HEADER CYTOKINE 20-JUN-25 9VJJ TITLE CRYSTAL STRUCTURE OF HUMAN LATENT TGF-BETA1 IN COMPLEX WITH SOF10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-1 PROPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SOF10 FAB HEAVY CHAIN; COMPND 8 CHAIN: H, I; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: SOF10 FAB LIGHT CHAIN; COMPND 12 CHAIN: L, M; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: TGFB1, TGFB; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE293F CELL; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1 CELLS; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1 CELLS KEYWDS LATENT TGF-BETA1, CYTOKINE, FAB, ANTIBODY, FIBROSIS EXPDTA X-RAY DIFFRACTION AUTHOR H.KAWAUCHI,M.KANAMORI,I.SATO,T.A.FUKAMI,M.IRIE,T.TORIZAWA,H.SHIMADA REVDAT 1 04-FEB-26 9VJJ 0 JRNL AUTH M.KANAMORI,I.SATO,H.KAWAUCHI,H.SHIMADA JRNL TITL SELECTIVE BLOCKADE OF LATENT TGF-BETA1 ACTIVATION SUPPRESSES JRNL TITL 2 TISSUE FIBROSIS WITH GOOD SAFETY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.48 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.8 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.12 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 62.9 REMARK 3 NUMBER OF REFLECTIONS : 54729 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.283 REMARK 3 R VALUE (WORKING SET) : 0.281 REMARK 3 FREE R VALUE : 0.310 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2765 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.71 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.29 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3315 REMARK 3 BIN FREE R VALUE : 0.3764 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 62 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8302 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 112 REMARK 3 SOLVENT ATOMS : 4 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.47620 REMARK 3 B22 (A**2) : 1.56710 REMARK 3 B33 (A**2) : -3.04330 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.08470 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.500 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.475 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.336 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.513 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.350 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.881 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8646 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 11802 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2852 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1453 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8646 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 1145 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 6292 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.94 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.71 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.73 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9VJJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1300060817. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-SEP-20 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 : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000006 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JAN 26, 2018 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4, STARANISO 2.3.46 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54758 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.477 REMARK 200 RESOLUTION RANGE LOW (A) : 119.549 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 7.030 REMARK 200 R MERGE (I) : 0.05800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 119.5 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 6.89 REMARK 200 R MERGE FOR SHELL (I) : 0.02880 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 48.38 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 (%): 64.