HEADER IMMUNE SYSTEM 06-AUG-23 8TQ6 TITLE CRYSTAL STRUCTURE OF FAB.B1.23.2 IN COMPLEX WITH MHC-I (HLA-B*44:05) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN B ALPHA CHAIN (HLA- COMPND 3 B*44:05); COMPND 4 CHAIN: A, C; COMPND 5 SYNONYM: MHC-I HLA-B44*05 A-CHAIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 9 CHAIN: B, D; COMPND 10 FRAGMENT: UNP RESIDUES 21-119; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: MHC CLASS II ANTIGEN PEPTIDE; COMPND 14 CHAIN: E, P; COMPND 15 FRAGMENT: HLA-DPA1*02:01 DERIVED PEPTIDE 77-85 (UNP RESIDUES 36-44); COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: FAB B1.23.2 HEAVY CHAIN; COMPND 18 CHAIN: F, H; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: FAB B1.23.2 LIGHT CHAIN; COMPND 22 CHAIN: G, L; COMPND 23 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: HLA-B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3A; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 21 ORGANISM_TAXID: 32630; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_COMMON: MOUSE; SOURCE 25 ORGANISM_TAXID: 10090; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1; SOURCE 32 MOL_ID: 5; SOURCE 33 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 34 ORGANISM_COMMON: MOUSE; SOURCE 35 ORGANISM_TAXID: 10090; SOURCE 36 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 37 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 39 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 40 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 41 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1 KEYWDS HISTOCOMPATIBILITY COMPLEX CLASS I, MHC-I, IMMUNE RESPONSE, IMMUNE KEYWDS 2 SYSTEM FAB, ANTIBODY, ANTI-MHC ANTIBODY, CANCER TUMOR, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.JIANG,K.NATARAJAN,L.F.BOYD,D.H.MARGULIES REVDAT 1 05-FEB-25 8TQ6 0 JRNL AUTH J.JIANG,K.NATARAJAN,L.F.BOYD,D.H.MARGULIES JRNL TITL CRYSTAL STRUCTURE OF FAB.B1.23.2 IN COMPLEX WITH MHC-I JRNL TITL 2 (HLA-B*44:05) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.21 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.680 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 31020 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.253 REMARK 3 R VALUE (WORKING SET) : 0.240 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 1612 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 72.2100 - 7.1200 0.92 2901 153 0.2339 0.2444 REMARK 3 2 7.1100 - 5.6500 0.91 2728 144 0.3034 0.3416 REMARK 3 3 5.6500 - 4.9300 0.91 2680 139 0.2574 0.2892 REMARK 3 4 4.9300 - 4.4800 0.91 2664 140 0.2215 0.2201 REMARK 3 5 4.4800 - 4.1600 0.92 2706 139 0.2262 0.2442 REMARK 3 6 4.1600 - 3.9200 0.92 2669 141 0.2426 0.2508 REMARK 3 7 3.9200 - 3.7200 0.91 2652 139 0.2470 0.3147 REMARK 3 8 3.7200 - 3.5600 0.91 2652 136 0.2484 0.3225 REMARK 3 9 3.5600 - 3.4200 0.91 2631 138 0.2588 0.3330 REMARK 3 10 3.4200 - 3.3000 0.90 2600 132 0.2773 0.3260 REMARK 3 11 3.3000 - 3.2000 0.90 2599 137 0.2966 0.3206 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.291 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 45.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.74 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 : 0.003 12834 REMARK 3 ANGLE : 0.720 17479 REMARK 3 CHIRALITY : 0.048 1901 REMARK 3 PLANARITY : 0.007 2263 REMARK 3 DIHEDRAL : 17.481 4575 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 : 5 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 43 or REMARK 3 resid 45 or resid 47 through 88 or (resid REMARK 3 89 through 90 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 91 through 107 or resid 109 through 110 REMARK 3 or resid 112 through 147 or resid 149 REMARK 3 through 175 or (resid 176 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 177 through 180 or (resid 181 REMARK 3 through 182 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 183 through 185 or resid 187 through 190 REMARK 3 or (resid 191 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 192 through 193 or (resid 194 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 195 or (resid 196 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 197 or (resid 198 through 199 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 