HEADER CELL ADHESION 22-JAN-25 9MYL TITLE FERTILIZATION IZUMO1 PROTEIN ECTODOMAIN IN COMPLEX WITH ANTI-SPERM TITLE 2 ANTIBODY OBF13 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IZUMO SPERM-EGG FUSION PROTEIN 1; COMPND 3 CHAIN: C, D; COMPND 4 SYNONYM: OOCYTE BINDING/FUSION FACTOR,OBF,SPERM-SPECIFIC PROTEIN COMPND 5 IZUMO; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ANTI-SPERM ANTIBODY OBF13 HEAVY CHAIN; COMPND 9 CHAIN: H, A; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: ANTI-SPERM ANTIBODY OBF13 LIGHT CHAIN; COMPND 13 CHAIN: L, B; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: IZUMO1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_COMMON: MOUSE; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F KEYWDS FERTILIZATION, ANTI-SPERM ANTIBODY, IZUMO1, INFERTILITY, KEYWDS 2 CONTRACEPTION, CELL ADHESION EXPDTA X-RAY DIFFRACTION AUTHOR S.TANG REVDAT 1 19-MAR-25 9MYL 0 JRNL AUTH Y.LU,M.IKAWA,S.TANG JRNL TITL ALLOSTERIC INHIBITION OF THE IZUMO1-JUNO FERTILIZATION JRNL TITL 2 COMPLEX BY THE NATURALLY OCCURRING ANTISPERM ANTIBODY OBF13. JRNL REF PROC.NATL.ACAD.SCI.USA V. 122 52122 2025 JRNL REFN ESSN 1091-6490 JRNL PMID 40042902 JRNL DOI 10.1073/PNAS.2425952122 REMARK 2 REMARK 2 RESOLUTION. 3.18 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 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) : 3.18 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.06 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.7 REMARK 3 NUMBER OF REFLECTIONS : 34758 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840 REMARK 3 FREE R VALUE TEST SET COUNT : 1683 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 40.0620 - 7.2607 0.91 2740 156 0.1806 0.2284 REMARK 3 2 7.2607 - 5.7686 0.91 2726 158 0.2348 0.2594 REMARK 3 3 5.7686 - 5.0410 0.94 2885 131 0.1967 0.2948 REMARK 3 4 5.0410 - 4.5808 0.87 2649 131 0.1711 0.2417 REMARK 3 5 4.5808 - 4.2529 0.92 2772 151 0.1821 0.2010 REMARK 3 6 4.2529 - 4.0024 0.92 2786 163 0.1987 0.2522 REMARK 3 7 4.0024 - 3.8021 0.92 2829 136 0.2338 0.2710 REMARK 3 8 3.8021 - 3.6367 0.84 2561 136 0.2550 0.3284 REMARK 3 9 3.6367 - 3.4968 0.89 2744 124 0.2595 0.3144 REMARK 3 10 3.4968 - 3.3762 0.91 2803 114 0.2714 0.3157 REMARK 3 11 3.3762 - 3.2707 0.92 2787 144 0.2922 0.3711 REMARK 3 12 3.2707 - 3.1772 0.93 2793 139 0.3152 0.3701 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) : 0.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.160 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 : 0.006 9425 REMARK 3 ANGLE : 1.032 12877 REMARK 3 CHIRALITY : 0.045 1484 REMARK 3 PLANARITY : 0.003 1659 REMARK 3 DIHEDRAL : 10.593 3088 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 9MYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000292095. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 80 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) : 0.97946 REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE REMARK 200 CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34758 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.177 REMARK 200 RESOLUTION RANGE LOW (A) : 40.062 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.7 REMARK 200 DATA REDUNDANCY : 2.200 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) : 3.18 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM L-PROLINE, 100 MM HEPES PH 7.4, REMARK 280 9% PEG 3,350, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, B 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 ALA C 70 REMARK 465 HIS C 173 REMARK 465 GLU C 176 REMARK 465 VAL C 179 REMARK 