HEADER IMMUNE SYSTEM 03-JUL-25 9PF9 TITLE X-RAY CRYSTAL STRUCTURE OF ATX-350-2 FAB BOUND TO EPSTEIN-BARR VIRUS TITLE 2 GLYCOPROTEIN 350 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB ATX-350-2 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB ATX-350-2 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: BLLF1; COMPND 11 CHAIN: G; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 7 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 8 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 9 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 10 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 13 MOL_ID: 2; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 19 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 20 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 21 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 22 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 25 MOL_ID: 3; SOURCE 26 ORGANISM_SCIENTIFIC: HUMAN GAMMAHERPESVIRUS 4; SOURCE 27 ORGANISM_COMMON: EPSTEIN-BARR VIRUS; SOURCE 28 ORGANISM_TAXID: 10376; SOURCE 29 STRAIN: B95-8; SOURCE 30 GENE: BLLF1; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM_CELL_LINE: HEK293-EBNA1-6E; SOURCE 34 EXPRESSION_SYSTEM_ATCC_NUMBER: CVCL_HF20; SOURCE 35 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 36 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 37 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 39 EXPRESSION_SYSTEM_PLASMID: PTT3 KEYWDS VIRAL PROTEIN, COMPLEX, ANTIBODY, EBV, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR K.LANG,G.KHER,N.T.ALDRIDGE,M.PANCERA REVDAT 1 24-DEC-25 9PF9 0 JRNL AUTH C.B.CHAN,K.LANG,A.R.DAVIS,Y.H.WAN,N.T.ALDRIDGE,G.KHER, JRNL AUTH 2 S.C.SCHARFFENBERGER,S.R.HARDY,R.IURENIEV,N.V.GILTIAY, JRNL AUTH 3 K.R.EDWARDS,S.RADTKE,H.P.KIEM,M.PANCERA,A.MCGUIRE JRNL TITL TRANSGENIC MOUSE-DERIVED HUMAN MONOCLONAL ANTIBODIES JRNL TITL 2 TARGETING EBV GP350 AND GP42 PROVIDE BASIS FOR THERAPEUTIC JRNL TITL 3 DEVELOPMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 2.0_5793 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) : 3.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.900 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 12880 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.244 REMARK 3 R VALUE (WORKING SET) : 0.242 REMARK 3 FREE R VALUE : 0.282 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 624 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 46.2600 - 6.2300 1.00 3246 148 0.2311 0.2459 REMARK 3 2 6.2300 - 4.9500 1.00 3067 146 0.2396 0.2915 REMARK 3 3 4.9500 - 4.3200 1.00 2988 159 0.2431 0.3187 REMARK 3 4 4.3200 - 3.9300 0.99 2955 171 0.2765 0.3245 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) : 0.541 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.710 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 154.8 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 154.8 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 6665 REMARK 3 ANGLE : 0.588 9109 REMARK 3 CHIRALITY : 0.043 1054 REMARK 3 PLANARITY : 0.010 1161 REMARK 3 DIHEDRAL : 11.599 2416 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 9PF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000297535. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-DEC-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000040 REMARK 200 MONOCHROMATOR : LIQUID NITROGEN COOLED DUAL REMARK 200 CRYSTAL SI(111) RH/PT COATED SI REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.8.2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12880 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.928 REMARK 200 RESOLUTION RANGE LOW (A) : 46.260 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 12.70 REMARK 200 R MERGE (I) : 0.32800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.32 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.69500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE:HCL PH 5. 3.15 M REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 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 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 100.01500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.33750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.33750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 150.02250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.33750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.33750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.00750 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.33750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.33750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 150.02250 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.33750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.33750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.00750 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 100.01500 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, G, A 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 GLU L 1 REMARK 465 GLN H 1 REMARK 465 MET G 1 REMARK 465 GLU G 2 REMARK 465 ALA G 3 REMARK 465 ALA G 4 REMARK 465 LEU G 5 REMARK 465 LEU G 6 REMARK 465 VAL G 251 REMARK 465 ALA G 252 REMARK 465 THR G 253 REMARK 465 PRO G 254 REMARK 465 ILE G 255 REMARK 465 PRO G 290 REMARK 465 LYS G 291 REMARK 465 ALA G 292 REMARK 465 SER G 293 REMARK 465 SER G 427 REMARK 465 THR G 428 REMARK 465 THR G 429 REMARK 465 THR G 430 REMARK 465 SER G 431 REMARK 465 PRO G 432 REMARK 465 THR G 433 REMARK 465 LEU G 434 REMARK 465 ASN G 435 REMARK 465 THR G 436 REMARK 465 THR G 437 REMARK 465 GLY G 438 REMARK 465 PHE G 439 REMARK 465 ALA G 440 REMARK 465 ASP G 441 REMARK 465 PRO G 442 REMARK 465 ASN G 443 REMARK 465 THR G 444 REMARK 465 THR G 445 REMARK 465 THR G 446 REMARK 465 GLY G 447 REMARK 465 LEU G 448 REMARK 465 PRO G 449 REMARK 465 SER G 450 REMARK 465 SER G 451 REMARK 465 THR G 452 REMARK 465 HIS G 453 REMARK 465 VAL G 454 REMARK 465 PRO G 455 REMARK 465 THR G 456 REMARK 465 ASN G 457 REMARK 465 LEU G 458 REMARK 465 THR G 459 REMARK 465 ALA G 460 REMARK 465 PRO G 461 REMARK 465 ALA G 462 REMARK 465 SER G 463 REMARK 465 THR G 464 REMARK 465 GLY G 465 REMARK 465 PRO G 466 REMARK 465 THR G 467 REMARK 465 VAL G 468 REMARK 465 SER G 469 REMARK 465 THR G 470 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 ALA L 51 -5.75 70.71 REMARK 500 SER L 52 -33.81 -132.44 REMARK 500 SER L 65 -173.54 -170.93 REMARK 500 THR H 15 -1.16 65.87 REMARK 500 ARG H 33 -7.72 76.78 REMARK 500 ASN H 75 