE2 107.9 63.5
REMARK 620 4 GLU F 253 OE1 90.4 111.7 48.4
REMARK 620 5 ASP F 256 OD2 75.9 167.0 110.8 62.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 384 OD2
REMARK 620 2 HOH C 18 O 70.0
REMARK 620 3 HOH C 140 O 85.7 109.4
REMARK 620 4 GLU C 336 OE1 148.1 89.9 77.7
REMARK 620 5 ASN C 365 OD1 90.6 158.8 76.6 111.3
REMARK 620 6 ASP C 367 OD2 78.7 73.6 162.0 120.2 94.6
REMARK 620 7 ASP C 367 OD1 126.8 102.7 141.0 80.8 81.5 50.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 332 OD1
REMARK 620 2 ASP B 332 OD2 52.9
REMARK 620 3 GLU B 336 OE1 97.2 80.2
REMARK 620 4 GLU B 336 OE2 117.9 68.6 50.1
REMARK 620 5 ASN B 362 OD1 160.5 144.2 81.2 75.9
REMARK 620 6 GLU B 366 O 92.5 126.9 150.4 143.9 80.5
REMARK 620 7 ASP B 367 OD1 67.4 108.6 71.5 121.5 93.9 86.8
REMARK 620 8 HOH B 400 O 110.8 83.1 127.9 77.8 84.6 73.0 159.8
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 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 359 OE1
REMARK 620 2 ASN B 361 OD1 73.8
REMARK 620 3 GLU B 366 OE1 144.2 73.0
REMARK 620 4 ASN B 377 OD1 74.4 147.3 139.7
REMARK 620 5 ASP B 378 OD1 69.7 84.1 93.9 92.0
REMARK 620 6 ASP B 378 O 130.6 130.3 66.6 77.8 71.3
REMARK 620 7 FUC H 2 O3 142.4 119.4 68.3 82.8 141.8 70.5
REMARK 620 8 FUC H 2 O4 77.8 82.6 110.5 83.4 147.2 138.0 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 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 336 OE1
REMARK 620 2 ASN B 365 OD1 111.5
REMARK 620 3 ASP B 367 OD1 70.2 96.6
REMARK 620 4 ASP B 367 OD2 120.3 87.6 51.2
REMARK 620 5 HOH B 401 O 77.8 168.7 92.6 93.1
REMARK 620 6 HOH B 402 O 148.5 89.4 132.6 82.4 79.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 253 OE1
REMARK 620 2 GLU B 253 OE2 45.9
REMARK 620 3 ASP B 256 OD2 108.3 97.1
REMARK 620 4 GLU E 230 OE2 106.8 152.4 88.1
REMARK 620 5 GLU E 230 OE1 68.0 111.8 88.0 41.0
REMARK 620 6 GLN E 233 OE1 77.3 101.8 157.4 69.5 73.7
REMARK 620 7 HOH F 424 O 149.4 130.8 102.3 73.5 113.6 74.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 230 OE1
REMARK 620 2 GLU B 230 OE2 44.1
REMARK 620 3 GLN B 233 OE1 97.8 78.9
REMARK 620 4 GLU E 253 OE1 88.7 132.4 121.9
REMARK 620 5 GLU E 253 OE2 94.3 123.0 69.6 52.4
REMARK 620 6 ASP E 256 OD2 81.1 99.9 178.8 58.7 111.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 17 O
REMARK 620 2 ASP C 332 OD2 94.5
REMARK 620 3 ASP C 332 OD1 112.0 51.1
REMARK 620 4 GLU C 336 OE1 125.6 78.3 104.6
REMARK 620 5 GLU C 336 OE2 75.6 71.8 122.4 50.7
REMARK 620 6 ASN C 362 OD1 85.6 148.9 154.9 76.5 78.2
REMARK 620 7 GLU C 366 O 76.9 132.9 89.0 143.6 144.3 77.4
REMARK 620 8 ASP C 367 OD1 151.4 109.7 74.9 75.6 125.5 81.2 75.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 359 OE1
REMARK 620 2 ASN C 361 OD1 75.6
REMARK 620 3 GLU C 366 OE1 143.8 73.2
REMARK 620 4 ASN C 377 OD1 68.9 141.9 144.8
REMARK 620 5 ASP C 378 O 120.9 132.8 71.0 79.4
REMARK 620 6 ASP C 378 OD1 66.2 84.6 92.7 93.2 67.5
REMARK 620 7 FUC I 2 O3 136.2 124.5 78.1 76.7 76.3 143.7
REMARK 620 8 FUC I 2 O4 81.6 78.5 109.5 83.0 142.8 146.5 67.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 137 O
REMARK 620 2 GLU C 253 OE1 86.2
REMARK 620 3 ASP C 256 OD2 111.3 108.7
REMARK 620 4 GLU D 230 OE2 153.5 111.3 82.7
REMARK 620 5 GLU D 230 OE1 155.0 69.6 83.4 44.0
REMARK 620 6 GLN D 233 OE1 97.7 81.8 149.5 66.8 73.5
