HEADER IMMUNE SYSTEM 26-MAR-20 6WAS TITLE STRUCTURE OF D19.PA8 FAB IN COMPLEX WITH 1FD6 16055 V1V2 SCAFFOLD CAVEAT 6WAS THE GAP DISTANCE ( 23.77 ANGSTROM ) BETWEEN RESIDUES ( G LYS CAVEAT 2 6WAS 168 ) AND ( G LYS 171 ) IS TOO LARGE. THERE ARE ONLY 2 CAVEAT 3 6WAS RESIDUES BETWEEN THEM. IT IS NOT ENOUGH TO COVER THIS GAP. CAVEAT 4 6WAS THE GAP DISTANCE ( 25.15 ANGSTROM ) BETWEEN RESIDUES ( J CAVEAT 5 6WAS LYS 168 ) AND ( J VAL 172 ) IS TOO LARGE. THERE ARE ONLY 3 CAVEAT 6 6WAS RESIDUES BETWEEN THEM. IT IS NOT ENOUGH TO COVER THIS GAP. COMPND MOL_ID: 1; COMPND 2 MOLECULE: GN1_PA8 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GN1_PA8 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 1FD6 16055 V1V2 SCAFFOLD; COMPND 11 CHAIN: G, J; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; 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: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606 KEYWDS FRAGMENT BINDING ANTIGEN AND PEPTIDE COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.SINGH,T.J.LIBAN,M.PANCERA REVDAT 1 31-MAR-21 6WAS 0 JRNL AUTH T.LIBAN,S.ALJEDANI,S.SINGH,J.RODARTE JRNL TITL STRUCTURAL BASIS FOR POTENT TIER 2 AUTOLOGOUS NEUTRALIZATION JRNL TITL 2 ELICITED BY VACCINATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.14_3260 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.3 REMARK 3 NUMBER OF REFLECTIONS : 84538 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910 REMARK 3 FREE R VALUE TEST SET COUNT : 4155 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 31.9030 - 5.9036 0.96 3143 170 0.2071 0.2440 REMARK 3 2 5.9036 - 4.6906 1.00 3102 177 0.1612 0.1777 REMARK 3 3 4.6906 - 4.0991 1.00 3063 172 0.1373 0.1635 REMARK 3 4 4.0991 - 3.7249 1.00 3069 171 0.1641 0.2027 REMARK 3 5 3.7249 - 3.4583 1.00 3094 135 0.1724 0.1908 REMARK 3 6 3.4583 - 3.2546 1.00 3056 156 0.1720 0.2156 REMARK 3 7 3.2546 - 3.0918 1.00 3040 153 0.1886 0.2372 REMARK 3 8 3.0918 - 2.9573 1.00 3042 147 0.1987 0.2382 REMARK 3 9 2.9573 - 2.8435 0.99 3012 166 0.1968 0.2263 REMARK 3 10 2.8435 - 2.7454 0.99 3041 144 0.1974 0.2416 REMARK 3 11 2.7454 - 2.6596 1.00 2996 167 0.2021 0.2738 REMARK 3 12 2.6596 - 2.5836 1.00 3025 159 0.2012 0.2427 REMARK 3 13 2.5836 - 2.5157 0.99 2999 152 0.2119 0.2639 REMARK 3 14 2.5157 - 2.4543 0.99 2975 170 0.2176 0.2441 REMARK 3 15 2.4543 - 2.3985 1.00 3020 154 0.2170 0.2525 REMARK 3 16 2.3985 - 2.3475 0.99 3007 172 0.2157 0.2438 REMARK 3 17 2.3475 - 2.3006 0.99 2963 151 0.2165 0.2455 REMARK 3 18 2.3006 - 2.2572 0.99 3016 159 0.2257 0.2485 REMARK 3 19 2.2572 - 2.2169 0.99 2955 155 0.2201 0.2647 REMARK 3 20 2.2169 - 2.1793 0.99 2977 151 0.2178 0.2429 REMARK 3 21 2.1793 - 2.1441 0.98 2959 168 0.2294 0.2857 REMARK 3 22 2.1441 - 2.1112 0.97 2903 129 0.2281 0.2884 REMARK 3 23 2.1112 - 2.0801 0.93 2806 127 0.2235 0.2690 REMARK 3 24 2.0801 - 2.0508 0.86 2579 115 0.2435 0.2603 REMARK 3 25 2.0508 - 2.0231 0.76 2311 119 0.2409 0.2472 REMARK 3 26 2.0231 - 1.9968 0.65 1910 100 0.2420 0.2893 REMARK 3 27 1.9968 - 1.9719 0.49 1470 86 0.2351 0.2351 REMARK 3 28 1.9719 - 1.9481 0.39 1153 60 0.2673 0.3326 REMARK 3 29 1.9481 - 1.9255 0.31 921 42 0.2677 0.2911 REMARK 3 30 1.9255 - 1.9040 0.26 776 28 0.2907 0.3011 