200 through 201 REMARK 3 or (resid 202 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 203 through 211 or resid 213 through 218 REMARK 3 or resid 220 through 225 or resid 227 REMARK 3 through 233 or (resid 234 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 235 through 263 or resid 265 or REMARK 3 (resid 266 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 267 REMARK 3 through 268)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 43 or REMARK 3 resid 45 or resid 47 or (resid 48 through REMARK 3 49 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 50 through REMARK 3 107 or resid 109 through 110 or resid 112 REMARK 3 through 147 or resid 149 through 185 or REMARK 3 resid 187 through 211 or resid 213 REMARK 3 through 217 or (resid 218 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 220 through 225 or resid 227 REMARK 3 through 231 or (resid 232 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 233 through 259 or (resid 260 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 261 through 263 REMARK 3 or resid 265 through 268)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 0 through 1 or REMARK 3 (resid 2 through 3 and (name N or name CA REMARK 3 or name C or name O or name CB )) or REMARK 3 resid 4 through 5 or (resid 6 through 7 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 8 through 9 or REMARK 3 (resid 10 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 11 REMARK 3 through 26 or (resid 27 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 28 through 44 or resid 46 REMARK 3 through 74 or resid 76 through 99)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 0 through 44 or REMARK 3 resid 46 through 57 or (resid 58 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 59 through 74 or REMARK 3 resid 76 through 99)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 through 4 or REMARK 3 resid 6 through 9)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "P" and (resid 1 through 4 or REMARK 3 resid 6 through 7 or (resid 8 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 9)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_4 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 2 through 62 or REMARK 3 (resid 63 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 64 REMARK 3 through 173 or resid 175 through 213)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 2 through 12 or REMARK 3 (resid 13 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 14 REMARK 3 through 114 or (resid 115 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 116 through 129 or (resid 130 REMARK 3 through 131 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 132 through 173 or resid 175 through 213)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_5 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "G" and (resid 2 through 14 or REMARK 3 (resid 15 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 16 REMARK 3 through 36 or (resid 37 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 38 through 41 or resid 43 REMARK 3 through 52 or resid 54 through 80 or REMARK 3 resid 82 through 93 or resid 95 through REMARK 3 121 or resid 123 through 153 or (resid REMARK 3 154 through 155 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 156 through 158 or (resid 159 and (name N REMARK 3 or name CA or name C or name O or name CB REMARK 3 )) or resid 160 through 186 or resid 188 REMARK 3 through 193 or resid 195 through 210)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and ((resid 2 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 3 through 23 or (resid 24 REMARK 3 through 25 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 26 REMARK 3 through 28 or (resid 29 through 31 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 32 through 41 or REMARK 3 resid 43 through 52 or resid 54 through REMARK 3 80 or resid 82 through 93 or resid 95 REMARK 3 through 121 or resid 123 through 186 or REMARK 3 resid 188 through 193 or resid 195 REMARK 3 through 209 or (resid 210 and (name N or REMARK 3 name CA or name C or name O or name CB ))) REMARK 3 ) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8TQ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-23. REMARK 100 THE DEPOSITION ID IS D_1000276347. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-NOV-22 REMARK 200 TEMPERATURE (KELVIN) : 273 REMARK 200 PH : 8.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31179 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 72.210 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.32900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.35000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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 7TUE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG3350, 0.04 M SODIUM CITRATE, REMARK 280 0.06 M BIS-TRIS, PH 8.8, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K 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 44.75000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.90500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.42000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.90500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.75000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.42000 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, P 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: F, G REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 223.75000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 92.84000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -114.90500 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 PRO C 269 REMARK 465 LEU C 270 REMARK 465 THR C 271 REMARK 465 LEU C 272 REMARK 465 ARG C 273 REMARK 465 TRP C 274 REMARK 465 CYS G 213 REMARK 465 GLU L 212 REMARK 465 CYS L 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 ARG A 48 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 58 CG CD OE1 OE2 REMARK 470 GLN A 218 CG CD OE1 NE2 REMARK 470 GLU A 232 CG CD OE1 OE2 REMARK 470 HIS A 260 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 268 CG CD CE NZ REMARK 470 LEU A 272 CG CD1 CD2 REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2 REMARK 470 TRP A 274 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 274 CZ3 CH2 REMARK 470 MET B 0 CG SD CE REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 GLU C 58 CG CD OE1 OE2 REMARK 470 GLU C 89 CG CD OE1 OE2 REMARK 470 LYS C 176 CG CD CE NZ REMARK 470 ARG C 181 CG CD NE CZ NH1 NH2 REMARK 470 HIS C 191 CG ND1 CD2 CE1 NE2 REMARK 470 ILE C 194 CG1 CG2 CD1 REMARK 470 ASP C 196 CG OD1 OD2 REMARK 470 GLU C 198 CG CD OE1 OE2 REMARK 470 VAL C 199 CG1 CG2 REMARK 470 ARG C 202 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 234 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 266 CG CD1 CD2 REMARK 470 LYS C 268 CG CD CE NZ REMARK 470 MET D 0 CG SD CE REMARK 470 GLN D 2 CG CD OE1 NE2 REMARK 470 ARG D 3 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 6 CG CD CE NZ REMARK 470 ILE D 7 CG1 CG2 CD1 REMARK 470 TYR D 10 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL D 27 CG1 CG2 REMARK 470 GLU D 44 CG CD OE1 OE2 REMARK 470 SER E 8 OG REMARK 470 GLN F 3 CG CD OE1 NE2 REMARK 470 ARG F 13 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 115 CG CD CE NZ REMARK 470 ASP F 130 CG OD1 OD2 REMARK 470 THR F 131 OG1 CG2 REMARK 470 LYS F 209 CG CD CE NZ REMARK 470 THR G 2 OG1 CG2 REMARK 470 LYS G 24 CG CD CE NZ REMARK 470 ILE G 29 CG1 CG2 CD1 REMARK 470 ASN G 30 CG OD1 ND2 REMARK 470 SER G 31 OG REMARK 470 GLU G 93 CG CD OE1 OE2 REMARK 470 ARG G 210 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 LYS H 63 CG CD CE NZ REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 LEU L 15 CG CD1 CD2 REMARK 470 GLN L 37 CG CD OE1 NE2 REMARK 470 GLU L 93 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 LEU L 159 CG CD1 CD2 REMARK 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY. REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 ILE C 194 REMARK 475 GLY F 129 REMARK 475 THR F 131 REMARK 475 GLY H 129 REMARK 475 THR H 131 REMARK 475 GLY H 133 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLU C 198 CA O REMARK 480 VAL C 199 N CA C CB REMARK 480 ASP F 130 N CA C CB REMARK 480 CYS H 128 CA C O CB SG REMARK 480 ASP H 130 N CA C O CB REMARK 480 THR H 132 N CA C O REMARK 480 GLU P 1 N 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 ASP A 29 -129.24 57.33 REMARK 500 