REMARK 620 7 HOH D 425 O 79.0 161.5 87.2 79.3 123.2 89.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 4 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 230 OE1
REMARK 620 2 GLN C 233 OE1 100.3
REMARK 620 3 GLU D 253 OE1 90.2 66.6
REMARK 620 4 GLU D 253 OE2 123.8 100.7 53.2
REMARK 620 5 ASP D 256 OD2 81.6 169.1 124.2 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 332 OD1
REMARK 620 2 ASP D 332 OD2 49.6
REMARK 620 3 GLU D 336 OE1 102.5 78.5
REMARK 620 4 GLU D 336 OE2 120.2 71.4 50.7
REMARK 620 5 ASN D 362 OD1 160.8 149.1 83.2 77.7
REMARK 620 6 GLU D 366 O 89.7 132.6 142.2 146.6 75.3
REMARK 620 7 ASP D 367 OD1 69.4 100.3 69.4 120.1 96.3 82.2
REMARK 620 8 HOH D 401 O 104.4 93.7 136.3 85.8 82.5 71.6 153.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 359 OE1
REMARK 620 2 ASN D 361 OD1 72.7
REMARK 620 3 GLU D 366 OE1 142.5 71.9
REMARK 620 4 ASN D 377 OD1 66.1 138.1 150.0
REMARK 620 5 ASP D 378 O 130.0 134.5 71.6 81.0
REMARK 620 6 ASP D 378 OD1 73.0 85.8 92.7 89.1 69.9
REMARK 620 7 FUC J 2 O3 139.0 115.7 69.6 91.9 74.8 144.1
REMARK 620 8 FUC J 2 O4 72.5 81.0 113.1 79.9 138.8 145.3 69.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 336 OE1
REMARK 620 2 ASN D 365 OD1 102.9
REMARK 620 3 ASP D 367 OD1 69.0 85.4
REMARK 620 4 ASP D 367 OD2 119.6 84.7 51.7
REMARK 620 5 HOH D 402 O 83.9 170.9 91.5 86.7
REMARK 620 6 ASP F 384 OD2 85.5 89.3 152.0 154.9 97.4
REMARK 620 7 HOH F 404 O 157.9 94.7 126.5 74.9 80.3 81.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 384 OD2
REMARK 620 2 HOH D 400 O 74.0
REMARK 620 3 GLU E 336 OE1 89.2 156.4
REMARK 620 4 ASN E 365 OD1 84.5 91.1 103.9
REMARK 620 5 ASP E 367 OD1 155.0 128.4 72.1 84.2
REMARK 620 6 ASP E 367 OD2 148.5 76.2 122.2 86.3 52.2
REMARK 620 7 HOH E 401 O 95.8 78.1 87.5 168.6 99.6 87.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 332 OD1
REMARK 620 2 ASP E 332 OD2 49.5
REMARK 620 3 GLU E 336 OE1 102.6 81.3
REMARK 620 4 GLU E 336 OE2 120.6 72.1 52.5
REMARK 620 5 ASN E 362 OD1 155.7 153.2 81.4 81.1
REMARK 620 6 GLU E 366 O 87.2 126.9 145.8 146.1 77.3
REMARK 620 7 ASP E 367 OD1 67.9 105.2 76.0 128.5 90.3 77.7
REMARK 620 8 HOH E 400 O 101.0 85.6 134.9 82.4 92.2 72.7 148.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 359 OE1
REMARK 620 2 ASN E 361 OD1 69.2
REMARK 620 3 GLU E 366 OE1 143.8 77.3
REMARK 620 4 ASN E 377 OD1 71.1 139.0 143.7
REMARK 620 5 ASP E 378 O 130.0 139.9 70.9 76.1
REMARK 620 6 ASP E 378 OD1 71.9 85.2 92.3 92.1 72.7
REMARK 620 7 FUC K 2 O3 134.1 120.0 75.1 81.8 74.6 147.2
REMARK 620 8 FUC K 2 O4 72.4 81.4 116.5 77.2 134.6 144.3 65.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 384 OD2
REMARK 620 2 HOH E 404 O 76.2
REMARK 620 3 GLU F 336 OE1 82.2 152.6
REMARK 620 4 ASN F 365 OD1 86.3 95.1 100.1
REMARK 620 5 ASP F 367 OD1 154.3 128.3 76.2 84.1
REMARK 620 6 ASP F 367 OD2 151.8 76.6 126.0 88.7 51.7
REMARK 620 7 HOH F 401 O 93.0 78.9 85.8 174.0 98.9 89.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 332 OD2
REMARK 620 2 ASP F 332 OD1 49.9
REMARK 620 3 GLU F 336 OE2 74.2 123.1
REMARK 620 4 GLU F 336 OE1 86.5 109.9 49.9
REMARK 620 5 ASN F 362 OD1 148.0 162.0 74.1 76.3
REMARK 620 6 GLU F 366 O 128.4 87.6 144.4 141.5 78.2
REMARK 620 7 ASP F 367 OD1 109.7 74.3 124.5 74.7 91.7 77.8
REMARK 620 8 HOH F 400 O 86.0 102.5 80.3 129.7 84.7 75.3 153.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 359 OE1
REMARK 620 2 ASN F 361 OD1 73.2
REMARK 620 3 GLU F 366 OE1 149.7 78.6