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M REMARK 280 IMIDAZOLE HYDROCHLORIDE (PH 8.0), 10.0% W/V POLYETHYLENE GLYCOL REMARK 280 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 112.93900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.85350 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 112.93900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.85350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16950 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45420 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I, L, M, X, C, D, E 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 ASP A 22 REMARK 465 TYR A 23 REMARK 465 LYS A 24 REMARK 465 ASP A 25 REMARK 465 ASP A 26 REMARK 465 ASP A 27 REMARK 465 ASP A 28 REMARK 465 LYS A 29 REMARK 465 LEU A 30 REMARK 465 SER A 31 REMARK 465 THR A 32 REMARK 465 SER A 33 REMARK 465 LYS A 34 REMARK 465 THR A 35 REMARK 465 ILE A 36 REMARK 465 SER A 227 REMARK 465 ARG A 228 REMARK 465 ASP A 229 REMARK 465 ASN A 230 REMARK 465 THR A 231 REMARK 465 LEU A 232 REMARK 465 GLN A 233 REMARK 465 VAL A 234 REMARK 465 ASP A 235 REMARK 465 ILE A 236 REMARK 465 ASN A 237 REMARK 465 GLY A 238 REMARK 465 PHE A 239 REMARK 465 THR A 240 REMARK 465 THR A 241 REMARK 465 GLY A 242 REMARK 465 ARG A 243 REMARK 465 ARG A 244 REMARK 465 GLY A 245 REMARK 465 HIS A 270 REMARK 465 LEU A 271 REMARK 465 GLN A 272 REMARK 465 SER A 273 REMARK 465 SER A 274 REMARK 465 ARG A 275 REMARK 465 HIS A 276 REMARK 465 ARG A 277 REMARK 465 ARG A 278 REMARK 465 ALA A 279 REMARK 465 LEU A 280 REMARK 465 ASP A 281 REMARK 465 THR A 282 REMARK 465 ASN A 283 REMARK 465 TYR A 284 REMARK 465 CYS A 285 REMARK 465 PHE A 286 REMARK 465 SER A 287 REMARK 465 SER A 288 REMARK 465 ILE A 329 REMARK 465 TRP A 330 REMARK 465 SER A 331 REMARK 465 LEU A 332 REMARK 465 ASP A 333 REMARK 465 THR A 334 REMARK 465 GLN A 335 REMARK 465 TYR A 336 REMARK 465 SER A 337 REMARK 465 LYS A 338 REMARK 465 VAL A 339 REMARK 465 LEU A 340 REMARK 465 ALA A 341 REMARK 465 ASP B 22 REMARK 465 TYR B 23 REMARK 465 LYS B 24 REMARK 465 ASP B 25 REMARK 465 ASP B 26 REMARK 465 ASP B 27 REMARK 465 ASP B 28 REMARK 465 LYS B 29 REMARK 465 LEU B 30 REMARK 465 SER B 31 REMARK 465 THR B 32 REMARK 465 SER B 33 REMARK 465 LYS B 34 REMARK 465 THR B 35 REMARK 465 ILE B 36 REMARK 465 SER B 227 REMARK 465 ARG B 228 REMARK 465 ASP B 229 REMARK 465 ASN B 230 REMARK 465 THR B 231 REMARK 465 LEU B 232 REMARK 465 GLN B 233 REMARK 465 VAL B 234 REMARK 465 ASP B 235 REMARK 465 ILE B 236 REMARK 465 ASN B 237 REMARK 465 GLY B 238 REMARK 465 PHE B 239 REMARK 465 THR B 240 REMARK 465 THR B 241 REMARK 465 GLY B 242 REMARK 465 ARG B 243 REMARK 465 ARG B 244 REMARK 465 GLY B 245 REMARK 465 HIS B 270 REMARK 465 LEU B 271 REMARK 465 GLN B 272 REMARK 465 SER B 273 REMARK 465 SER B 274 REMARK 465 ARG B 275 REMARK 465 HIS B 276 REMARK 465 ARG B 277 REMARK 465 ARG B 278 REMARK 465 ALA B 279 REMARK 465 LEU B 332 REMARK 465 ASP B 333 REMARK 465 THR B 334 REMARK 465 GLN B 335 REMARK 465 TYR B 336 REMARK 465 SER B 337 REMARK 465 LYS B 338 REMARK 465 VAL B 339 REMARK 465 ALA H 123 REMARK 465 SER H 124 REMARK 465 THR H 125 REMARK 465 LYS H 126 REMARK 465 GLY H 127 REMARK 465 PRO H 128 REMARK 465 SER H 129 REMARK 465 VAL H 130 REMARK 465 PHE H 131 REMARK 465 PRO H 132 REMARK 465 LEU H 133 REMARK 465 ALA H 134 REMARK 465 PRO H 135 REMARK 465 SER H 136 REMARK 465 SER H 137 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 GLY H 143 REMARK 465 THR H 144 REMARK 465 ALA H 145 REMARK 465 ALA H 146 REMARK 465 LEU H 147 REMARK 465 GLY H 148 REMARK 465 CYS H 149 REMARK 465 LEU H 150 REMARK 465 VAL H 151 REMARK 465 LYS H 152 REMARK 465 ASP H 153 REMARK 465 TYR H 154 REMARK 465 PHE H 155 REMARK 465 PRO H 156 REMARK 465 GLU H 157 REMARK 465 PRO H 158 REMARK 465 VAL H 159 REMARK 465 THR H 160 REMARK 465 VAL H 161 REMARK 465 SER H 162 REMARK 465 TRP H 163 REMARK 465 ASN H 164 REMARK 465 SER H 165 REMARK 465 GLY H 166 REMARK 465 ALA H 167 REMARK 465 LEU H 168 REMARK 465 THR H 169 REMARK 465 SER H 170 REMARK 465 GLY H 171 REMARK 465 VAL H 172 REMARK 465 HIS H 173 REMARK 465 THR H 174 REMARK 465 PHE H 175 REMARK 465 PRO H 176 REMARK 465 ALA H 177 REMARK 465 VAL H 178 REMARK 465 LEU H 179 REMARK 465 GLN H 180 REMARK 465 SER H 181 REMARK 465 SER H 182 REMARK 465 GLY H 183 REMARK 465 LEU H 184 REMARK 465 TYR H 185 REMARK 465 SER H 186 REMARK 465 LEU H 187 REMARK 465 SER H 188 REMARK 465 SER H 189 REMARK 465 VAL H 190 REMARK 465 VAL H 191 REMARK 465 THR H 192 REMARK 465 VAL H 193 REMARK 465 PRO H 194 REMARK 465 SER H 195 REMARK 465 SER H 196 REMARK 465 SER H 197 REMARK 465 LEU H 198 REMARK 465 GLY H 199 REMARK 465 THR H 200 REMARK 465 GLN H 201 REMARK 