HEADER VIRAL PROTEIN/IMMUNE SYSTEM 27-MAY-24 9C0U TITLE CRYSTAL STRUCTURE OF CHIMERIC HEMAGGLUTININ CH5/1 IN COMPLEX WITH TITLE 2 BROAD PROTECTIVE ANTIBODY 31.B.09 CAVEAT 9C0U NAG S 2 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMAGGLUTININ; COMPND 3 CHAIN: B, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY 31.B.09 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ANTIBODY 31.B.09 FAB LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: HA; SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.K.Y.NGUYEN,X.ZHU,I.A.WILSON REVDAT 1 07-MAY-25 9C0U 0 JRNL AUTH T.K.Y.NGUYEN JRNL TITL CRYSTAL STRUCTURE OF CHIMERIC HEMAGGLUTININ CH5/1 IN COMPLEX JRNL TITL 2 WITH BROAD PROTECTIVE ANTIBODY 31.B.09 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.59 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???) 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) : 3.59 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.87 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 15950 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.297 REMARK 3 R VALUE (WORKING SET) : 0.294 REMARK 3 FREE R VALUE : 0.344 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 788 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 48.8700 - 6.5200 1.00 2768 146 0.2369 0.2832 REMARK 3 2 6.5100 - 5.1800 1.00 2674 144 0.3157 0.3784 REMARK 3 3 5.1700 - 4.5200 1.00 2659 130 0.2947 0.3694 REMARK 3 4 4.5200 - 4.1100 1.00 2667 123 0.3075 0.3520 REMARK 3 5 4.1100 - 3.8200 0.83 2172 129 0.3979 0.4422 REMARK 3 6 3.8100 - 3.5900 0.84 2222 116 0.4175 0.4059 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 : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.770 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.410 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.005 7447 REMARK 3 ANGLE : 0.827 10115 REMARK 3 CHIRALITY : 0.050 1123 REMARK 3 PLANARITY : 0.008 1302 REMARK 3 DIHEDRAL : 7.402 1011 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 9C0U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000284514. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAY-22 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16876 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.590 REMARK 200 RESOLUTION RANGE LOW (A) : 48.870 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 39.60 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.59 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.61 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5, 20% W/V PEG1000, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+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 81.03950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.03950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.03950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.03950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 81.03950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.03950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 81.03950 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 81.03950 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 81.03950 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 81.03950 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 81.03950 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 81.03950 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 81.03950 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 81.03950 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 81.03950 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 81.03950 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 81.03950 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 81.03950 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 