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) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.790 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.51 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 3.9055 44.9910 85.5705 REMARK 3 T TENSOR REMARK 3 T11: 0.0698 T22: 0.0840 REMARK 3 T33: 0.0779 T12: 0.0261 REMARK 3 T13: -0.0171 T23: 0.0268 REMARK 3 L TENSOR REMARK 3 L11: 0.0175 L22: 0.0052 REMARK 3 L33: 0.0449 L12: 0.0078 REMARK 3 L13: -0.0216 L23: 0.0058 REMARK 3 S TENSOR REMARK 3 S11: -0.0137 S12: -0.0040 S13: -0.0042 REMARK 3 S21: -0.0060 S22: 0.0177 S23: 0.0001 REMARK 3 S31: -0.0046 S32: 0.0140 S33: 0.0019 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 6WAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-20. REMARK 100 THE DEPOSITION ID IS D_1000247388. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-AUG-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84549 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 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: PDB ENTRY 5TDN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5, 18% PEG6000, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 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 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 36.84850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.00750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.94650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.00750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.84850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.94650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 CYS L 211 REMARK 465 SER L 212 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 215 REMARK 465 CYS B 211 REMARK 465 SER B 212 REMARK 465 MET G 118 REMARK 465 THR G 119 REMARK 465 THR G 120 REMARK 465 PHE G 121 REMARK 465 LYS G 122 REMARK 465 LEU G 123 REMARK 465 ALA G 124 REMARK 465 ALA G 125 REMARK 465 THR G 139 REMARK 465 THR G 140 REMARK 465 ASN G 141 REMARK 465 ALA G 142 REMARK 465 THR G 143 REMARK 465 SER G 144 REMARK 465 SER G 145 REMARK 465 VAL G 146 REMARK 465 ASN G 147 REMARK 465 VAL G 148 REMARK 465 THR G 149 REMARK 465 ASN G 150 REMARK 465 GLY G 151 REMARK 465 LYS G 169 REMARK 465 GLN G 170 REMARK 465 GLN G 197 REMARK 465 THR G 198 REMARK 465 THR G 199 REMARK 465 THR G 200 REMARK 465 THR G 201 REMARK 465 GLU G 202 REMARK 465 ALA G 203 REMARK 465 VAL G 204 REMARK 465 ASP G 205 REMARK 465 ALA G 206 REMARK 465 ALA G 207 REMARK 465 THR G 208 REMARK 465 ALA G 209 REMARK 465 ALA G 210 REMARK 465 LYS G 211 REMARK 465 VAL G 212 REMARK 465 PHE G 213 REMARK 465 LYS G 214 REMARK 465 GLN G 215 REMARK 465 TYR G 216 REMARK 465 ALA G 217 REMARK 465 ASN G 218 REMARK 465 ASP G 219 REMARK 465 ASN G 220 REMARK 465 GLY G 221 REMARK 465 ILE G 222 REMARK 465 ASP G 223 REMARK 465 GLY G 224 REMARK 465 GLU G 225 REMARK 465 TRP G 226 REMARK 465 THR G 227 REMARK 465 TYR G 228 REMARK 465 ASP G 229 REMARK 465 ASP G 230 REMARK 465 ALA G 231 REMARK 465 THR G 232 REMARK 465 LYS G 233 REMARK 465 THR G 234 REMARK 465 PHE G 235 REMARK 465 THR G 236 REMARK 465 VAL G 237 REMARK 465 THR G 238 REMARK 465 GLU G 239 REMARK 465 GLY G 240 REMARK 465 LEU G 241 REMARK 465 GLU G 242 REMARK 465 VAL G 243 REMARK 465 LEU G 244 