REMARK 620 4 ASN F 377 OD1 64.6 136.5 144.7
REMARK 620 5 ASP F 378 OD1 74.7 87.6 93.4 91.1
REMARK 620 6 ASP F 378 O 125.2 141.0 72.6 76.6 68.7
REMARK 620 7 FUC L 2 O4 73.2 83.7 114.9 74.7 147.9 132.2
REMARK 620 8 FUC L 2 O3 133.5 119.9 71.2 84.6 143.3 74.8 65.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF 1SL6 A 216 399 GB 12084795 AAG13815 216 399
DBREF 1SL6 B 216 399 GB 12084795 AAG13815 216 399
DBREF 1SL6 C 216 399 GB 12084795 AAG13815 216 399
DBREF 1SL6 D 216 399 GB 12084795 AAG13815 216 399
DBREF 1SL6 E 216 399 GB 12084795 AAG13815 216 399
DBREF 1SL6 F 216 399 GB 12084795 AAG13815 216 399
SEQRES 1 A 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 A 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 A 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 A 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 A 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 A 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 A 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 A 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 A 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 A 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 A 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 A 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 A 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 A 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 A 184 ASP GLU
SEQRES 1 B 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 B 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 B 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 B 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 B 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 B 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 B 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 B 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 B 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 B 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 B 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 B 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 B 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 B 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 B 184 ASP GLU
SEQRES 1 C 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 C 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 C 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 C 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 C 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 C 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 C 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 C 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 C 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 C 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 C 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 C 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 C 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 C 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 C 184 ASP GLU
