HEADER VIRAL PROTEIN/IMMUNE SYSTEM 12-AUG-09 3INB
TITLE STRUCTURE OF THE MEASLES VIRUS HEMAGGLUTININ BOUND TO THE CD46
TITLE 2 RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMAGGLUTININ GLYCOPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEAD DOMAIN, RESIDUES 179-617;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MEMBRANE COFACTOR PROTEIN;
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: SUSHI DOMAINS 1 AND 2, RESIDUES 35-160;
COMPND 10 SYNONYM: TROPHOBLAST LEUKOCYTE COMMON ANTIGEN, TLX;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEASLES VIRUS STRAIN EDMONSTON;
SOURCE 3 ORGANISM_COMMON: VIRUSES;
SOURCE 4 ORGANISM_TAXID: 11235;
SOURCE 5 STRAIN: EDMONSTON;
SOURCE 6 GENE: H;
SOURCE 7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: CHO-LEC 3281;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: CD46, MCP, MIC10;
SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: CHO-LEC 3281;
SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PBJ5-GS
KEYWDS MEASLES, BETA PROPELLER, ENVELOPE PROTEIN, HEMAGGLUTININ, VIRAL
KEYWDS 2 PROTEIN. MEMBRANE COFACTOR PROTEIN, MCP, CD46, VIRUS RECEPTOR
KEYWDS 3 COMPLEX, SCR, COMPLEMENT CONTROL PROTEIN, IMMUNE SYSTEM COMPLEX,
KEYWDS 4 MEMBRANE, TRANSMEMBRANE, VIRION, CELL MEMBRANE, GLYCOPROTEIN, HOST-
KEYWDS 5 VIRUS INTERACTION, SIGNAL-ANCHOR, COMPLEMENT PATHWAY, DISEASE
KEYWDS 6 MUTATION, DISULFIDE BOND, FERTILIZATION, IMMUNE RESPONSE, INNATE
KEYWDS 7 IMMUNITY, PHOSPHOPROTEIN, SUSHI, VIRAL PROTEIN, IMMUNE SYSTEM, VIRAL
KEYWDS 8 PROTEIN-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SANTIAGO,M.L.CELMA,T.STEHLE,J.M.CASASNOVAS
REVDAT 6 06-SEP-23 3INB 1 REMARK
REVDAT 5 13-OCT-21 3INB 1 SEQADV HETSYN
REVDAT 4 29-JUL-20 3INB 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 13-JUL-11 3INB 1 VERSN
REVDAT 2 19-JAN-10 3INB 1 JRNL
REVDAT 1 22-DEC-09 3INB 0
JRNL AUTH C.SANTIAGO,M.L.CELMA,T.STEHLE,J.M.CASASNOVAS
JRNL TITL STRUCTURE OF THE MEASLES VIRUS HEMAGGLUTININ BOUND TO THE
JRNL TITL 2 CD46 RECEPTOR
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 124 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20010840
JRNL DOI 10.1038/NSMB.1726
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 31869
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1588
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 14.9762 - 6.7018 0.95 2874 147 0.1964 0.2195
REMARK 3 2 6.7018 - 5.4011 0.96 2807 159 0.1992 0.2415
REMARK 3 3 5.4011 - 4.7432 0.96 2774 137 0.1720 0.2028
REMARK 3 4 4.7432 - 4.3209 0.96 2772 146 0.1747 0.2435
REMARK 3 5 4.3209 - 4.0177 0.96 2762 134 0.2044 0.2395
REMARK 3 6 4.0177 - 3.7848 0.96 2707 166 0.2366 0.2562
REMARK 3 7 3.7848 - 3.5980 0.96 2731 137 0.2746 0.2937
REMARK 3 8 3.5980 - 3.4434 0.96 2732 148 0.2880 0.3504
REMARK 3 9 3.4434 - 3.3123 0.96 2706 140 0.3284 0.3292
REMARK 3 10 3.3123 - 3.1991 0.96 2710 126 0.3694 0.4041
REMARK 3 11 3.1991 - 3.1000 0.96 2706 148 0.4083 0.4465
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.26
REMARK 3 B_SOL : 80.68
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 101.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 56.34380
REMARK 3 B22 (A**2) : -40.09220
REMARK 3 B33 (A**2) : -16.25160
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 8588
REMARK 3 ANGLE : 1.497 11673
REMARK 3 CHIRALITY : 0.112 1287
REMARK 3 PLANARITY : 0.008 1473
REMARK 3 DIHEDRAL : 26.624 5144
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9447 59.8731 29.0226
REMARK 3 T TENSOR
REMARK 3 T11: 0.6063 T22: 0.6838
REMARK 3 T33: 0.3920 T12: 0.3106