465 THR H 202 REMARK 465 TYR H 203 REMARK 465 ILE H 204 REMARK 465 CYS H 205 REMARK 465 ASN H 206 REMARK 465 VAL H 207 REMARK 465 ASN H 208 REMARK 465 HIS H 209 REMARK 465 LYS H 210 REMARK 465 PRO H 211 REMARK 465 SER H 212 REMARK 465 ASN H 213 REMARK 465 THR H 214 REMARK 465 LYS H 215 REMARK 465 VAL H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 ARG H 219 REMARK 465 VAL H 220 REMARK 465 GLU H 221 REMARK 465 PRO H 222 REMARK 465 LYS H 223 REMARK 465 SER H 224 REMARK 465 CYS H 225 REMARK 465 ASP H 226 REMARK 465 LYS H 227 REMARK 465 GLN I 1 REMARK 465 ALA I 123 REMARK 465 SER I 124 REMARK 465 THR I 125 REMARK 465 LYS I 126 REMARK 465 GLY I 127 REMARK 465 PRO I 128 REMARK 465 SER I 129 REMARK 465 VAL I 130 REMARK 465 PHE I 131 REMARK 465 PRO I 132 REMARK 465 LEU I 133 REMARK 465 ALA I 134 REMARK 465 PRO I 135 REMARK 465 SER I 136 REMARK 465 SER I 137 REMARK 465 LYS I 138 REMARK 465 SER I 139 REMARK 465 THR I 140 REMARK 465 SER I 141 REMARK 465 GLY I 142 REMARK 465 GLY I 143 REMARK 465 THR I 144 REMARK 465 ALA I 145 REMARK 465 ALA I 146 REMARK 465 LEU I 147 REMARK 465 GLY I 148 REMARK 465 CYS I 149 REMARK 465 LEU I 150 REMARK 465 VAL I 151 REMARK 465 LYS I 152 REMARK 465 ASP I 153 REMARK 465 TYR I 154 REMARK 465 PHE I 155 REMARK 465 PRO I 156 REMARK 465 GLU I 157 REMARK 465 PRO I 158 REMARK 465 VAL I 159 REMARK 465 THR I 160 REMARK 465 VAL I 161 REMARK 465 SER I 162 REMARK 465 TRP I 163 REMARK 465 ASN I 164 REMARK 465 SER I 165 REMARK 465 GLY I 166 REMARK 465 ALA I 167 REMARK 465 LEU I 168 REMARK 465 THR I 169 REMARK 465 SER I 170 REMARK 465 GLY I 171 REMARK 465 VAL I 172 REMARK 465 HIS I 173 REMARK 465 THR I 174 REMARK 465 PHE I 175 REMARK 465 PRO I 176 REMARK 465 ALA I 177 REMARK 465 VAL I 178 REMARK 465 LEU I 179 REMARK 465 GLN I 180 REMARK 465 SER I 181 REMARK 465 SER I 182 REMARK 465 GLY I 183 REMARK 465 LEU I 184 REMARK 465 TYR I 185 REMARK 465 SER I 186 REMARK 465 LEU I 187 REMARK 465 SER I 188 REMARK 465 SER I 189 REMARK 465 VAL I 190 REMARK 465 VAL I 191 REMARK 465 THR I 192 REMARK 465 VAL I 193 REMARK 465 PRO I 194 REMARK 465 SER I 195 REMARK 465 SER I 196 REMARK 465 SER I 197 REMARK 465 LEU I 198 REMARK 465 GLY I 199 REMARK 465 THR I 200 REMARK 465 GLN I 201 REMARK 465 THR I 202 REMARK 465 TYR I 203 REMARK 465 ILE I 204 REMARK 465 CYS I 205 REMARK 465 ASN I 206 REMARK 465 VAL I 207 REMARK 465 ASN I 208 REMARK 465 HIS I 209 REMARK 465 LYS I 210 REMARK 465 PRO I 211 REMARK 465 SER I 212 REMARK 465 ASN I 213 REMARK 465 THR I 214 REMARK 465 LYS I 215 REMARK 465 VAL I 216 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 ARG I 219 REMARK 465 VAL I 220 REMARK 465 GLU I 221 REMARK 465 PRO I 222 REMARK 465 LYS I 223 REMARK 465 SER I 224 REMARK 465 CYS I 225 REMARK 465 ASP I 226 REMARK 465 LYS I 227 REMARK 465 LYS L 108 REMARK 465 ARG L 109 REMARK 465 THR L 110 REMARK 465 VAL L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 PHE L 117 REMARK 465 ILE L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 ASP L 123 REMARK 465 GLU L 124 REMARK 465 GLN L 125 REMARK 465 LEU L 126 REMARK 465 LYS L 127 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 THR L 130 REMARK 465 ALA L 131 REMARK 465 SER L 132 REMARK 465 VAL L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 LEU L 137 REMARK 465 ASN L 138 REMARK 465 ASN L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 ARG L 143 REMARK 465 GLU L 144 REMARK 465 ALA L 145 REMARK 465 LYS L 146 REMARK 465 VAL L 147 REMARK 465 GLN L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 ASP L 152 REMARK 465 ASN L 153 REMARK 465 ALA L 154 REMARK 465 LEU L 155 REMARK 465 GLN L 156 REMARK 465 SER L 157 REMARK 465 GLY L 158 REMARK 465 ASN L 159 REMARK 465 SER L 160 REMARK 465 GLN L 161 REMARK 465 GLU L 162 REMARK 465 SER L 163 REMARK 465 VAL L 164 REMARK 465 THR L 165 REMARK 465 GLU L 166 REMARK 465 GLN L 167 REMARK 465 ASP L 168 REMARK 465 SER L 169 REMARK 465 LYS L 170 REMARK 465 ASP L 171 REMARK 465 SER L 172 REMARK 465 THR L 173 REMARK 465 TYR L 174 REMARK 465 SER L 175 REMARK 465 LEU L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 THR L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 LEU L 182 REMARK 465 SER L 183 REMARK 465 LYS L 184 REMARK 465 ALA L 185 REMARK 465 ASP L 186 REMARK 465 TYR L 187 REMARK 465 GLU L 188 REMARK 465 LYS L 189 