SEQRES 1 D 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 D 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 D 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 D 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 D 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 D 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 D 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 D 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 D 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 D 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 D 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 D 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 D 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 D 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 D 184 ASP GLU
SEQRES 1 E 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 E 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 E 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 E 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 E 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 E 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 E 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 E 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 E 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 E 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 E 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 E 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 E 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 E 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 E 184 ASP GLU
SEQRES 1 F 184 GLY GLU LEU PRO GLU LYS SER LYS LEU GLN GLU ILE TYR
SEQRES 2 F 184 GLN GLU LEU THR GLN LEU LYS ALA ALA VAL GLY GLU LEU
SEQRES 3 F 184 PRO ASP GLN SER LYS GLN GLN GLN ILE TYR GLN GLU LEU
SEQRES 4 F 184 THR ASP LEU LYS THR ALA PHE GLU ARG LEU CYS ARG HIS
SEQRES 5 F 184 CYS PRO LYS ASP TRP THR PHE PHE GLN GLY ASN CYS TYR
SEQRES 6 F 184 PHE MET SER ASN SER GLN ARG ASN TRP HIS ASP SER VAL
SEQRES 7 F 184 THR ALA CYS GLN GLU VAL ARG ALA GLN LEU VAL VAL ILE
SEQRES 8 F 184 LYS THR ALA GLU GLU GLN ASN PHE LEU GLN LEU GLN THR
SEQRES 9 F 184 SER ARG SER ASN ARG PHE SER TRP MET GLY LEU SER ASP
SEQRES 10 F 184 LEU ASN GLN GLU GLY THR TRP GLN TRP VAL ASP GLY SER
SEQRES 11 F 184 PRO LEU SER PRO SER PHE GLN ARG TYR TRP ASN SER GLY
SEQRES 12 F 184 GLU PRO ASN ASN SER GLY ASN GLU ASP CYS ALA GLU PHE
SEQRES 13 F 184 SER GLY SER GLY TRP ASN ASP ASN ARG CYS ASP VAL ASP
SEQRES 14 F 184 ASN TYR TRP ILE CYS LYS LYS PRO ALA ALA CYS PHE ARG
SEQRES 15 F 184 ASP GLU
HET NDG G 1 15
HET FUC G 2 10
HET GAL G 3 11
HET NDG H 1 15
HET FUC H 2 10
HET GAL H 3 11
HET NDG I 1 15
HET FUC I 2 10
HET GAL I 3 11
HET NDG J 1 15
HET FUC J 2 10
HET GAL J 3 11
HET NDG K 1 15
HET FUC K 2 10
HET GAL K 3 11
HET NDG L 1 15
HET FUC L 2 10
HET GAL L 3 11
HET CA A 1 1
HET CA A 2 1
HET CA A 3 1
HET CA A 4 1
HET CA B 1 1
HET CA B 2 1
HET CA B 3 1
HET CA B 4 1
HET CA C 1 1
HET CA C 2 1
HET CA C 3 1
HET CA C 4 1
HET CA D 1 1
HET CA D 2 1
HET CA D 3 1
HET CA D 4 1
HET CA E 1 1
HET CA E 2 1
HET CA E 3 1
HET CA E 4 1
HET CA F 1 1
HET CA F 2 1
HET CA F 3 1
HET CA F 4 1
HETNAM NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CA CALCIUM ION
FORMUL 7 NDG 6(C8 H15 N O6)
FORMUL 7 FUC 6(C6 H12 O5)
FORMUL 7 GAL 6(C6 H12 O6)
FORMUL 13 CA 24(CA 2+)
FORMUL 37 HOH *236(H2 O)
HELIX 1 1 PRO A 219 GLN A 233 1 15
HELIX 2 2 GLN A 247 ARG A 263 1 17
HELIX 3 3 ASN A 288 GLU A 298 1 11
HELIX 4 4 THR A 308 SER A 322 1 15
HELIX 5 5 SER A 348 TRP A 355 5 8
HELIX 6 6 PRO B 219 GLN B 233 1 15
HELIX 7 7 GLN B 247 ARG B 263 1 17
HELIX 8 8 ASN B 288 GLU B 298 1 11