REMARK 3 T13: -0.2406 T23: 0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 4.3477 L22: 9.0793
REMARK 3 L33: 2.9049 L12: -3.0623
REMARK 3 L13: -1.9540 L23: 1.0948
REMARK 3 S TENSOR
REMARK 3 S11: 0.7408 S12: 0.7549 S13: 0.0134
REMARK 3 S21: -2.7767 S22: -0.6039 S23: 1.0231
REMARK 3 S31: -0.1844 S32: -0.4868 S33: 0.0180
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D AND (RESSEQ 65:126 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 65:126 )
REMARK 3 ATOM PAIRS NUMBER : 491
REMARK 3 RMSD : 0.080
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 201:238 OR RESSEQ
REMARK 3 250:262 OR RESSEQ 264:309 OR RESSEQ 317:
REMARK 3 340 OR RESSEQ 344:351 OR RESSEQ 353:372
REMARK 3 OR RESSEQ 374:388 OR RESSEQ 391 OR RESSEQ
REMARK 3 393:395 OR RESSEQ 397:419 OR RESSEQ 422:
REMARK 3 458 OR RESSEQ 461 OR RESSEQ 465:487 OR
REMARK 3 RESSEQ 493:499 OR RESSEQ 509:528 OR
REMARK 3 RESSEQ 536:554 OR RESSEQ 564:585 OR
REMARK 3 RESSEQ 594:602 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 201:238 OR RESSEQ
REMARK 3 250:262 OR RESSEQ 264:309 OR RESSEQ 317:
REMARK 3 340 OR RESSEQ 344:351 OR RESSEQ 353:372
REMARK 3 OR RESSEQ 374:388 OR RESSEQ 391 OR RESSEQ
REMARK 3 393:395 OR RESSEQ 397:419 OR RESSEQ 422:
REMARK 3 458 OR RESSEQ 461 OR RESSEQ 465:487 OR
REMARK 3 RESSEQ 493:499 OR RESSEQ 509:528 OR
REMARK 3 RESSEQ 536:554 OR RESSEQ 564:585 OR
REMARK 3 RESSEQ 594:602 )
REMARK 3 ATOM PAIRS NUMBER : 2600
REMARK 3 RMSD : 0.046
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3INB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.845
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33285
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: PDB ENTRIES 2ZB6, 1CKL, AND 2O39
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG-8000, 0.2 M AMMONIUM SULPHATE
REMARK 280 2% PEG-400, 1% 1,2,3 HEPTANETRIOL, 1 MM SODIUM TUNGSTATE, 0.1 M
REMARK 280 MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.35500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.35500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 TYR A 152
REMARK 465 PRO A 153
REMARK 465 TYR A 154
REMARK 465 ASP A 155
REMARK 465 VAL A 156
REMARK 465 PRO A 157
REMARK 465 ASP A 158
REMARK 465 TYR A 159
REMARK 465 ALA A 160
REMARK 465 GLY A 161
REMARK 465 ALA A 162
REMARK 465 GLN A 163
REMARK 465 PRO A 164
REMARK 465 ALA A 165
REMARK 465 ARG A 166
REMARK 465 SER A 167
REMARK 465 PRO A 168
REMARK 465 GLY A 169
REMARK 465 ILE A 170
REMARK 465 ARG A 171
REMARK 465 GLY A 172
REMARK 465 LEU A 173
REMARK 465 VAL A 174
REMARK 465 PRO A 175
REMARK 465 ARG A 176
REMARK 465 GLY A 177
REMARK 465 SER A 178
REMARK 465 GLN A 179
REMARK 465 PHE A 180
REMARK 465 LEU A 181
REMARK 465 ALA A 182
REMARK 465 VAL A 183
REMARK 465 SER A 184
REMARK 465 LYS A 185
REMARK 465 GLY A 186
REMARK 465 ASN A 187
REMARK 465 CYS A 188
REMARK 465 SER A 189
REMARK 465 GLY A 190
REMARK 465 PRO A 191
REMARK 465 THR A 192
REMARK 465 SER A 240
REMARK 465 SER A 241
REMARK 465 LYS A 242
REMARK 465 ARG A 243
REMARK 465 SER A 244
REMARK 465 GLU A 245
REMARK 465 LEU A 246
REMARK 465 SER A 247
REMARK 465 GLN A 248
REMARK 465 LEU A 249
REMARK 465 GLN A 311
REMARK 465 GLY A 312
REMARK 465 SER A 313
REMARK 465 GLY A 314
REMARK 465 LYS A 315
REMARK 465 VAL A 508
REMARK 465 ASP A 587
REMARK 465 SER A 588
REMARK 465 GLU A 589
REMARK 465 SER A 590
REMARK 465 GLY A 591
REMARK 465 GLY A 603
REMARK 465 VAL A 604
REMARK 465 SER A 605
REMARK 465 CYS A 606
REMARK 465 THR A 607
REMARK 465 VAL A 608
REMARK 465 THR A 609
REMARK 465 ARG A 610
REMARK 465 GLU A 611
REMARK 465 ASP A 612
REMARK 465 GLY A 613