REMARK 465 HIS L 190 REMARK 465 LYS L 191 REMARK 465 VAL L 192 REMARK 465 TYR L 193 REMARK 465 ALA L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 VAL L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 GLN L 200 REMARK 465 GLY L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 VAL L 206 REMARK 465 THR L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 LYS M 108 REMARK 465 ARG M 109 REMARK 465 THR M 110 REMARK 465 VAL M 111 REMARK 465 ALA M 112 REMARK 465 ALA M 113 REMARK 465 PRO M 114 REMARK 465 SER M 115 REMARK 465 VAL M 116 REMARK 465 PHE M 117 REMARK 465 ILE M 118 REMARK 465 PHE M 119 REMARK 465 PRO M 120 REMARK 465 PRO M 121 REMARK 465 SER M 122 REMARK 465 ASP M 123 REMARK 465 GLU M 124 REMARK 465 GLN M 125 REMARK 465 LEU M 126 REMARK 465 LYS M 127 REMARK 465 SER M 128 REMARK 465 GLY M 129 REMARK 465 THR M 130 REMARK 465 ALA M 131 REMARK 465 SER M 132 REMARK 465 VAL M 133 REMARK 465 VAL M 134 REMARK 465 CYS M 135 REMARK 465 LEU M 136 REMARK 465 LEU M 137 REMARK 465 ASN M 138 REMARK 465 ASN M 139 REMARK 465 PHE M 140 REMARK 465 TYR M 141 REMARK 465 PRO M 142 REMARK 465 ARG M 143 REMARK 465 GLU M 144 REMARK 465 ALA M 145 REMARK 465 LYS M 146 REMARK 465 VAL M 147 REMARK 465 GLN M 148 REMARK 465 TRP M 149 REMARK 465 LYS M 150 REMARK 465 VAL M 151 REMARK 465 ASP M 152 REMARK 465 ASN M 153 REMARK 465 ALA M 154 REMARK 465 LEU M 155 REMARK 465 GLN M 156 REMARK 465 SER M 157 REMARK 465 GLY M 158 REMARK 465 ASN M 159 REMARK 465 SER M 160 REMARK 465 GLN M 161 REMARK 465 GLU M 162 REMARK 465 SER M 163 REMARK 465 VAL M 164 REMARK 465 THR M 165 REMARK 465 GLU M 166 REMARK 465 GLN M 167 REMARK 465 ASP M 168 REMARK 465 SER M 169 REMARK 465 LYS M 170 REMARK 465 ASP M 171 REMARK 465 SER M 172 REMARK 465 THR M 173 REMARK 465 TYR M 174 REMARK 465 SER M 175 REMARK 465 LEU M 176 REMARK 465 SER M 177 REMARK 465 SER M 178 REMARK 465 THR M 179 REMARK 465 LEU M 180 REMARK 465 THR M 181 REMARK 465 LEU M 182 REMARK 465 SER M 183 REMARK 465 LYS M 184 REMARK 465 ALA M 185 REMARK 465 ASP M 186 REMARK 465 TYR M 187 REMARK 465 GLU M 188 REMARK 465 LYS M 189 REMARK 465 HIS M 190 REMARK 465 LYS M 191 REMARK 465 VAL M 192 REMARK 465 TYR M 193 REMARK 465 ALA M 194 REMARK 465 CYS M 195 REMARK 465 GLU M 196 REMARK 465 VAL M 197 REMARK 465 THR M 198 REMARK 465 HIS M 199 REMARK 465 GLN M 200 REMARK 465 GLY M 201 REMARK 465 LEU M 202 REMARK 465 SER M 203 REMARK 465 SER M 204 REMARK 465 PRO M 205 REMARK 465 VAL M 206 REMARK 465 THR M 207 REMARK 465 LYS M 208 REMARK 465 SER M 209 REMARK 465 PHE M 210 REMARK 465 ASN M 211 REMARK 465 ARG M 212 REMARK 465 GLY M 213 REMARK 465 GLU M 214 REMARK 465 CYS M 215 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 GLU A 67 CG CD OE1 OE2 REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 96 CG CD OE1 OE2 REMARK 470 GLU A 100 CG CD OE1 OE2 REMARK 470 GLU A 119 CG CD OE1 OE2 REMARK 470 LYS A 123 CG CD CE NZ REMARK 470 LYS A 125 CG CD CE NZ REMARK 470 LYS A 291 CD CE NZ REMARK 470 ARG A 303 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 304 CG CD CE NZ REMARK 470 LYS A 309 CG CD CE NZ REMARK 470 ARG A 372 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 373 CG CD CE NZ REMARK 470 ASP B 37 CG OD1 OD2 REMARK 470 LYS B 44 CE NZ REMARK 470 ARG B 58 NE CZ NH1 NH2 REMARK 470 ARG B 87 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 100 CG CD OE1 OE2 REMARK 470 GLU B 119 CG CD OE1 OE2 REMARK 470 LYS B 123 CG CD CE NZ REMARK 470 LYS B 125 CG CD CE NZ REMARK 470 LYS B 161 CG CD CE NZ REMARK 470 LYS B 163 CD CE NZ REMARK 470 ASP B 246 CG OD1 OD2 REMARK 470 LEU B 247 CG CD1 CD2 REMARK 470 LEU B 280 CG CD1 CD2 REMARK 470 ASN B 283 CG OD1 ND2 REMARK 470 LYS B 291 CG CD CE NZ REMARK 470 LYS B 309 NZ REMARK 470 LEU B 340 CG CD1 CD2 REMARK 470 ARG B 372 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 373 CG CD CE NZ REMARK 470 LYS B 375 CE NZ REMARK 470 LYS B 388 CG CD CE NZ REMARK 470 GLN H 1 CG CD OE1 NE2 REMARK 470 GLN H 13 CG CD OE1 NE2 REMARK 470 ARG H 16 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 43 CD CE NZ REMARK 470 ARG H 86 CG CD NE CZ NH1 NH2 REMARK 470 GLN I 13 CG CD OE1 NE2 REMARK 470 ARG I 16 CG CD NE CZ NH1 NH2 REMARK 470 LYS I 43 CG CD CE NZ REMARK 470 LYS I 75 CG CD CE NZ REMARK 470 ARG I 86 CG CD NE CZ NH1 NH2 REMARK 470 GLU I 88 CG CD OE1 OE2 REMARK 470 