HEADER IMMUNE SYSTEM 27-MAR-24 8YUB TITLE CRYSTAL STRUCTURE OF SARS-COV-2 CONSP RBD IN COMPLEX WITH NEUTRALIZING TITLE 2 ANTIBODY CC25.4 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTRALIZING ANTIBODY CC25.4 HEAVY CHAIN; COMPND 3 CHAIN: A, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NEUTRALIZING ANTIBODY CC25.4 LIGHT CHAIN; COMPND 7 CHAIN: B, E; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SPIKE PROTEIN S2'; COMPND 11 CHAIN: C, F; COMPND 12 FRAGMENT: RBD; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 15 2; SOURCE 16 ORGANISM_TAXID: 2697049; SOURCE 17 GENE: S, 2; SOURCE 18 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 2, SPIKE PROTEIN, KEYWDS 2 RECEPTOR BINDING DOMAIN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.M.KANG,M.YUAN,B.W.HAN,I.A.WILSON REVDAT 1 01-OCT-25 8YUB 0 JRNL AUTH J.M.KANG,M.YUAN,B.W.HAN,I.A.WILSON JRNL TITL STRUCTURE AND ANTIGENIC CHARACTERISTICS OF CONSENSUS JRNL TITL 2 SEQUENCE-BASED SARS-COV-2 ANTIGEN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 78.8 REMARK 3 NUMBER OF REFLECTIONS : 45759 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 2279 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 41.2000 - 6.2700 0.99 3481 181 0.1757 0.2191 REMARK 3 2 6.2600 - 4.9800 1.00 3485 183 0.1649 0.1967 REMARK 3 3 4.9800 - 4.3500 1.00 3468 177 0.1450 0.1638 REMARK 3 4 4.3500 - 3.9500 1.00 3436 186 0.1656 0.2364 REMARK 3 5 3.9500 - 3.6700 1.00 3419 179 0.1923 0.2471 REMARK 3 6 3.6700 - 3.4500 1.00 3458 183 0.2180 0.2889 REMARK 3 7 3.4500 - 3.2800 0.99 3413 180 0.2327 0.3131 REMARK 3 8 3.2800 - 3.1400 0.99 3431 176 0.2425 0.3147 REMARK 3 9 3.1400 - 3.0200 0.99 3370 175 0.2586 0.3129 REMARK 3 10 3.0200 - 2.9100 0.97 3353 173 0.2804 0.3162 REMARK 3 11 2.9100 - 2.8200 0.86 2964 153 0.2776 0.3163 REMARK 3 12 2.8200 - 2.7400 0.68 2330 134 0.2833 0.3087 REMARK 3 13 2.7400 - 2.6700 0.47 1633 85 0.2873 0.3712 REMARK 3 14 2.6700 - 2.6000 0.31 1080 50 0.2790 0.2816 REMARK 3 15 2.6000 - 2.5400 0.21 733 40 0.3145 0.3813 REMARK 3 16 2.5400 - 2.4900 0.13 426 24 0.3625 0.3328 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.351 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.727 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.35 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.46 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.002 10173 REMARK 3 ANGLE : 0.477 13871 REMARK 3 CHIRALITY : 0.043 1528 REMARK 3 PLANARITY : 0.004 1790 REMARK 3 DIHEDRAL : 10.201 3641 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8YUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1300046373. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-MAY-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53558 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490 REMARK 200 RESOLUTION RANGE LOW (A) : 41.