465 GLY C 229 REMARK 465 VAL C 251 REMARK 465 LEU C 252 REMARK 465 PRO C 253 REMARK 465 PRO C 254 REMARK 465 LYS C 255 REMARK 465 GLU C 256 REMARK 465 PRO C 257 REMARK 465 GLU C 258 REMARK 465 ALA C 259 REMARK 465 SER D 69 REMARK 465 LYS D 138 REMARK 465 CYS D 139 REMARK 465 GLY D 140 REMARK 465 VAL D 141 REMARK 465 CYS D 165 REMARK 465 GLY D 166 REMARK 465 GLU D 167 REMARK 465 ARG D 168 REMARK 465 HIS D 169 REMARK 465 ILE D 170 REMARK 465 GLU D 171 REMARK 465 VAL D 172 REMARK 465 HIS D 173 REMARK 465 ARG D 174 REMARK 465 SER D 175 REMARK 465 GLU D 176 REMARK 465 ASP D 177 REMARK 465 LEU D 178 REMARK 465 VAL D 179 REMARK 465 LEU D 180 REMARK 465 ASP D 181 REMARK 465 LEU D 218 REMARK 465 THR D 219 REMARK 465 LYS D 220 REMARK 465 SER D 221 REMARK 465 MET D 222 REMARK 465 VAL D 223 REMARK 465 GLY D 224 REMARK 465 ALA D 228 REMARK 465 GLY D 229 REMARK 465 ASN D 230 REMARK 465 TYR D 231 REMARK 465 ARG D 232 REMARK 465 ASP D 249 REMARK 465 VAL D 250 REMARK 465 VAL D 251 REMARK 465 LEU D 252 REMARK 465 PRO D 253 REMARK 465 PRO D 254 REMARK 465 LYS D 255 REMARK 465 GLU D 256 REMARK 465 PRO D 257 REMARK 465 GLU D 258 REMARK 465 ALA D 259 REMARK 465 GLY H 129 REMARK 465 SER H 130 REMARK 465 ALA H 131 REMARK 465 ALA H 132 REMARK 465 GLN H 133 REMARK 465 THR H 134 REMARK 465 ASN H 135 REMARK 465 ASP H 216 REMARK 465 CYS H 217 REMARK 465 ARG L 210 REMARK 465 ASN L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 REMARK 465 SER A 130 REMARK 465 ALA A 131 REMARK 465 ALA A 132 REMARK 465 GLN A 133 REMARK 465 CYS A 217 REMARK 465 ASN B 211 REMARK 465 GLU B 212 REMARK 465 CYS B 213 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS C 51 CG CD CE NZ REMARK 470 VAL C 67 CG1 CG2 REMARK 470 GLU C 71 CG CD OE1 OE2 REMARK 470 ASP C 72 CG OD1 OD2 REMARK 470 TYR C 74 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU C 75 CG CD1 CD2 REMARK 470 ASN C 81 CG OD1 ND2 REMARK 470 ARG C 127 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 130 CG CD OE1 NE2 REMARK 470 LYS C 131 CG CD CE NZ REMARK 470 LYS C 138 CG CD CE NZ REMARK 470 SER C 143 OG REMARK 470 GLN C 155 CG CD OE1 NE2 REMARK 470 ARG C 160 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 161 CG CD CE NZ REMARK 470 GLU C 167 CG CD OE1 OE2 REMARK 470 ARG C 168 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 170 CG1 CG2 CD1 REMARK 470 GLU C 171 CG CD OE1 OE2 REMARK 470 VAL C 172 CG1 CG2 REMARK 470 ARG C 174 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 191 CG CD CE NZ REMARK 470 ASP C 195 CG OD1 OD2 REMARK 470 TYR C 196 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG C 200 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 203 CG CD OE1 OE2 REMARK 470 SER C 206 OG REMARK 470 GLU C 207 CG CD OE1 OE2 REMARK 470 LEU C 209 CG CD1 CD2 REMARK 470 ILE C 210 CG1 CG2 CD1 REMARK 470 LYS C 212 CG CD CE NZ REMARK 470 LYS C 214 CG CD CE NZ REMARK 470 GLU C 215 CG CD OE1 OE2 REMARK 470 LEU C 218 CG CD1 CD2 REMARK 470 LYS C 220 CG CD CE NZ REMARK 470 MET C 222 CG SD CE REMARK 470 ARG C 232 CG CD NE CZ NH1 NH2 REMARK 470 HIS C 242 CG ND1 CD2 CE1 NE2 REMARK 470 ILE C 246 CG1 CG2 CD1 REMARK 470 ARG C 247 CG CD NE CZ NH1 NH2 REMARK 470 VAL C 250 CG1 CG2 REMARK 470 LYS D 34 CG CD CE NZ REMARK 470 VAL D 67 CG1 CG2 REMARK 470 THR D 68 OG1 CG2 REMARK 470 GLU D 71 CG CD OE1 OE2 REMARK 470 SER D 73 OG REMARK 470 TYR D 74 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU D 75 CG CD1 CD2 REMARK 470 ASN D 81 CG OD1 ND2 REMARK 470 GLN D 85 CG CD OE1 NE2 REMARK 470 LYS D 92 CG CD CE NZ REMARK 470 ARG D 127 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 