GLN L 27 CG CD OE1 NE2 REMARK 470 ASP M 1 CG OD1 OD2 REMARK 470 GLN M 3 CG CD OE1 NE2 REMARK 470 GLN M 27 CG CD OE1 NE2 REMARK 470 LYS M 45 CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 63 157.27 -40.12 REMARK 500 GLU A 67 35.77 -78.82 REMARK 500 PRO A 74 160.15 -46.29 REMARK 500 PRO A 99 -1.95 -59.83 REMARK 500 GLU A 100 -44.17 80.59 REMARK 500 LYS A 125 -167.09 -75.94 REMARK 500 THR A 128 -83.21 61.83 REMARK 500 SER A 175 -138.25 61.85 REMARK 500 ASN A 292 -170.43 -63.94 REMARK 500 CYS A 294 155.61 178.66 REMARK 500 ASN A 320 -173.87 51.06 REMARK 500 ALA A 350 57.05 34.78 REMARK 500 GLN B 65 31.21 39.59 REMARK 500 GLU B 67 10.03 -69.42 REMARK 500 ALA B 89 97.60 -63.23 REMARK 500 GLU B 100 -45.35 81.42 REMARK 500 GLU B 119 26.35 -73.57 REMARK 500 LYS B 125 -171.66 -67.50 REMARK 500 SER B 127 1.50 53.85 REMARK 500 THR B 128 -47.38 68.82 REMARK 500 SER B 175 -178.77 63.28 REMARK 500 LEU B 247 31.17 -93.43 REMARK 500 THR B 289 84.03 54.14 REMARK 500 ASN B 320 -169.34 59.69 REMARK 500 LEU B 342 43.99 -101.25 REMARK 500 ASN B 347 63.31 -162.73 REMARK 500 GLN B 359 -65.28 -100.73 REMARK 500 SER H 84 53.80 32.64 REMARK 500 ARG I 64 92.29 -68.26 REMARK 500 SER L 30 -119.48 50.84 REMARK 500 ALA L 51 -36.20 60.38 REMARK 500 LEU L 78 98.87 -40.21 REMARK 500 TYR L 91 42.17 -154.37 REMARK 500 SER M 28 108.81 -52.25 REMARK 500 SER M 30 -118.60 52.14 REMARK 500 ALA M 51 -37.69 61.33 REMARK 500 SER M 67 72.96 -155.31 REMARK 500 LEU M 78 101.50 -53.19 REMARK 500 TYR M 91 30.85 -154.23 REMARK 500 SER M 96 39.05 -145.05 REMARK 500 REMARK 500 REMARK: NULL DBREF 9VJJ A 30 390 UNP P01137 TGFB1_HUMAN 30 390 DBREF 9VJJ B 30 390 UNP P01137 TGFB1_HUMAN 30 390 DBREF 9VJJ H 1 227 PDB 9VJJ 9VJJ 1 227 DBREF 9VJJ I 1 227 PDB 9VJJ 9VJJ 1 227 DBREF 9VJJ L 1 215 PDB 9VJJ 9VJJ 1 215 DBREF 9VJJ M 1 215 PDB 9VJJ 9VJJ 1 215 SEQADV 9VJJ ASP A 22 UNP P01137 EXPRESSION TAG SEQADV 9VJJ TYR A 23 UNP P01137 EXPRESSION TAG SEQADV 9VJJ LYS A 24 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP A 25 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP A 26 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP A 27 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP A 28 UNP P01137 EXPRESSION TAG SEQADV 9VJJ LYS A 29 UNP P01137 EXPRESSION TAG SEQADV 9VJJ SER A 33 UNP P01137 CYS 33 ENGINEERED MUTATION SEQADV 9VJJ ASP B 22 UNP P01137 EXPRESSION TAG SEQADV 9VJJ TYR B 23 UNP P01137 EXPRESSION TAG SEQADV 9VJJ LYS B 24 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP B 25 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP B 26 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP B 27 UNP P01137 EXPRESSION TAG SEQADV 9VJJ ASP B 28 UNP P01137 EXPRESSION TAG SEQADV 9VJJ LYS B 29 UNP P01137 EXPRESSION TAG SEQADV 9VJJ SER B 33 UNP P01137 CYS 33 ENGINEERED MUTATION SEQRES 1 A 369 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER THR SER LYS SEQRES 2 A 369 THR ILE ASP MET GLU LEU VAL LYS ARG LYS ARG ILE GLU SEQRES 3 A 369 ALA ILE ARG GLY GLN ILE LEU SER LYS LEU ARG LEU ALA SEQRES 4 A 369 SER PRO PRO SER GLN GLY GLU VAL PRO PRO GLY PRO LEU SEQRES 5 A 369 PRO GLU ALA VAL LEU ALA LEU TYR ASN SER THR ARG ASP SEQRES 6 A 369 ARG VAL ALA GLY GLU SER ALA GLU PRO GLU PRO GLU PRO SEQRES 7 A 369 GLU ALA ASP TYR TYR ALA LYS GLU VAL THR ARG VAL LEU SEQRES 8 A 369 MET VAL GLU THR HIS ASN GLU ILE TYR ASP LYS PHE LYS SEQRES 9 A 369 GLN SER THR HIS SER ILE TYR MET PHE PHE ASN THR SER SEQRES 10 A 369 GLU LEU ARG GLU ALA VAL PRO GLU PRO VAL LEU LEU SER SEQRES 11 A 369 ARG ALA GLU LEU ARG LEU LEU ARG LEU LYS LEU LYS VAL SEQRES 12 A 369 GLU GLN HIS VAL GLU LEU TYR GLN LYS TYR SER ASN ASN SEQRES 13 A 369 SER TRP ARG TYR LEU SER ASN ARG LEU LEU ALA PRO SER SEQRES 14 A 369 ASP SER PRO GLU TRP LEU SER PHE ASP VAL THR GLY VAL SEQRES 15 A 369 VAL ARG GLN TRP LEU SER ARG GLY GLY GLU ILE GLU GLY SEQRES 16 A 369 PHE ARG LEU SER ALA HIS CYS SER CYS ASP SER ARG ASP SEQRES 17 A 369 ASN THR LEU GLN VAL ASP ILE ASN GLY PHE THR THR GLY SEQRES 18 A 369 ARG ARG GLY ASP LEU ALA THR ILE HIS GLY MET ASN ARG SEQRES 19 A 369 PRO PHE LEU LEU LEU MET ALA THR PRO LEU GLU ARG ALA SEQRES 20 A 369 GLN HIS LEU GLN SER SER ARG HIS ARG ARG ALA LEU ASP SEQRES 21 A 369 THR ASN TYR CYS PHE SER SER THR GLU LYS ASN CYS CYS SEQRES 22 A 369 VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS ASP LEU GLY SEQRES 23 A 369 TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR HIS ALA ASN SEQRES 24 A 369 PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP SER LEU ASP SEQRES 25 A 369 THR GLN TYR SER LYS VAL LEU ALA LEU TYR ASN GLN HIS SEQRES 26 A 369 ASN PRO GLY ALA SER ALA ALA PRO CYS CYS VAL PRO GLN SEQRES 27 A 369 ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR VAL GLY ARG SEQRES 28 A 369 LYS PRO LYS VAL GLU GLN LEU SER ASN MET ILE VAL ARG SEQRES 29 A 369 SER CYS LYS CYS SER SEQRES 1 B 369 ASP TYR LYS ASP ASP ASP ASP LYS LEU SER THR SER LYS SEQRES 2 B 369 THR ILE ASP MET GLU LEU VAL LYS ARG LYS ARG ILE GLU SEQRES 3 B 369 ALA ILE ARG GLY GLN ILE LEU SER LYS LEU ARG LEU ALA SEQRES 4 B 369 SER PRO PRO SER GLN GLY GLU VAL PRO PRO GLY PRO LEU SEQRES 5 B 369 PRO GLU ALA VAL LEU ALA LEU TYR ASN SER THR ARG ASP SEQRES 6 B 369 ARG VAL ALA GLY GLU SER ALA GLU PRO GLU PRO GLU PRO SEQRES 7 B 369 GLU ALA ASP TYR TYR ALA LYS GLU VAL THR ARG VAL LEU SEQRES 8 B 369 MET VAL GLU THR HIS ASN GLU ILE TYR ASP LYS PHE LYS SEQRES 9 B 369 GLN SER THR HIS SER ILE TYR MET PHE PHE ASN THR SER SEQRES 10 B 369 GLU LEU ARG GLU ALA VAL PRO GLU PRO VAL LEU LEU SER SEQRES 11 B 369 ARG ALA GLU LEU ARG LEU LEU ARG LEU LYS LEU LYS VAL SEQRES 12 B 369 GLU GLN HIS VAL GLU LEU TYR GLN LYS TYR SER ASN ASN SEQRES 13 B 369 SER TRP ARG TYR LEU SER ASN ARG LEU LEU ALA PRO SER SEQRES 14 B 369 ASP SER PRO GLU TRP LEU SER PHE ASP VAL THR GLY VAL SEQRES 15 B 369 VAL ARG GLN TRP LEU SER ARG GLY GLY GLU ILE GLU GLY SEQRES 16 B 369 PHE ARG LEU SER ALA HIS CYS SER CYS ASP SER ARG ASP SEQRES 17 B 369 ASN THR LEU GLN VAL ASP ILE ASN GLY PHE THR THR GLY SEQRES 18 B 369 ARG ARG GLY ASP LEU ALA THR ILE HIS GLY MET ASN ARG SEQRES 19 B 369 PRO PHE LEU LEU LEU MET ALA THR PRO LEU GLU ARG ALA SEQRES 20 B 369 GLN HIS LEU GLN SER SER ARG HIS ARG ARG ALA LEU ASP SEQRES 21 B 369 THR ASN TYR CYS PHE SER SER THR GLU LYS ASN CYS CYS SEQRES 22 B 369 VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS ASP LEU GLY SEQRES 23 B 369 TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR HIS ALA ASN SEQRES 24 B 369 PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP SER LEU ASP SEQRES 25 B 369 THR GLN TYR SER LYS VAL LEU ALA LEU TYR ASN GLN HIS SEQRES 26 B 369 ASN PRO GLY ALA SER ALA ALA PRO CYS CYS VAL PRO GLN SEQRES 27 B 369 ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR VAL GLY ARG SEQRES 28 B 369 LYS PRO LYS VAL GLU GLN LEU SER ASN MET ILE VAL ARG SEQRES 29 B 369 SER CYS LYS CYS SER SEQRES 1 H 227 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 227 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 227 PHE THR PHE SER SER GLU ALA MET ASN TRP ILE ARG GLN SEQRES 4 H 227 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 227 THR SER GLY THR THR TYR ARG ALA ASN TRP ALA ARG GLY SEQRES 6 H 227 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 H 227 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 227 VAL TYR TYR CYS ALA ARG GLY THR GLY ILE TYR ASP TYR SEQRES 9 H 227 TYR TYR TRP VAL MET ASP LEU TRP GLY PRO GLY THR LEU SEQRES 10 H 227 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 227 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 227 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 227 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 227 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 227 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 227 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 227 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 227 PRO LYS SER CYS ASP LYS SEQRES 1 I 227 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 I 227 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 I 227 PHE THR PHE SER SER GLU ALA MET ASN TRP ILE ARG GLN SEQRES 4 I 227 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 I 227 THR SER GLY THR THR TYR ARG ALA ASN TRP ALA ARG GLY SEQRES 6 I 227 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 I 227 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 I 227 VAL TYR TYR CYS ALA ARG GLY THR GLY ILE TYR ASP TYR SEQRES 9 I 227 TYR TYR TRP VAL MET ASP LEU TRP GLY PRO GLY THR LEU SEQRES 10 I 227 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 I 227 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 I 227 