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.8 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 7VYR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 15% (W/V) PEG 6000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 62.45050 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 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 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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 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 212 102.28 -58.15 REMARK 500 ASN B 27B -88.68 -116.74 REMARK 500 ASN B 51 -54.62 72.86 REMARK 500 LEU B 95 -133.93 61.43 REMARK 500 LYS B 156 -78.76 -99.33 REMARK 500 ALA C 352 55.88 -115.35 REMARK 500 PRO C 373 82.14 -67.81 REMARK 500 PHE C 400 -177.11 -170.84 REMARK 500 ASN C 422 -59.94 -130.28 REMARK 500 ASP C 428 32.19 -91.42 REMARK 500 ASN C 487 16.94 58.99 REMARK 500 TYR D 100D 51.41 -140.13 REMARK 500 ASN E 27B -100.21 -89.22 REMARK 500 ASN E 51 -49.36 71.11 REMARK 500 LEU E 95 -138.38 58.34 REMARK 500 TYR E 140 127.54 -170.97 REMARK 500 ASP E 151 -91.57 57.00 REMARK 500 ASN E 170 14.34 56.78 REMARK 500 SER E 190 108.39 -163.06 REMARK 500 ASN F 370 4.15 -69.69 REMARK 500 PHE F 371 52.13 -110.47 REMARK 500 ALA F 372 179.39 66.42 REMARK 500 ASN F 405 2.19 -69.39 REMARK 500 ASN F 422 -57.01 -124.99 REMARK 500 ASP F 428 36.40 -86.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 EDO B 301 DBREF 8YUB A 1 214 PDB 8YUB 8YUB 1 214 DBREF 8YUB B 1 212 PDB 8YUB 8YUB 1 212 DBREF 8YUB C 333 529 UNP P0DTC2 SPIKE_SARS2 333 529 DBREF 8YUB D 1 214 PDB 8YUB 8YUB 1 214 DBREF 8YUB E 1 212 PDB 8YUB 8YUB 1 212 DBREF 8YUB F 333 529 UNP P0DTC2 SPIKE_SARS2 333 529 SEQADV 8YUB HIS C 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 8YUB THR C 346 UNP P0DTC2 ARG 346 VARIANT SEQADV 8YUB ILE C 368 UNP P0DTC2 LEU 368 VARIANT SEQADV 8YUB PHE C 371 UNP P0DTC2 SER 371 VARIANT SEQADV 8YUB PRO C 373 UNP P0DTC2 SER 373 VARIANT SEQADV 8YUB PHE C 375 UNP P0DTC2 SER 375 VARIANT SEQADV 8YUB ALA C 376 UNP P0DTC2 THR 376 VARIANT SEQADV 8YUB ASN C 405 UNP P0DTC2 ASP 405 VARIANT SEQADV 8YUB SER C 408 UNP P0DTC2 ARG 408 VARIANT SEQADV 8YUB ASN C 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 8YUB LYS C 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 8YUB THR C 444 UNP P0DTC2 LYS 444 VARIANT SEQADV 8YUB PRO C 445 UNP P0DTC2 VAL 445 VARIANT SEQADV 8YUB SER C 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 8YUB ARG C 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 8YUB LYS C 460 UNP P0DTC2 ASN 460 VARIANT SEQADV 8YUB ASN C 477 UNP P0DTC2 SER 477 VARIANT SEQADV 8YUB LYS C 478 UNP P0DTC2 THR 478 VARIANT SEQADV 8YUB ALA C 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 8YUB PRO C 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 8YUB SER C 490 UNP P0DTC2 PHE 490 VARIANT SEQADV 8YUB ARG C 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 8YUB TYR C 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 8YUB HIS C 505 UNP P0DTC2 TYR 505 VARIANT SEQADV 8YUB HIS F 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 8YUB THR F 346 UNP P0DTC2 ARG 346 VARIANT SEQADV 8YUB ILE F 368 UNP P0DTC2 LEU 368 VARIANT SEQADV 8YUB PHE F 371 UNP P0DTC2 SER 371 VARIANT SEQADV 8YUB PRO F 373 UNP P0DTC2 SER 373 VARIANT SEQADV 8YUB PHE F 375 UNP P0DTC2 SER 375 VARIANT SEQADV 8YUB ALA F 376 UNP P0DTC2 THR 376 VARIANT SEQADV 8YUB ASN F 405 UNP P0DTC2 ASP 405 VARIANT SEQADV 8YUB SER F 408 UNP P0DTC2 ARG 408 VARIANT SEQADV 8YUB ASN F 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 8YUB LYS F 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 8YUB THR F 444 UNP P0DTC2 