REMARK 465 PHE G 245 REMARK 465 GLN G 246 REMARK 465 GLY G 247 REMARK 465 PRO G 248 REMARK 465 GLY G 249 REMARK 465 HIS G 250 REMARK 465 HIS G 251 REMARK 465 HIS G 252 REMARK 465 HIS G 253 REMARK 465 HIS G 254 REMARK 465 HIS G 255 REMARK 465 HIS G 256 REMARK 465 HIS G 257 REMARK 465 SER G 258 REMARK 465 ALA G 259 REMARK 465 TRP G 260 REMARK 465 SER G 261 REMARK 465 HIS G 262 REMARK 465 PRO G 263 REMARK 465 GLN G 264 REMARK 465 PHE G 265 REMARK 465 GLU G 266 REMARK 465 LYS G 267 REMARK 465 MET J 118 REMARK 465 THR J 119 REMARK 465 THR J 120 REMARK 465 PHE J 121 REMARK 465 LYS J 122 REMARK 465 LEU J 123 REMARK 465 ALA J 124 REMARK 465 ALA J 125 REMARK 465 THR J 139 REMARK 465 THR J 140 REMARK 465 ASN J 141 REMARK 465 ALA J 142 REMARK 465 THR J 143 REMARK 465 SER J 144 REMARK 465 SER J 145 REMARK 465 VAL J 146 REMARK 465 ASN J 147 REMARK 465 VAL J 148 REMARK 465 THR J 149 REMARK 465 ASN J 150 REMARK 465 GLY J 151 REMARK 465 LYS J 169 REMARK 465 GLN J 170 REMARK 465 LYS J 171 REMARK 465 GLN J 197 REMARK 465 THR J 198 REMARK 465 THR J 199 REMARK 465 THR J 200 REMARK 465 THR J 201 REMARK 465 GLU J 202 REMARK 465 ALA J 203 REMARK 465 VAL J 204 REMARK 465 ASP J 205 REMARK 465 ALA J 206 REMARK 465 ALA J 207 REMARK 465 THR J 208 REMARK 465 ALA J 209 REMARK 465 ALA J 210 REMARK 465 LYS J 211 REMARK 465 VAL J 212 REMARK 465 PHE J 213 REMARK 465 LYS J 214 REMARK 465 GLN J 215 REMARK 465 TYR J 216 REMARK 465 ALA J 217 REMARK 465 ASN J 218 REMARK 465 ASP J 219 REMARK 465 ASN J 220 REMARK 465 GLY J 221 REMARK 465 ILE J 222 REMARK 465 ASP J 223 REMARK 465 GLY J 224 REMARK 465 GLU J 225 REMARK 465 TRP J 226 REMARK 465 THR J 227 REMARK 465 TYR J 228 REMARK 465 ASP J 229 REMARK 465 ASP J 230 REMARK 465 ALA J 231 REMARK 465 THR J 232 REMARK 465 LYS J 233 REMARK 465 THR J 234 REMARK 465 PHE J 235 REMARK 465 THR J 236 REMARK 465 VAL J 237 REMARK 465 THR J 238 REMARK 465 GLU J 239 REMARK 465 GLY J 240 REMARK 465 LEU J 241 REMARK 465 GLU J 242 REMARK 465 VAL J 243 REMARK 465 LEU J 244 REMARK 465 PHE J 245 REMARK 465 GLN J 246 REMARK 465 GLY J 247 REMARK 465 PRO J 248 REMARK 465 GLY J 249 REMARK 465 HIS J 250 REMARK 465 HIS J 251 REMARK 465 HIS J 252 REMARK 465 HIS J 253 REMARK 465 HIS J 254 REMARK 465 HIS J 255 REMARK 465 HIS J 256 REMARK 465 HIS J 257 REMARK 465 SER J 258 REMARK 465 ALA J 259 REMARK 465 TRP J 260 REMARK 465 SER J 261 REMARK 465 HIS J 262 REMARK 465 PRO J 263 REMARK 465 GLN J 264 REMARK 465 PHE J 265 REMARK 465 GLU J 266 REMARK 465 LYS J 267 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 LEU H 11 CD1 REMARK 470 GLU H 72 CD OE1 OE2 REMARK 470 SER H 127 CB OG REMARK 470 SER H 132 OG REMARK 470 LYS H 201 CE NZ REMARK 470 LYS H 206 CE NZ REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 LYS L 186 CG CD CE NZ REMARK 470 GLU L 210 CG CD OE1 OE2 REMARK 470 GLN A 171 CD OE1 NE2 REMARK 470 LYS A 201 CE NZ REMARK 470 LYS A 206 CE NZ REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 214 CG CD CE NZ REMARK 470 GLU B 210 CG CD OE1 OE2 REMARK 470 ASN G 135 CG OD1 ND2 REMARK 470 GLU G 152 CG CD OE1 OE2 REMARK 470 ASN G 195 CG OD1 ND2 REMARK 470 GLN J 133 CG CD OE1 NE2 REMARK 470 GLU J 152 CG CD OE1 OE2 REMARK 470 GLU J 153 CG CD OE1 OE2 REMARK 470 THR J 163 OG1 CG2 