REMARK 465 THR A 614
REMARK 465 ASN A 615
REMARK 465 ARG A 616
REMARK 465 ARG A 617
REMARK 465 TYR B 152
REMARK 465 PRO B 153
REMARK 465 TYR B 154
REMARK 465 ASP B 155
REMARK 465 VAL B 156
REMARK 465 PRO B 157
REMARK 465 ASP B 158
REMARK 465 TYR B 159
REMARK 465 ALA B 160
REMARK 465 GLY B 161
REMARK 465 ALA B 162
REMARK 465 GLN B 163
REMARK 465 PRO B 164
REMARK 465 ALA B 165
REMARK 465 ARG B 166
REMARK 465 SER B 167
REMARK 465 PRO B 168
REMARK 465 GLY B 169
REMARK 465 ILE B 170
REMARK 465 ARG B 171
REMARK 465 GLY B 172
REMARK 465 LEU B 173
REMARK 465 VAL B 174
REMARK 465 PRO B 175
REMARK 465 ARG B 176
REMARK 465 GLY B 177
REMARK 465 SER B 178
REMARK 465 GLN B 179
REMARK 465 PHE B 180
REMARK 465 LEU B 181
REMARK 465 ALA B 182
REMARK 465 VAL B 183
REMARK 465 SER B 240
REMARK 465 SER B 241
REMARK 465 LYS B 242
REMARK 465 ARG B 243
REMARK 465 SER B 244
REMARK 465 GLU B 245
REMARK 465 LEU B 246
REMARK 465 SER B 247
REMARK 465 GLN B 311
REMARK 465 GLY B 312
REMARK 465 SER B 313
REMARK 465 GLY B 314
REMARK 465 LYS B 315
REMARK 465 VAL B 508
REMARK 465 SER B 588
REMARK 465 GLU B 589
REMARK 465 SER B 590
REMARK 465 GLY B 591
REMARK 465 GLY B 592
REMARK 465 HIS B 593
REMARK 465 THR B 607
REMARK 465 VAL B 608
REMARK 465 THR B 609
REMARK 465 ARG B 610
REMARK 465 GLU B 611
REMARK 465 ASP B 612
REMARK 465 GLY B 613
REMARK 465 THR B 614
REMARK 465 ASN B 615
REMARK 465 ARG B 616
REMARK 465 ARG B 617
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 PHE A 555 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 556 CG CD NE CZ NH1 NH2
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 SG CYS A 386 CB CYS A 394 1.74
REMARK 500 SG CYS B 386 CB CYS B 394 1.79
REMARK 500 ND2 ASN A 215 C2 NAG A 1215 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 265 CA - CB - CG ANGL. DEV. = 20.6 DEGREES
REMARK 500 PRO A 397 C - N - CA ANGL. DEV. = 16.8 DEGREES
REMARK 500 PRO A 397 C - N - CD ANGL. DEV. = -16.1 DEGREES
REMARK 500 ASP B 343 N - CA - C ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO B 344 C - N - CA ANGL. DEV. = 12.1 DEGREES
REMARK 500 PRO C 4 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG C 69 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 69 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 PRO D 4 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG D 69 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG D 69 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 194 -174.55 49.37
REMARK 500 ARG A 195 162.43 167.39
REMARK 500 GLN A 197 133.60 -178.67
REMARK 500 SER A 202 137.01 -175.35
REMARK 500 LEU A 203 42.20 -95.25
REMARK 500 LEU A 210 -74.40 -59.31
REMARK 500 SER A 224 128.24 159.88
REMARK 500 PRO A 263 12.77 -67.82
REMARK 500 ASN A 282 -169.95 -177.89
REMARK 500 LEU A 284 -0.59 -143.79
REMARK 500 GLU A 303 -168.20 82.35
REMARK 500 ASP A 304 -2.86 -147.51
REMARK 500 PRO A 309 -148.77 -84.68
REMARK 500 PRO A 330 -1.27 -58.99
REMARK 500 SER A 335 149.81 178.11
REMARK 500 ASP A 343 55.68 80.04
REMARK 500 PRO A 344 16.95 -59.23
REMARK 500 ASP A 347 -61.36 -108.41
REMARK 500 SER A 352 -128.51 -147.78
REMARK 500 MET A 378 -9.56 -143.23
REMARK 500 PHE A 382 -88.50 -69.61
REMARK 500 ILE A 390 10.67 -171.74
REMARK 500 GLN A 391 -65.97 24.16
REMARK 500 THR A 392 -73.82 -41.61
REMARK 500 GLU A 395 39.37 -157.64
REMARK 500 ASN A 396 92.36 -165.94
REMARK 500 PRO A 397 162.82 -29.28
REMARK 500 GLU A 398 -4.94 -162.42
REMARK 500 ASP A 404 38.06 -89.70
REMARK 500 ASN A 405 34.45 27.44
REMARK 500 LEU A 419 67.53 -65.53
REMARK 500 THR A 420 -153.08 -142.69