HELIX 9 9 THR B 308 SER B 322 1 15
HELIX 10 10 SER B 348 TRP B 355 5 8
HELIX 11 11 PRO C 219 GLN C 233 1 15
HELIX 12 12 GLN C 247 ARG C 263 1 17
HELIX 13 13 ASN C 288 GLU C 298 1 11
HELIX 14 14 THR C 308 ASN C 323 1 16
HELIX 15 15 SER C 348 TRP C 355 5 8
HELIX 16 16 LYS D 223 ALA D 236 1 14
HELIX 17 17 GLN D 249 CYS D 265 1 17
HELIX 18 18 ASN D 288 VAL D 299 1 12
HELIX 19 19 THR D 308 ASN D 323 1 16
HELIX 20 20 SER D 348 TRP D 355 5 8
HELIX 21 21 PRO E 219 SER E 222 5 4
HELIX 22 22 LYS E 223 ALA E 236 1 14
HELIX 23 23 GLN E 249 CYS E 265 1 17
HELIX 24 24 ASN E 288 VAL E 299 1 12
HELIX 25 25 THR E 308 SER E 322 1 15
HELIX 26 26 SER E 348 TRP E 355 5 8
HELIX 27 27 PRO F 219 SER F 222 5 4
HELIX 28 28 LYS F 223 ALA F 236 1 14
HELIX 29 29 GLN F 249 CYS F 265 1 17
HELIX 30 30 ASN F 288 GLU F 298 1 11
HELIX 31 31 THR F 308 ASN F 323 1 16
HELIX 32 32 SER F 348 TRP F 355 5 8
SHEET 1 A 5 THR A 273 PHE A 275 0
SHEET 2 A 5 ASN A 278 MET A 282 -1 O TYR A 280 N THR A 273
SHEET 3 A 5 TYR A 386 PRO A 392 -1 O LYS A 391 N CYS A 279
SHEET 4 A 5 SER A 326 SER A 331 1 N TRP A 327 O TYR A 386
SHEET 5 A 5 GLN A 340 TRP A 341 -1 O GLN A 340 N SER A 331
SHEET 1 B 5 GLN A 302 LEU A 303 0
SHEET 2 B 5 TYR A 386 PRO A 392 -1 O LYS A 390 N GLN A 302
SHEET 3 B 5 SER A 326 SER A 331 1 N TRP A 327 O TYR A 386
SHEET 4 B 5 CYS A 368 SER A 372 -1 O PHE A 371 N SER A 326
SHEET 5 B 5 GLY A 375 ASN A 379 -1 O ASN A 379 N CYS A 368
SHEET 1 C 5 THR B 273 PHE B 275 0
SHEET 2 C 5 ASN B 278 MET B 282 -1 O TYR B 280 N THR B 273
SHEET 3 C 5 TYR B 386 PRO B 392 -1 O LYS B 391 N CYS B 279
SHEET 4 C 5 SER B 326 SER B 331 1 N TRP B 327 O TYR B 386
SHEET 5 C 5 GLN B 340 TRP B 341 -1 O GLN B 340 N SER B 331
SHEET 1 D 5 GLN B 302 LEU B 303 0
SHEET 2 D 5 TYR B 386 PRO B 392 -1 O LYS B 390 N GLN B 302
SHEET 3 D 5 SER B 326 SER B 331 1 N TRP B 327 O TYR B 386
SHEET 4 D 5 CYS B 368 SER B 372 -1 O PHE B 371 N SER B 326
SHEET 5 D 5 GLY B 375 ASN B 379 -1 O ASN B 379 N CYS B 368
SHEET 1 E 5 THR C 273 PHE C 275 0
SHEET 2 E 5 ASN C 278 MET C 282 -1 O TYR C 280 N THR C 273
SHEET 3 E 5 TYR C 386 PRO C 392 -1 O LYS C 391 N CYS C 279
SHEET 4 E 5 SER C 326 SER C 331 1 N TRP C 327 O TYR C 386
SHEET 5 E 5 GLN C 340 TRP C 341 -1 O GLN C 340 N SER C 331
SHEET 1 F 5 GLN C 302 LEU C 303 0
SHEET 2 F 5 TYR C 386 PRO C 392 -1 O LYS C 390 N GLN C 302
SHEET 3 F 5 SER C 326 SER C 331 1 N TRP C 327 O TYR C 386
SHEET 4 F 5 CYS C 368 SER C 372 -1 O PHE C 371 N SER C 326
SHEET 5 F 5 GLY C 375 ASN C 379 -1 O ASN C 379 N CYS C 368
SHEET 1 G 5 THR D 273 PHE D 275 0
SHEET 2 G 5 ASN D 278 MET D 282 -1 O ASN D 278 N PHE D 275
SHEET 3 G 5 TYR D 386 PRO D 392 -1 O LYS D 391 N CYS D 279
SHEET 4 G 5 SER D 326 SER D 331 1 N TRP D 327 O TYR D 386
SHEET 5 G 5 GLN D 340 TRP D 341 -1 O GLN D 340 N SER D 331
SHEET 1 H 5 GLN D 302 LEU D 303 0
SHEET 2 H 5 TYR D 386 PRO D 392 -1 O LYS D 390 N GLN D 302
SHEET 3 H 5 SER D 326 SER D 331 1 N TRP D 327 O TYR D 386
SHEET 4 H 5 CYS D 368 SER D 372 -1 O PHE D 371 N SER D 326
SHEET 5 H 5 GLY D 375 ASN D 379 -1 O ASN D 379 N CYS D 368
SHEET 1 I 5 THR E 273 PHE E 275 0
SHEET 2 I 5 ASN E 278 MET E 282 -1 O ASN E 278 N PHE E 275
SHEET 3 I 5 TYR E 386 PRO E 392 -1 O LYS E 391 N CYS E 279
SHEET 4 I 5 SER E 326 SER E 331 1 N TRP E 327 O TYR E 386
SHEET 5 I 5 GLN E 340 TRP E 341 -1 O GLN E 340 N SER E 331
SHEET 1 J 5 GLN E 302 LEU E 303 0