REMARK 470 GLU J 164 CG CD OE1 OE2 REMARK 470 ASP J 167 CG OD1 OD2 REMARK 470 ASN J 195 CG OD1 ND2 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 HB2 SER A 188 HG2 GLN A 192 1.24 REMARK 500 O HIS A 200 HG SER A 203 1.27 REMARK 500 HG CYS G 126 SG CYS G 196 1.33 REMARK 500 O PRO H 185 HG SER H 188 1.34 REMARK 500 HH TYR B 177 O HOH B 301 1.39 REMARK 500 HH TYR L 177 O HOH L 304 1.52 REMARK 500 OG1 THR L 181 H GLN L 184 1.53 REMARK 500 HG SER H 41 O HOH H 304 1.54 REMARK 500 HZ3 LYS L 110 O HOH L 309 1.54 REMARK 500 HE ARG L 54 O HOH L 310 1.55 REMARK 500 HH TYR H 91 O HOH H 305 1.56 REMARK 500 H SER A 156 OD1 ASN A 197 1.56 REMARK 500 O THR H 100B HH11 ARG L 34 1.57 REMARK 500 HH TYR L 172 O HOH L 306 1.59 REMARK 500 O HOH H 373 O HOH J 439 1.64 REMARK 500 O SER A 188 OE1 GLN A 192 1.66 REMARK 500 O HOH H 332 O HOH H 484 1.83 REMARK 500 O HOH A 1033 O HOH A 1036 1.84 REMARK 500 O HOH L 470 O HOH L 491 1.84 REMARK 500 O HOH L 397 O HOH L 501 1.84 REMARK 500 O HIS A 200 OG SER A 203 1.85 REMARK 500 O HOH A 1039 O HOH A 1052 1.88 REMARK 500 O HOH H 400 O HOH H 453 1.93 REMARK 500 OH TYR B 177 O HOH B 301 1.93 REMARK 500 OG SER H 161 O HOH H 301 1.93 REMARK 500 N VAL J 172 O HOH J 401 1.94 REMARK 500 OE1 GLN H 192 O HOH H 302 1.94 REMARK 500 O HOH L 486 O HOH J 428 1.95 REMARK 500 O HOH A 971 O HOH A 1034 1.95 REMARK 500 O HOH H 373 O HOH H 486 1.97 REMARK 500 O HOH H 481 O HOH L 394 1.98 REMARK 500 O HOH L 411 O HOH L 479 1.98 REMARK 500 O HOH L 316 O HOH L 529 2.01 REMARK 500 O HOH L 394 O HOH L 523 2.01 REMARK 500 O HOH A 1030 O HOH A 1066 2.01 REMARK 500 OE2 GLU L 123 O HOH L 301 2.03 REMARK 500 O HOH B 421 O HOH B 456 2.04 REMARK 500 O LEU L 180 O HOH L 302 2.05 REMARK 500 O PRO H 185 OG SER H 188 2.06 REMARK 500 NH2 ARG L 54 O HOH L 303 2.07 REMARK 500 O LYS A 143 O HOH A 901 2.09 REMARK 500 O HOH L 476 O HOH L 521 2.11 REMARK 500 OH TYR L 177 O HOH L 304 2.12 REMARK 500 O HOH L 548 O HOH L 566 2.13 REMARK 500 N TYR A 145 O HOH A 901 2.14 REMARK 500 O HOH A 978 O HOH G 444 2.15 REMARK 500 O HOH B 313 O HOH B 338 2.15 REMARK 500 O HOH H 444 O HOH H 477 2.16 REMARK 500 O HOH A 905 O HOH A 984 2.16 REMARK 500 O HOH L 468 O HOH L 564 2.16 REMARK 500 REMARK 500 THIS ENTRY HAS 55 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH H 447 O HOH L 422 4456 2.17 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 CYS H 196 CB CYS H 196 SG -0.098 REMARK 500 CYS A 140 CB CYS A 140 SG 0.130 REMARK 500 CYS A 140 CB CYS A 140 SG 0.132 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 ALA H 88 167.01 177.85 REMARK 500 ASP H 144 65.71 63.12 REMARK 500 ASP L 51 -48.58 73.47 REMARK 500 ASN L 52 17.48 -150.06 REMARK 500 SER L 90 -149.88 -150.45 REMARK 500 ARG L 107 19.53 -142.62 REMARK 500 ASP L 151 -111.84 56.72 REMARK 500 THR L 209 90.16 -67.03 REMARK 500 ALA A 88 165.48 178.70 REMARK 500 ASP A 144 68.07 60.59 REMARK 500 SER A 156 62.57 31.45 REMARK 500 ASN A 204 37.48 39.92 REMARK 500 ASP B 51 -47.97 73.44 REMARK 500 ASN B 52 16.27 -149.77 REMARK 500 SER B 90 -149.82 -147.29 REMARK 500 ASP B 92 -168.03 -110.03 REMARK 500 ASN J 195 2.96 -66.