LYS 444 VARIANT SEQADV 8YUB PRO F 445 UNP P0DTC2 VAL 445 VARIANT SEQADV 8YUB SER F 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 8YUB ARG F 452 UNP P0DTC2 LEU 452 VARIANT SEQADV 8YUB LYS F 460 UNP P0DTC2 ASN 460 VARIANT SEQADV 8YUB ASN F 477 UNP P0DTC2 SER 477 VARIANT SEQADV 8YUB LYS F 478 UNP P0DTC2 THR 478 VARIANT SEQADV 8YUB ALA F 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 8YUB PRO F 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 8YUB SER F 490 UNP P0DTC2 PHE 490 VARIANT SEQADV 8YUB ARG F 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 8YUB TYR F 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 8YUB HIS F 505 UNP P0DTC2 TYR 505 VARIANT SEQRES 1 A 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 A 228 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 228 TYR THR PHE THR ASP TYR PHE LEU HIS TRP VAL ARG GLN SEQRES 4 A 228 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 A 228 PRO ASP SER GLY GLY THR ASN TYR ALA GLN ARG PHE GLN SEQRES 6 A 228 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 A 228 ALA TYR MET GLU VAL SER ARG LEU ARG SER ASP ASP THR SEQRES 8 A 228 ALA VAL TYR TYR CYS ALA ARG ASP ASN GLU ARG TYR GLN SEQRES 9 A 228 MET GLN ASN TYR TYR HIS TYR TYR GLY MET ASP VAL TRP SEQRES 10 A 228 GLY GLN GLY THR THR VAL THR VAL VAL SER ARG ARG LEU SEQRES 11 A 228 PRO PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 A 228 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 A 228 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 A 228 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 A 228 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 A 228 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 A 228 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 A 228 LYS LYS VAL GLU PRO LYS SER SEQRES 1 B 217 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2 B 217 PRO GLY GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 B 217 SER ASN ILE GLY SER ASN THR VAL ASN TRP TYR GLN GLN SEQRES 4 B 217 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER ASN SEQRES 5 B 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 B 217 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 B 217 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8 B 217 TRP ASP ASP SER LEU ASN GLY TYR VAL VAL PHE GLY GLY SEQRES 9 B 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 B 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 B 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 B 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 B 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 B 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 B 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 B 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 B 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 197 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR SEQRES 2 C 197 THR PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 C 197 SER ASN CYS VAL ALA ASP TYR SER VAL ILE TYR ASN PHE SEQRES 4 C 197 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 C 197 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 C 197 ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN ILE SEQRES 7 C 197 