HEADER LECTIN 03-AUG-06 2J0H
TITLE L-FICOLIN COMPLEXED TO ACETYL-CHOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FICOLIN-2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: C-TERMINAL BINDING DOMAIN, RESIDUES 96-313;
COMPND 5 SYNONYM: COLLAGEN/FIBRINOGEN DOMAIN-CONTAINING PROTEIN 2, FICOLIN-B,
COMPND 6 FICOLIN B, SERUM LECTIN P35, EBP-37, HUCOLIN, L-FICOLIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS GLYCOPROTEIN, FICRINOGEN-LIKE, INNATE IMMUNITY, PATTERN RECOGNITION
KEYWDS 2 PROTEIN, LECTIN, COLLAGEN, IMMUNOLOGY, LECTIN- LIKE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.GARLATTI,C.GABORIAUD
REVDAT 5 13-DEC-23 2J0H 1 REMARK HETSYN
REVDAT 4 29-JUL-20 2J0H 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 03-APR-19 2J0H 1 SOURCE REMARK LINK
REVDAT 2 24-FEB-09 2J0H 1 VERSN
REVDAT 1 23-JAN-07 2J0H 0
JRNL AUTH V.GARLATTI,N.BELLOY,L.MARTIN,M.LACROIX,M.MATSUSHITA,Y.ENDO,
JRNL AUTH 2 T.FUJITA,J.C.FONTECILLA-CAMPS,G.J.ARLAUD,N.M.THIELENS,
JRNL AUTH 3 C.GABORIAUD
JRNL TITL STRUCTURAL INSIGHTS INTO THE INNATE IMMUNE RECOGNITION
JRNL TITL 2 SPECIFICITIES OF L- AND H-FICOLINS.
JRNL REF EMBO J. V. 26 623 2007
JRNL REFN ISSN 0261-4189
JRNL PMID 17215869
JRNL DOI 10.1038/SJ.EMBOJ.7601500
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31443
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1655
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2428
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10343
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 90
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -1.68000
REMARK 3 B12 (A**2) : 0.56000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.462
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.339
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10735 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14555 ; 1.399 ; 1.921
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1291 ; 6.634 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 573 ;30.861 ;23.682
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1612 ;19.221 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;17.972 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1452 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8511 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5271 ; 0.254 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7046 ; 0.336 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 801 ; 0.211 ; 0.500
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): 42 ; 0.272 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.298 ; 0.500
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): 6450 ; 0.902 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10088 ; 1.524 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4970 ; 1.109 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4467 ; 1.664 ; 4.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 79 A 84 2
REMARK 3 1 B 79 B 84 2
REMARK 3 1 C 79 C 84 2
REMARK 3 1 D 79 D 84 2
REMARK 3 1 E 79 E 84 2
REMARK 3 1 F 79 F 84 2
REMARK 3 2 A 87 A 96 2
REMARK 3 2 B 87 B 96 2
REMARK 3 2 C 87 C 96 2
REMARK 3 2 D 87 D 96 2
REMARK 3 2 E 87 E 96 2
REMARK 3 2 F 87 F 96 2
REMARK 3 3 A 106 A 121 2
REMARK 3 3 B 106 B 121 2
REMARK 3 3 C 106 C 121 2
REMARK 3 3 D 106 D 121 2
REMARK 3 3 E 106 E 121 2
REMARK 3 3 F 106 F 121 2
REMARK 3 4 A 123 A 157 2
REMARK 3 4 B 123 B 157 2
REMARK 3 4 C 123 C 157 2
REMARK 3 4 D 123 D 157 2