SHEET 2 J 5 TYR E 386 PRO E 392 -1 O LYS E 390 N GLN E 302
SHEET 3 J 5 SER E 326 SER E 331 1 N TRP E 327 O TYR E 386
SHEET 4 J 5 CYS E 368 SER E 372 -1 O PHE E 371 N SER E 326
SHEET 5 J 5 GLY E 375 ASN E 379 -1 O GLY E 375 N SER E 372
SHEET 1 K 5 THR F 273 PHE F 275 0
SHEET 2 K 5 ASN F 278 MET F 282 -1 O TYR F 280 N THR F 273
SHEET 3 K 5 TYR F 386 PRO F 392 -1 O LYS F 391 N CYS F 279
SHEET 4 K 5 SER F 326 SER F 331 1 N TRP F 327 O TYR F 386
SHEET 5 K 5 GLN F 340 TRP F 341 -1 O GLN F 340 N SER F 331
SHEET 1 L 5 GLN F 302 LEU F 303 0
SHEET 2 L 5 TYR F 386 PRO F 392 -1 O LYS F 390 N GLN F 302
SHEET 3 L 5 SER F 326 SER F 331 1 N TRP F 327 O TYR F 386
SHEET 4 L 5 CYS F 368 SER F 372 -1 O PHE F 371 N SER F 326
SHEET 5 L 5 GLY F 375 ASN F 379 -1 O ASN F 379 N CYS F 368
SSBOND 1 CYS A 265 CYS A 395 1555 1555 2.04
SSBOND 2 CYS A 268 CYS A 279 1555 1555 2.05
SSBOND 3 CYS B 265 CYS B 395 1555 1555 2.04
SSBOND 4 CYS B 268 CYS B 279 1555 1555 2.05
SSBOND 5 CYS B 296 CYS B 389 1555 1555 2.06
SSBOND 6 CYS B 368 CYS B 381 1555 1555 2.05
SSBOND 7 CYS C 265 CYS C 395 1555 1555 2.04
SSBOND 8 CYS C 268 CYS C 279 1555 1555 2.05
SSBOND 9 CYS C 296 CYS C 389 1555 1555 2.05
SSBOND 10 CYS D 265 CYS D 395 1555 1555 2.04
SSBOND 11 CYS D 268 CYS D 279 1555 1555 2.04
SSBOND 12 CYS D 296 CYS D 389 1555 1555 2.06
SSBOND 13 CYS E 265 CYS E 395 1555 1555 2.03
SSBOND 14 CYS E 268 CYS E 279 1555 1555 2.04
SSBOND 15 CYS E 296 CYS E 389 1555 1555 2.06
SSBOND 16 CYS F 265 CYS F 395 1555 1555 2.04
SSBOND 17 CYS F 268 CYS F 279 1555 1555 2.04
SSBOND 18 CYS F 296 CYS F 389 1555 1555 2.05
LINK O3 NDG G 1 C1 FUC G 2 1555 1555 1.40
LINK O4 NDG G 1 C1 GAL G 3 1555 1555 1.39
LINK O3 NDG H 1 C1 FUC H 2 1555 1555 1.40
LINK O4 NDG H 1 C1 GAL H 3 1555 1555 1.39
LINK O3 NDG I 1 C1 FUC I 2 1555 1555 1.40
LINK O4 NDG I 1 C1 GAL I 3 1555 1555 1.39
LINK O3 NDG J 1 C1 FUC J 2 1555 1555 1.40
LINK O4 NDG J 1 C1 GAL J 3 1555 1555 1.39
LINK O3 NDG K 1 C1 FUC K 2 1555 1555 1.40
LINK O4 NDG K 1 C1 GAL K 3 1555 1555 1.39
LINK O3 NDG L 1 C1 FUC L 2 1555 1555 1.41
LINK O4 NDG L 1 C1 GAL L 3 1555 1555 1.39
LINK CA CA A 1 OD1 ASP A 332 1555 1555 2.66
LINK CA CA A 1 OD2 ASP A 332 1555 1555 2.47
LINK CA CA A 1 OE2 GLU A 336 1555 1555 2.23
LINK CA CA A 1 OE1 GLU A 336 1555 1555 2.59
LINK CA CA A 1 OD1 ASN A 362 1555 1555 2.35
LINK CA CA A 1 O GLU A 366 1555 1555 2.38
LINK CA CA A 1 OD1 ASP A 367 1555 1555 2.19
LINK CA CA A 1 O HOH A 400 1555 1555 2.44
LINK CA CA A 2 OE1 GLU A 359 1555 1555 2.90
LINK CA CA A 2 OD1 ASN A 361 1555 1555 2.63
LINK CA CA A 2 OE1 GLU A 366 1555 1555 2.48
LINK CA CA A 2 OD1 ASN A 377 1555 1555 2.52
LINK CA CA A 2 O ASP A 378 1555 1555 2.52
LINK CA CA A 2 OD1 ASP A 378 1555 1555 2.31
LINK CA CA A 2 O3 FUC G 2 1555 1555 2.48
LINK CA CA A 2 O4 FUC G 2 1555 1555 2.39
LINK CA CA A 3 OE1 GLU A 336 1555 1555 2.20
LINK CA CA A 3 OD1 ASN A 365 1555 1555 2.36
LINK CA CA A 3 OD1 ASP A 367 1555 1555 2.56
LINK CA CA A 3 OD2 ASP A 367 1555 1555 2.46
LINK CA CA A 3 O HOH A 401 1555 1555 2.44
LINK CA CA A 3 O HOH A 402 1555 1555 2.47
LINK CA CA A 4 OE1 GLU A 253 1555 1555 2.75
LINK CA CA A 4 OD2 ASP A 256 1555 1555 2.50
LINK CA CA A 4 O HOH E 422 1555 1555 2.60
LINK CA CA A 4 OE1 GLU F 230 1555 5555 2.68
LINK CA CA A 4 OE2 GLU F 230 1555 5555 2.77
LINK CA CA A 4 OE1 GLN F 233 1555 5555 2.37
LINK OE1 GLU A 230 CA CA E 4 1555 1555 2.46
LINK OE1 GLN A 233 CA CA E 4 1555 1555 2.27