131 CG CD CE NZ REMARK 470 GLU D 132 CG CD OE1 OE2 REMARK 470 GLN D 144 CG CD OE1 NE2 REMARK 470 LYS D 154 CG CD CE NZ REMARK 470 ILE D 158 CG1 CG2 CD1 REMARK 470 ARG D 160 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 161 CG CD CE NZ REMARK 470 SER D 162 OG REMARK 470 LEU D 163 CG CD1 CD2 REMARK 470 ASP D 164 CG OD1 OD2 REMARK 470 LEU D 183 CG CD1 CD2 REMARK 470 SER D 185 OG REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 191 CG CD CE NZ REMARK 470 LEU D 193 CG CD1 CD2 REMARK 470 THR D 194 OG1 CG2 REMARK 470 ASP D 195 CG OD1 OD2 REMARK 470 ARG D 200 CG CD NE CZ NH1 NH2 REMARK 470 VAL D 201 CG1 CG2 REMARK 470 GLU D 203 CG CD OE1 OE2 REMARK 470 SER D 205 OG REMARK 470 SER D 206 OG REMARK 470 GLU D 207 CG CD OE1 OE2 REMARK 470 THR D 208 OG1 CG2 REMARK 470 LEU D 209 CG CD1 CD2 REMARK 470 ILE D 210 CG1 CG2 CD1 REMARK 470 LYS D 212 CG CD CE NZ REMARK 470 LYS D 214 CG CD CE NZ REMARK 470 GLU D 215 CG CD OE1 OE2 REMARK 470 GLU D 226 CG CD OE1 OE2 REMARK 470 VAL D 245 CG1 CG2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 LYS H 30 CG CD CE NZ REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 ASN H 55 CG OD1 ND2 REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 LYS H 117 CG CD CE NZ REMARK 470 LYS H 145 CG CD CE NZ REMARK 470 LEU H 161 CG CD1 CD2 REMARK 470 GLN H 173 CG CD OE1 NE2 REMARK 470 SER H 187 OG REMARK 470 SER H 192 OG REMARK 470 VAL H 195 CG1 CG2 REMARK 470 LYS H 211 CG CD CE NZ REMARK 470 VAL H 213 CG1 CG2 REMARK 470 ARG H 215 CG CD NE CZ NH1 NH2 REMARK 470 SER L 7 OG REMARK 470 GLN L 8 CG CD OE1 NE2 REMARK 470 LYS L 9 CG CD CE NZ REMARK 470 ARG L 18 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 30 CG OD1 OD2 REMARK 470 LYS L 45 CG CD CE NZ REMARK 470 ARG L 54 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 103 CG CD CE NZ REMARK 470 LEU L 104 CG CD1 CD2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 ASP L 109 CG OD1 OD2 REMARK 470 VAL L 114 CG1 CG2 REMARK 470 ILE L 116 CG1 CG2 CD1 REMARK 470 GLN L 123 CG CD OE1 NE2 REMARK 470 LEU L 124 CG CD1 CD2 REMARK 470 THR L 125 OG1 CG2 REMARK 470 SER L 130 OG REMARK 470 VAL L 131 CG1 CG2 REMARK 470 ASN L 136 CG OD1 ND2 REMARK 470 LYS L 141 CG CD CE NZ REMARK 470 ASP L 142 CG OD1 OD2 REMARK 470 VAL L 145 CG1 CG2 REMARK 470 LYS L 146 CG CD CE NZ REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 ILE L 149 CG1 CG2 CD1 REMARK 470 SER L 152 OG REMARK 470 GLU L 153 CG CD OE1 OE2 REMARK 470 ARG L 154 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 155 CG CD OE1 NE2 REMARK 470 ASN L 156 CG OD1 ND2 REMARK 470 VAL L 158 CG1 CG2 REMARK 470 LEU L 159 CG CD1 CD2 REMARK 470 THR L 163 OG1 CG2 REMARK 470 ASP L 164 CG OD1 OD2 REMARK 470 SER L 167 OG REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 ASP L 169 CG OD1 OD2 REMARK 470 SER L 170 OG REMARK 470 LEU L 178 CG CD1 CD2 REMARK 470 THR L 179 OG1 CG2 REMARK 470 LEU L 180 CG CD1 CD2 REMARK 470 THR L 181 OG1 CG2 REMARK 470 GLU L 184 CG CD OE1 OE2 REMARK 470 ARG L 187 CG CD NE CZ NH1 NH2 REMARK 470 ASN L 189 CG OD1 ND2 REMARK 470 GLU L 194 CG CD OE1 OE2 REMARK 470 THR L 196 OG1 CG2 REMARK 470 LYS L 198 CG CD CE NZ REMARK 470 SER L 200 OG REMARK 470 THR L 201 OG1 CG2 REMARK 470 SER L 202 OG REMARK 470 ILE L 204 CG1 CG2 CD1 REMARK 470 VAL L 205 CG1 CG2 REMARK 470 LYS L 206 CG CD CE NZ REMARK 470 LYS A 30 CG CD CE NZ REMARK 470 GLU A 42 CG CD OE1 OE2 REMARK 470 LYS A 117 CG CD CE NZ REMARK 470 ASN A 135 CG OD1 ND2 REMARK 470 MET A 137 CG SD CE REMARK 470 LEU A 140 CG CD1 CD2 REMARK 470 THR A 189 OG1 CG2 REMARK 470 VAL