REMARK 500 VAL A 421 12.36 58.41
REMARK 500 LEU A 423 130.41 -38.53
REMARK 500 PRO A 433 104.62 -49.24
REMARK 500 LEU A 434 125.08 -37.65
REMARK 500 THR A 436 -6.04 -147.73
REMARK 500 MET A 441 96.47 -171.47
REMARK 500 MET A 459 89.23 -65.71
REMARK 500 ASN A 461 -22.43 79.58
REMARK 500 LEU A 462 -85.73 -90.29
REMARK 500 TRP A 472 -1.71 -145.94
REMARK 500 TYR A 481 -14.77 -156.47
REMARK 500 LYS A 488 -25.71 -35.99
REMARK 500 GLU A 489 5.99 -59.65
REMARK 500 GLU A 492 -6.42 64.56
REMARK 500 CYS A 494 126.63 -177.87
REMARK 500 THR A 498 95.71 -66.58
REMARK 500 GLU A 503 31.48 -96.34
REMARK 500 ASP A 505 37.23 -56.73
REMARK 500
REMARK 500 THIS ENTRY HAS 186 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 341 ASP A 342 143.44
REMARK 500 ASP A 342 ASP A 343 -139.70
REMARK 500 ILE A 473 PRO A 474 142.60
REMARK 500 TYR A 529 ASP A 530 145.71
REMARK 500 LEU A 557 PRO A 558 133.14
REMARK 500 ASP B 342 ASP B 343 -130.69
REMARK 500 ILE B 473 PRO B 474 142.20
REMARK 500 LEU B 557 PRO B 558 -148.92
REMARK 500 ARG C 48 ASN C 49 -148.79
REMARK 500 PRO C 54 VAL C 55 -109.11
REMARK 500 ARG D 25 VAL D 26 -145.21
REMARK 500 LEU D 53 PRO D 54 -128.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RKC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MEASLES VIRUS HEMAGGLUTININ
REMARK 900 RELATED ID: 2ZB5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MEASLES VIRUS HEMAGGLUTININ (COMPLEX-SUGAR-
REMARK 900 TYPE)
REMARK 900 RELATED ID: 2ZB6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MEASLES VIRUS HEMAGGLUTININ (OLIGO-SUGAR
REMARK 900 TYPE)
REMARK 900 RELATED ID: 1CKL RELATED DB: PDB
REMARK 900 N-TERMINAL TWO DOMAINS OF HUMAN CD46 (MEMBRANE COFACTOR PROTEIN,MCP)
REMARK 900 RELATED ID: 2O39 RELATED DB: PDB
REMARK 900 HUMAN ADENOVIRUS TYPE 11 KNOB IN COMPLEX WITH DOMAINS SCR1 AND SCR2
REMARK 900 OF CD46 (MEMBRANE COFACTOR PROTEIN, MCP)
DBREF 3INB A 179 617 UNP P08362 HEMA_MEASE 179 617
DBREF 3INB B 179 617 UNP P08362 HEMA_MEASE 179 617
DBREF 3INB C 1 126 UNP P15529 MCP_HUMAN 35 160
DBREF 3INB D 1 126 UNP P15529 MCP_HUMAN 35 160
SEQADV 3INB TYR A 152 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO A 153 UNP P08362 EXPRESSION TAG
SEQADV 3INB TYR A 154 UNP P08362 EXPRESSION TAG
SEQADV 3INB ASP A 155 UNP P08362 EXPRESSION TAG
SEQADV 3INB VAL A 156 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO A 157 UNP P08362 EXPRESSION TAG
SEQADV 3INB ASP A 158 UNP P08362 EXPRESSION TAG
SEQADV 3INB TYR A 159 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA A 160 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY A 161 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA A 162 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLN A 163 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO A 164 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA A 165 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG A 166 UNP P08362 EXPRESSION TAG
SEQADV 3INB SER A 167 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO A 168 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY A 169 UNP P08362 EXPRESSION TAG
SEQADV 3INB ILE A 170 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG A 171 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY A 172 UNP P08362 EXPRESSION TAG
SEQADV 3INB LEU A 173 UNP P08362 EXPRESSION TAG
SEQADV 3INB VAL A 174 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO A 175 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG A 176 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY A 177 UNP P08362 EXPRESSION TAG