APPLY THE FOLLOWING TO CHAINS: B, H, L, A, S, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY B -326 REMARK 465 ASP B -325 REMARK 465 THR B -324 REMARK 465 LEU B -323 REMARK 465 CYS B -322 REMARK 465 ILE B -321 REMARK 465 GLY B -320 REMARK 465 TYR B -319 REMARK 465 HIS B -318 REMARK 465 ALA B -317 REMARK 465 ASN B -316 REMARK 465 ASN B -315 REMARK 465 SER B -314 REMARK 465 THR B -313 REMARK 465 ASP B -312 REMARK 465 THR B -311 REMARK 465 VAL B -310 REMARK 465 ASP B -309 REMARK 465 THR B -308 REMARK 465 VAL B -307 REMARK 465 LEU B -306 REMARK 465 GLU B -305 REMARK 465 LYS B -304 REMARK 465 ASN B -303 REMARK 465 VAL B -302 REMARK 465 THR B -301 REMARK 465 VAL B -300 REMARK 465 THR B -299 REMARK 465 HIS B -298 REMARK 465 SER B -297 REMARK 465 VAL B -296 REMARK 465 ASN B -295 REMARK 465 LEU B -294 REMARK 465 LEU B -293 REMARK 465 GLU B -292 REMARK 465 ASP B -291 REMARK 465 LYS B -290 REMARK 465 HIS B -289 REMARK 465 ASN B -288 REMARK 465 GLY B -287 REMARK 465 LYS B -286 REMARK 465 LEU B -285 REMARK 465 CYS B -284 REMARK 465 ASP B -283 REMARK 465 LEU B -282 REMARK 465 ASP B -281 REMARK 465 GLY B -280 REMARK 465 VAL B -279 REMARK 465 LYS B -278 REMARK 465 PRO B -277 REMARK 465 LEU B -276 REMARK 465 ILE B -275 REMARK 465 LEU B -274 REMARK 465 ARG B -273 REMARK 465 ASP B -272 REMARK 465 CYS B -271 REMARK 465 SER B -270 REMARK 465 VAL B -269 REMARK 465 ALA B -268 REMARK 465 GLY B -267 REMARK 465 TRP B -266 REMARK 465 LEU B -265 REMARK 465 LEU B -264 REMARK 465 GLY B -263 REMARK 465 ASN B -262 REMARK 465 PRO B -261 REMARK 465 MET B -260 REMARK 465 CYS B -259 REMARK 465 ASP B -258 REMARK 465 GLU B -257 REMARK 465 PHE B -256 REMARK 465 ILE B -255 REMARK 465 ASN B -254 REMARK 465 VAL B -253 REMARK 465 PRO B -252 REMARK 465 GLU B -251 REMARK 465 TRP B -250 REMARK 465 SER B -249 REMARK 465 TYR B -248 REMARK 465 ILE B -247 REMARK 465 VAL B -246 REMARK 465 GLU B -245 REMARK 465 LYS B -244 REMARK 465 ALA B -243 REMARK 465 ASN B -242 REMARK 465 PRO B -241 REMARK 465 VAL B -240 REMARK 465 ASN B -239 REMARK 465 ASP B -238 REMARK 465 LEU B -237 REMARK 465 CYS B -236 REMARK 465 TYR B -235 REMARK 465 PRO B -234 REMARK 465 GLY B -233 REMARK 465 ASP B -232 REMARK 465 PHE B -231 REMARK 465 ASN B -230 REMARK 465 ASP B -229 REMARK 465 TYR B -228 REMARK 465 GLU B -227 REMARK 465 GLU B -226 REMARK 465 LEU B -225 REMARK 465 LYS B -224 REMARK 465 HIS B -223 REMARK 465 LEU B -222 REMARK 465 LEU B -221 REMARK 465 SER B -220 REMARK 465 ARG B -219 REMARK 465 ILE B -218 REMARK 465 ASN B -217 REMARK 465 HIS B -216 REMARK 465 PHE B -215 REMARK 465 GLU B -214 REMARK 465 LYS B -213 REMARK 465 ILE B -212 REMARK 465 GLN B -211 REMARK 465 ILE B -210 REMARK 465 ILE B -209 REMARK 465 PRO B -208 REMARK 465 LYS B -207 REMARK 465 SER B -206 REMARK 465 SER B -205 REMARK 465 TRP B -204 REMARK 465 SER B -203 REMARK 465 SER B -202 REMARK 465 HIS B -201 REMARK 465 GLU B -200 REMARK 465 ALA B -199 REMARK 465 SER B -198 REMARK 465 LEU B -197 REMARK 465 GLY B -196 REMARK 465 VAL B -195 REMARK 465 SER B -194 REMARK 465 SER B -193 REMARK 465 ALA B -192 REMARK 465 CYS B -191 REMARK 465 PRO B -190 REMARK 465 TYR B -189 REMARK 465 GLN B -188 REMARK 465 GLY B -187 REMARK 465 LYS B -186 REMARK 465 SER B -185 REMARK 465 SER B -184 REMARK 465 PHE B -183 REMARK 465 PHE B -182 REMARK 465 ARG B -181 REMARK 465 ASN B -180 REMARK 465 VAL B -179 REMARK 465 VAL B -178 REMARK 465 TRP B -177 REMARK 465 LEU B -176 REMARK 465 ILE B -175 REMARK 465 LYS B -174 REMARK 465 LYS B -173 REMARK 465 ASN B -172 REMARK 465 SER B -171 REMARK 465 THR B -170 REMARK 465 TYR B -169 REMARK 465 PRO B -168 REMARK 465 THR B -167 REMARK 465 ILE B -166 REMARK 465 LYS B -165 REMARK 465 ARG B -164 REMARK 465 SER B -163 REMARK 465 TYR B -162 REMARK 