A 195 CG1 CG2 REMARK 470 THR A 196 OG1 CG2 REMARK 470 LYS A 211 CG CD CE NZ REMARK 470 ILE A 212 CG1 CG2 CD1 REMARK 470 VAL A 213 CG1 CG2 REMARK 470 ARG A 215 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 216 CG OD1 OD2 REMARK 470 LYS B 9 CG CD CE NZ REMARK 470 VAL B 15 CG1 CG2 REMARK 470 VAL B 21 CG1 CG2 REMARK 470 THR B 22 OG1 CG2 REMARK 470 LYS B 24 CG CD CE NZ REMARK 470 VAL B 33 CG1 CG2 REMARK 470 LYS B 39 CG CD CE NZ REMARK 470 LYS B 45 CG CD CE NZ REMARK 470 LYS B 103 CG CD CE NZ REMARK 470 LYS B 107 CG CD CE NZ REMARK 470 ASP B 109 CG OD1 OD2 REMARK 470 VAL B 114 CG1 CG2 REMARK 470 ILE B 116 CG1 CG2 CD1 REMARK 470 LEU B 124 CG CD1 CD2 REMARK 470 SER B 126 OG REMARK 470 VAL B 131 CG1 CG2 REMARK 470 VAL B 132 CG1 CG2 REMARK 470 LYS B 141 CG CD CE NZ REMARK 470 ILE B 143 CG1 CG2 CD1 REMARK 470 VAL B 145 CG1 CG2 REMARK 470 LYS B 146 CG CD CE NZ REMARK 470 LYS B 148 CG CD CE NZ REMARK 470 ILE B 149 CG1 CG2 CD1 REMARK 470 ASP B 150 CG OD1 OD2 REMARK 470 SER B 152 OG REMARK 470 GLU B 153 CG CD OE1 OE2 REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2 REMARK 470 VAL B 158 CG1 CG2 REMARK 470 LYS B 168 CG CD CE NZ REMARK 470 SER B 176 OG REMARK 470 THR B 177 OG1 CG2 REMARK 470 LEU B 180 CG CD1 CD2 REMARK 470 THR B 181 OG1 CG2 REMARK 470 LYS B 182 CG CD CE NZ REMARK 470 ASP B 183 CG OD1 OD2 REMARK 470 GLU B 186 CG CD OE1 OE2 REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 194 CG CD OE1 OE2 REMARK 470 LYS B 198 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD2 ASP B 169 OG1 THR B 171 1.70 REMARK 500 SG CYS H 142 SG CYS H 197 1.71 REMARK 500 SG CYS L 133 SG CYS L 193 1.77 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 THR C 39 -48.99 -130.73 REMARK 500 CYS C 165 36.09 -94.47 REMARK 500 LEU C 209 101.77 -58.89 REMARK 500 ARG C 232 119.86 -164.85 REMARK 500 LEU D 163 93.43 -66.82 REMARK 500 CYS H 22 109.39 -165.01 REMARK 500 PHE H 148 138.52 -170.62 REMARK 500 ALA L 51 -23.65 70.52 REMARK 500 SER L 52 -33.16 -133.19 REMARK 500 ASN L 137 73.87 61.25 REMARK 500 PRO L 140 102.93 -57.70 REMARK 500 TYR A 101 78.60 40.60 REMARK 500 SER A 115 55.77 -108.56 REMARK 500 SER B 14 -169.70 -127.34 REMARK 500 THR B 31 39.94 35.74 REMARK 500 ASN B 32 76.39 -118.28 REMARK 500 LEU B 47 -62.68 -96.83 REMARK 500 SER B 50 55.34 -141.08 REMARK 500 ALA B 51 -27.25 59.00 REMARK 500 ASN B 137 69.63 61.03 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 C 301 REMARK 610 PRO C 302 REMARK 610 PRO D 302 DBREF 9MYL C 22 255 UNP Q9D9J7 IZUM1_MOUSE 22 256 DBREF 9MYL D 22 255 UNP Q9D9J7 IZUM1_MOUSE 22 256 DBREF 9MYL H 1 217 PDB 9MYL 9MYL 1 217 DBREF 9MYL L 1 213 PDB 9MYL 9MYL 1 213 DBREF 9MYL A 1 217 PDB 9MYL 9MYL 1 217 DBREF 9MYL B 1 213 PDB 9MYL 9MYL 1 213 SEQADV 9MYL C UNP Q9D9J7 THR 251 DELETION SEQADV 9MYL GLU C 256 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL PRO C 257 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL GLU C 258 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL ALA C 259 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL D UNP Q9D9J7 THR 251 DELETION SEQADV 9MYL GLU D 256 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL PRO D 257 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL GLU D 258 UNP Q9D9J7 EXPRESSION TAG SEQADV 9MYL ALA D 259 UNP Q9D9J7 EXPRESSION TAG SEQRES 1 C 238 CYS ILE LYS CYS ASP GLN PHE VAL THR ASP ALA LEU LYS SEQRES 2 C 238 THR PHE GLU ASN THR TYR LEU ASN ASP HIS LEU PRO HIS SEQRES 3 C 238 ASP ILE HIS LYS ASN VAL MET ARG MET VAL ASN HIS GLU SEQRES 4 C 238 VAL SER SER PHE GLY VAL VAL THR SER ALA GLU ASP SER