SEQADV 3INB SER A 178 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA A 331 UNP P08362 THR 331 ENGINEERED MUTATION
SEQADV 3INB THR A 392 UNP P08362 ALA 392 ENGINEERED MUTATION
SEQADV 3INB THR A 484 UNP P08362 ASN 484 ENGINEERED MUTATION
SEQADV 3INB GLY A 546 UNP P08362 SER 546 ENGINEERED MUTATION
SEQADV 3INB VAL A 600 UNP P08362 GLU 600 ENGINEERED MUTATION
SEQADV 3INB TYR B 152 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO B 153 UNP P08362 EXPRESSION TAG
SEQADV 3INB TYR B 154 UNP P08362 EXPRESSION TAG
SEQADV 3INB ASP B 155 UNP P08362 EXPRESSION TAG
SEQADV 3INB VAL B 156 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO B 157 UNP P08362 EXPRESSION TAG
SEQADV 3INB ASP B 158 UNP P08362 EXPRESSION TAG
SEQADV 3INB TYR B 159 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA B 160 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY B 161 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA B 162 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLN B 163 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO B 164 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA B 165 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG B 166 UNP P08362 EXPRESSION TAG
SEQADV 3INB SER B 167 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO B 168 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY B 169 UNP P08362 EXPRESSION TAG
SEQADV 3INB ILE B 170 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG B 171 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY B 172 UNP P08362 EXPRESSION TAG
SEQADV 3INB LEU B 173 UNP P08362 EXPRESSION TAG
SEQADV 3INB VAL B 174 UNP P08362 EXPRESSION TAG
SEQADV 3INB PRO B 175 UNP P08362 EXPRESSION TAG
SEQADV 3INB ARG B 176 UNP P08362 EXPRESSION TAG
SEQADV 3INB GLY B 177 UNP P08362 EXPRESSION TAG
SEQADV 3INB SER B 178 UNP P08362 EXPRESSION TAG
SEQADV 3INB ALA B 331 UNP P08362 THR 331 ENGINEERED MUTATION
SEQADV 3INB THR B 392 UNP P08362 ALA 392 ENGINEERED MUTATION
SEQADV 3INB THR B 484 UNP P08362 ASN 484 ENGINEERED MUTATION
SEQADV 3INB GLY B 546 UNP P08362 SER 546 ENGINEERED MUTATION
SEQADV 3INB VAL B 600 UNP P08362 GLU 600 ENGINEERED MUTATION
SEQRES 1 A 466 TYR PRO TYR ASP VAL PRO ASP TYR ALA GLY ALA GLN PRO
SEQRES 2 A 466 ALA ARG SER PRO GLY ILE ARG GLY LEU VAL PRO ARG GLY
SEQRES 3 A 466 SER GLN PHE LEU ALA VAL SER LYS GLY ASN CYS SER GLY
SEQRES 4 A 466 PRO THR THR ILE ARG GLY GLN PHE SER ASN MET SER LEU
SEQRES 5 A 466 SER LEU LEU ASP LEU TYR LEU GLY ARG GLY TYR ASN VAL
SEQRES 6 A 466 SER SER ILE VAL THR MET THR SER GLN GLY MET TYR GLY
SEQRES 7 A 466 GLY THR TYR LEU VAL GLU LYS PRO ASN LEU SER SER LYS
SEQRES 8 A 466 ARG SER GLU LEU SER GLN LEU SER MET TYR ARG VAL PHE
SEQRES 9 A 466 GLU VAL GLY VAL ILE ARG ASN PRO GLY LEU GLY ALA PRO
SEQRES 10 A 466 VAL PHE HIS MET THR ASN TYR LEU GLU GLN PRO VAL SER
SEQRES 11 A 466 ASN ASP LEU SER ASN CYS MET VAL ALA LEU GLY GLU LEU
SEQRES 12 A 466 LYS LEU ALA ALA LEU CYS HIS GLY GLU ASP SER ILE THR
SEQRES 13 A 466 ILE PRO TYR GLN GLY SER GLY LYS GLY VAL SER PHE GLN
SEQRES 14 A 466 LEU VAL LYS LEU GLY VAL TRP LYS SER PRO ALA ASP MET
SEQRES 15 A 466 GLN SER TRP VAL PRO LEU SER THR ASP ASP PRO VAL ILE
SEQRES 16 A 466 ASP ARG LEU TYR LEU SER SER HIS ARG GLY VAL ILE ALA
SEQRES 17 A 466 ASP ASN GLN ALA LYS TRP ALA VAL PRO THR THR ARG THR
SEQRES 18 A 466 ASP ASP LYS LEU ARG MET GLU THR CYS PHE GLN GLN ALA
SEQRES 19 A 466 CYS LYS GLY LYS ILE GLN THR LEU CYS GLU ASN PRO GLU
SEQRES 20 A 466 TRP ALA PRO LEU LYS ASP ASN ARG ILE PRO SER TYR GLY
SEQRES 21 A 466 VAL LEU SER VAL ASP LEU SER LEU THR VAL GLU LEU LYS