ASP A 39 49.27 -96.30 REMARK 500 PRO A 43 109.14 -54.32 REMARK 500 ARG A 48 25.65 -141.64 REMARK 500 LEU A 110 -63.62 -109.68 REMARK 500 TYR A 123 -63.17 -105.29 REMARK 500 SER A 131 -28.68 -146.49 REMARK 500 PRO A 210 -163.13 -77.21 REMARK 500 ASP A 220 25.41 48.70 REMARK 500 GLN A 224 71.26 -116.44 REMARK 500 GLU A 253 32.00 -85.00 REMARK 500 ARG A 273 90.31 -172.07 REMARK 500 ILE B 1 94.87 59.52 REMARK 500 ARG B 12 -75.42 -69.63 REMARK 500 PRO B 32 -163.20 -66.90 REMARK 500 SER B 57 -164.77 -124.90 REMARK 500 ASP C 29 -129.60 56.93 REMARK 500 ASP C 39 46.79 -92.47 REMARK 500 PRO C 43 93.61 -57.40 REMARK 500 ARG C 48 22.83 -142.86 REMARK 500 TYR C 123 -63.08 -107.83 REMARK 500 SER C 131 -29.63 -145.93 REMARK 500 PRO C 210 -163.12 -75.39 REMARK 500 GLN C 224 72.97 -109.34 REMARK 500 ASP C 227 31.02 -92.15 REMARK 500 GLU C 253 30.18 -85.42 REMARK 500 ILE D 1 76.01 57.51 REMARK 500 ARG D 12 -76.26 -69.01 REMARK 500 PRO D 32 -164.77 -67.17 REMARK 500 SER D 57 -162.96 -124.67 REMARK 500 THR F 30 59.72 -101.90 REMARK 500 SER F 31 -0.38 -159.61 REMARK 500 ILE F 48 -63.87 -99.12 REMARK 500 ASN F 55 6.95 -156.85 REMARK 500 TYR F 99 39.68 39.99 REMARK 500 PHE F 146 141.21 -170.18 REMARK 500 PRO F 147 -127.88 -77.80 REMARK 500 SER F 172 77.67 60.67 REMARK 500 ASP F 173 -35.11 73.16 REMARK 500 SER F 185 63.96 -58.48 REMARK 500 SER F 186 -18.01 -163.84 REMARK 500 ALA F 213 -166.77 -126.28 REMARK 500 ALA G 51 -22.98 66.61 REMARK 500 ASN G 52 25.95 -150.61 REMARK 500 VAL G 58 133.34 62.73 REMARK 500 GLU G 81 11.68 -69.76 REMARK 500 GLU G 93 87.29 62.73 REMARK 500 LEU G 94 163.58 67.86 REMARK 500 ALA G 129 105.37 -162.37 REMARK 500 ASN G 137 91.38 31.59 REMARK 500 REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8TQ4 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ5 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ7 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ8 RELATED DB: PDB REMARK 900 RELATED ID: 8TQ9 RELATED DB: PDB REMARK 900 RELATED ID: 8TQA RELATED DB: PDB DBREF 8TQ6 A 2 274 UNP Q860B7 Q860B7_HUMAN 1 273 DBREF 8TQ6 B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 8TQ6 C 2 274 UNP Q860B7 Q860B7_HUMAN 1 273 DBREF 8TQ6 D 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 8TQ6 E 1 9 UNP Q9TQB0 Q9TQB0_HUMAN 36 44 DBREF 8TQ6 F 2 214 PDB 8TQ6 8TQ6 2 214 DBREF 8TQ6 G 2 213 PDB 8TQ6 8TQ6 2 213 DBREF 8TQ6 H 2 214 PDB 8TQ6 8TQ6 2 214 DBREF 8TQ6 L 2 213 PDB 8TQ6 8TQ6 2 213 DBREF 8TQ6 P 1 9 UNP Q9TQB0 Q9TQB0_HUMAN 36 44 SEQADV 8TQ6 GLY A 1 UNP Q860B7 EXPRESSION TAG SEQADV 8TQ6 MET B 0 UNP P61769 INITIATING METHIONINE SEQADV 8TQ6 GLY C 1 UNP Q860B7 EXPRESSION TAG SEQADV 8TQ6 MET D 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 274 GLY SER HIS SER MET ARG TYR PHE TYR THR ALA MET SER SEQRES 2 A 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE THR VAL GLY SEQRES 3 A 274 TYR VAL ASP ASP THR LEU PHE VAL ARG PHE ASP SER ASP SEQRES 4 A 274 ALA THR SER PRO ARG LYS GLU PRO ARG ALA PRO TRP ILE SEQRES 5 A 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR GLN SEQRES 6 A 274 ILE SER LYS THR ASN THR GLN THR TYR ARG GLU ASN LEU SEQRES 7 A 274 ARG THR ALA LEU ARG TYR TYR ASN GLN SER GLU ALA GLY SEQRES 8 A 274 SER HIS ILE ILE GLN ARG MET TYR GLY CYS ASP VAL GLY SEQRES 9 A 274 PRO ASP GLY ARG LEU LEU ARG GLY TYR ASP GLN TYR ALA SEQRES 10 A 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU SEQRES 11 A 274 SER SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR SEQRES 12 A 274 GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN ASP SEQRES 13 A 274 ARG ALA TYR LEU GLU GLY LEU CYS VAL GLU SER LEU ARG SEQRES 14 A 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG ALA SEQRES 15 A 274 ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER SEQRES 16 A 274 ASP HIS GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE SEQRES 17 A 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY SEQRES 18 A 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG SEQRES 19 A 274 PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL SEQRES 20 A 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS SEQRES 21 A 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG SEQRES 22 A 274 TRP SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 