REMARK 3 4 E 123 E 157 2
REMARK 3 4 F 123 F 157 2
REMARK 3 5 A 184 A 191 2
REMARK 3 5 B 184 B 191 2
REMARK 3 5 C 184 C 191 2
REMARK 3 5 D 184 D 191 2
REMARK 3 5 E 184 E 191 2
REMARK 3 5 F 184 F 191 2
REMARK 3 6 A 248 A 271 2
REMARK 3 6 B 248 B 271 2
REMARK 3 6 C 248 C 271 2
REMARK 3 6 D 248 D 271 2
REMARK 3 6 E 248 E 271 2
REMARK 3 6 F 248 F 271 2
REMARK 3 7 A 273 A 286 2
REMARK 3 7 B 273 B 286 2
REMARK 3 7 C 273 C 286 2
REMARK 3 7 D 273 D 286 2
REMARK 3 7 E 273 E 286 2
REMARK 3 7 F 273 F 286 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 452 ; .00 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 452 ; .00 ; .05
REMARK 3 TIGHT POSITIONAL 1 C (A): 452 ; .00 ; .05
REMARK 3 TIGHT POSITIONAL 1 D (A): 452 ; .00 ; .05
REMARK 3 TIGHT POSITIONAL 1 E (A): 452 ; .00 ; .05
REMARK 3 TIGHT POSITIONAL 1 F (A): 452 ; .00 ; .05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 433 ; .13 ; .50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 433 ; .12 ; .50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 433 ; .10 ; .50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 433 ; .14 ; .50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 433 ; .12 ; .50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 433 ; .11 ; .50
REMARK 3 TIGHT THERMAL 1 A (A**2): 452 ; .01 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 452 ; .01 ; .50
REMARK 3 TIGHT THERMAL 1 C (A**2): 452 ; .00 ; .50
REMARK 3 TIGHT THERMAL 1 D (A**2): 452 ; .01 ; .50
REMARK 3 TIGHT THERMAL 1 E (A**2): 452 ; .01 ; .50
REMARK 3 TIGHT THERMAL 1 F (A**2): 452 ; .00 ; .50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 433 ; .08 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 433 ; .06 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 433 ; .06 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 433 ; .07 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 433 ; .06 ; 2.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 433 ; .06 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C B E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 224 C 231 2
REMARK 3 1 B 224 B 231 2
REMARK 3 1 E 224 E 231 2
REMARK 3 1 F 224 F 231 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 32 ; .01 ; .05
REMARK 3 TIGHT POSITIONAL 2 B (A): 32 ; .01 ; .05
REMARK 3 TIGHT POSITIONAL 2 E (A): 32 ; .02 ; .05
REMARK 3 TIGHT POSITIONAL 2 F (A): 32 ; .01 ; .05
REMARK 3 MEDIUM POSITIONAL 2 C (A): 27 ; .13 ; .50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 27 ; .09 ; .50
REMARK 3 MEDIUM POSITIONAL 2 E (A): 27 ; .14 ; .50
REMARK 3 MEDIUM POSITIONAL 2 F (A): 27 ; .12 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 32 ; .01 ; .50
REMARK 3 TIGHT THERMAL 2 B (A**2): 32 ; .01 ; .50
REMARK 3 TIGHT THERMAL 2 E (A**2): 32 ; .01 ; .50
REMARK 3 TIGHT THERMAL 2 F (A**2): 32 ; .01 ; .50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 27 ; .07 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 27 ; .07 ; 2.00
REMARK 3 MEDIUM THERMAL 2 E (A**2): 27 ; .06 ; 2.00
REMARK 3 MEDIUM THERMAL 2 F (A**2): 27 ; .06 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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 2J0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029551.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 19.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1JC9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 93.33333