465 ASN B -161 REMARK 465 ASN B -160 REMARK 465 THR B -159 REMARK 465 ASN B -158 REMARK 465 GLN B -157 REMARK 465 GLU B -156 REMARK 465 ASP B -155 REMARK 465 LEU B -154 REMARK 465 LEU B -153 REMARK 465 VAL B -152 REMARK 465 LEU B -151 REMARK 465 TRP B -150 REMARK 465 GLY B -149 REMARK 465 ILE B -148 REMARK 465 HIS B -147 REMARK 465 HIS B -146 REMARK 465 PRO B -145 REMARK 465 ASN B -144 REMARK 465 ASP B -143 REMARK 465 ALA B -142 REMARK 465 ALA B -141 REMARK 465 GLU B -140 REMARK 465 GLN B -139 REMARK 465 THR B -138 REMARK 465 LYS B -137 REMARK 465 LEU B -136 REMARK 465 TYR B -135 REMARK 465 GLN B -134 REMARK 465 ASN B -133 REMARK 465 PRO B -132 REMARK 465 THR B -131 REMARK 465 THR B -130 REMARK 465 TYR B -129 REMARK 465 ILE B -128 REMARK 465 SER B -127 REMARK 465 VAL B -126 REMARK 465 GLY B -125 REMARK 465 THR B -124 REMARK 465 SER B -123 REMARK 465 THR B -122 REMARK 465 LEU B -121 REMARK 465 ASN B -120 REMARK 465 GLN B -119 REMARK 465 ARG B -118 REMARK 465 LEU B -117 REMARK 465 VAL B -116 REMARK 465 PRO B -115 REMARK 465 ARG B -114 REMARK 465 ILE B -113 REMARK 465 ALA B -112 REMARK 465 THR B -111 REMARK 465 ARG B -110 REMARK 465 SER B -109 REMARK 465 LYS B -108 REMARK 465 VAL B -107 REMARK 465 ASN B -106 REMARK 465 GLY B -105 REMARK 465 GLN B -104 REMARK 465 SER B -103 REMARK 465 GLY B -102 REMARK 465 ARG B -101 REMARK 465 MET B -100 REMARK 465 GLU B -99 REMARK 465 PHE B -98 REMARK 465 PHE B -97 REMARK 465 TRP B -96 REMARK 465 THR B -95 REMARK 465 ILE B -94 REMARK 465 LEU B -93 REMARK 465 LYS B -92 REMARK 465 PRO B -91 REMARK 465 ASN B -90 REMARK 465 ASP B -89 REMARK 465 ALA B -88 REMARK 465 ILE B -87 REMARK 465 ASN B -86 REMARK 465 PHE B -85 REMARK 465 GLU B -84 REMARK 465 SER B -83 REMARK 465 ASN B -82 REMARK 465 GLY B -81 REMARK 465 ASN B -80 REMARK 465 PHE B -79 REMARK 465 ILE B -78 REMARK 465 ALA B -77 REMARK 465 PRO B -76 REMARK 465 GLU B -75 REMARK 465 TYR B -74 REMARK 465 ALA B -73 REMARK 465 TYR B -72 REMARK 465 LYS B -71 REMARK 465 ILE B -70 REMARK 465 VAL B -69 REMARK 465 LYS B -68 REMARK 465 LYS B -67 REMARK 465 GLY B -66 REMARK 465 ASP B -65 REMARK 465 SER B -64 REMARK 465 THR B -63 REMARK 465 ILE B -62 REMARK 465 MET B -61 REMARK 465 LYS B -60 REMARK 465 SER B -59 REMARK 465 GLU B -58 REMARK 465 LEU B -57 REMARK 465 GLU B -56 REMARK 465 TYR B -55 REMARK 465 GLY B -54 REMARK 465 ASN B -53 REMARK 465 CYS B -52 REMARK 465 ASN B -51 REMARK 465 THR B -50 REMARK 465 THR B -49 REMARK 465 CYS B -48 REMARK 465 GLN B -47 REMARK 465 THR B -46 REMARK 465 PRO B -45 REMARK 465 LYS B -44 REMARK 465 GLY B -43 REMARK 465 ALA B -42 REMARK 465 ILE B -41 REMARK 465 ASN B -40 REMARK 465 THR B -39 REMARK 465 SER B -38 REMARK 465 LEU B -37 REMARK 465 PRO B -36 REMARK 465 PHE B -35 REMARK 465 GLN B -34 REMARK 465 ASN B -33 REMARK 465 ILE B -32 REMARK 465 HIS B -31 REMARK 465 PRO B -30 REMARK 465 ILE B -29 REMARK 465 THR B -28 REMARK 465 ILE B -27 REMARK 465 GLY B -26 REMARK 465 LYS B -25 REMARK 465 CYS B -24 REMARK 465 PRO B -23 REMARK 465 LYS B -22 REMARK 465 TYR B -21 REMARK 465 VAL B -20 REMARK 465 LYS B -19 REMARK 465 SER B -18 REMARK 465 THR B -17 REMARK 465 LYS B -16 REMARK 465 LEU B -15 REMARK 465 ARG B -14 REMARK 465 LEU B -13 REMARK 465 ALA B -12 REMARK 465 THR B -11 REMARK 465 GLY B -10 REMARK 465 LEU B -9 REMARK 465 ARG B -8 REMARK 465 ASN B -7 REMARK 465 VAL B -6 REMARK 465 PRO B -5 REMARK 465 SER B -4 REMARK 465 ILE B -3 REMARK 465 GLN B -2 REMARK 465 SER B -1 REMARK 465 ARG B 0 REMARK 465 GLY B 1 REMARK 465 LEU B 2 REMARK 465 PHE B 3 REMARK 465 GLY B 4 REMARK 465 ALA B 5 REMARK 465 ILE B 6 REMARK 465 ALA B 7 REMARK 465 GLY B 8 REMARK 465 PHE B 9 REMARK 465 SER B 175 REMARK 465 GLY B 176 REMARK 465 ARG B 177 REMARK 465 ILE A 326 REMARK 465 GLN A 327 REMARK 