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 513 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH H 514 DISTANCE = 6.75 ANGSTROMS REMARK 525 HOH A1080 DISTANCE = 6.25 ANGSTROMS REMARK 525 HOH B 492 DISTANCE = 6.10 ANGSTROMS DBREF 6WAS H 1 215 PDB 6WAS 6WAS 1 215 DBREF 6WAS L 1 212 PDB 6WAS 6WAS 1 212 DBREF 6WAS A 1 215 PDB 6WAS 6WAS 1 215 DBREF 6WAS B 1 212 PDB 6WAS 6WAS 1 212 DBREF 6WAS G 118 267 PDB 6WAS 6WAS 118 267 DBREF 6WAS J 118 267 PDB 6WAS 6WAS 118 267 SEQRES 1 H 223 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 H 223 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 223 ILE THR PHE SER GLU ASP TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA SER GLY LYS GLY LEU GLU TRP VAL SER ARG ILE SER SEQRES 5 H 223 TYR ASP SER ASP ASN THR TRP TYR ALA ASP SER VAL LYS SEQRES 6 H 223 GLY ARG PHE THR ILE SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 H 223 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA ARG ALA PRO VAL TRP THR GLY SEQRES 9 H 223 TYR THR SER LEU ASP VAL TRP GLY ARG GLY VAL LEU VAL SEQRES 10 H 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 223 LYS SER SEQRES 1 L 217 PCA VAL VAL PHE SER GLN PRO HIS SER VAL SER GLY SER SEQRES 2 L 217 PRO GLY GLN THR VAL THR ILE SER CYS THR ARG SER SER SEQRES 3 L 217 GLY SER ILE ASP ASN GLU TYR VAL ARG TRP TYR GLN GLN SEQRES 4 L 217 ARG PRO GLY SER VAL PRO THR ILE VAL ILE TYR LYS ASP SEQRES 5 L 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 L 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU ALA ILE SEQRES 7 L 217 SER GLY LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 L 217 GLN SER SER ASP ASP ASN PHE ASN TRP VAL PHE GLY GLY SEQRES 9 L 217 GLY THR ARG LEU THR VAL LEU ARG GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 A 223 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 A 223 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 223 ILE THR PHE SER GLU ASP TYR MET HIS TRP VAL ARG GLN SEQRES 4 A 223 ALA SER GLY LYS GLY LEU GLU TRP VAL SER ARG ILE SER SEQRES 5 A 223 TYR ASP SER ASP ASN THR TRP TYR ALA ASP SER VAL LYS SEQRES 6 A 223 GLY ARG PHE THR ILE SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 A 223 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR SEQRES 8 A 223 ALA VAL TYR TYR CYS ALA ARG ALA PRO VAL TRP THR GLY SEQRES 9 A 223 TYR THR SER LEU ASP VAL TRP GLY ARG GLY VAL LEU VAL SEQRES 10 A 223 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 A 223 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 A 223 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 A 223 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 A 223 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 A 223 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 A 223 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 A 223 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 A 223 LYS SER SEQRES 1 B 217 PCA VAL VAL PHE SER GLN PRO HIS SER VAL SER GLY SER SEQRES 2 B 217 PRO GLY GLN THR VAL THR ILE SER CYS THR ARG SER SER SEQRES 3 B 217 GLY SER ILE ASP ASN GLU TYR VAL ARG TRP TYR GLN GLN SEQRES 4 B 217 ARG PRO GLY SER VAL PRO THR ILE VAL ILE TYR LYS ASP SEQRES 5 B 217 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 B 217 SER ILE ASP SER SER SER ASN SER ALA SER LEU ALA ILE SEQRES 7 B 217 SER GLY LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 