SEQRES 5 C 238 TYR LEU GLY ALA VAL ASP GLU ASN THR LEU GLU GLN ALA SEQRES 6 C 238 THR TRP SER PHE LEU LYS ASP LEU LYS ARG ILE THR ASP SEQRES 7 C 238 SER ASP LEU LYS GLY GLU LEU PHE ILE LYS GLU LEU LEU SEQRES 8 C 238 TRP MET LEU ARG HIS GLN LYS ASP ILE PHE ASN ASN LEU SEQRES 9 C 238 ALA ARG GLN PHE GLN LYS GLU VAL LEU CYS PRO ASN LYS SEQRES 10 C 238 CYS GLY VAL MET SER GLN THR LEU ILE TRP CYS LEU LYS SEQRES 11 C 238 CYS GLU LYS GLN LEU HIS ILE CYS ARG LYS SER LEU ASP SEQRES 12 C 238 CYS GLY GLU ARG HIS ILE GLU VAL HIS ARG SER GLU ASP SEQRES 13 C 238 LEU VAL LEU ASP CYS LEU LEU SER TRP HIS ARG ALA SER SEQRES 14 C 238 LYS GLY LEU THR ASP TYR SER PHE TYR ARG VAL TRP GLU SEQRES 15 C 238 ASN SER SER GLU THR LEU ILE ALA LYS GLY LYS GLU PRO SEQRES 16 C 238 TYR LEU THR LYS SER MET VAL GLY PRO GLU ASP ALA GLY SEQRES 17 C 238 ASN TYR ARG CYS VAL LEU ASP THR ILE ASN GLN GLY HIS SEQRES 18 C 238 ALA THR VAL ILE ARG TYR ASP VAL VAL LEU PRO PRO LYS SEQRES 19 C 238 GLU PRO GLU ALA SEQRES 1 D 238 CYS ILE LYS CYS ASP GLN PHE VAL THR ASP ALA LEU LYS SEQRES 2 D 238 THR PHE GLU ASN THR TYR LEU ASN ASP HIS LEU PRO HIS SEQRES 3 D 238 ASP ILE HIS LYS ASN VAL MET ARG MET VAL ASN HIS GLU SEQRES 4 D 238 VAL SER SER PHE GLY VAL VAL THR SER ALA GLU ASP SER SEQRES 5 D 238 TYR LEU GLY ALA VAL ASP GLU ASN THR LEU GLU GLN ALA SEQRES 6 D 238 THR TRP SER PHE LEU LYS ASP LEU LYS ARG ILE THR ASP SEQRES 7 D 238 SER ASP LEU LYS GLY GLU LEU PHE ILE LYS GLU LEU LEU SEQRES 8 D 238 TRP MET LEU ARG HIS GLN LYS ASP ILE PHE ASN ASN LEU SEQRES 9 D 238 ALA ARG GLN PHE GLN LYS GLU VAL LEU CYS PRO ASN LYS SEQRES 10 D 238 CYS GLY VAL MET SER GLN THR LEU ILE TRP CYS LEU LYS SEQRES 11 D 238 CYS GLU LYS GLN LEU HIS ILE CYS ARG LYS SER LEU ASP SEQRES 12 D 238 CYS GLY GLU ARG HIS ILE GLU VAL HIS ARG SER GLU ASP SEQRES 13 D 238 LEU VAL LEU ASP CYS LEU LEU SER TRP HIS ARG ALA SER SEQRES 14 D 238 LYS GLY LEU THR ASP TYR SER PHE TYR ARG VAL TRP GLU SEQRES 15 D 238 ASN SER SER GLU THR LEU ILE ALA LYS GLY LYS GLU PRO SEQRES 16 D 238 TYR LEU THR LYS SER MET VAL GLY PRO GLU ASP ALA GLY SEQRES 17 D 238 ASN TYR ARG CYS VAL LEU ASP THR ILE ASN GLN GLY HIS SEQRES 18 D 238 ALA THR VAL ILE ARG TYR ASP VAL VAL LEU PRO PRO LYS SEQRES 19 D 238 GLU PRO GLU ALA SEQRES 1 H 217 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 H 217 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 H 217 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 H 217 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 H 217 PRO ALA ASN GLY ASN SER LYS TYR ASP PRO LYS PHE GLN SEQRES 6 H 217 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 H 217 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 H 217 ALA VAL TYR TYR CYS ALA ARG TRP ASP TYR GLY VAL TYR SEQRES 9 H 217 TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA LYS SEQRES 10 H 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 H 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 H 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 H 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 H 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 H 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 H 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 H 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 L 213 ASP ILE VAL LEU THR GLN SER GLN LYS PHE MET SER THR SEQRES 2 L 213 SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS ALA SER SEQRES 3 L 213 GLN ASN VAL ASP THR ASN VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY GLN SER PRO LYS ALA LEU ILE TYR SER ALA SER SEQRES 5 L 213 TYR ARG