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 8 C 197 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 C 197 ASN SER ASN LYS LEU ASP SER THR PRO SER GLY ASN TYR SEQRES 10 C 197 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER LYS LEU LYS SEQRES 11 C 197 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 C 197 GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PRO ASN CYS SEQRES 13 C 197 TYR SER PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR SEQRES 14 C 197 GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 C 197 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 C 197 LYS LYS SEQRES 1 D 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 D 228 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 228 TYR THR PHE THR ASP TYR PHE LEU HIS TRP VAL ARG GLN SEQRES 4 D 228 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 D 228 PRO ASP SER GLY GLY THR ASN TYR ALA GLN ARG PHE GLN SEQRES 6 D 228 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 D 228 ALA TYR MET GLU VAL SER ARG LEU ARG SER ASP ASP THR SEQRES 8 D 228 ALA VAL TYR TYR CYS ALA ARG ASP ASN GLU ARG TYR GLN SEQRES 9 D 228 MET GLN ASN TYR TYR HIS TYR TYR GLY MET ASP VAL TRP SEQRES 10 D 228 GLY GLN GLY THR THR VAL THR VAL VAL SER ARG ARG LEU SEQRES 11 D 228 PRO PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 12 D 228 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 13 D 228 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 14 D 228 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 15 D 228 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 16 D 228 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 17 D 228 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 18 D 228 LYS LYS VAL GLU PRO LYS SER SEQRES 1 E 217 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2 E 217 PRO GLY GLN ARG VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 E 217 SER ASN ILE GLY SER ASN THR VAL ASN TRP TYR GLN GLN SEQRES 4 E 217 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER ASN SEQRES 5 E 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 E 217 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 E 217 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS ALA ALA SEQRES 8 E 217 TRP ASP ASP SER LEU ASN GLY TYR VAL VAL PHE GLY GLY SEQRES 9 E 217 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10 E 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 E 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 E 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 E 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 E 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 E 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 E 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 E 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 F 197 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR SEQRES 2 F 197 THR PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 F 197 SER ASN CYS VAL ALA ASP TYR SER VAL ILE TYR ASN PHE SEQRES 4 F 197 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 F 197 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 F 197 ASP SER PHE VAL ILE ARG GLY ASN GLU VAL SER GLN ILE SEQRES 7 F 197 