B 217 GLN SER SER ASP ASP ASN PHE ASN TRP VAL PHE GLY GLY SEQRES 9 B 217 GLY THR ARG LEU THR VAL LEU ARG GLN PRO LYS ALA ALA SEQRES 10 B 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 B 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 B 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 B 217 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 B 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 B 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 B 217 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 B 217 LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 G 151 MET THR THR PHE LYS LEU ALA ALA CYS VAL THR LEU GLU SEQRES 2 G 151 CYS ARG GLN VAL ASN THR THR ASN ALA THR SER SER VAL SEQRES 3 G 151 ASN VAL THR ASN GLY GLU GLU ILE LYS ASN CYS SER PHE SEQRES 4 G 151 ASN ALA THR THR GLU ILE ARG ASP LYS LYS GLN LYS VAL SEQRES 5 G 151 TYR ALA LEU PHE TYR ARG LEU ASP ILE VAL PRO LEU GLU SEQRES 6 G 151 GLU GLU ARG LYS GLY ASN SER SER LYS TYR ARG LEU ILE SEQRES 7 G 151 ASN CYS GLN THR THR THR THR GLU ALA VAL ASP ALA ALA SEQRES 8 G 151 THR ALA ALA LYS VAL PHE LYS GLN TYR ALA ASN ASP ASN SEQRES 9 G 151 GLY ILE ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS SEQRES 10 G 151 THR PHE THR VAL THR GLU GLY LEU GLU VAL LEU PHE GLN SEQRES 11 G 151 GLY PRO GLY HIS HIS HIS HIS HIS HIS HIS HIS SER ALA SEQRES 12 G 151 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 J 151 MET THR THR PHE LYS LEU ALA ALA CYS VAL THR LEU GLU SEQRES 2 J 151 CYS ARG GLN VAL ASN THR THR ASN ALA THR SER SER VAL SEQRES 3 J 151 ASN VAL THR ASN GLY GLU GLU ILE LYS ASN CYS SER PHE SEQRES 4 J 151 ASN ALA THR THR GLU ILE ARG ASP LYS LYS GLN LYS VAL SEQRES 5 J 151 TYR ALA LEU PHE TYR ARG LEU ASP ILE VAL PRO LEU GLU SEQRES 6 J 151 GLU GLU ARG LYS GLY ASN SER SER LYS TYR ARG LEU ILE SEQRES 7 J 151 ASN CYS GLN THR THR THR THR GLU ALA VAL ASP ALA ALA SEQRES 8 J 151 THR ALA ALA LYS VAL PHE LYS GLN TYR ALA ASN ASP ASN SEQRES 9 J 151 GLY ILE ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS SEQRES 10 J 151 THR PHE THR VAL THR GLU GLY LEU GLU VAL LEU PHE GLN SEQRES 11 J 151 GLY PRO GLY HIS HIS HIS HIS HIS HIS HIS HIS SER ALA SEQRES 12 J 151 TRP SER HIS PRO GLN PHE GLU LYS HET PCA H 1 14 HET PCA L 1 14 HET PCA A 1 14 HET PCA B 1 14 HET NAG G 301 28 HET NAG G 302 28 HET NAG J 301 28 HET NAG J 302 28 HETNAM PCA PYROGLUTAMIC ACID 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 1 PCA 4(C5 H7 N O3) FORMUL 7 NAG 4(C8 H15 N O6) FORMUL 11 HOH *956(H2 O) HELIX 1 AA1 THR H 28 ASP H 32 5 5 HELIX 2 AA2 ASN H 73 LYS H 75 5 3 HELIX 3 AA3 ARG H 83 THR H 87 5 5 HELIX 4 AA4 PRO H 96 GLY H 100 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 SER L 27B GLU L 31 5 5 HELIX 8 AA8 SER L 66B SER L 68 5 3 HELIX 9 AA9 GLN L 79 GLU L 83 5 5 HELIX 10 AB1 SER L 121 ALA L 127 1 7 HELIX 11 AB2 THR L 181 SER L 187 1 7 HELIX 12 AB3 THR A 28 ASP A 32 5 5 HELIX 13 AB4 ASN A 73 LYS A 75 5 3 HELIX 14 AB5 ARG A 83 THR A 87 5 5 HELIX 15 AB6 PRO A 96 GLY A 100 5 5 HELIX 16 AB7 SER B 27B GLU B 31 5 5 HELIX 17 AB8 SER B 66B SER B 68 5 3 HELIX 18 AB9 GLN B 79 GLU B 83 5 5 HELIX 19 AC1 SER B 121 ALA B 127 1 7 HELIX 20 AC2 THR B 181 HIS B 188 1 8 SHEET 1 AA1 4 LEU H 4 GLY H 8 0 SHEET 2 AA1 4 LEU H 18 ALA H 