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 46.66667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, 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 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 ASN A 71
REMARK 465 PRO A 72
REMARK 465 CYS A 73
REMARK 465 LEU A 74
REMARK 465 ASN B 71
REMARK 465 ASN C 71
REMARK 465 PRO C 72
REMARK 465 ASN D 71
REMARK 465 PRO D 72
REMARK 465 CYS D 73
REMARK 465 LEU D 74
REMARK 465 ASN F 71
REMARK 465 PRO F 72
REMARK 465 CYS F 73
REMARK 465 LEU F 74
REMARK 465 THR F 75
REMARK 465 GLY F 76
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 78 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 81 CB CG CD CE NZ
REMARK 480 LYS C 186 CB CG CD CE NZ
REMARK 480 ARG D 78 CB CG CD NE CZ NH1 NH2
REMARK 480 GLN D 161 CB CG CD OE1 NE2
REMARK 480 GLU D 192 CB CG CD OE1 OE2
REMARK 480 CYS D 232 CB SG
REMARK 480 ARG D 253 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS E 81 CB CG CD CE NZ
REMARK 480 GLN E 161 CB CG CD OE1 NE2
REMARK 480 LYS F 186 CB CG CD CE 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 ND2 ASN E 215 C2 NAG H 1 2.08
REMARK 500 ND2 ASN B 215 C2 NAG G 1 2.19
REMARK 500 O ASN E 228 O GLY E 230 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS D 232 CA CYS D 232 CB -0.113
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 PRO A 77 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 CYS D 232 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO E 72 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLN E 161 CB - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 ASP E 226 CB - CG - OD1 ANGL. DEV. = 6.0 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 PRO A 77 103.27 -14.00
REMARK 500 ASP A 111 -51.37 -122.46
REMARK 500 VAL A 124 -27.79 -144.63
REMARK 500 ASP A 125 -5.96 -150.08
REMARK 500 LEU A 166 154.65 -48.35
REMARK 500 TYR A 194 26.89 48.68
REMARK 500 VAL A 202 -91.39 -79.68
REMARK 500 SER A 209 44.15 -106.33
REMARK 500 LEU A 210 -30.69 -145.79
REMARK 500 GLN A 237 83.48 57.22
REMARK 500 LYS A 243 -81.55 -113.86
REMARK 500 ASN A 244 59.52 -162.29
REMARK 500 ASN A 249 54.25 -146.35
REMARK 500 ARG A 256 63.16 66.43
REMARK 500 ASP B 111 -52.04 -122.49
REMARK 500 ARG B 122 114.62 -166.38
REMARK 500 VAL B 124 -26.83 -144.95
REMARK 500 ASP B 125 -6.54 -149.82
REMARK 500 ALA B 160 -101.62 -57.26
REMARK 500 TYR B 194 42.81 37.69
REMARK 500 GLU B 203 175.91 165.41
REMARK 500 SER B 209 39.04 -146.61
REMARK 500 LEU B 210 -37.28 -137.36
REMARK 500 THR B 229 -9.44 -47.64
REMARK 500 LYS B 243 -79.14 -123.30
REMARK 500 ASN B 244 44.19 -160.34
REMARK 500 ASN B 249 54.29 -146.17
REMARK 500 ARG B 256 63.31 66.35
REMARK 500 PRO B 287 110.63 -33.33
REMARK 500 LEU C 74 -50.14 60.37
REMARK 500 PRO C 99 -8.75 -53.45
REMARK 500 ASP C 111 -51.26 -122.51
REMARK 500 VAL C 124 -27.08 -145.08
REMARK 500 ASP C 125 -6.38 -150.24
REMARK 500 GLN C 161 48.30 -81.93
REMARK 500 THR C 229 -9.71 -47.32
REMARK 500 PHE C 236 24.11 -142.65
REMARK 500 GLN C 237 65.90 31.11
REMARK 500 LYS C 243 -84.24 -102.15
REMARK 500 ASN C 244 55.37 -152.93
REMARK 500 ASN C 249 54.37 -146.42
REMARK 500 ARG C 256 62.80 67.01
REMARK 500 ASP D 111 -50.93 -122.67
REMARK 500 VAL D 124 -27.25 -144.59
REMARK 500 ASP D 125 -6.45 -149.95
REMARK 500 ASN D 195 130.96 -31.84
REMARK 500 VAL D 202 -82.47 -81.31
REMARK 500 ASP D 226 -140.39 -83.63
REMARK 500 GLN D 237 84.94 53.12
REMARK 500 TRP D 241 54.85 -68.75
REMARK 500
REMARK 500 THIS ENTRY HAS 77 RAMACHANDRAN OUTLIERS.