465 SER A 328 REMARK 465 ARG A 329 REMARK 465 GLY A 330 REMARK 465 LEU A 331 REMARK 465 PHE A 332 REMARK 465 GLY A 333 REMARK 465 ALA A 334 REMARK 465 ILE A 335 REMARK 465 ALA A 336 REMARK 465 GLY A 337 REMARK 465 PHE A 338 REMARK 465 ILE A 339 REMARK 465 GLU A 340 REMARK 465 GLY A 341 REMARK 465 GLY A 342 REMARK 465 TRP A 343 REMARK 465 THR A 344 REMARK 465 GLY A 345 REMARK 465 MET A 346 REMARK 465 VAL A 347 REMARK 465 ASP A 348 REMARK 465 GLY A 349 REMARK 465 TRP A 350 REMARK 465 TYR A 351 REMARK 465 GLY A 352 REMARK 465 TYR A 353 REMARK 465 HIS A 354 REMARK 465 HIS A 355 REMARK 465 GLN A 356 REMARK 465 ASN A 357 REMARK 465 GLU A 358 REMARK 465 GLN A 359 REMARK 465 GLY A 360 REMARK 465 SER A 361 REMARK 465 GLY A 362 REMARK 465 TYR A 363 REMARK 465 ALA A 364 REMARK 465 ALA A 365 REMARK 465 ASP A 366 REMARK 465 LEU A 367 REMARK 465 LYS A 368 REMARK 465 SER A 369 REMARK 465 THR A 370 REMARK 465 GLN A 371 REMARK 465 ASN A 372 REMARK 465 ALA A 373 REMARK 465 ILE A 374 REMARK 465 ASP A 375 REMARK 465 GLY A 376 REMARK 465 ILE A 377 REMARK 465 THR A 378 REMARK 465 ASN A 379 REMARK 465 LYS A 380 REMARK 465 VAL A 381 REMARK 465 ASN A 382 REMARK 465 SER A 383 REMARK 465 VAL A 384 REMARK 465 ILE A 385 REMARK 465 GLU A 386 REMARK 465 LYS A 387 REMARK 465 MET A 388 REMARK 465 ASN A 389 REMARK 465 THR A 390 REMARK 465 GLN A 391 REMARK 465 PHE A 392 REMARK 465 THR A 393 REMARK 465 ALA A 394 REMARK 465 VAL A 395 REMARK 465 GLY A 396 REMARK 465 LYS A 397 REMARK 465 GLU A 398 REMARK 465 PHE A 399 REMARK 465 ASN A 400 REMARK 465 HIS A 401 REMARK 465 LEU A 402 REMARK 465 GLU A 403 REMARK 465 LYS A 404 REMARK 465 ARG A 405 REMARK 465 ILE A 406 REMARK 465 GLU A 407 REMARK 465 ASN A 408 REMARK 465 LEU A 409 REMARK 465 ASN A 410 REMARK 465 LYS A 411 REMARK 465 LYS A 412 REMARK 465 VAL A 413 REMARK 465 ASP A 414 REMARK 465 ASP A 415 REMARK 465 GLY A 416 REMARK 465 PHE A 417 REMARK 465 LEU A 418 REMARK 465 ASP A 419 REMARK 465 ILE A 420 REMARK 465 TRP A 421 REMARK 465 THR A 422 REMARK 465 TYR A 423 REMARK 465 ASN A 424 REMARK 465 ALA A 425 REMARK 465 GLU A 426 REMARK 465 LEU A 427 REMARK 465 LEU A 428 REMARK 465 VAL A 429 REMARK 465 LEU A 430 REMARK 465 LEU A 431 REMARK 465 GLU A 432 REMARK 465 ASN A 433 REMARK 465 GLU A 434 REMARK 465 ARG A 435 REMARK 465 THR A 436 REMARK 465 LEU A 437 REMARK 465 ASP A 438 REMARK 465 TYR A 439 REMARK 465 HIS A 440 REMARK 465 ASP A 441 REMARK 465 SER A 442 REMARK 465 ASN A 443 REMARK 465 VAL A 444 REMARK 465 LYS A 445 REMARK 465 ASN A 446 REMARK 465 LEU A 447 REMARK 465 TYR A 448 REMARK 465 GLU A 449 REMARK 465 LYS A 450 REMARK 465 VAL A 451 REMARK 465 ARG A 452 REMARK 465 SER A 453 REMARK 465 GLN A 454 REMARK 465 LEU A 455 REMARK 465 LYS A 456 REMARK 465 ASN A 457 REMARK 465 ASN A 458 REMARK 465 ALA A 459 REMARK 465 LYS A 460 REMARK 465 GLU A 461 REMARK 465 ILE A 462 REMARK 465 GLY A 463 REMARK 465 ASN A 464 REMARK 465 GLY A 465 REMARK 465 CYS A 466 REMARK 465 PHE A 467 REMARK 465 GLU A 468 REMARK 465 PHE A 469 REMARK 465 TYR A 470 REMARK 465 HIS A 471 REMARK 465 LYS A 472 REMARK 465 CYS A 473 REMARK 465 ASP A 474 REMARK 465 ASN A 475 REMARK 465 THR A 476 REMARK 465 CYS A 477 REMARK 465 MET A 478 REMARK 465 GLU A 479 REMARK 465 SER A 480 REMARK 465 VAL A 481 REMARK 465 LYS A 482 REMARK 465 ASN A 483 REMARK 465 GLY A 484 REMARK 465 THR A 485 REMARK 465 TYR A 486 REMARK 465 ASP A 487 REMARK 465 TYR A 488 REMARK 465 PRO A 489 REMARK 465 LYS A 490 REMARK 465 TYR A 491 REMARK 465 SER A 492 REMARK 465 GLU A 493 REMARK 465 GLU A 494 REMARK 465 ALA A 495 REMARK 465 LYS A 496 REMARK 465 LEU A 497 REMARK 465 ASN A 498 REMARK 465 ARG A 499 REMARK 465 GLU A 500 REMARK 465 GLU A 501 REMARK 465 ILE A 502 REMARK 465 ASP A 503 REMARK 465 SER A 504 REMARK 465 GLY A 505 