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 8 F 197 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 F 197 ASN SER ASN LYS LEU ASP SER THR PRO SER GLY ASN TYR SEQRES 10 F 197 ASN TYR ARG TYR ARG LEU PHE ARG LYS SER LYS LEU LYS SEQRES 11 F 197 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 F 197 GLY ASN LYS PRO CYS ASN GLY VAL ALA GLY PRO ASN CYS SEQRES 13 F 197 TYR SER PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR SEQRES 14 F 197 GLY VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 F 197 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 F 197 LYS LYS HET NAG G 1 14 HET FUC G 2 10 HET NAG H 1 14 HET FUC H 2 10 HET EDO B 301 3 HET EDO E 301 4 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN EDO ETHYLENE GLYCOL FORMUL 7 NAG 2(C8 H15 N O6) FORMUL 7 FUC 2(C6 H12 O5) FORMUL 9 EDO 2(C2 H6 O2) FORMUL 11 HOH *302(H2 O) HELIX 1 AA1 GLN A 61 GLN A 64 5 4 HELIX 2 AA2 ARG A 83 THR A 87 5 5 HELIX 3 AA3 MET A 100A TYR A 100E 5 5 HELIX 4 AA4 THR A 130 GLY A 132 5 3 HELIX 5 AA5 SER A 155 ALA A 157 5 3 HELIX 6 AA6 SER A 186 THR A 190 5 5 HELIX 7 AA7 LYS A 200 ASN A 203 5 4 HELIX 8 AA8 GLN B 79 GLU B 83 5 5 HELIX 9 AA9 SER B 121 GLN B 126 1 6 HELIX 10 AB1 THR B 181 LYS B 186 1 6 HELIX 11 AB2 PHE C 338 ASN C 343 1 6 HELIX 12 AB3 ASP C 364 PHE C 371 5 8 HELIX 13 AB4 PRO C 373 PHE C 377 5 5 HELIX 14 AB5 SER C 383 ASP C 389 5 7 HELIX 15 AB6 ASN C 405 ILE C 410 5 6 HELIX 16 AB7 GLY C 416 ASN C 422 1 7 HELIX 17 AB8 SER C 438 SER C 443 1 6 HELIX 18 AB9 GLY C 502 HIS C 505 5 4 HELIX 19 AC1 THR D 28 TYR D 32 5 5 HELIX 20 AC2 ARG D 83 THR D 87 5 5 HELIX 21 AC3 MET D 100A TYR D 100E 5 5 HELIX 22 AC4 SER D 186 LEU D 188 5 3 HELIX 23 AC5 LYS D 200 ASN D 203 5 4 HELIX 24 AC6 SER E 121 GLN E 126 1 6 HELIX 25 AC7 THR E 181 HIS E 188 1 8 HELIX 26 AC8 PRO F 337 ASN F 343 1 7 HELIX 27 AC9 ASP F 364 PHE F 371 5 8 HELIX 28 AD1 SER F 383 LEU F 387 5 5 HELIX 29 AD2 ASN F 405 ILE F 410 5 6 HELIX 30 AD3 GLY F 416 ASN F 422 1 7 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 77 VAL A 82 -1 O ALA A 78 N CYS A 22 SHEET 4 AA1 4 VAL A 67 ASP A 72 -1 N THR A 70 O TYR A 79 SHEET 1 AA2 6 GLU A 10 LYS A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 108 N GLU A 10 SHEET 3 AA2 6 ALA A 88 ASP A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA2 6 LEU A 34 GLN A 39 -1 N HIS A 35 O ALA A 93 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O ASN A 58 N TRP A 50 SHEET 1 AA3 4 GLU A 10 LYS A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 108 N GLU A 10 SHEET 3 AA3 4 ALA A 88 ASP A 95 -1 N TYR A 90 O THR A 107 SHEET 4 AA3 4 MET A 100J TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AA4 4 SER A 119 LEU A 123 0 SHEET 2 AA4 4 THR A 134 TYR A 144 -1 O LEU A 140 N PHE A 121 SHEET 3 AA4 4 TYR A 175 PRO A 184 -1 O TYR A 175 N TYR A 144 SHEET 4 AA4 4 VAL A 162 THR A 164 -1 N HIS A 163 O VAL A 180 SHEET 1 AA5 4 SER A 119 LEU A 123 0 SHEET 2 AA5 4 THR A 134 TYR A 144 -1 O LEU A 140 N PHE A 121 SHEET 3 AA5 4 TYR A 175 PRO A 184 -1 O TYR A 175 N TYR A 144 SHEET 4 AA5 4 VAL A 168 LEU A 169 -1 N VAL A 168 O SER A 176 SHEET 1 AA6 3 THR A 150 TRP A 153 0 SHEET 2 AA6 3 ILE A 194 HIS A 199 -1 O ASN A 196 N SER A 152 SHEET 3 AA6 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AA7 