24 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 GLU H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 6 GLY H 10 ALA H 12 0 SHEET 2 AA2 6 VAL H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA2 6 ALA H 88 ALA H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA2 6 TYR H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O TRP H 58 N ARG H 50 SHEET 1 AA3 4 GLY H 10 ALA H 12 0 SHEET 2 AA3 4 VAL H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA3 4 ALA H 88 ALA H 95 -1 N TYR H 90 O VAL H 107 SHEET 4 AA3 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 PHE L 4 SER L 5 0 SHEET 2 AA7 4 VAL L 19 ARG L 25 -1 O THR L 24 N SER L 5 SHEET 3 AA7 4 SER L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AA7 4 PHE L 62 ASP L 66A-1 N ASP L 66A O SER L 70 SHEET 1 AA8 5 SER L 9 GLY L 13 0 SHEET 2 AA8 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA8 5 ALA L 84 SER L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 5 ARG L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA8 5 THR L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 1 AA9 4 SER L 9 GLY L 13 0 SHEET 2 AA9 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA9 4 ALA L 84 SER L 91 -1 N ALA L 84 O LEU L 104 SHEET 4 AA9 4 TRP L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB1 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136 SHEET 4 AB1 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177 SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O ALA L 174 N ILE L 136 SHEET 4 AB2 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173 SHEET 1 AB3 4 SER L 153 VAL L 155 0 SHEET 2 AB3 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AB3 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147 SHEET 4 AB3 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195 SHEET 1 AB4 4 LEU A 4 SER A 7 0 SHEET 2 AB4 4 LEU A 18 ALA A 24 -1 O SER A 21 N SER A 7 SHEET 3 AB4 4 THR A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AB4 4 PHE A 67 GLU A 72 -1 N SER A 70 O TYR A 79 SHEET 1 AB5 6 GLY A 10 ALA A 12 0 SHEET 2 AB5 6 VAL A 107 VAL A 111 1 O THR A 110 N GLY A 10 SHEET 3 AB5 6 ALA A 88 ALA A 95 -1 N TYR A 90 O VAL A 107 SHEET 4 AB5 6 TYR A 33 GLN A 39 -1 N VAL A 37 O TYR A 91 SHEET 5 AB5 6 LEU A 45 ILE A 51 -1 O SER A 49 N TRP A 36 SHEET 6 AB5 6 THR A 57 TYR A 59 -1 O TRP A 58 N ARG A 50 SHEET 1 AB6 4 GLY A 10 ALA A 12 0 SHEET 2 AB6 4 VAL A 107 VAL A 111 1 O THR A 110 N GLY A 10 SHEET 3 AB6 4 ALA A 88 ALA A 95 -1 N TYR A 90 O VAL A 107 SHEET 4 AB6 4 VAL A 102 TRP A 103 -1 O VAL A 102 N ARG A 94 SHEET 1 AB7 4 SER A 120 SER A 127 0 SHEET 2 AB7 4 THR A 135 TYR A 145 -1 O ALA A 137 N SER A 127 SHEET 3 AB7 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AB7 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB8 4 SER A 120 SER A 127 0 SHEET 2 AB8 4 THR A 135 TYR A 145 -1 O ALA A 137 N SER A 127 SHEET 3 AB8 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AB8 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB9 3 THR A 151 TRP A 154 0 SHEET 2 AB9 3 TYR A 194 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB9 3 THR A 205 VAL A 211 -1 O VAL A 207 N VAL A 198 SHEET 1 AC1 4 PHE B 4 SER B 5 0 SHEET 2 AC1 4 VAL B 19 ARG B 25 -1 O THR B 24 N SER B 5 SHEET 