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 A1289 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 224 OD1
REMARK 620 2 ASP A 224 OD2 48.3
REMARK 620 3 ASP A 226 OD1 75.3 80.5
REMARK 620 4 ASN A 228 O 133.4 118.8 58.1
REMARK 620 5 GLY A 230 O 114.1 69.8 74.5 57.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1290 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 224 OD2
REMARK 620 2 ASP B 224 OD1 44.0
REMARK 620 3 ASP B 226 OD1 85.9 60.4
REMARK 620 4 ASN B 228 O 118.4 132.5 77.0
REMARK 620 5 GLY B 230 O 65.9 93.1 72.7 52.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C1290 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 224 OD1
REMARK 620 2 ASP C 224 OD2 46.5
REMARK 620 3 ASP C 226 OD1 65.1 96.3
REMARK 620 4 ASN C 228 O 128.7 122.3 68.3
REMARK 620 5 GLY C 230 O 93.6 69.4 73.9 52.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D1289 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 224 OD1
REMARK 620 2 ASP D 224 OD2 47.3
REMARK 620 3 ASP D 226 OD1 69.7 98.6
REMARK 620 4 ASN D 228 O 131.6 165.2 70.4
REMARK 620 5 GLY D 230 O 135.2 93.6 102.8 79.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1290 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 224 OD1
REMARK 620 2 ASP E 224 OD2 42.9
REMARK 620 3 ASP E 226 OD1 56.7 85.6
REMARK 620 4 ASN E 228 O 122.4 117.6 70.6
REMARK 620 5 GLY E 230 O 88.5 68.3 69.0 49.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F1290 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 224 OD2
REMARK 620 2 ASP F 224 OD1 47.1
REMARK 620 3 ASP F 226 OD1 96.5 68.2
REMARK 620 4 ASN F 228 O 114.7 132.3 72.6
REMARK 620 5 GLY F 230 O 66.0 93.5 73.4 49.0
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2J0G RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-MANNOSAMINE
REMARK 900 RELATED ID: 2J0Y RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO B-1,3-D-GLUCAN
REMARK 900 RELATED ID: 2J1G RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN
REMARK 900 RELATED ID: 2J2P RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-CYSTEIN ( 150MM)
REMARK 900 RELATED ID: 2J3F RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-D- GALACTOSAMIN
REMARK 900 RELATED ID: 2J3G RELATED DB: PDB
REMARK 900 L-FICOLIN
REMARK 900 RELATED ID: 2J3O RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-D- GLUCOSAMIN
REMARK 900 RELATED ID: 2J3U RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO GALACTOSE
REMARK 900 RELATED ID: 2J61 RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYLGLUCOSAMINE ( FORME C)
DBREF 2J0H A 71 288 UNP Q15485 FCN2_HUMAN 96 313
DBREF 2J0H B 71 288 UNP Q15485 FCN2_HUMAN 96 313
DBREF 2J0H C 71 288 UNP Q15485 FCN2_HUMAN 96 313
DBREF 2J0H D 71 288 UNP Q15485 FCN2_HUMAN 96 313
DBREF 2J0H E 71 288 UNP Q15485 FCN2_HUMAN 96 313
DBREF 2J0H F 71 288 UNP Q15485 FCN2_HUMAN 96 313
SEQADV 2J0H THR A 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR A 247 UNP Q15485 VAL 272 CONFLICT
SEQADV 2J0H THR B 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR B 247 UNP Q15485 VAL 272 CONFLICT
SEQADV 2J0H THR C 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR C 247 UNP Q15485 VAL 272 CONFLICT
SEQADV 2J0H THR D 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR D 247 UNP Q15485 VAL 272 CONFLICT
SEQADV 2J0H ASN E 71 UNP Q15485 GLN 96 CONFLICT
SEQADV 2J0H THR E 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR E 247 UNP Q15485 VAL 272 CONFLICT
SEQADV 2J0H THR F 168 UNP Q15485 VAL 193 CONFLICT
SEQADV 2J0H THR F 247 UNP Q15485 VAL 272 CONFLICT