5 SER B 9 GLY B 13 0 SHEET 2 AA7 5 THR B 102 VAL B 106 1 O THR B 105 N ALA B 11 SHEET 3 AA7 5 ASP B 85 ASP B 92 -1 N TYR B 86 O THR B 102 SHEET 4 AA7 5 VAL B 33 GLN B 38 -1 N GLN B 38 O ASP B 85 SHEET 5 AA7 5 LYS B 45 ILE B 48 -1 O LEU B 47 N TRP B 35 SHEET 1 AA8 4 SER B 9 GLY B 13 0 SHEET 2 AA8 4 THR B 102 VAL B 106 1 O THR B 105 N ALA B 11 SHEET 3 AA8 4 ASP B 85 ASP B 92 -1 N TYR B 86 O THR B 102 SHEET 4 AA8 4 TYR B 95C PHE B 98 -1 O TYR B 95C N ASP B 92 SHEET 1 AA9 3 VAL B 19 SER B 24 0 SHEET 2 AA9 3 SER B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 3 AA9 3 PHE B 62 SER B 67 -1 N SER B 63 O ALA B 74 SHEET 1 AB1 4 SER B 114 PHE B 118 0 SHEET 2 AB1 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116 SHEET 3 AB1 4 TYR B 172 LEU B 180 -1 O ALA B 174 N ILE B 136 SHEET 4 AB1 4 VAL B 159 THR B 161 -1 N GLU B 160 O TYR B 177 SHEET 1 AB2 4 SER B 114 PHE B 118 0 SHEET 2 AB2 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116 SHEET 3 AB2 4 TYR B 172 LEU B 180 -1 O ALA B 174 N ILE B 136 SHEET 4 AB2 4 SER B 165 LYS B 166 -1 N SER B 165 O ALA B 173 SHEET 1 AB3 3 THR B 145 ALA B 150 0 SHEET 2 AB3 3 TYR B 191 HIS B 197 -1 O GLN B 194 N ALA B 147 SHEET 3 AB3 3 SER B 200 VAL B 206 -1 O SER B 200 N HIS B 197 SHEET 1 AB4 5 ASN C 354 ILE C 358 0 SHEET 2 AB4 5 ASN C 394 ARG C 403 -1 O VAL C 395 N ILE C 358 SHEET 3 AB4 5 PRO C 507 GLU C 516 -1 O VAL C 512 N ASP C 398 SHEET 4 AB4 5 GLY C 431 ASN C 437 -1 N CYS C 432 O LEU C 513 SHEET 5 AB4 5 LYS C 378 TYR C 380 -1 N TYR C 380 O GLY C 431 SHEET 1 AB5 3 CYS C 361 VAL C 362 0 SHEET 2 AB5 3 VAL C 524 CYS C 525 1 O CYS C 525 N CYS C 361 SHEET 3 AB5 3 CYS C 391 PHE C 392 -1 N PHE C 392 O VAL C 524 SHEET 1 AB6 2 ARG C 452 ARG C 454 0 SHEET 2 AB6 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AB7 2 TYR C 473 GLN C 474 0 SHEET 2 AB7 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SHEET 1 AB8 4 GLN D 3 GLN D 6 0 SHEET 2 AB8 4 VAL D 18 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 AB8 4 THR D 77 VAL D 82 -1 O MET D 80 N VAL D 20 SHEET 4 AB8 4 VAL D 67 ASP D 72 -1 N ASP D 72 O THR D 77 SHEET 1 AB9 6 GLU D 10 LYS D 12 0 SHEET 2 AB9 6 THR D 107 VAL D 111 1 O THR D 108 N GLU D 10 SHEET 3 AB9 6 ALA D 88 ASP D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AB9 6 LEU D 34 GLN D 39 -1 N VAL D 37 O TYR D 91 SHEET 5 AB9 6 GLU D 46 ILE D 51 -1 O MET D 48 N TRP D 36 SHEET 6 AB9 6 THR D 57 TYR D 59 -1 O ASN D 58 N TRP D 50 SHEET 1 AC1 4 GLU D 10 LYS D 12 0 SHEET 2 AC1 4 THR D 107 VAL D 111 1 O THR D 108 N GLU D 10 SHEET 3 AC1 4 ALA D 88 ASP D 95 -1 N TYR D 90 O THR D 107 SHEET 4 AC1 4 MET D 100J TRP D 103 -1 O VAL D 102 N ARG D 94 SHEET 1 AC2 4 SER D 119 LEU D 123 0 SHEET 2 AC2 4 THR D 134 TYR D 144 -1 O GLY D 138 N LEU D 123 SHEET 3 AC2 4 TYR D 175 PRO D 184 -1 O VAL D 183 N ALA D 135 SHEET 4 AC2 4 VAL D 162 THR D 164 -1 N HIS D 163 O VAL D 180 SHEET 1 AC3 4 SER D 119 LEU D 123 0 SHEET 2 AC3 4 THR D 134 TYR D 144 -1 O GLY D 138 N LEU D 123 SHEET 3 AC3 4 TYR D 175 PRO D 184 -1 O VAL D 183 N ALA D 135 SHEET 4 AC3 4 VAL D 168 LEU D 169 -1 N VAL D 168 O SER D 176 SHEET 1 AC4 3 THR D 150 TRP D 153 0 SHEET 2 AC4 3 ILE D 194 HIS D 199 -1 O ASN D 196 N SER D 152 SHEET 3 AC4 3 THR D 204 LYS D 209 -1 O THR D 204 N HIS D 