REMARK 465 ARG A 506 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 52 O CYS A 277 1.89 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 PRO A 198 CD PRO A 198 N -0.098 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 ALA H 123 N - CA - CB ANGL. DEV. = 11.4 DEGREES REMARK 500 ARG L 51 CB - CA - C ANGL. DEV. = -14.0 DEGREES REMARK 500 LEU L 52 N - CA - CB ANGL. DEV. = -12.7 DEGREES REMARK 500 PRO L 100 N - CA - C ANGL. DEV. = -16.2 DEGREES REMARK 500 ASN L 143 CB - CA - C ANGL. DEV. = -18.4 DEGREES REMARK 500 CYS L 199 O - C - N ANGL. DEV. = 13.4 DEGREES REMARK 500 ASP A 55 N - CA - CB ANGL. DEV. = 11.8 DEGREES REMARK 500 GLU A 131 N - CA - CB ANGL. DEV. = -13.1 DEGREES REMARK 500 GLN A 142 CB - CA - C ANGL. DEV. = 18.7 DEGREES REMARK 500 ASN A 170 N - CA - C ANGL. DEV. = -18.6 DEGREES REMARK 500 THR A 171 N - CA - C ANGL. DEV. = -22.9 DEGREES REMARK 500 PRO A 254 CB - CA - C ANGL. DEV. = -14.7 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 HIS B 72 -0.82 66.71 REMARK 500 ASP B 90 -11.70 72.48 REMARK 500 LYS B 127 -134.75 53.26 REMARK 500 ASN B 154 1.75 -68.93 REMARK 500 SER H 25 -168.78 -168.86 REMARK 500 PHE H 29 53.75 -102.98 REMARK 500 SER H 31 2.99 59.75 REMARK 500 ASN H 55 -156.07 -132.87 REMARK 500 LYS H 138 -3.11 64.24 REMARK 500 SER H 139 -138.23 57.52 REMARK 500 ASN L 39 109.07 -53.23 REMARK 500 LEU L 52 -80.11 -115.42 REMARK 500 ASN L 55 -127.62 58.21 REMARK 500 GLU L 84 -157.21 -102.79 REMARK 500 LYS L 112 -157.71 -145.26 REMARK 500 VAL L 151 99.87 -69.67 REMARK 500 THR L 177 93.26 -163.83 REMARK 500 SER L 181 66.27 -150.98 REMARK 500 PHE L 214 66.01 61.17 REMARK 500 ASN L 215 172.41 -59.57 REMARK 500 ASN A 20 -156.43 -126.48 REMARK 500 ASP A 55 46.90 -146.45 REMARK 500 ARG A 62 -123.73 40.36 REMARK 500 ILE A 80 -64.80 -127.80 REMARK 500 ASN A 81 35.53 -98.80 REMARK 500 PRO A 83 -173.44 -64.65 REMARK 500 CYS A 97 9.38 53.91 REMARK 500 TYR A 98 164.50 67.50 REMARK 500 ASP A 104 44.15 38.11 REMARK 500 GLU A 131 -160.52 -125.69 REMARK 500 GLN A 142 -56.35 -139.65 REMARK 500 GLU A 174 148.32 -170.15 REMARK 500 THR A 206 -159.20 -119.64 REMARK 500 ILE A 217 77.17 -102.44 REMARK 500 ALA A 218 116.82 -168.11 REMARK 500 THR A 219 -157.76 -142.76 REMARK 500 ARG A 220 -157.04 -118.42 REMARK 500 SER A 265 -167.77 -160.30 REMARK 500 THR A 266 -168.81 -163.44 REMARK 500 ASN A 276 66.76 -103.03 REMARK 500 THR A 290 -154.93 -116.14 REMARK 500 CYS A 305 125.11 -177.30 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 B 76 0.20 SIDE CHAIN REMARK 500 ARG H 98 0.23 SIDE CHAIN REMARK 500 ARG L 50 0.13 SIDE CHAIN REMARK 500 ARG L 51 0.13 SIDE CHAIN REMARK 500 ARG L 113 0.28 SIDE CHAIN REMARK 500 ARG A 216 0.09 SIDE CHAIN 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 NAG S 1 REMARK 610 NAG C 1 REMARK 610 NAG A 601 DBREF 9C0U B -326 177 PDB 9C0U 9C0U -326 177 DBREF 9C0U H 1 224 PDB 9C0U 9C0U 1 224 DBREF 9C0U L 1 218 PDB 9C0U 9C0U 1 218 DBREF 9C0U A 10 506 PDB 9C0U 9C0U 10 506 SEQRES 1 B 504 GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN ASN SER SEQRES 2 B 504 THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR SEQRES 3 B 504 VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS HIS ASN SEQRES 4 B 504 GLY LYS LEU CYS ASP LEU ASP GLY VAL LYS PRO LEU ILE SEQRES 5 B 504 LEU ARG ASP CYS SER VAL ALA GLY TRP LEU LEU GLY ASN SEQRES 6 B 504 PRO MET CYS ASP GLU PHE ILE ASN VAL PRO GLU TRP SER SEQRES 7 B 504 TYR ILE VAL GLU LYS ALA ASN PRO VAL ASN ASP LEU CYS SEQRES 8 B 504 TYR PRO GLY ASP PHE ASN ASP TYR GLU GLU LEU LYS HIS SEQRES 9 B 504 LEU LEU SER ARG ILE ASN HIS PHE GLU LYS ILE GLN ILE SEQRES 10 B 504 ILE PRO LYS SER SER TRP SER SER HIS GLU ALA SER LEU SEQRES 11 B 504 GLY VAL SER SER ALA CYS PRO TYR GLN GLY LYS SER SER SEQRES 12 