SEQRES 1 A 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 A 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 A 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 A 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 A 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 A 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 A 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 A 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 A 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 A 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 A 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 A 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 A 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 A 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 A 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 A 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 A 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 B 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 B 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 B 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 B 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 B 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 B 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 B 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 B 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 B 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 B 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 B 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 B 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 B 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 B 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 B 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 B 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 B 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 C 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 C 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 C 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 C 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 C 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 C 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 C 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 C 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 C 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 C 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 C 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 C 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 C 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 C 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 C 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 C 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 C 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 D 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 D 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 D 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 D 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 D 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 D 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 D 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 D 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 D 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 D 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 D 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 D 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 D 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 D 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 D 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 D 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 D 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 E 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 E 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 E 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 E 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 E 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 E 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 E 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 E 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 E 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 E 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 E 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 E 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 E 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 E 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 E 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 E 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 E 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 F 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 F 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 F 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 F 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 F 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 F 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 F 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 F 218 GLY THR SER GLU LEU ARG THR ASP LEU VAL ASP PHE GLU
SEQRES 9 F 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 F 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 F 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 F 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 F 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 F 218 TRP TRP TYR LYS ASN CYS HIS THR SER ASN LEU ASN GLY
SEQRES 15 F 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 F 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 F 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
MODRES 2J0H ASN B 215 ASN GLYCOSYLATION SITE
MODRES 2J0H ASN E 215 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET NAG H 1 14
HET NAG H 2 14
HET CA A1289 1
HET ACH A1290 10
HET ACH B1289 10
HET CA B1290 1
HET ACH C1289 10
HET CA C1290 1
HET CA D1289 1
HET ACH E1289 10
HET CA E1290 1
HET ACH F1289 10
HET CA F1290 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM ACH ACETYLCHOLINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 7 NAG 4(C8 H15 N O6)
FORMUL 7 BMA C6 H12 O6
FORMUL 9 CA 6(CA 2+)
FORMUL 10 ACH 5(C7 H16 N O2 1+)
FORMUL 20 HOH *90(H2 O)
HELIX 1 1 THR A 79 ARG A 86 1 8
HELIX 2 2 ASP A 111 GLY A 115 5 5
HELIX 3 3 ASP A 133 GLY A 140 1 8
HELIX 4 4 GLY A 151 GLN A 161 1 11
HELIX 5 5 ASP A 189 LYS A 193 5 5
HELIX 6 6 LEU A 210 ASN A 214 5 5
HELIX 7 7 ASN A 231 GLN A 237 1 7
HELIX 8 8 THR B 79 ARG B 86 1 8
HELIX 9 9 ASP B 111 GLY B 115 5 5
HELIX 10 10 ASP B 133 GLY B 140 1 8
HELIX 11 11 GLY B 151 ALA B 160 1 10
HELIX 12 12 ASP B 189 LYS B 193 5 5
HELIX 13 13 LEU B 210 ASN B 214 5 5
HELIX 14 14 ASN B 231 PHE B 236 1 6
HELIX 15 15 THR C 79 ARG C 86 1 8
HELIX 16 16 ASP C 111 GLY C 115 5 5
HELIX 17 17 ASP C 133 GLY C 140 1 8
HELIX 18 18 GLY C 151 ALA C 160 1 10
HELIX 19 19 ASP C 189 LYS C 193 5 5
HELIX 20 20 LEU C 210 ASN C 214 5 5
HELIX 21 21 ASN C 231 PHE C 236 1 6
HELIX 22 22 THR D 79 ARG D 86 1 8
HELIX 23 23 ASP D 111 GLY D 115 5 5
HELIX 24 24 ASP D 133 GLY D 140 1 8
HELIX 25 25 GLY D 151 GLN D 161 1 11
HELIX 26 26 LEU D 210 ASN D 214 5 5
HELIX 27 27 ASN D 231 GLN D 237 1 7
HELIX 28 28 ASN E 71 GLY E 76 1 6
HELIX 29 29 THR E 79 ARG E 86 1 8
HELIX 30 30 ASP E 111 GLY E 115 5 5
HELIX 31 31 ASP E 133 GLY E 140 1 8
HELIX 32 32 GLY E 151 ALA E 160 1 10
HELIX 33 33 ASP E 189 LYS E 193 5 5
HELIX 34 34 LEU E 210 ASN E 214 5 5
HELIX 35 35 ASN E 231 PHE E 236 1 6
HELIX 36 36 THR F 79 ARG F 86 1 8
HELIX 37 37 ASP F 111 GLY F 115 5 5
HELIX 38 38 ASP F 133 GLY F 140 1 8
HELIX 39 39 GLY F 151 ALA F 160 1 10