LINK OD2 ASP A 384 CA CA C 3 2654 1555 2.57
LINK CA CA B 1 OD1 ASP B 332 1555 1555 2.52
LINK CA CA B 1 OD2 ASP B 332 1555 1555 2.37
LINK CA CA B 1 OE1 GLU B 336 1555 1555 2.55
LINK CA CA B 1 OE2 GLU B 336 1555 1555 2.63
LINK CA CA B 1 OD1 ASN B 362 1555 1555 2.45
LINK CA CA B 1 O GLU B 366 1555 1555 2.52
LINK CA CA B 1 OD1 ASP B 367 1555 1555 2.23
LINK CA CA B 1 O HOH B 400 1555 1555 2.28
LINK CA CA B 2 OE1 GLU B 359 1555 1555 2.54
LINK CA CA B 2 OD1 ASN B 361 1555 1555 2.50
LINK CA CA B 2 OE1 GLU B 366 1555 1555 2.53
LINK CA CA B 2 OD1 ASN B 377 1555 1555 2.36
LINK CA CA B 2 OD1 ASP B 378 1555 1555 2.23
LINK CA CA B 2 O ASP B 378 1555 1555 2.45
LINK CA CA B 2 O3 FUC H 2 1555 1555 2.40
LINK CA CA B 2 O4 FUC H 2 1555 1555 2.48
LINK CA CA B 3 OE1 GLU B 336 1555 1555 2.38
LINK CA CA B 3 OD1 ASN B 365 1555 1555 2.23
LINK CA CA B 3 OD1 ASP B 367 1555 1555 2.50
LINK CA CA B 3 OD2 ASP B 367 1555 1555 2.61
LINK CA CA B 3 O HOH B 401 1555 1555 2.41
LINK CA CA B 3 O HOH B 402 1555 1555 2.28
LINK CA CA B 4 OE1 GLU B 253 1555 1555 2.23
LINK CA CA B 4 OE2 GLU B 253 1555 1555 3.06
LINK CA CA B 4 OD2 ASP B 256 1555 1555 2.68
LINK CA CA B 4 OE2 GLU E 230 1555 5555 3.27
LINK CA CA B 4 OE1 GLU E 230 1555 5555 2.93
LINK CA CA B 4 OE1 GLN E 233 1555 5555 2.28
LINK CA CA B 4 O HOH F 424 1555 1555 2.31
LINK OE1 GLU B 230 CA CA F 4 1555 1555 2.59
LINK OE2 GLU B 230 CA CA F 4 1555 1555 3.12
LINK OE1 GLN B 233 CA CA F 4 1555 1555 2.55
LINK CA CA C 1 O HOH C 17 1555 1555 2.37
LINK CA CA C 1 OD2 ASP C 332 1555 1555 2.36
LINK CA CA C 1 OD1 ASP C 332 1555 1555 2.67
LINK CA CA C 1 OE1 GLU C 336 1555 1555 2.58
LINK CA CA C 1 OE2 GLU C 336 1555 1555 2.55
LINK CA CA C 1 OD1 ASN C 362 1555 1555 2.41
LINK CA CA C 1 O GLU C 366 1555 1555 2.39
LINK CA CA C 1 OD1 ASP C 367 1555 1555 2.49
LINK CA CA C 2 OE1 GLU C 359 1555 1555 2.39
LINK CA CA C 2 OD1 ASN C 361 1555 1555 2.57
LINK CA CA C 2 OE1 GLU C 366 1555 1555 2.62
LINK CA CA C 2 OD1 ASN C 377 1555 1555 2.43
LINK CA CA C 2 O ASP C 378 1555 1555 2.48
LINK CA CA C 2 OD1 ASP C 378 1555 1555 2.13
LINK CA CA C 2 O3 FUC I 2 1555 1555 2.50
LINK CA CA C 2 O4 FUC I 2 1555 1555 2.42
LINK CA CA C 3 O HOH C 18 1555 1555 2.26
LINK CA CA C 3 O HOH C 140 1555 1555 2.50
LINK CA CA C 3 OE1 GLU C 336 1555 1555 2.30
LINK CA CA C 3 OD1 ASN C 365 1555 1555 2.17
LINK CA CA C 3 OD2 ASP C 367 1555 1555 2.67
LINK CA CA C 3 OD1 ASP C 367 1555 1555 2.49
LINK CA CA C 4 O HOH C 137 1555 1555 2.67
LINK CA CA C 4 OE1 GLU C 253 1555 1555 2.61
LINK CA CA C 4 OD2 ASP C 256 1555 1555 2.83
LINK CA CA C 4 OE2 GLU D 230 1555 5555 2.93
LINK CA CA C 4 OE1 GLU D 230 1555 5555 2.93
LINK CA CA C 4 OE1 GLN D 233 1555 5555 2.37
LINK CA CA C 4 O HOH D 425 1555 1555 2.71
LINK OE1 GLU C 230 CA CA D 4 5555 1555 2.84
LINK OE1 GLN C 233 CA CA D 4 5555 1555 2.56
LINK CA CA D 1 OD1 ASP D 332 1555 1555 2.70
LINK CA CA D 1 OD2 ASP D 332 1555 1555 2.52
LINK CA CA D 1 OE1 GLU D 336 1555 1555 2.58
LINK CA CA D 1 OE2 GLU D 336 1555 1555 2.58
LINK CA CA D 1 OD1 ASN D 362 1555 1555 2.43
LINK CA CA D 1 O GLU D 366 1555 1555 2.39
LINK CA CA D 1 OD1 ASP D 367 1555 1555 2.31
LINK CA CA D 1 O HOH D 401 1555 1555 2.44
LINK CA CA D 2 OE1 GLU D 359 1555 1555 2.65
LINK CA CA D 2 OD1 ASN D 361 1555 1555 2.43
LINK CA CA D 2 OE1 GLU D 366 1555 1555 2.48
LINK CA CA D 2 OD1 ASN D 377 1555 1555 2.41
LINK CA CA D 2 O ASP D 378 1555 1555 2.50