SEQRES 22 A 466 ILE LYS ILE ALA SER GLY PHE GLY PRO LEU ILE THR HIS
SEQRES 23 A 466 GLY SER GLY MET ASP LEU TYR LYS SER ASN HIS ASN ASN
SEQRES 24 A 466 VAL TYR TRP LEU THR ILE PRO PRO MET LYS ASN LEU ALA
SEQRES 25 A 466 LEU GLY VAL ILE ASN THR LEU GLU TRP ILE PRO ARG PHE
SEQRES 26 A 466 LYS VAL SER PRO TYR LEU PHE THR VAL PRO ILE LYS GLU
SEQRES 27 A 466 ALA GLY GLU ASP CYS HIS ALA PRO THR TYR LEU PRO ALA
SEQRES 28 A 466 GLU VAL ASP GLY ASP VAL LYS LEU SER SER ASN LEU VAL
SEQRES 29 A 466 ILE LEU PRO GLY GLN ASP LEU GLN TYR VAL LEU ALA THR
SEQRES 30 A 466 TYR ASP THR SER ARG VAL GLU HIS ALA VAL VAL TYR TYR
SEQRES 31 A 466 VAL TYR SER PRO GLY ARG SER PHE SER TYR PHE TYR PRO
SEQRES 32 A 466 PHE ARG LEU PRO ILE LYS GLY VAL PRO ILE GLU LEU GLN
SEQRES 33 A 466 VAL GLU CYS PHE THR TRP ASP GLN LYS LEU TRP CYS ARG
SEQRES 34 A 466 HIS PHE CYS VAL LEU ALA ASP SER GLU SER GLY GLY HIS
SEQRES 35 A 466 ILE THR HIS SER GLY MET VAL GLY MET GLY VAL SER CYS
SEQRES 36 A 466 THR VAL THR ARG GLU ASP GLY THR ASN ARG ARG
SEQRES 1 B 466 TYR PRO TYR ASP VAL PRO ASP TYR ALA GLY ALA GLN PRO
SEQRES 2 B 466 ALA ARG SER PRO GLY ILE ARG GLY LEU VAL PRO ARG GLY
SEQRES 3 B 466 SER GLN PHE LEU ALA VAL SER LYS GLY ASN CYS SER GLY
SEQRES 4 B 466 PRO THR THR ILE ARG GLY GLN PHE SER ASN MET SER LEU
SEQRES 5 B 466 SER LEU LEU ASP LEU TYR LEU GLY ARG GLY TYR ASN VAL
SEQRES 6 B 466 SER SER ILE VAL THR MET THR SER GLN GLY MET TYR GLY
SEQRES 7 B 466 GLY THR TYR LEU VAL GLU LYS PRO ASN LEU SER SER LYS
SEQRES 8 B 466 ARG SER GLU LEU SER GLN LEU SER MET TYR ARG VAL PHE
SEQRES 9 B 466 GLU VAL GLY VAL ILE ARG ASN PRO GLY LEU GLY ALA PRO
SEQRES 10 B 466 VAL PHE HIS MET THR ASN TYR LEU GLU GLN PRO VAL SER
SEQRES 11 B 466 ASN ASP LEU SER ASN CYS MET VAL ALA LEU GLY GLU LEU
SEQRES 12 B 466 LYS LEU ALA ALA LEU CYS HIS GLY GLU ASP SER ILE THR
SEQRES 13 B 466 ILE PRO TYR GLN GLY SER GLY LYS GLY VAL SER PHE GLN
SEQRES 14 B 466 LEU VAL LYS LEU GLY VAL TRP LYS SER PRO ALA ASP MET
SEQRES 15 B 466 GLN SER TRP VAL PRO LEU SER THR ASP ASP PRO VAL ILE
SEQRES 16 B 466 ASP ARG LEU TYR LEU SER SER HIS ARG GLY VAL ILE ALA
SEQRES 17 B 466 ASP ASN GLN ALA LYS TRP ALA VAL PRO THR THR ARG THR
SEQRES 18 B 466 ASP ASP LYS LEU ARG MET GLU THR CYS PHE GLN GLN ALA
SEQRES 19 B 466 CYS LYS GLY LYS ILE GLN THR LEU CYS GLU ASN PRO GLU
SEQRES 20 B 466 TRP ALA PRO LEU LYS ASP ASN ARG ILE PRO SER TYR GLY
SEQRES 21 B 466 VAL LEU SER VAL ASP LEU SER LEU THR VAL GLU LEU LYS
SEQRES 22 B 466 ILE LYS ILE ALA SER GLY PHE GLY PRO LEU ILE THR HIS
SEQRES 23 B 466 GLY SER GLY MET ASP LEU TYR LYS SER ASN HIS ASN ASN
SEQRES 24 B 466 VAL TYR TRP LEU THR ILE PRO PRO MET LYS ASN LEU ALA
SEQRES 25 B 466 LEU GLY VAL ILE ASN THR LEU GLU TRP ILE PRO ARG PHE
SEQRES 26 B 466 LYS VAL SER PRO TYR LEU PHE THR VAL PRO ILE LYS GLU
SEQRES 27 B 466 ALA GLY GLU ASP CYS HIS ALA PRO THR TYR LEU PRO ALA
SEQRES 28 B 466 GLU VAL ASP GLY ASP VAL LYS LEU SER SER ASN LEU VAL
SEQRES 29 B 466 ILE LEU PRO GLY GLN ASP LEU GLN TYR VAL LEU ALA THR
SEQRES 30 B 466 TYR ASP THR SER ARG VAL GLU HIS ALA VAL VAL TYR TYR
SEQRES 31 B 466 VAL TYR SER PRO GLY ARG SER PHE SER TYR PHE TYR PRO
SEQRES 32 B 466 PHE ARG LEU PRO ILE LYS GLY VAL PRO ILE GLU LEU GLN
SEQRES 33 B 466 VAL GLU CYS PHE THR TRP ASP GLN LYS LEU TRP CYS ARG
SEQRES 34 B 466 HIS PHE CYS VAL LEU ALA ASP SER GLU SER GLY GLY HIS
SEQRES 35 B 466 ILE THR HIS SER GLY MET VAL GLY MET GLY VAL SER CYS
SEQRES 36 B 466 THR VAL THR ARG GLU ASP GLY THR ASN ARG ARG
SEQRES 1 C 126 CYS GLU GLU PRO PRO THR PHE GLU ALA MET GLU LEU ILE
SEQRES 2 C 126 GLY LYS PRO LYS PRO TYR TYR GLU ILE GLY GLU ARG VAL