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 I 227 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 I 227 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 I 227 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 I 227 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 I 227 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 I 227 PRO LYS SER CYS ASP LYS SEQRES 1 L 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 215 GLN SER ILE SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 215 THR LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN SER TYR SEQRES 8 L 215 SER ASP GLY ASP SER VAL GLY PHE GLY GLN GLY THR LYS SEQRES 9 L 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 M 215 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 M 215 GLN SER ILE SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 M 215 PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 M 215 THR LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 M 215 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 M 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN SER TYR SEQRES 8 M 215 SER ASP GLY ASP SER VAL GLY PHE GLY GLN GLY THR LYS SEQRES 9 M 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 M 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 M 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 M 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 M 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 M 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 M 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 M 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 M 215 SER PHE ASN ARG GLY GLU CYS HET NAG X 1 14 HET NAG X 2 14 HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 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 7 NAG 8(C8 H15 N O6) FORMUL 11 HOH *4(H2 O) HELIX 1 AA1 ASP A 37 LEU A 57 1 21 HELIX 2 AA2 PRO A 74 ASP A 86 1 13 HELIX 3 AA3 GLU A 100 TYR A 104 5 5 HELIX 4 AA4 ASN A 118 ASP A 122 5 5 HELIX 5 AA5 THR A 137 VAL A 144 1 8 HELIX 6 AA6 VAL A 200 GLY A 211 1 12 HELIX 7 AA7 PRO A 264 GLN A 269 1 6 HELIX 8 AA8 PHE A 302 GLY A 307 1 6 HELIX 9 AA9 TYR A 343 ASN A 347 1 5 HELIX 10 AB1 MET B 38 LEU B 57 1 20 HELIX 11 AB2 PRO B 74 ASP B 86 1 13 HELIX 12 AB3 GLU B 100 TYR B 104 5 5 HELIX 13 AB4 THR B 137 VAL B 144 1 8 HELIX 14 AB5 GLU B 146 VAL B 148 5 3 HELIX 15 AB6 VAL B 200 GLY B 211 1 12 HELIX 16 AB7 PRO B 264 ALA B 268 5 5 HELIX 17 AB8 ASP B 281 THR B 289 1 9 HELIX 18 AB9 PHE B 302 GLY B 307 1 6 HELIX 19 AC1 LEU B 342 ASN B 347 1 6 HELIX 20 AC2 THR H 28 GLU H 32 5 5 HELIX 21 AC3 ASN H 73 LYS H 75 5 3 HELIX 22 AC4 ARG H 86 THR H 90 5 5 HELIX 23 AC5 TYR H 104 TRP H 107 5 4 HELIX 24 AC6 THR I 28 GLU I 32 5 5 HELIX 25 AC7 ARG I 86 THR I 90 5 5 HELIX 26 AC8 TYR I 104 TRP I 107 5 4 HELIX 27 AC9 GLN L 79 PHE L 83 5 5 HELIX 28 AD1 ASP L 93 ASP L 95 5 3 HELIX 29 AD2 ASP M 93 VAL M 97 5 5 SHEET 1 AA1 7 GLU A 194 ASP A 199 0 SHEET 2 AA1 7 LEU A 150 ARG A 159 -1 N ARG A 159 O GLU A 194 SHEET 3 AA1 7 PHE A 257 ALA A 262 -1 O PHE A 257 N ARG A 156 SHEET 4 AA1 7 LYS A 106 LEU A 112 -1 N THR A 109 O LEU A 260 SHEET 5 AA1 7 LYS B 373 VAL B 384 -1 O VAL B 376 N VAL A 108 SHEET 6 AA1 7 LEU B 361 VAL B 370 -1 N LEU B 364 O LEU B 379 SHEET 7 AA1 7 ILE B 311 GLU B 313 -1 N GLU B 313 O VAL B 367 SHEET 1 AA2 4 ILE A 131 ASN A 136 0 SHEET 2 AA2 4 ILE A 214 ALA A 221 -1 O GLU A 215 N PHE A 135 SHEET 3 AA2 4 GLN A 166 TYR A 174 -1 N TYR A 171 O ARG A 218 SHEET 4 AA2 4 SER A 178 LEU A 187 -1 O LEU A 187 N GLN A 166 SHEET 1 AA3 2 VAL A 295 ARG A 296 0 SHEET 2 AA3 2 PHE A 321 CYS A 322 -1 O PHE A 321 N ARG A 296 SHEET 1 AA4 2 ILE A 300 ASP A 301 0 SHEET 2 AA4 2 GLY A 316 TYR A 317 -1 O TYR A 317 N ILE A 300 SHEET 1 AA5 7 ILE A 311 GLU A 313 0 SHEET 2 AA5 7 CYS A 355 VAL A 370 -1 O VAL A 367 N GLU A 313 SHEET 3 AA5 7 LYS A 373 SER A 390 -1 O LYS A 375 N TYR A 368 SHEET 4 AA5 7 LYS B 106 LEU B 112 -1 O VAL B 108 N VAL A 376 SHEET 5 AA5 7 PHE B 257 ALA B 262 -1 O LEU B 260 N THR B 109 SHEET 6 AA5 7 LEU B 150 ARG B 159 -1 N ARG B 152 O MET B 261 SHEET 7 AA5 7 GLU B 194 ASP B 199 -1 O LEU B 196 N LEU B 157 SHEET 1 AA6 4 SER B 130 ASN B 136 0 SHEET 2 AA6 4 ILE B 214 ALA B 221 -1 O GLU B 215 N PHE B 135 SHEET 3 AA6 4 GLN B 166 TYR B 174 -1 N LYS B 173 O GLY B 216 SHEET 4 AA6 4 SER B 178 LEU B 187 -1 O SER B 178 N TYR B 174 SHEET 1 AA7 2 CYS B 294 ARG B 296 0 SHEET 2 AA7 2 PHE B 321 LEU B 323 -1 O PHE B 321 N ARG B 296 SHEET 1 AA8 2 TYR B 299 ASP B 301 0 SHEET 2 AA8 2 GLY B 316 HIS B 318 -1 O TYR B 317 N ILE B 300 SHEET 1 AA9 2 CYS B 356 PRO B 358 0 SHEET 2 AA9 2 CYS B 387 CYS B 389 -1 O LYS B 388 N VAL B 357 SHEET 1 AB1 4 GLN H 3 SER H 7 0 SHEET 2 AB1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB1 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AB1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AB2 6 VAL H 11 VAL H 12 0 SHEET 2 AB2 6 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AB2 6 ALA H 91 GLY H 98 -1 N TYR H 93 O THR H 116 SHEET 4 AB2 6 MET H 34 GLN H 39 -1 N ASN H 35 O ALA H 96 SHEET 5 AB2 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AB2 6 THR H 57 ARG H 59 -1 O TYR H 58 N TYR H 50 SHEET 1 AB3 4 VAL H 11 VAL H 12 0 SHEET 2 AB3 4 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AB3 4 ALA H 91 GLY H 98 -1 N TYR H 93 O THR H 116 SHEET 4 AB3 4 MET H 109 TRP H 112 -1 O LEU H 111 N ARG H 97 SHEET 1 AB4 4 GLN I 3 SER I 7 0 SHEET 2 AB4 4 LEU I 18 SER I 25 -1 O ALA I 23 N VAL I 5 SHEET 3 AB4 4 THR I 77 MET I 82 -1 O MET I 82 N LEU I 18 SHEET 4 AB4 4 PHE I 67 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AB5 6 VAL I 11 VAL I 12 0 SHEET 2 AB5 6 THR I 116 VAL I 120 1 O THR I 119 N VAL I 12 SHEET 3 AB5 6 ALA I 91 GLY I 98 -1 N TYR I 93 O THR I 116 SHEET 4 AB5 6 MET I 34 GLN I 39 -1 N ILE I 37 O TYR I 94 SHEET 5 AB5 6 GLU I 46 ILE I 51 -1 O GLY I 49 N TRP I 36 SHEET 6 AB5 6 THR I 57 ARG I 59 -1 O TYR I 58 N TYR I 50 SHEET 1 AB6 4 VAL I 11 VAL I 12 0 SHEET 2 AB6 4 THR I 116 VAL I 120 1 O THR I 119 N VAL I 12 SHEET 3 AB6 4 ALA I 91 GLY I 98 -1 N TYR I 93 O THR I 116 SHEET 4 AB6 4 MET I 109 TRP I 112 -1 O LEU I 111 N ARG I 97 SHEET 1 AB7 4 MET L 4 SER L 7 0 SHEET 2 AB7 4 VAL L 19 ALA L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AB7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB8 6 SER L 10 SER L 12 0 SHEET 2 AB8 6 THR L 103 GLU L 106 1 O GLU L 106 N LEU L 11 SHEET 3 AB8 6 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 103 SHEET 4 AB8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB8 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB9 4 SER L 10 SER L 12 0 SHEET 2 AB9 4 THR L 103 GLU L 106 1 O GLU L 106 N LEU L 11 SHEET 3 AB9 4 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 103 SHEET 4 AB9 4 VAL L 97 PHE L 99 -1 O GLY L 98 N SER L 90 SHEET 1 AC1 4 MET M 4 SER M 7 0 SHEET 2 AC1 4 VAL M 19 ALA M 25 -1 O GLN M 24 N THR M 5 SHEET 3 AC1 4 ASP M 70 ILE M 75 -1 O LEU M 73 N ILE M 21 SHEET 4 AC1 4 PHE M 62 GLY M 66 -1 N SER M 63 O THR M 74 SHEET 1 AC2 6 SER M 10 SER M 12 0 SHEET 2 AC2 6 THR M 103 GLU M 106 1 O GLU M 106 N LEU M 11 SHEET 3 AC2 6 THR M 85 SER M 90 -1 N TYR M 86 O THR M 103 SHEET 4 AC2 6 LEU M 33 GLN M 38 -1 N TYR M 36 O TYR M 87 SHEET 5 AC2 6 LYS M 45 TYR M 49 -1 O ILE M 48 N TRP M 35 SHEET 6 AC2 6 THR M 53 LEU M 54 -1 O THR M 53 N TYR M 49 SSBOND 1 CYS A 223 CYS B 225 1555 1555 2.04 SSBOND 2 CYS A 225 CYS B 223 1555 1555 2.05 SSBOND 3 CYS A 293 CYS A 356 1555 1555 2.03 SSBOND 4 CYS A 322 CYS A 387 1555 1555 2.03 SSBOND 5 CYS A 326 CYS A 389 1555 1555 2.04 SSBOND 6 CYS A 355 CYS B 355 1555 1555 2.02 SSBOND 7 CYS B 285 CYS B 294 1555 1555 2.04 SSBOND 8 CYS B 293 CYS B 356 1555 1555 2.02 SSBOND 9 CYS B 322 CYS B 387 1555 1555 2.03 SSBOND 10 CYS B 326 CYS B 389 1555 1555 2.03 SSBOND 11 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 12 CYS I 22 CYS I 95 1555 1555 2.03 SSBOND 13 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 14 CYS M 23 CYS M 88 1555 1555 2.03 LINK ND2 ASN A 82 C1 NAG E 1 1555 1555 1.43 LINK ND2 ASN A 136 C1 NAG C 1 1555 1555 1.43 LINK ND2 ASN B 82 C1 NAG X 1 1555 1555 1.43 LINK ND2 ASN B 136 C1 NAG D 1 1555 1555 1.43 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.42 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.41 CISPEP 1 GLU A 313 PRO A 314 0 -0.88 CISPEP 2 GLU B 313 PRO B 314 0 -4.15 CISPEP 3 SER L 7 PRO L 8 0 -2.76 CISPEP 4 SER M 7 PRO M 8 0 1.14 CRYST1 225.878 91.707 126.120 90.00 108.58 90.00 C 1 2 1 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 0.004427 0.000000 0.001488 0.00000 SCALE2 0.000000 0.010904 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008365 0.00000