31.98 -140.68 REMARK 500 ARG H 99 49.44 -91.65 REMARK 500 TRP H 100 -111.96 52.21 REMARK 500 SER H 127 -178.84 -68.91 REMARK 500 SER H 132 141.00 -171.40 REMARK 500 ASP H 144 62.53 62.55 REMARK 500 THR G 38 -5.24 73.84 REMARK 500 PRO G 149 174.90 -59.95 REMARK 500 GLU G 155 146.57 -173.70 REMARK 500 GLN G 177 -5.69 67.03 REMARK 500 THR G 189 -104.21 63.33 REMARK 500 GLU G 206 -8.29 74.13 REMARK 500 THR G 267 80.81 -160.46 REMARK 500 PRO G 270 46.61 -96.29 REMARK 500 SER G 343 75.03 52.50 REMARK 500 CYS G 376 74.01 58.05 REMARK 500 ASN G 378 -5.33 74.11 REMARK 500 ARG G 387 -7.07 74.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG H 58 0.17 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9PF9 L 1 213 PDB 9PF9 9PF9 1 213 DBREF 9PF9 H 1 212 PDB 9PF9 9PF9 1 212 DBREF1 9PF9 G 1 470 UNP A0A0C7T6S7_EBVG DBREF2 9PF9 G A0A0C7T6S7 1 470 SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR LEU GLN SEQRES 4 L 214 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 214 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 214 SER GLY SER GLY THR ASP PHE THR LEU THR ILE ASN ARG SEQRES 7 L 214 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 214 TYR GLY SER SER HIS THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 220 GLN ILE THR LEU LYS GLU SER GLY PRO THR LEU VAL LYS SEQRES 2 H 220 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 H 220 PHE SER LEU ASN THR SER ARG VAL GLY VAL GLY TRP ILE SEQRES 4 H 220 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA LEU SEQRES 5 H 220 ILE TYR TRP ASN ASP ASP LYS ARG TYR SER PRO SER LEU SEQRES 6 H 220 LYS SER ARG LEU THR ILE THR LYS ASP THR SER ASN GLN SEQRES 7 H 220 VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP THR SEQRES 8 H 220 ALA THR TYR TYR CYS ALA HIS ARG TYR SER SER ARG TRP SEQRES 9 H 220 TYR TRP TYR PHE ASP LEU TRP GLY ARG GLY THR LEU VAL SEQRES 10 H 220 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 220 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 220 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 220 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 220 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 220 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 220 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 220 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 1 G 470 MET GLU ALA ALA LEU LEU VAL CYS GLN TYR THR ILE GLN SEQRES 2 G 470 SER LEU ILE HIS LEU THR GLY GLU ASP PRO GLY PHE PHE SEQRES 3 G 470 ASN VAL GLU ILE PRO GLU PHE PRO PHE TYR PRO THR CYS SEQRES 4 G 470 ASN VAL CYS THR ALA ASP VAL ASN VAL THR ILE ASN PHE SEQRES 5 G 470 ASP VAL GLY GLY LYS LYS HIS GLN LEU ASP LEU ASP PHE SEQRES 6 G 470 GLY GLN LEU THR PRO HIS THR LYS ALA VAL TYR GLN PRO SEQRES 7 G 470 ARG GLY ALA PHE GLY GLY SER GLU ASN ALA THR ASN LEU SEQRES 8 G 470 PHE LEU LEU GLU LEU LEU GLY ALA GLY GLU LEU ALA LEU SEQRES 9 G 470 THR MET ARG SER LYS LYS LEU PRO ILE ASN VAL THR THR SEQRES 10 G 470 GLY GLU GLU GLN GLN VAL SER LEU GLU SER VAL ASP VAL SEQRES 11 G 470 TYR PHE GLN ASP VAL PHE GLY THR MET TRP CYS HIS HIS SEQRES 12 G 470 ALA GLU MET GLN ASN PRO VAL TYR LEU ILE PRO GLU THR SEQRES 13 G 470 VAL PRO TYR ILE LYS TRP ASP ASN CYS ASN SER THR ASN SEQRES 14 G 470 ILE THR ALA VAL VAL ARG ALA GLN GLY LEU