SEQRES 3 C 126 ASP TYR LYS CYS LYS LYS GLY TYR PHE TYR ILE PRO PRO
SEQRES 4 C 126 LEU ALA THR HIS THR ILE CYS ASP ARG ASN HIS THR TRP
SEQRES 5 C 126 LEU PRO VAL SER ASP ASP ALA CYS TYR ARG GLU THR CYS
SEQRES 6 C 126 PRO TYR ILE ARG ASP PRO LEU ASN GLY GLN ALA VAL PRO
SEQRES 7 C 126 ALA ASN GLY THR TYR GLU PHE GLY TYR GLN MET HIS PHE
SEQRES 8 C 126 ILE CYS ASN GLU GLY TYR TYR LEU ILE GLY GLU GLU ILE
SEQRES 9 C 126 LEU TYR CYS GLU LEU LYS GLY SER VAL ALA ILE TRP SER
SEQRES 10 C 126 GLY LYS PRO PRO ILE CYS GLU LYS VAL
SEQRES 1 D 126 CYS GLU GLU PRO PRO THR PHE GLU ALA MET GLU LEU ILE
SEQRES 2 D 126 GLY LYS PRO LYS PRO TYR TYR GLU ILE GLY GLU ARG VAL
SEQRES 3 D 126 ASP TYR LYS CYS LYS LYS GLY TYR PHE TYR ILE PRO PRO
SEQRES 4 D 126 LEU ALA THR HIS THR ILE CYS ASP ARG ASN HIS THR TRP
SEQRES 5 D 126 LEU PRO VAL SER ASP ASP ALA CYS TYR ARG GLU THR CYS
SEQRES 6 D 126 PRO TYR ILE ARG ASP PRO LEU ASN GLY GLN ALA VAL PRO
SEQRES 7 D 126 ALA ASN GLY THR TYR GLU PHE GLY TYR GLN MET HIS PHE
SEQRES 8 D 126 ILE CYS ASN GLU GLY TYR TYR LEU ILE GLY GLU GLU ILE
SEQRES 9 D 126 LEU TYR CYS GLU LEU LYS GLY SER VAL ALA ILE TRP SER
SEQRES 10 D 126 GLY LYS PRO PRO ILE CYS GLU LYS VAL
MODRES 3INB ASN A 200 ASN GLYCOSYLATION SITE
MODRES 3INB ASN A 215 ASN GLYCOSYLATION SITE
MODRES 3INB ASN B 200 ASN GLYCOSYLATION SITE
MODRES 3INB ASN B 215 ASN GLYCOSYLATION SITE
MODRES 3INB ASN C 80 ASN GLYCOSYLATION SITE
MODRES 3INB ASN D 80 ASN GLYCOSYLATION SITE
HET NAG A1200 14
HET NAG A1215 14
HET SO4 A 3 5
HET NAG B1200 14
HET NAG B1215 14
HET SO4 B 1 5
HET SO4 B 2 5
HET NAG C1080 14
HET NAG D1080 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
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
FORMUL 5 NAG 6(C8 H15 N O6)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 14 HOH *8(H2 O)
HELIX 1 1 SER A 204 ARG A 212 1 9
HELIX 2 2 ASP A 373 LYS A 387 1 15
HELIX 3 3 THR A 392 ASN A 396 5 5
HELIX 4 4 TRP A 399 ASP A 404 1 6
HELIX 5 5 SER B 204 ARG B 212 1 9
HELIX 6 6 ASP B 373 LYS B 387 1 15
HELIX 7 7 THR B 392 ASN B 396 5 5
HELIX 8 8 TRP B 399 ASP B 404 1 6
SHEET 1 A 4 PHE A 198 SER A 199 0
SHEET 2 A 4 ILE A 594 MET A 602 -1 O MET A 599 N SER A 199
SHEET 3 A 4 LYS A 576 ALA A 586 -1 N HIS A 581 O GLY A 598
SHEET 4 A 4 VAL A 562 TRP A 573 -1 N ILE A 564 O VAL A 584
SHEET 1 B 4 VAL A 216 SER A 224 0
SHEET 2 B 4 MET A 227 GLU A 235 -1 O LEU A 233 N SER A 217
SHEET 3 B 4 MET A 251 ARG A 261 -1 O VAL A 254 N TYR A 232
SHEET 4 B 4 VAL A 269 PRO A 279 -1 O GLN A 278 N ARG A 253
SHEET 1 C 9 SER A 285 LEU A 291 0
SHEET 2 C 9 LYS A 295 GLY A 302 -1 O ALA A 297 N ALA A 290
SHEET 3 C 9 SER A 318 GLY A 325 -1 O GLN A 320 N CYS A 300
SHEET 4 C 9 TRP A 336 SER A 340 -1 O VAL A 337 N PHE A 319
SHEET 5 C 9 ILE A 425 GLY A 430 1 O ILE A 425 N PRO A 338
SHEET 6 C 9 SER A 409 ASP A 416 -1 N SER A 414 O LYS A 426
SHEET 7 C 9 GLN A 362 THR A 369 -1 N VAL A 367 O GLY A 411
SHEET 8 C 9 ARG A 355 ILE A 358 -1 N VAL A 357 O LYS A 364
SHEET 9 C 9 SER A 285 LEU A 291 1 N LEU A 291 O ILE A 358
SHEET 1 D 2 SER A 305 THR A 307 0
SHEET 2 D 2 ARG A 348 TYR A 350 -1 O LEU A 349 N ILE A 306
SHEET 1 E 4 ASP A 442 LYS A 445 0
SHEET 2 E 4 VAL A 451 ILE A 456 -1 O TRP A 453 N TYR A 444
SHEET 3 E 4 VAL A 466 GLU A 471 -1 O LEU A 470 N TYR A 452
SHEET 4 E 4 LYS A 477 LEU A 482 -1 O LYS A 477 N GLU A 471
SHEET 1 F 2 THR A 484 PRO A 486 0
SHEET 2 F 2 HIS A 495 PRO A 497 -1 O ALA A 496 N VAL A 485
SHEET 1 G 4 LEU A 510 SER A 511 0
SHEET 2 G 4 TYR A 524 TYR A 529 -1 O TYR A 529 N LEU A 510
SHEET 3 G 4 ALA A 537 SER A 544 -1 O VAL A 539 N THR A 528