TYR SER GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 213 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 L 213 GLN SER GLU ASP LEU ALA GLU TYR PHE CYS GLN GLN TYR SEQRES 8 L 213 ASN SER TYR PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 213 GLU ILE LYS ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 L 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 L 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 L 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 L 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 L 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 L 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 L 213 ASN ARG ASN GLU CYS SEQRES 1 A 217 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS SEQRES 2 A 217 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY SEQRES 3 A 217 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN SEQRES 4 A 217 ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 A 217 PRO ALA ASN GLY ASN SER LYS TYR ASP PRO LYS PHE GLN SEQRES 6 A 217 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR SEQRES 7 A 217 ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 A 217 ALA VAL TYR TYR CYS ALA ARG TRP ASP TYR GLY VAL TYR SEQRES 9 A 217 TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA LYS SEQRES 10 A 217 THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SER SEQRES 11 A 217 ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS LEU SEQRES 12 A 217 VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP SEQRES 13 A 217 ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO SEQRES 14 A 217 ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER SEQRES 15 A 217 VAL THR VAL PRO SER SER THR TRP PRO SER GLU THR VAL SEQRES 16 A 217 THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL SEQRES 17 A 217 ASP LYS LYS ILE VAL PRO ARG ASP CYS SEQRES 1 B 213 ASP ILE VAL LEU THR GLN SER GLN LYS PHE MET SER THR SEQRES 2 B 213 SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS ALA SER SEQRES 3 B 213 GLN ASN VAL ASP THR ASN VAL ALA TRP TYR GLN GLN LYS SEQRES 4 B 213 PRO GLY GLN SER PRO LYS ALA LEU ILE TYR SER ALA SER SEQRES 5 B 213 TYR ARG TYR SER GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 213 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 B 213 GLN SER GLU ASP LEU ALA GLU TYR PHE CYS GLN GLN TYR SEQRES 8 B 213 ASN SER TYR PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 B 213 GLU ILE LYS ALA ASP ALA ALA PRO THR VAL SER ILE PHE SEQRES 10 B 213 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER SEQRES 11 B 213 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE SEQRES 12 B 213 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN SEQRES 13 B 213 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SEQRES 14 B 213 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS SEQRES 15 B 213 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA SEQRES 16 B 213 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE SEQRES 17 B 213 ASN ARG ASN GLU CYS HET NAG C 301 14 HET PRO C 302 7 HET NAG D 301 14 HET PRO D 302 7 HET CL L 301 1 HET CL A 301 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM PRO PROLINE HETNAM CL CHLORIDE ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 7 NAG 2(C8 H15 N O6) FORMUL 8 PRO 2(C5 H9 N O2) FORMUL 11 CL 2(CL 1-) HELIX 1 AA1 CYS C 22 CYS C 25 5 4 HELIX 2 AA2 ASP C 26 THR C 39 1 14 HELIX 3 AA3 TYR C 40 HIS C 44 5 5 HELIX 4 AA4 PRO C 46 ASP C 48 5 3 HELIX 5 AA5 ILE C 49 SER C 62 1 14 HELIX 6 AA6 SER C 73 LEU C 75 5 3 HELIX 7 AA7 GLU C 80 