ASP VAL THR SEQRES 15 G 470 LEU PRO LEU SER LEU PRO THR SER ALA GLN ASP SER ASN SEQRES 16 G 470 PHE SER VAL LYS THR GLN MET LEU GLY ASN GLU ILE ASP SEQRES 17 G 470 ILE GLU CYS ILE MET GLU ASP GLY GLU ILE SER GLN VAL SEQRES 18 G 470 LEU PRO GLY ASP ASN LYS PHE ASN ILE THR CYS SER GLY SEQRES 19 G 470 TYR GLU SER HIS VAL PRO SER GLY GLY ILE LEU THR SER SEQRES 20 G 470 THR SER PRO VAL ALA THR PRO ILE PRO GLY THR GLY TYR SEQRES 21 G 470 ALA TYR SER LEU ARG LEU THR PRO ARG PRO VAL SER ARG SEQRES 22 G 470 PHE LEU GLY ASN ASN SER ILE LEU TYR VAL PHE TYR SER SEQRES 23 G 470 GLY ASN GLY PRO LYS ALA SER GLY GLY ASP TYR CYS ILE SEQRES 24 G 470 GLN SER ASN ILE VAL PHE SER ASP GLU ILE PRO ALA SER SEQRES 25 G 470 GLN ASP MET PRO THR ASN THR THR ASP ILE THR TYR VAL SEQRES 26 G 470 GLY ASP ASN ALA THR TYR SER VAL PRO MET VAL THR SER SEQRES 27 G 470 GLU ASP ALA ASN SER PRO ASN VAL THR VAL THR ALA PHE SEQRES 28 G 470 TRP ALA TRP PRO ASN ASN THR GLU THR ASP PHE LYS CYS SEQRES 29 G 470 LYS TRP THR LEU THR SER GLY THR PRO SER GLY CYS GLU SEQRES 30 G 470 ASN ILE SER GLY ALA PHE ALA SER ASN ARG THR PHE ASP SEQRES 31 G 470 ILE THR VAL SER GLY LEU GLY THR ALA PRO LYS THR LEU SEQRES 32 G 470 ILE ILE THR ARG THR ALA THR ASN ALA THR THR THR THR SEQRES 33 G 470 HIS LYS VAL ILE PHE SER LYS ALA PRO GLU SER THR THR SEQRES 34 G 470 THR SER PRO THR LEU ASN THR THR GLY PHE ALA ASP PRO SEQRES 35 G 470 ASN THR THR THR GLY LEU PRO SER SER THR HIS VAL PRO SEQRES 36 G 470 THR ASN LEU THR ALA PRO ALA SER THR GLY PRO THR VAL SEQRES 37 G 470 SER THR HET NAG A 1 27 HET NAG A 2 28 HET NAG G 501 28 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 4 NAG 3(C8 H15 N O6) FORMUL 6 HOH *6(H2 O) HELIX 1 AA1 GLU L 79 PHE L 83 5 5 HELIX 2 AA2 SER L 120 LYS L 125 1 6 HELIX 3 AA3 LYS L 182 LYS L 187 1 6 HELIX 4 AA4 PRO H 61 LYS H 64 5 4 HELIX 5 AA5 ASP H 83 THR H 87 5 5 HELIX 6 AA6 SER H 127 LYS H 129 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 ASN G 87 ASN G 90 5 4 HELIX 9 AA9 GLU G 119 GLN G 121 5 3 HELIX 10 AB1 SER G 272 GLY G 276 5 5 SHEET 1 AA1 4 LEU L 4 GLN L 6 0 SHEET 2 AA1 4 LEU L 21 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA1 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA2 6 LEU L 11 LEU L 13 0 SHEET 2 AA2 6 THR L 101 ILE L 105 1 O LYS L 102 N LEU L 11 SHEET 3 AA2 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA2 6 ARG L 45 TYR L 49 -1 O ARG L 45 N LEU L 37 SHEET 6 AA2 6 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA3 4 LEU L 11 LEU L 13 0 SHEET 2 AA3 4 THR L 101 ILE L 105 1 O LYS L 102 N LEU L 11 SHEET 3 AA3 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AA3 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 90 SHEET 1 AA4 4 VAL L 114 PHE L 117 0 SHEET 2 AA4 4 THR L 128 PHE L 138 -1 O VAL L 132 N PHE L 117 SHEET 3 AA4 4 TYR L 172 SER L 181 -1 O LEU L 178 N VAL L 131 SHEET 4 AA4 4 SER L 158 THR L 163 -1 N GLN L 159 O THR L 177 SHEET 1 AA5 4 ALA L 152 LEU L 153 0 SHEET 2 AA5 4 ALA L 143 VAL L 149 -1 N VAL L 149 O ALA L 152 SHEET 3 AA5 4 VAL L 190 HIS L 197 -1 O GLU L 194 N GLN L 146 SHEET 4 AA5 4 VAL L 204 ASN L 209 -1 O VAL L 204 N VAL L 195 SHEET 1 AA6 4 THR H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA6 4 GLN H 76 MET H 81 -1 O MET H 81 N LEU H 18 SHEET 4 AA6 4 