SHEET 4 G 4 ARG A 547 PRO A 554 -1 O TYR A 551 N TYR A 540
SHEET 1 H 4 ARG B 195 SER B 199 0
SHEET 2 H 4 THR B 595 GLY B 603 -1 O GLY B 603 N ARG B 195
SHEET 3 H 4 LYS B 576 ALA B 586 -1 N HIS B 581 O GLY B 598
SHEET 4 H 4 VAL B 562 TRP B 573 -1 N ILE B 564 O VAL B 584
SHEET 1 I 4 VAL B 216 SER B 224 0
SHEET 2 I 4 MET B 227 LYS B 236 -1 O LEU B 233 N SER B 217
SHEET 3 I 4 SER B 250 ARG B 261 -1 O VAL B 254 N TYR B 232
SHEET 4 I 4 VAL B 269 PRO B 279 -1 O GLN B 278 N ARG B 253
SHEET 1 J 9 SER B 285 LEU B 291 0
SHEET 2 J 9 LYS B 295 GLY B 302 -1 O ALA B 297 N ALA B 290
SHEET 3 J 9 SER B 318 GLY B 325 -1 O GLN B 320 N CYS B 300
SHEET 4 J 9 TRP B 336 SER B 340 -1 O VAL B 337 N PHE B 319
SHEET 5 J 9 ILE B 425 GLY B 430 1 O ILE B 425 N PRO B 338
SHEET 6 J 9 SER B 409 ASP B 416 -1 N SER B 414 O LYS B 426
SHEET 7 J 9 GLN B 362 THR B 369 -1 N VAL B 367 O GLY B 411
SHEET 8 J 9 ARG B 355 ILE B 358 -1 N VAL B 357 O LYS B 364
SHEET 9 J 9 SER B 285 LEU B 291 1 N LEU B 291 O ILE B 358
SHEET 1 K 2 SER B 305 THR B 307 0
SHEET 2 K 2 ARG B 348 TYR B 350 -1 O LEU B 349 N ILE B 306
SHEET 1 L 4 ASP B 442 LYS B 445 0
SHEET 2 L 4 VAL B 451 ILE B 456 -1 O TRP B 453 N TYR B 444
SHEET 3 L 4 VAL B 466 GLU B 471 -1 O LEU B 470 N TYR B 452
SHEET 4 L 4 LYS B 477 LEU B 482 -1 O LYS B 477 N GLU B 471
SHEET 1 M 2 THR B 484 PRO B 486 0
SHEET 2 M 2 HIS B 495 PRO B 497 -1 O ALA B 496 N VAL B 485
SHEET 1 N 4 LEU B 510 SER B 511 0
SHEET 2 N 4 TYR B 524 ASP B 530 -1 O TYR B 529 N LEU B 510
SHEET 3 N 4 ALA B 537 SER B 544 -1 O VAL B 539 N THR B 528
SHEET 4 N 4 ARG B 547 PRO B 554 -1 O TYR B 551 N TYR B 540
SHEET 1 O 2 ARG C 25 ASP C 27 0
SHEET 2 O 2 HIS C 43 ILE C 45 -1 O THR C 44 N VAL C 26
SHEET 1 P 2 TYR C 34 TYR C 36 0
SHEET 2 P 2 CYS C 60 ARG C 62 -1 O TYR C 61 N PHE C 35
SHEET 1 Q 2 GLN C 88 HIS C 90 0
SHEET 2 Q 2 ILE C 104 TYR C 106 -1 O LEU C 105 N MET C 89
SHEET 1 R 2 TYR D 34 TYR D 36 0
SHEET 2 R 2 CYS D 60 ARG D 62 -1 O TYR D 61 N PHE D 35
SHEET 1 S 2 ILE D 45 CYS D 46 0
SHEET 2 S 2 TRP D 52 LEU D 53 -1 O LEU D 53 N ILE D 45
SHEET 1 T 2 GLN D 88 HIS D 90 0
SHEET 2 T 2 ILE D 104 TYR D 106 -1 O LEU D 105 N MET D 89
SSBOND 1 CYS A 287 CYS A 300 1555 1555 2.03
SSBOND 2 CYS A 381 CYS A 494 1555 1555 2.03
SSBOND 3 CYS A 386 CYS A 394 1555 1555 2.04
SSBOND 4 CYS A 570 CYS A 579 1555 1555 2.04
SSBOND 5 CYS B 188 CYS B 606 1555 1555 2.06
SSBOND 6 CYS B 287 CYS B 300 1555 1555 2.03
SSBOND 7 CYS B 381 CYS B 494 1555 1555 2.04
SSBOND 8 CYS B 386 CYS B 394 1555 1555 2.04
SSBOND 9 CYS B 570 CYS B 579 1555 1555 2.04
SSBOND 10 CYS C 1 CYS C 46 1555 1555 2.04
SSBOND 11 CYS C 30 CYS C 60 1555 1555 2.05
SSBOND 12 CYS C 65 CYS C 107 1555 1555 2.03
SSBOND 13 CYS C 93 CYS C 123 1555 1555 2.05
SSBOND 14 CYS D 1 CYS D 46 1555 1555 2.04
SSBOND 15 CYS D 30 CYS D 60 1555 1555 2.04
SSBOND 16 CYS D 65 CYS D 107 1555 1555 2.03
SSBOND 17 CYS D 93 CYS D 123 1555 1555 2.05
LINK ND2 ASN A 200 C1 NAG A1200 1555 1555 1.45
LINK ND2 ASN A 215 C1 NAG A1215 1555 1555 1.44
LINK ND2 ASN B 200 C1 NAG B1200 1555 1555 1.44
LINK ND2 ASN B 215 C1 NAG B1215 1555 1555 1.44
LINK ND2 ASN C 80 C1 NAG C1080 1555 1555 1.44
LINK ND2 ASN D 80 C1 NAG D1080 1555 1555 1.44
CISPEP 1 LYS B 185 GLY B 186 0 -0.27
CISPEP 2 GLY B 190 PRO B 191 0 -0.09
CISPEP 3 PRO C 38 PRO C 39 0 1.75
CISPEP 4 GLU D 21 ILE D 22 0 28.04
CISPEP 5 ASP D 27 TYR D 28 0 13.38
CISPEP 6 PRO D 38 PRO D 39 0 -11.65
CRYST1 81.365 105.833 208.710 90.00 90.00 90.00 P 2 2 21 8
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 0.012290 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END