SER C 100 1 21 HELIX 8 AA8 GLY C 104 VAL C 133 1 30 HELIX 9 AA9 TRP C 186 SER C 190 5 5 HELIX 10 AB1 ASP D 26 THR D 39 1 14 HELIX 11 AB2 TYR D 40 HIS D 44 5 5 HELIX 12 AB3 PRO D 46 ASP D 48 5 3 HELIX 13 AB4 ILE D 49 SER D 62 1 14 HELIX 14 AB5 ASP D 72 LEU D 75 5 4 HELIX 15 AB6 GLU D 80 ASP D 99 1 20 HELIX 16 AB7 GLY D 104 VAL D 133 1 30 HELIX 17 AB8 ASN H 28 THR H 32 5 5 HELIX 18 AB9 PRO H 62 GLN H 65 5 4 HELIX 19 AC1 THR H 87 THR H 91 5 5 HELIX 20 AC2 SER H 158 SER H 160 5 3 HELIX 21 AC3 GLN L 79 LEU L 83 5 5 HELIX 22 AC4 SER L 120 SER L 126 1 7 HELIX 23 AC5 LYS L 182 ARG L 187 1 6 HELIX 24 AC6 ASN A 28 THR A 32 5 5 HELIX 25 AC7 THR A 87 THR A 91 5 5 HELIX 26 AC8 PRO A 202 SER A 205 5 4 HELIX 27 AC9 GLN B 79 LEU B 83 5 5 HELIX 28 AD1 SER B 120 SER B 126 1 7 HELIX 29 AD2 LYS B 182 GLU B 186 1 5 SHEET 1 AA1 3 ALA C 77 ASP C 79 0 SHEET 2 AA1 3 MET C 142 TRP C 148 -1 O ILE C 147 N VAL C 78 SHEET 3 AA1 3 GLU C 153 CYS C 159 -1 O CYS C 159 N MET C 142 SHEET 1 AA2 5 ASP C 164 ARG C 168 0 SHEET 2 AA2 5 HIS C 242 TYR C 248 1 O VAL C 245 N CYS C 165 SHEET 3 AA2 5 TYR C 231 THR C 237 -1 N CYS C 233 O ILE C 246 SHEET 4 AA2 5 LEU C 193 VAL C 201 -1 N SER C 197 O VAL C 234 SHEET 5 AA2 5 GLU C 207 GLY C 213 -1 O GLY C 213 N TYR C 196 SHEET 1 AA3 3 ALA D 77 ASP D 79 0 SHEET 2 AA3 3 SER D 143 TRP D 148 -1 O ILE D 147 N VAL D 78 SHEET 3 AA3 3 GLU D 153 ILE D 158 -1 O GLU D 153 N TRP D 148 SHEET 1 AA4 2 LEU D 193 SER D 197 0 SHEET 2 AA4 2 VAL D 234 THR D 237 -1 O VAL D 234 N SER D 197 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA5 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA5 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA6 6 GLU H 10 VAL H 12 0 SHEET 2 AA6 6 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12 SHEET 3 AA6 6 ALA H 92 TRP H 99 -1 N ALA H 92 O LEU H 111 SHEET 4 AA6 6 MET H 34 ARG H 40 -1 N VAL H 37 O TYR H 95 SHEET 5 AA6 6 GLY H 44 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA6 6 SER H 58 TYR H 60 -1 O LYS H 59 N ARG H 50 SHEET 1 AA7 4 GLU H 10 VAL H 12 0 SHEET 2 AA7 4 THR H 109 VAL H 113 1 O THR H 112 N VAL H 12 SHEET 3 AA7 4 ALA H 92 TRP H 99 -1 N ALA H 92 O LEU H 111 SHEET 4 AA7 4 VAL H 103 TRP H 105 -1 O TYR H 104 N ARG H 98 SHEET 1 AA8 4 SER H 122 LEU H 126 0 SHEET 2 AA8 4 MET H 137 TYR H 147 -1 O GLY H 141 N LEU H 126 SHEET 3 AA8 4 TYR H 177 PRO H 186 -1 O VAL H 183 N LEU H 140 SHEET 4 AA8 4 VAL H 171 LEU H 172 -1 N VAL H 171 O THR H 178 SHEET 1 AA9 3 THR H 153 TRP H 156 0 SHEET 2 AA9 3 THR H 196 HIS H 201 -1 O ALA H 200 N THR H 153 SHEET 3 AA9 3 THR H 206 LYS H 211 -1 O LYS H 210 N CYS H 197 SHEET 1 AB1 4 LEU L 4 THR L 5 0 SHEET 2 AB1 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AB1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N VAL L 21 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74 SHEET 1 AB2 2 PHE L 10 THR L 13 0 SHEET 2 AB2 2 LYS L 103 ILE L 106 1 O GLU L 105 N MET L 11 SHEET 1 AB3 4 TYR L 53 ARG L 54 0 SHEET 2 AB3 4 LYS L 45 TYR L 49 -1 N TYR L 49 O TYR L 53 SHEET 3 AB3 4 VAL L 33 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 4 AB3 4 GLU L 85 GLN L 90 -1 O GLN L 89 N ALA L 34 SHEET 1 AB4 4 THR L 113 PHE L 117 0 SHEET 2 AB4 4 GLY L 128 PHE L 138 -1 O PHE L 134 N SER L 115 SHEET 3 AB4 4 TYR L 172 THR L 181 -1 O MET L 174 N LEU L 135 SHEET 4 AB4 4 VAL L 158 TRP L 162 -1 N LEU L 159 O THR L 177 SHEET 1 AB5 4 SER L 152 GLU L 153 0 SHEET 2 AB5 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152 SHEET 3 AB5 4 TYR L 191 THR L 196 -1 O THR L 196 N ASN L 144 SHEET 4 AB5 4 ILE L 204 PHE L 208 -1 O LYS L 206 N CYS