HELIX 40 40 ASP F 189 LYS F 193 5 5
HELIX 41 41 LEU F 210 ASN F 214 5 5
HELIX 42 42 ASN F 231 PHE F 236 1 6
SHEET 1 AA 6 GLY A 92 TYR A 97 0
SHEET 2 AA 6 PRO A 103 ASP A 109 -1 O LEU A 104 N ILE A 96
SHEET 3 AA 6 TRP A 117 ARG A 123 -1 O TRP A 117 N ASP A 109
SHEET 4 AA 6 VAL A 280 VAL A 285 -1 O SER A 281 N ARG A 123
SHEET 5 AA 6 ARG A 167 VAL A 171 -1 O ARG A 167 N LYS A 284
SHEET 6 AA 6 TYR A 177 LYS A 181 -1 O GLN A 178 N LEU A 170
SHEET 1 AB 5 GLY A 92 TYR A 97 0
SHEET 2 AB 5 PRO A 103 ASP A 109 -1 O LEU A 104 N ILE A 96
SHEET 3 AB 5 TRP A 117 ARG A 123 -1 O TRP A 117 N ASP A 109
SHEET 4 AB 5 PHE A 148 TRP A 149 -1 O PHE A 148 N ARG A 122
SHEET 5 AB 5 PHE A 141 GLY A 142 -1 O PHE A 141 N TRP A 149
SHEET 1 AC 2 PHE A 185 VAL A 187 0
SHEET 2 AC 2 LEU A 196 LEU A 198 -1 O VAL A 197 N LYS A 186
SHEET 1 AD 2 GLY A 257 THR A 258 0
SHEET 2 AD 2 TYR A 276 SER A 277 -1 O SER A 277 N GLY A 257
SHEET 1 BA 6 GLY B 92 TYR B 97 0
SHEET 2 BA 6 PRO B 103 ASP B 109 -1 O LEU B 104 N ILE B 96
SHEET 3 BA 6 TRP B 117 ARG B 123 -1 O TRP B 117 N ASP B 109
SHEET 4 BA 6 VAL B 280 PRO B 287 -1 O SER B 281 N ARG B 123
SHEET 5 BA 6 SER B 164 VAL B 171 -1 O GLU B 165 N ARG B 286
SHEET 6 BA 6 TYR B 177 VAL B 187 -1 O GLN B 178 N LEU B 170
SHEET 1 BB 5 GLY B 92 TYR B 97 0
SHEET 2 BB 5 PRO B 103 ASP B 109 -1 O LEU B 104 N ILE B 96
SHEET 3 BB 5 TRP B 117 ARG B 123 -1 O TRP B 117 N ASP B 109
SHEET 4 BB 5 PHE B 148 TRP B 149 -1 O PHE B 148 N ARG B 122
SHEET 5 BB 5 PHE B 141 GLY B 142 -1 O PHE B 141 N TRP B 149
SHEET 1 BC 2 GLY B 257 THR B 258 0
SHEET 2 BC 2 TYR B 276 SER B 277 -1 O SER B 277 N GLY B 257
SHEET 1 CA 7 GLY C 92 TYR C 97 0
SHEET 2 CA 7 PRO C 103 ASP C 109 -1 O LEU C 104 N ILE C 96
SHEET 3 CA 7 TRP C 117 ARG C 123 -1 O TRP C 117 N ASP C 109
SHEET 4 CA 7 VAL C 280 PRO C 287 -1 O SER C 281 N ARG C 123
SHEET 5 CA 7 SER C 164 VAL C 171 -1 O GLU C 165 N ARG C 286
SHEET 6 CA 7 TYR C 177 TYR C 182 -1 O GLN C 178 N LEU C 170
SHEET 7 CA 7 PHE C 201 GLU C 203 -1 N VAL C 202 O LYS C 181
SHEET 1 CB 5 GLY C 92 TYR C 97 0
SHEET 2 CB 5 PRO C 103 ASP C 109 -1 O LEU C 104 N ILE C 96
SHEET 3 CB 5 TRP C 117 ARG C 123 -1 O TRP C 117 N ASP C 109
SHEET 4 CB 5 PHE C 148 TRP C 149 -1 O PHE C 148 N ARG C 122
SHEET 5 CB 5 PHE C 141 GLY C 142 -1 O PHE C 141 N TRP C 149
SHEET 1 CC 2 PHE C 185 VAL C 187 0
SHEET 2 CC 2 LEU C 196 LEU C 198 -1 O VAL C 197 N LYS C 186
SHEET 1 CD 2 GLY C 257 THR C 258 0
SHEET 2 CD 2 TYR C 276 SER C 277 -1 O SER C 277 N GLY C 257
SHEET 1 DA10 GLY D 92 LEU D 98 0
SHEET 2 DA10 ARG D 102 ASP D 109 -1 O ARG D 102 N LEU D 98
SHEET 3 DA10 TRP D 117 ARG D 123 -1 O TRP D 117 N ASP D 109
SHEET 4 DA10 PHE D 141 GLY D 142 0
SHEET 5 DA10 PHE D 148 TRP D 149 -1 O TRP D 149 N PHE D 141
SHEET 6 DA10 TRP D 117 ARG D 123 -1 O ARG D 122 N PHE D 148
SHEET 7 DA10 TYR D 177 LYS D 181 0
SHEET 8 DA10 SER D 164 VAL D 171 -1 O THR D 168 N ALA D 180
SHEET 9 DA10 VAL D 280 PRO D 287 -1 O VAL D 280 N VAL D 171
SHEET 10 DA10 TRP D 117 ARG D 123 -1 O THR D 118 N VAL D 285
SHEET 1 DB 2 PHE D 185 VAL D 187 0
SHEET 2 DB 2 LEU D 196 LEU D 198 -1 O VAL D 197 N LYS D 186
SHEET 1 DC 2 GLY D 257 THR D 258 0
SHEET 2 DC 2 TYR D 276 SER D 277 -1 O SER D 277 N GLY D 257
SHEET 1 EA11 GLY E 92 TYR E 97 0
SHEET 2 EA11 PRO E 103 ASP E 109 -1 O LEU E 104 N ILE E 96
SHEET 3 EA11 TRP E 117 ARG E 123 -1 O TRP E 117 N ASP E 109
SHEET 4 EA11 PHE E 141 GLY E 142 0
SHEET 5 EA11 PHE E 148 TRP E 149 -1 O TRP E 149 N PHE E 141
SHEET 6 EA11 TRP E 117 ARG E 123 -1 O ARG E 122 N PHE E 148
SHEET 7 EA11 PHE E 201 GLU E 203 0
SHEET 8 EA11 TYR E 177 TYR E 182 -1 O LYS E 181 N VAL E 202
SHEET 9 EA11 GLU E 165 VAL E 171 -1 O LEU E 166 N TYR E 182
SHEET 10 EA11 VAL E 280 ARG E 286 -1 O VAL E 280 N VAL E 171