B 504 PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS ASN SER SEQRES 13 B 504 THR TYR PRO THR ILE LYS ARG SER TYR ASN ASN THR ASN SEQRES 14 B 504 GLN GLU ASP LEU LEU VAL LEU TRP GLY ILE HIS HIS PRO SEQRES 15 B 504 ASN ASP ALA ALA GLU GLN THR LYS LEU TYR GLN ASN PRO SEQRES 16 B 504 THR THR TYR ILE SER VAL GLY THR SER THR LEU ASN GLN SEQRES 17 B 504 ARG LEU VAL PRO ARG ILE ALA THR ARG SER LYS VAL ASN SEQRES 18 B 504 GLY GLN SER GLY ARG MET GLU PHE PHE TRP THR ILE LEU SEQRES 19 B 504 LYS PRO ASN ASP ALA ILE ASN PHE GLU SER ASN GLY ASN SEQRES 20 B 504 PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL LYS LYS SEQRES 21 B 504 GLY ASP SER THR ILE MET LYS SER GLU LEU GLU TYR GLY SEQRES 22 B 504 ASN CYS ASN THR THR CYS GLN THR PRO LYS GLY ALA ILE SEQRES 23 B 504 ASN THR SER LEU PRO PHE GLN ASN ILE HIS PRO ILE THR SEQRES 24 B 504 ILE GLY LYS CYS PRO LYS TYR VAL LYS SER THR LYS LEU SEQRES 25 B 504 ARG LEU ALA THR GLY LEU ARG ASN VAL PRO SER ILE GLN SEQRES 26 B 504 SER ARG GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU SEQRES 27 B 504 GLY GLY TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR SEQRES 28 B 504 HIS HIS GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP SEQRES 29 B 504 LEU LYS SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN SEQRES 30 B 504 LYS VAL ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE SEQRES 31 B 504 THR ALA VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG SEQRES 32 B 504 ILE GLU ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU SEQRES 33 B 504 ASP ILE TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU SEQRES 34 B 504 GLU ASN GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL SEQRES 35 B 504 LYS ASN LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN SEQRES 36 B 504 ASN ALA LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR SEQRES 37 B 504 HIS LYS CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN SEQRES 38 B 504 GLY THR TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS SEQRES 39 B 504 LEU ASN ARG GLU GLU ILE ASP SER GLY ARG SEQRES 1 H 224 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 224 TYR SER PHE SER SER TYR GLY ILE SER TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE SER SEQRES 5 H 224 ALA TYR ASN GLY ASN THR ASN TYR ALA GLN LYS LEU GLN SEQRES 6 H 224 GLY ARG VAL THR MET THR THR ASP THR SER THR SER THR SEQRES 7 H 224 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR SEQRES 8 H 224 ALA VAL PHE TYR CYS ALA ARG ASP ARG PRO HIS ILE LEU SEQRES 9 H 224 THR GLY PHE ASP PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 H 224 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 224 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 224 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 224 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 224 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 224 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 224 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 224 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 224 PRO LYS SER SEQRES 1 L 218 ASP VAL VAL MET THR GLN SER PRO VAL SER LEU PRO VAL SEQRES 2 L 218 THR LEU GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 218 GLN GLY LEU VAL TYR ILE ASP GLY ASN THR TYR LEU ASN SEQRES 4 L 218 TRP PHE GLN GLN ARG PRO GLY GLN SER PRO ARG ARG LEU SEQRES 5 L 218 ILE TYR ASN VAL PHE THR ARG ASP SER GLY VAL PRO ASP SEQRES 6 L 218 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 218 LYS ILE THR THR VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 L 218 TYR CYS MET GLN GLY THR HIS TRP PRO TYR THR PHE GLY SEQRES 9 L 218 GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 218 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 