L 193 SHEET 1 AB6 4 GLN A 3 GLN A 6 0 SHEET 2 AB6 4 VAL A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AB6 4 THR A 78 LEU A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AB6 4 ALA A 68 ASP A 73 -1 N THR A 71 O TYR A 80 SHEET 1 AB7 6 LEU A 11 VAL A 12 0 SHEET 2 AB7 6 THR A 109 VAL A 113 1 O THR A 112 N VAL A 12 SHEET 3 AB7 6 ALA A 92 TRP A 99 -1 N TYR A 94 O THR A 109 SHEET 4 AB7 6 TYR A 33 ARG A 40 -1 N HIS A 35 O ALA A 97 SHEET 5 AB7 6 GLY A 44 ILE A 51 -1 O GLU A 46 N LYS A 38 SHEET 6 AB7 6 SER A 58 TYR A 60 -1 O LYS A 59 N ARG A 50 SHEET 1 AB8 4 LEU A 11 VAL A 12 0 SHEET 2 AB8 4 THR A 109 VAL A 113 1 O THR A 112 N VAL A 12 SHEET 3 AB8 4 ALA A 92 TRP A 99 -1 N TYR A 94 O THR A 109 SHEET 4 AB8 4 VAL A 103 TRP A 105 -1 O TYR A 104 N ARG A 98 SHEET 1 AB9 4 SER A 122 LEU A 126 0 SHEET 2 AB9 4 MET A 137 TYR A 147 -1 O LEU A 143 N TYR A 124 SHEET 3 AB9 4 LEU A 176 PRO A 186 -1 O LEU A 179 N VAL A 144 SHEET 4 AB9 4 VAL A 165 THR A 167 -1 N HIS A 166 O SER A 182 SHEET 1 AC1 4 SER A 122 LEU A 126 0 SHEET 2 AC1 4 MET A 137 TYR A 147 -1 O LEU A 143 N TYR A 124 SHEET 3 AC1 4 LEU A 176 PRO A 186 -1 O LEU A 179 N VAL A 144 SHEET 4 AC1 4 VAL A 171 GLN A 173 -1 N GLN A 173 O LEU A 176 SHEET 1 AC2 3 THR A 153 TRP A 156 0 SHEET 2 AC2 3 THR A 196 HIS A 201 -1 O ALA A 200 N THR A 153 SHEET 3 AC2 3 THR A 206 LYS A 211 -1 O LYS A 210 N CYS A 197 SHEET 1 AC3 4 LEU B 4 THR B 5 0 SHEET 2 AC3 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AC3 4 ASP B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 4 AC3 4 PHE B 62 GLY B 66 -1 N THR B 63 O THR B 74 SHEET 1 AC4 2 PHE B 10 THR B 13 0 SHEET 2 AC4 2 LYS B 103 ILE B 106 1 O GLU B 105 N MET B 11 SHEET 1 AC5 4 LYS B 45 ILE B 48 0 SHEET 2 AC5 4 VAL B 33 GLN B 38 -1 N GLN B 37 O LYS B 45 SHEET 3 AC5 4 GLU B 85 GLN B 90 -1 O GLN B 89 N ALA B 34 SHEET 4 AC5 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AC6 4 THR B 113 PHE B 117 0 SHEET 2 AC6 4 GLY B 128 PHE B 138 -1 O PHE B 134 N SER B 115 SHEET 3 AC6 4 TYR B 172 THR B 181 -1 O MET B 174 N LEU B 135 SHEET 4 AC6 4 VAL B 158 THR B 163 -1 N THR B 163 O SER B 173 SHEET 1 AC7 4 SER B 152 ARG B 154 0 SHEET 2 AC7 4 ASN B 144 ILE B 149 -1 N ILE B 149 O SER B 152 SHEET 3 AC7 4 TYR B 191 THR B 196 -1 O THR B 196 N ASN B 144 SHEET 4 AC7 4 ILE B 204 PHE B 208 -1 O ILE B 204 N ALA B 195 SSBOND 1 CYS C 22 CYS C 149 1555 1555 2.03 SSBOND 2 CYS C 25 CYS C 152 1555 1555 2.03 SSBOND 3 CYS C 135 CYS C 159 1555 1555 2.03 SSBOND 4 CYS C 139 CYS C 165 1555 1555 2.03 SSBOND 5 CYS C 182 CYS C 233 1555 1555 2.03 SSBOND 6 CYS D 22 CYS D 149 1555 1555 2.02 SSBOND 7 CYS D 25 CYS D 152 1555 1555 2.03 SSBOND 8 CYS D 135 CYS D 159 1555 1555 2.03 SSBOND 9 CYS D 182 CYS D 233 1555 1555 2.03 SSBOND 10 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 12 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 13 CYS A 142 CYS A 197 1555 1555 2.03 SSBOND 14 CYS B 23 CYS B 88 1555 1555 2.03 SSBOND 15 CYS B 133 CYS B 193 1555 1555 2.03 LINK ND2 ASN D 204 C1 NAG D 301 1555 1555 1.46 CISPEP 1 PHE H 148 PRO H 149 0 -6.00 CISPEP 2 GLU H 150 PRO H 151 0 1.58 CISPEP 3 TRP H 190 PRO H 191 0 -0.39 CISPEP 4 TYR L 94 PRO L 95 0 -3.19 CISPEP 5 PHE A 148 PRO A 149 0 -5.71 CISPEP 6 GLU A 150 PRO A 151 0 2.43 CISPEP 7 TRP A 190 PRO A 191 0 -1.24 CISPEP 8 TYR B 94 PRO B 95 0 -5.21 CISPEP 9 TYR B 139 PRO B 140 0 2.35 CRYST1 81.069 83.208 92.605 82.85 89.72 71.40 P 1 2 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 0.012335 -0.004151 0.000482 0.00000 SCALE2 0.000000 0.012680 -0.001659 0.00000 SCALE3 0.000000 0.000000 0.010891 0.00000