SHEET 11 EA11 TRP E 117 ARG E 123 -1 O THR E 118 N VAL E 285
SHEET 1 EB 2 PHE E 185 VAL E 187 0
SHEET 2 EB 2 LEU E 196 LEU E 198 -1 O VAL E 197 N LYS E 186
SHEET 1 EC 2 GLY E 257 THR E 258 0
SHEET 2 EC 2 TYR E 276 SER E 277 -1 O SER E 277 N GLY E 257
SHEET 1 FA11 GLY F 92 TYR F 97 0
SHEET 2 FA11 PRO F 103 ASP F 109 -1 O LEU F 104 N ILE F 96
SHEET 3 FA11 TRP F 117 ARG F 123 -1 O TRP F 117 N ASP F 109
SHEET 4 FA11 PHE F 141 GLY F 142 0
SHEET 5 FA11 PHE F 148 TRP F 149 -1 O TRP F 149 N PHE F 141
SHEET 6 FA11 TRP F 117 ARG F 123 -1 O ARG F 122 N PHE F 148
SHEET 7 FA11 PHE F 201 GLU F 203 0
SHEET 8 FA11 TYR F 177 TYR F 182 -1 O LYS F 181 N VAL F 202
SHEET 9 FA11 SER F 164 VAL F 171 -1 O LEU F 166 N TYR F 182
SHEET 10 FA11 VAL F 280 PRO F 287 -1 O VAL F 280 N VAL F 171
SHEET 11 FA11 TRP F 117 ARG F 123 -1 O THR F 118 N VAL F 285
SHEET 1 FB 2 PHE F 185 VAL F 187 0
SHEET 2 FB 2 LEU F 196 LEU F 198 -1 O VAL F 197 N LYS F 186
SHEET 1 FC 2 GLY F 257 THR F 258 0
SHEET 2 FC 2 TYR F 276 SER F 277 -1 O SER F 277 N GLY F 257
SSBOND 1 CYS A 80 CYS A 108 1555 1555 2.05
SSBOND 2 CYS A 232 CYS A 245 1555 1555 2.06
SSBOND 3 CYS B 73 CYS B 101 1555 1555 2.06
SSBOND 4 CYS B 80 CYS B 108 1555 1555 2.04
SSBOND 5 CYS B 232 CYS B 245 1555 1555 2.03
SSBOND 6 CYS C 73 CYS C 101 1555 1555 2.05
SSBOND 7 CYS C 80 CYS C 108 1555 1555 2.03
SSBOND 8 CYS C 232 CYS C 245 1555 1555 2.06
SSBOND 9 CYS D 80 CYS D 108 1555 1555 2.05
SSBOND 10 CYS D 232 CYS D 245 1555 1555 1.47
SSBOND 11 CYS E 73 CYS E 101 1555 1555 2.04
SSBOND 12 CYS E 80 CYS E 108 1555 1555 2.04
SSBOND 13 CYS E 232 CYS E 245 1555 1555 2.03
SSBOND 14 CYS F 80 CYS F 108 1555 1555 2.03
SSBOND 15 CYS F 232 CYS F 245 1555 1555 2.04
LINK ND2 ASN B 215 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN E 215 C1 NAG H 1 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.46
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK OD1 ASP A 224 CA CA A1289 1555 1555 2.74
LINK OD2 ASP A 224 CA CA A1289 1555 1555 2.61
LINK OD1 ASP A 226 CA CA A1289 1555 1555 2.88
LINK O ASN A 228 CA CA A1289 1555 1555 2.35
LINK O GLY A 230 CA CA A1289 1555 1555 2.88
LINK OD2 ASP B 224 CA CA B1290 1555 1555 2.90
LINK OD1 ASP B 224 CA CA B1290 1555 1555 2.85
LINK OD1 ASP B 226 CA CA B1290 1555 1555 2.53
LINK O ASN B 228 CA CA B1290 1555 1555 2.30
LINK O GLY B 230 CA CA B1290 1555 1555 2.70
LINK OD1 ASP C 224 CA CA C1290 1555 1555 2.86
LINK OD2 ASP C 224 CA CA C1290 1555 1555 2.73
LINK OD1 ASP C 226 CA CA C1290 1555 1555 2.80
LINK O ASN C 228 CA CA C1290 1555 1555 2.35
LINK O GLY C 230 CA CA C1290 1555 1555 2.60
LINK OD1 ASP D 224 CA CA D1289 1555 1555 2.95
LINK OD2 ASP D 224 CA CA D1289 1555 1555 2.31
LINK OD1 ASP D 226 CA CA D1289 1555 1555 2.71
LINK O ASN D 228 CA CA D1289 1555 1555 2.31
LINK O GLY D 230 CA CA D1289 1555 1555 2.42
LINK OD1 ASP E 224 CA CA E1290 1555 1555 3.11
LINK OD2 ASP E 224 CA CA E1290 1555 1555 2.83
LINK OD1 ASP E 226 CA CA E1290 1555 1555 2.66
LINK O ASN E 228 CA CA E1290 1555 1555 2.47
LINK O GLY E 230 CA CA E1290 1555 1555 2.74
LINK OD2 ASP F 224 CA CA F1290 1555 1555 2.80
LINK OD1 ASP F 224 CA CA F1290 1555 1555 2.78
LINK OD1 ASP F 226 CA CA F1290 1555 1555 2.59
LINK O ASN F 228 CA CA F1290 1555 1555 2.44
LINK O GLY F 230 CA CA F1290 1555 1555 2.81
CISPEP 1 ASN A 244 CYS A 245 0 -0.88
CISPEP 2 ASN B 244 CYS B 245 0 2.71
CISPEP 3 ASN C 244 CYS C 245 0 -5.08
CISPEP 4 ASN D 244 CYS D 245 0 -3.15
CISPEP 5 ASN E 244 CYS E 245 0 8.12
CISPEP 6 ASN F 244 CYS F 245 0 -3.69
CRYST1 97.060 97.060 140.000 90.00 90.00 120.00 P 32 18
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 0.010303 0.005948 0.000000 0.00000
SCALE2 0.000000 0.011897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007143 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