218 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 218 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 218 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 218 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 218 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 218 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 218 PRO VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 1 A 504 GLY ASP THR LEU CYS ILE GLY TYR HIS ALA ASN ASN SER SEQRES 2 A 504 THR ASP THR VAL ASP THR VAL LEU GLU LYS ASN VAL THR SEQRES 3 A 504 VAL THR HIS SER VAL ASN LEU LEU GLU ASP LYS HIS ASN SEQRES 4 A 504 GLY LYS LEU CYS ASP LEU ASP GLY VAL LYS PRO LEU ILE SEQRES 5 A 504 LEU ARG ASP CYS SER VAL ALA GLY TRP LEU LEU GLY ASN SEQRES 6 A 504 PRO MET CYS ASP GLU PHE ILE ASN VAL PRO GLU TRP SER SEQRES 7 A 504 TYR ILE VAL GLU LYS ALA ASN PRO VAL ASN ASP LEU CYS SEQRES 8 A 504 TYR PRO GLY ASP PHE ASN ASP TYR GLU GLU LEU LYS HIS SEQRES 9 A 504 LEU LEU SER ARG ILE ASN HIS PHE GLU LYS ILE GLN ILE SEQRES 10 A 504 ILE PRO LYS SER SER TRP SER SER HIS GLU ALA SER LEU SEQRES 11 A 504 GLY VAL SER SER ALA CYS PRO TYR GLN GLY LYS SER SER SEQRES 12 A 504 PHE PHE ARG ASN VAL VAL TRP LEU ILE LYS LYS ASN SER SEQRES 13 A 504 THR TYR PRO THR ILE LYS ARG SER TYR ASN ASN THR ASN SEQRES 14 A 504 GLN GLU ASP LEU LEU VAL LEU TRP GLY ILE HIS HIS PRO SEQRES 15 A 504 ASN ASP ALA ALA GLU GLN THR LYS LEU TYR GLN ASN PRO SEQRES 16 A 504 THR THR TYR ILE SER VAL GLY THR SER THR LEU ASN GLN SEQRES 17 A 504 ARG LEU VAL PRO ARG ILE ALA THR ARG SER LYS VAL ASN SEQRES 18 A 504 GLY GLN SER GLY ARG MET GLU PHE PHE TRP THR ILE LEU SEQRES 19 A 504 LYS PRO ASN ASP ALA ILE ASN PHE GLU SER ASN GLY ASN SEQRES 20 A 504 PHE ILE ALA PRO GLU TYR ALA TYR LYS ILE VAL LYS LYS SEQRES 21 A 504 GLY ASP SER THR ILE MET LYS SER GLU LEU GLU TYR GLY SEQRES 22 A 504 ASN CYS ASN THR THR CYS GLN THR PRO LYS GLY ALA ILE SEQRES 23 A 504 ASN THR SER LEU PRO PHE GLN ASN ILE HIS PRO ILE THR SEQRES 24 A 504 ILE GLY LYS CYS PRO LYS TYR VAL LYS SER THR LYS LEU SEQRES 25 A 504 ARG LEU ALA THR GLY LEU ARG ASN VAL PRO SER ILE GLN SEQRES 26 A 504 SER ARG GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU SEQRES 27 A 504 GLY GLY TRP THR GLY MET VAL ASP GLY TRP TYR GLY TYR SEQRES 28 A 504 HIS HIS GLN ASN GLU GLN GLY SER GLY TYR ALA ALA ASP SEQRES 29 A 504 LEU LYS SER THR GLN ASN ALA ILE ASP GLY ILE THR ASN SEQRES 30 A 504 LYS VAL ASN SER VAL ILE GLU LYS MET ASN THR GLN PHE SEQRES 31 A 504 THR ALA VAL GLY LYS GLU PHE ASN HIS LEU GLU LYS ARG SEQRES 32 A 504 ILE GLU ASN LEU ASN LYS LYS VAL ASP ASP GLY PHE LEU SEQRES 33 A 504 ASP ILE TRP THR TYR ASN ALA GLU LEU LEU VAL LEU LEU SEQRES 34 A 504 GLU ASN GLU ARG THR LEU ASP TYR HIS ASP SER ASN VAL SEQRES 35 A 504 LYS ASN LEU TYR GLU LYS VAL ARG SER GLN LEU LYS ASN SEQRES 36 A 504 ASN ALA LYS GLU ILE GLY ASN GLY CYS PHE GLU PHE TYR SEQRES 37 A 504 HIS LYS CYS ASP ASN THR CYS MET GLU SER VAL LYS ASN SEQRES 38 A 504 GLY THR TYR ASP TYR PRO LYS TYR SER GLU GLU ALA LYS SEQRES 39 A 504 LEU ASN ARG GLU GLU ILE ASP SER GLY ARG HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET NAG C 1 14 HET NAG C 2 14 HET NAG A 601 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 5 NAG 5(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 HELIX 1 AA1 ASP B 37 GLU B 57 1 21 HELIX 2 AA2 ARG B 76 LEU B 89 1 14 HELIX 3 AA3 ILE B 91 LYS B 127 1 37 HELIX 4 AA4 ASP B 145 ASN B 154 1 10 HELIX 5 AA5 ASP B 158 ASP B 174 1 17 HELIX 6 AA6 GLU L 128 GLY L 133 1 6 HELIX 7 AA7 LYS L 188 HIS L 194 1 7 HELIX 8 AA8 SER A 65 GLY A 72 1 8 HELIX 9 AA9 ASP A 104 SER A 113 1 10 HELIX 10 AB1 LYS A 125A SER A 129 1 6 HELIX 11 AB2 ASP A 187 TYR A 195 1 9 HELIX 12 AB3 LYS A 222 GLN A 226 5 5 SHEET 1 AA1 5 SER B 32 ALA B 36 0 