LINK CA CA D 2 OD1 ASP D 378 1555 1555 2.37
LINK CA CA D 2 O3 FUC J 2 1555 1555 2.49
LINK CA CA D 2 O4 FUC J 2 1555 1555 2.40
LINK CA CA D 3 OE1 GLU D 336 1555 1555 2.45
LINK CA CA D 3 OD1 ASN D 365 1555 1555 2.43
LINK CA CA D 3 OD1 ASP D 367 1555 1555 2.47
LINK CA CA D 3 OD2 ASP D 367 1555 1555 2.55
LINK CA CA D 3 O HOH D 402 1555 1555 2.31
LINK CA CA D 3 OD2 ASP F 384 1555 1555 2.49
LINK CA CA D 3 O HOH F 404 1555 1555 2.32
LINK CA CA D 4 OE1 GLU D 253 1555 1555 2.48
LINK CA CA D 4 OE2 GLU D 253 1555 1555 2.42
LINK CA CA D 4 OD2 ASP D 256 1555 1555 3.00
LINK OD2 ASP D 384 CA CA E 3 1555 1555 2.43
LINK O HOH D 400 CA CA E 3 1555 1555 2.53
LINK CA CA E 1 OD1 ASP E 332 1555 1555 2.73
LINK CA CA E 1 OD2 ASP E 332 1555 1555 2.47
LINK CA CA E 1 OE1 GLU E 336 1555 1555 2.47
LINK CA CA E 1 OE2 GLU E 336 1555 1555 2.52
LINK CA CA E 1 OD1 ASN E 362 1555 1555 2.53
LINK CA CA E 1 O GLU E 366 1555 1555 2.52
LINK CA CA E 1 OD1 ASP E 367 1555 1555 2.27
LINK CA CA E 1 O HOH E 400 1555 1555 2.33
LINK CA CA E 2 OE1 GLU E 359 1555 1555 2.59
LINK CA CA E 2 OD1 ASN E 361 1555 1555 2.34
LINK CA CA E 2 OE1 GLU E 366 1555 1555 2.36
LINK CA CA E 2 OD1 ASN E 377 1555 1555 2.42
LINK CA CA E 2 O ASP E 378 1555 1555 2.44
LINK CA CA E 2 OD1 ASP E 378 1555 1555 2.32
LINK CA CA E 2 O3 FUC K 2 1555 1555 2.64
LINK CA CA E 2 O4 FUC K 2 1555 1555 2.45
LINK CA CA E 3 OE1 GLU E 336 1555 1555 2.44
LINK CA CA E 3 OD1 ASN E 365 1555 1555 2.40
LINK CA CA E 3 OD1 ASP E 367 1555 1555 2.53
LINK CA CA E 3 OD2 ASP E 367 1555 1555 2.44
LINK CA CA E 3 O HOH E 401 1555 1555 2.46
LINK CA CA E 4 OE2 GLU F 253 1555 5555 2.75
LINK CA CA E 4 OE1 GLU F 253 1555 5555 2.59
LINK CA CA E 4 OD2 ASP F 256 1555 5555 2.80
LINK OE1 GLU E 253 CA CA F 4 5555 1555 2.57
LINK OE2 GLU E 253 CA CA F 4 5555 1555 2.40
LINK OD2 ASP E 256 CA CA F 4 5555 1555 2.85
LINK OD2 ASP E 384 CA CA F 3 1555 1555 2.49
LINK O HOH E 404 CA CA F 3 1555 1555 2.46
LINK CA CA F 1 OD2 ASP F 332 1555 1555 2.33
LINK CA CA F 1 OD1 ASP F 332 1555 1555 2.77
LINK CA CA F 1 OE2 GLU F 336 1555 1555 2.42
LINK CA CA F 1 OE1 GLU F 336 1555 1555 2.73
LINK CA CA F 1 OD1 ASN F 362 1555 1555 2.54
LINK CA CA F 1 O GLU F 366 1555 1555 2.40
LINK CA CA F 1 OD1 ASP F 367 1555 1555 2.22
LINK CA CA F 1 O HOH F 400 1555 1555 2.37
LINK CA CA F 2 OE1 GLU F 359 1555 1555 2.56
LINK CA CA F 2 OD1 ASN F 361 1555 1555 2.33
LINK CA CA F 2 OE1 GLU F 366 1555 1555 2.39
LINK CA CA F 2 OD1 ASN F 377 1555 1555 2.50
LINK CA CA F 2 OD1 ASP F 378 1555 1555 2.22
LINK CA CA F 2 O ASP F 378 1555 1555 2.49
LINK CA CA F 2 O4 FUC L 2 1555 1555 2.49
LINK CA CA F 2 O3 FUC L 2 1555 1555 2.63
LINK CA CA F 3 OE1 GLU F 336 1555 1555 2.35
LINK CA CA F 3 OD1 ASN F 365 1555 1555 2.28
LINK CA CA F 3 OD1 ASP F 367 1555 1555 2.55
LINK CA CA F 3 OD2 ASP F 367 1555 1555 2.47
LINK CA CA F 3 O HOH F 401 1555 1555 2.31
CISPEP 1 GLU A 359 PRO A 360 0 -0.08
CISPEP 2 GLU B 359 PRO B 360 0 -0.52
CISPEP 3 GLU C 359 PRO C 360 0 -0.34
CISPEP 4 GLU D 359 PRO D 360 0 -0.48
CISPEP 5 GLU E 359 PRO E 360 0 -0.76
CISPEP 6 GLU F 359 PRO F 360 0 -0.74
CRYST1 153.750 153.750 128.702 90.00 90.00 120.00 P 32 2 1 36
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 0.006504 0.003755 0.000000 0.00000
SCALE2 0.000000 0.007510 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007770 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