LEU H 67 LYS H 71 -1 N THR H 70 O VAL H 78 SHEET 1 AA7 6 LEU H 11 VAL H 12 0 SHEET 2 AA7 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 6 ALA H 88 ARG H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 6 GLY H 35 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA7 6 GLU H 46 TYR H 52 -1 O ILE H 51 N VAL H 35A SHEET 6 AA7 6 LYS H 57 TYR H 59 -1 O ARG H 58 N LEU H 50 SHEET 1 AA8 4 LEU H 11 VAL H 12 0 SHEET 2 AA8 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA8 4 ALA H 88 ARG H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 4 LEU H 102 TRP H 103 -1 O LEU H 102 N HIS H 94 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA9 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB1 4 THR H 131 SER H 132 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB2 3 THR H 151 TRP H 154 0 SHEET 2 AB2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AB3 6 TYR G 10 LEU G 15 0 SHEET 2 AB3 6 MET G 139 GLU G 145 1 O HIS G 143 N ILE G 12 SHEET 3 AB3 6 VAL G 123 GLN G 133 -1 N PHE G 132 O TRP G 140 SHEET 4 AB3 6 ASP G 45 VAL G 54 -1 N THR G 49 O ASP G 129 SHEET 5 AB3 6 LYS G 57 GLN G 67 -1 O HIS G 59 N PHE G 52 SHEET 6 AB3 6 GLY G 80 ALA G 81 -1 O GLY G 80 N ASP G 64 SHEET 1 AB4 2 LEU G 18 THR G 19 0 SHEET 2 AB4 2 GLY G 234 TYR G 235 -1 O GLY G 234 N THR G 19 SHEET 1 AB5 4 PHE G 25 ILE G 30 0 SHEET 2 AB5 4 GLU G 101 ARG G 107 -1 O LEU G 104 N VAL G 28 SHEET 3 AB5 4 PHE G 92 GLY G 98 -1 N LEU G 93 O THR G 105 SHEET 4 AB5 4 VAL G 75 TYR G 76 -1 N TYR G 76 O LEU G 94 SHEET 1 AB610 GLY G 178 LEU G 179 0 SHEET 2 AB610 ALA G 172 ARG G 175 -1 N ARG G 175 O GLY G 178 SHEET 3 AB610 TYR G 297 PHE G 305 1 O VAL G 304 N VAL G 174 SHEET 4 AB610 ILE G 280 SER G 286 -1 N TYR G 285 O TYR G 297 SHEET 5 AB610 SER G 197 GLY G 204 -1 N LYS G 199 O PHE G 284 SHEET 6 AB610 ILE G 207 MET G 213 -1 O CYS G 211 N THR G 200 SHEET 7 AB610 ASP G 225 CYS G 232 -1 O THR G 231 N ILE G 212 SHEET 8 AB610 GLY G 242 THR G 246 -1 O LEU G 245 N ASN G 226 SHEET 9 AB610 GLY G 259 THR G 267 -1 O ARG G 265 N ILE G 244 SHEET 10 AB610 VAL G 181 PRO G 188 -1 N LEU G 185 O TYR G 262 SHEET 1 AB7 5 ASN G 318 ILE G 322 0 SHEET 2 AB7 5 THR G 415 PHE G 421 1 O ILE G 420 N ILE G 322 SHEET 3 AB7 5 LYS G 401 ALA G 409 -1 N LEU G 403 O VAL G 419 SHEET 4 AB7 5 VAL G 346 TRP G 352 -1 N PHE G 351 O ILE G 404 SHEET 5 AB7 5 LYS G 365 THR G 367 -1 O TRP G 366 N VAL G 348 SHEET 1 AB8 3 ALA G 329 VAL G 333 0 SHEET 2 AB8 3 PHE G 389 VAL G 393 -1 O PHE G 389 N VAL G 333 SHEET 3 AB8 3 ILE G 379 ALA G 382 -1 N SER G 380 O THR G 392 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 2 CYS L 133 CYS L 193 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 5 CYS G 8 CYS G 141 1555 1555 2.03 SSBOND 6 CYS G 39 CYS G 42 1555 1555 2.03 SSBOND 7 CYS G 165 CYS G 298 1555 1555 2.04 SSBOND 8 CYS G 211 CYS G 232 1555 1555 2.03 SSBOND 9 CYS G 364 CYS G 376 1555 1555 2.02 LINK ND2 ASN G 47 C1 NAG A 1 1555 1555 1.45 LINK ND2 ASN G 169 C1 NAG G 501 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 CRYST1 116.675 116.675 200.030 90.00 90.00 90.00 P 43 21 2 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 0.008571 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008571 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004999 0.00000