SHEET 2 AA1 5 GLY B 23 GLN B 27 -1 N TYR B 24 O ALA B 35 SHEET 3 AA1 5 THR A 12 GLY A 16 -1 O CYS A 14 N HIS B 25 SHEET 4 AA1 5 CYS B 137 PHE B 140 -1 N PHE B 138 O LEU A 13 SHEET 5 AA1 5 ALA B 130 ILE B 133 -1 N ILE B 133 O CYS B 137 SHEET 1 AA2 4 GLN H 3 GLN H 6 0 SHEET 2 AA2 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA2 4 THR H 78 LEU H 83 -1 O MET H 81 N VAL H 20 SHEET 4 AA2 4 VAL H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA3 5 GLU H 10 LYS H 12 0 SHEET 2 AA3 5 THR H 116 VAL H 120 1 O THR H 119 N LYS H 12 SHEET 3 AA3 5 ALA H 92 ASP H 99 -1 N ALA H 92 O VAL H 118 SHEET 4 AA3 5 GLY H 33 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA3 5 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 1 AA4 4 SER H 129 PRO H 132 0 SHEET 2 AA4 4 ALA H 145 LYS H 152 -1 O LEU H 150 N PHE H 131 SHEET 3 AA4 4 TYR H 185 VAL H 193 -1 O LEU H 187 N VAL H 151 SHEET 4 AA4 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AA5 3 THR H 160 TRP H 163 0 SHEET 2 AA5 3 ILE H 204 ASN H 208 -1 O ASN H 206 N SER H 162 SHEET 3 AA5 3 LYS H 215 ARG H 219 -1 O LYS H 218 N CYS H 205 SHEET 1 AA6 4 THR L 5 GLN L 6 0 SHEET 2 AA6 4 ALA L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23 SHEET 4 AA6 4 PHE L 67 GLY L 71 -1 N SER L 70 O THR L 77 SHEET 1 AA7 5 SER L 10 PRO L 12 0 SHEET 2 AA7 5 GLY L 106 GLU L 110 1 O LYS L 108 N LEU L 11 SHEET 3 AA7 5 VAL L 90 TYR L 92 -1 N TYR L 91 O THR L 107 SHEET 4 AA7 5 PHE L 41 GLN L 43 -1 N GLN L 43 O VAL L 90 SHEET 5 AA7 5 ARG L 50 ARG L 51 -1 O ARG L 50 N GLN L 42 SHEET 1 AA8 4 VAL L 120 PHE L 123 0 SHEET 2 AA8 4 THR L 134 LEU L 141 -1 O LEU L 140 N PHE L 121 SHEET 3 AA8 4 LEU L 180 SER L 187 -1 O LEU L 186 N ALA L 135 SHEET 4 AA8 4 SER L 164 GLN L 165 -1 N GLN L 165 O THR L 183 SHEET 1 AA9 3 LEU L 159 GLN L 160 0 SHEET 2 AA9 3 GLN L 152 VAL L 155 -1 N TRP L 153 O GLN L 160 SHEET 3 AA9 3 TYR L 197 GLU L 200 -1 O ALA L 198 N LYS L 154 SHEET 1 AB1 2 THR A 25 VAL A 26 0 SHEET 2 AB1 2 VAL A 34 THR A 35 -1 O VAL A 34 N VAL A 26 SHEET 1 AB2 2 SER A 39 ASN A 41 0 SHEET 2 AB2 2 ARG A 315 ALA A 317 -1 O LEU A 316 N VAL A 40 SHEET 1 AB3 2 LEU A 51 ASP A 53 0 SHEET 2 AB3 2 TYR A 274 ASN A 278 1 O CYS A 277 N ASP A 53 SHEET 1 AB4 3 LEU A 59 ILE A 60 0 SHEET 2 AB4 3 ILE A 87 GLU A 89 1 O VAL A 88 N LEU A 59 SHEET 3 AB4 3 ILE A 267 LYS A 269 1 O MET A 268 N GLU A 89 SHEET 1 AB5 3 HIS A 117 ILE A 121 0 SHEET 2 AB5 3 ALA A 257 VAL A 260A-1 O LYS A 259 N GLU A 119 SHEET 3 AB5 3 LEU A 176 LEU A 177 -1 N LEU A 177 O TYR A 258 SHEET 1 AB6 2 GLU A 131 ALA A 132 0 SHEET 2 AB6 2 ILE A 155 LYS A 156 -1 O ILE A 155 N ALA A 132 SHEET 1 AB7 4 VAL A 151 TRP A 153 0 SHEET 2 AB7 4 PHE A 251 PRO A 254 -1 O ALA A 253 N VAL A 152 SHEET 3 AB7 4 GLY A 181 HIS A 184 -1 N GLY A 181 O ILE A 252 SHEET 4 AB7 4 ARG A 229 PHE A 232 -1 O ARG A 229 N HIS A 184 SHEET 1 AB8 4 ILE A 164 ARG A 166 0 SHEET 2 AB8 4 PHE A 245 SER A 247 -1 O PHE A 245 N ARG A 166 SHEET 3 AB8 4 ILE A 202 SER A 203 -1 N SER A 203 O GLU A 246 SHEET 4 AB8 4 ARG A 212 LEU A 213 -1 O LEU A 213 N ILE A 202 SHEET 1 AB9 2 PHE A 294 GLN A 295 0 SHEET 2 AB9 2 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295 SSBOND 1 CYS B 137 CYS A 14 1555 1555 2.03 SSBOND 2 CYS B 144 CYS B 148 1555 1555 2.26 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 4 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 93 1555 1555 2.03 SSBOND 6 CYS A 52 CYS A 277 1555 1555 2.04 SSBOND 7 CYS A 64 CYS A 76 1555 1555 2.01 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 CRYST1 162.079 162.079 162.079 90.00 90.00 90.00 P 21 3 24 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 0.006170 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006170 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006170 0.00000