3 AC1 4 SER B 70 ILE B 75 -1 O ILE B 75 N VAL B 19 SHEET 4 AC1 4 PHE B 62 ASP B 66A-1 N ASP B 66A O SER B 70 SHEET 1 AC2 5 SER B 9 GLY B 13 0 SHEET 2 AC2 5 THR B 102 VAL B 106 1 O ARG B 103 N VAL B 11 SHEET 3 AC2 5 ALA B 84 SER B 91 -1 N TYR B 86 O THR B 102 SHEET 4 AC2 5 ARG B 34 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AC2 5 THR B 45 ILE B 48 -1 O ILE B 48 N TRP B 35 SHEET 1 AC3 4 SER B 9 GLY B 13 0 SHEET 2 AC3 4 THR B 102 VAL B 106 1 O ARG B 103 N VAL B 11 SHEET 3 AC3 4 ALA B 84 SER B 91 -1 N TYR B 86 O THR B 102 SHEET 4 AC3 4 TRP B 96 PHE B 98 -1 O VAL B 97 N SER B 90 SHEET 1 AC4 4 SER B 114 PHE B 118 0 SHEET 2 AC4 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116 SHEET 3 AC4 4 TYR B 172 LEU B 180 -1 O ALA B 174 N ILE B 136 SHEET 4 AC4 4 VAL B 159 THR B 161 -1 N GLU B 160 O TYR B 177 SHEET 1 AC5 4 SER B 114 PHE B 118 0 SHEET 2 AC5 4 ALA B 130 PHE B 139 -1 O LEU B 135 N THR B 116 SHEET 3 AC5 4 TYR B 172 LEU B 180 -1 O ALA B 174 N ILE B 136 SHEET 4 AC5 4 SER B 165 LYS B 166 -1 N SER B 165 O ALA B 173 SHEET 1 AC6 4 SER B 153 VAL B 155 0 SHEET 2 AC6 4 THR B 145 ALA B 150 -1 N TRP B 148 O VAL B 155 SHEET 3 AC6 4 TYR B 191 HIS B 197 -1 O GLN B 194 N ALA B 147 SHEET 4 AC6 4 SER B 200 VAL B 206 -1 O VAL B 202 N VAL B 195 SHEET 1 AC7 5 ALA G 174 TYR G 177 0 SHEET 2 AC7 5 ILE G 154 SER G 158 -1 N CYS G 157 O ALA G 174 SHEET 3 AC7 5 THR G 128 ARG G 132 -1 N ARG G 132 O ASN G 156 SHEET 4 AC7 5 SER G 189 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 AC7 5 ILE G 181 PRO G 183 -1 N VAL G 182 O ARG G 192 SHEET 1 AC8 5 TYR J 173 TYR J 177 0 SHEET 2 AC8 5 ILE J 154 SER J 158 -1 N LYS J 155 O PHE J 176 SHEET 3 AC8 5 THR J 128 GLN J 133 -1 N ARG J 132 O ASN J 156 SHEET 4 AC8 5 SER J 189 LEU J 193 -1 O TYR J 191 N LEU J 129 SHEET 5 AC8 5 ILE J 181 PRO J 183 -1 N VAL J 182 O ARG J 192 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.06 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.13 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 4 CYS L 134 CYS L 193 1555 1555 2.04 SSBOND 5 CYS A 22 CYS A 92 1555 1555 1.95 SSBOND 6 CYS A 140 CYS A 196 1555 1555 1.92 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.06 SSBOND 8 CYS B 134 CYS B 193 1555 1555 2.04 SSBOND 9 CYS G 126 CYS G 196 1555 1555 2.06 SSBOND 10 CYS G 131 CYS G 157 1555 1555 2.07 SSBOND 11 CYS J 126 CYS J 196 1555 1555 2.08 SSBOND 12 CYS J 131 CYS J 157 1555 1555 2.06 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA L 1 N VAL L 2 1555 1555 1.33 LINK C PCA A 1 N VAL A 2 1555 1555 1.33 LINK C PCA B 1 N VAL B 2 1555 1555 1.33 LINK ND2 ASN G 156 C1 NAG G 301 1555 1555 1.45 LINK ND2 ASN G 187 C1 NAG G 302 1555 1555 1.44 LINK ND2 ASN J 156 C1 NAG J 301 1555 1555 1.45 LINK ND2 ASN J 187 C1 NAG J 302 1555 1555 1.44 CISPEP 1 PHE H 146 PRO H 147 0 -6.99 CISPEP 2 GLU H 148 PRO H 149 0 -0.16 CISPEP 3 TYR L 140 PRO L 141 0 -0.63 CISPEP 4 PHE A 146 PRO A 147 0 -7.93 CISPEP 5 GLU A 148 PRO A 149 0 0.32 CISPEP 6 TYR B 140 PRO B 141 0 -0.73 CRYST1 73.697 97.893 168.015 90.00 90.00 90.00 P 21 21 21 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 0.013569 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010215 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005952 0.00000