199 SHEET 1 AC5 5 SER E 9 GLY E 13 0 SHEET 2 AC5 5 THR E 102 VAL E 106 1 O LYS E 103 N ALA E 11 SHEET 3 AC5 5 ASP E 85 ASP E 92 -1 N TYR E 86 O THR E 102 SHEET 4 AC5 5 VAL E 33 GLN E 38 -1 N TYR E 36 O TYR E 87 SHEET 5 AC5 5 LYS E 45 ILE E 48 -1 O LEU E 47 N TRP E 35 SHEET 1 AC6 4 SER E 9 GLY E 13 0 SHEET 2 AC6 4 THR E 102 VAL E 106 1 O LYS E 103 N ALA E 11 SHEET 3 AC6 4 ASP E 85 ASP E 92 -1 N TYR E 86 O THR E 102 SHEET 4 AC6 4 TYR E 95C PHE E 98 -1 O VAL E 97 N ALA E 90 SHEET 1 AC7 3 VAL E 19 SER E 24 0 SHEET 2 AC7 3 SER E 70 ILE E 75 -1 O ILE E 75 N VAL E 19 SHEET 3 AC7 3 PHE E 62 SER E 67 -1 N SER E 63 O ALA E 74 SHEET 1 AC8 4 SER E 114 PHE E 118 0 SHEET 2 AC8 4 ALA E 130 PHE E 139 -1 O VAL E 133 N PHE E 118 SHEET 3 AC8 4 TYR E 172 LEU E 180 -1 O ALA E 174 N ILE E 136 SHEET 4 AC8 4 VAL E 159 THR E 161 -1 N GLU E 160 O TYR E 177 SHEET 1 AC9 4 SER E 114 PHE E 118 0 SHEET 2 AC9 4 ALA E 130 PHE E 139 -1 O VAL E 133 N PHE E 118 SHEET 3 AC9 4 TYR E 172 LEU E 180 -1 O ALA E 174 N ILE E 136 SHEET 4 AC9 4 SER E 165 LYS E 166 -1 N SER E 165 O ALA E 173 SHEET 1 AD1 4 SER E 153 PRO E 154 0 SHEET 2 AD1 4 THR E 145 ALA E 150 -1 N ALA E 150 O SER E 153 SHEET 3 AD1 4 TYR E 191 HIS E 197 -1 O GLN E 194 N ALA E 147 SHEET 4 AD1 4 SER E 200 VAL E 206 -1 O VAL E 202 N VAL E 195 SHEET 1 AD2 5 ASN F 354 ILE F 358 0 SHEET 2 AD2 5 ASN F 394 ARG F 403 -1 O VAL F 395 N ILE F 358 SHEET 3 AD2 5 PRO F 507 GLU F 516 -1 O SER F 514 N TYR F 396 SHEET 4 AD2 5 GLY F 431 ASN F 437 -1 N CYS F 432 O LEU F 513 SHEET 5 AD2 5 ALA F 376 TYR F 380 -1 N TYR F 380 O GLY F 431 SHEET 1 AD3 2 CYS F 361 VAL F 362 0 SHEET 2 AD3 2 VAL F 524 CYS F 525 1 O CYS F 525 N CYS F 361 SHEET 1 AD4 2 ARG F 452 ARG F 454 0 SHEET 2 AD4 2 LEU F 492 SER F 494 -1 O GLN F 493 N TYR F 453 SHEET 1 AD5 2 TYR F 473 GLN F 474 0 SHEET 2 AD5 2 CYS F 488 TYR F 489 -1 O TYR F 489 N TYR F 473 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 2 CYS A 139 CYS A 195 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 4 CYS B 134 CYS B 193 1555 1555 2.03 SSBOND 5 CYS C 336 CYS C 361 1555 1555 2.03 SSBOND 6 CYS C 379 CYS C 432 1555 1555 2.03 SSBOND 7 CYS C 391 CYS C 525 1555 1555 2.03 SSBOND 8 CYS C 480 CYS C 488 1555 1555 2.04 SSBOND 9 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 10 CYS D 139 CYS D 195 1555 1555 2.03 SSBOND 11 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 12 CYS E 134 CYS E 193 1555 1555 2.03 SSBOND 13 CYS F 336 CYS F 361 1555 1555 2.03 SSBOND 14 CYS F 379 CYS F 432 1555 1555 2.03 SSBOND 15 CYS F 391 CYS F 525 1555 1555 2.03 SSBOND 16 CYS F 480 CYS F 488 1555 1555 2.03 LINK ND2 ASN C 343 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN F 343 C1 NAG H 1 1555 1555 1.44 LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.47 LINK O6 NAG H 1 C1 FUC H 2 1555 1555 1.45 CISPEP 1 PHE A 145 PRO A 146 0 -3.86 CISPEP 2 GLU A 147 PRO A 148 0 -1.73 CISPEP 3 TYR B 140 PRO B 141 0 1.49 CISPEP 4 PHE D 145 PRO D 146 0 -3.82 CISPEP 5 GLU D 147 PRO D 148 0 -0.89 CISPEP 6 TYR E 140 PRO E 141 0 4.59 CRYST1 81.352 124.901 85.740 90.00 104.37 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012292 0.000000 0.003149 0.00000 SCALE2 0.000000 0.008006 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012040 0.00000