C 274 GLY SER HIS SER MET ARG TYR PHE TYR THR ALA MET SER SEQRES 2 C 274 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE THR VAL GLY SEQRES 3 C 274 TYR VAL ASP ASP THR LEU PHE VAL ARG PHE ASP SER ASP SEQRES 4 C 274 ALA THR SER PRO ARG LYS GLU PRO ARG ALA PRO TRP ILE SEQRES 5 C 274 GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG GLU THR GLN SEQRES 6 C 274 ILE SER LYS THR ASN THR GLN THR TYR ARG GLU ASN LEU SEQRES 7 C 274 ARG THR ALA LEU ARG TYR TYR ASN GLN SER GLU ALA GLY SEQRES 8 C 274 SER HIS ILE ILE GLN ARG MET TYR GLY CYS ASP VAL GLY SEQRES 9 C 274 PRO ASP GLY ARG LEU LEU ARG GLY TYR ASP GLN TYR ALA SEQRES 10 C 274 TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU SEQRES 11 C 274 SER SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR SEQRES 12 C 274 GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN ASP SEQRES 13 C 274 ARG ALA TYR LEU GLU GLY LEU CYS VAL GLU SER LEU ARG SEQRES 14 C 274 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG ALA SEQRES 15 C 274 ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER SEQRES 16 C 274 ASP HIS GLU VAL THR LEU ARG CYS TRP ALA LEU GLY PHE SEQRES 17 C 274 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY SEQRES 18 C 274 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG SEQRES 19 C 274 PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL SEQRES 20 C 274 VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS SEQRES 21 C 274 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG SEQRES 22 C 274 TRP SEQRES 1 D 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 E 9 GLU GLU PHE GLY ARG ALA PHE SER PHE SEQRES 1 F 213 VAL GLN LEU GLU GLN SER GLY THR VAL LEU ALA ARG PRO SEQRES 2 F 213 GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY TYR SEQRES 3 F 213 SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN ARG SEQRES 4 F 213 PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR PRO SEQRES 5 F 213 GLY ASN SER ASP ALA THR TYR ASN GLN LYS PHE LYS GLY SEQRES 6 F 213 LYS ALA LYS LEU THR ALA VAL THR SER ALA ASN THR ALA SEQRES 7 F 213 TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER ALA SEQRES 8 F 213 VAL TYR TYR CYS THR ASN TYR PHE ASP GLN TRP GLY GLN SEQRES 9 F 213 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR ALA SEQRES 10 F 213 PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SEQRES 11 F 213 THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY SEQRES 12 F 213 TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SEQRES 13 F 213 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 14 F 213 GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL SEQRES 15 F 213 THR SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN SEQRES 16 F 213 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS SEQRES 17 F 213 ILE GLU PRO ALA ALA SEQRES 1 G 212 THR THR VAL THR GLN THR PRO SER SER MET TYR ALA SER SEQRES 2 G 212 LEU GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER GLN SEQRES 3 G 212 ASP ILE ASN SER TYR LEU ASN TRP PHE GLN LEU LYS PRO SEQRES 4 G 212 GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN ARG SEQRES 5 G 212 LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 G 212 SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU GLU SEQRES 7 G 212 TYR GLU ASP MET GLY ILE TYR TYR CYS LEU GLN TYR ASP SEQRES 8 G 212 GLU LEU TYR THR PHE GLY GLY GLY THR LYS LEU GLU MET SEQRES 9 G 212 LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO SEQRES 10 G 212 PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL SEQRES 11 G 212 VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN SEQRES 12 G 212 VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY SEQRES 13 G 212 VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER SEQRES 14 G 212 THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP SEQRES 15 G 212 GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR SEQRES 16 G 212 HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN SEQRES 17 G 212 ARG ASN GLU CYS SEQRES 1 H 213 VAL GLN LEU GLU GLN SER GLY THR VAL LEU ALA ARG PRO SEQRES 2 H 213 GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY TYR SEQRES 3 H 213 SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN ARG SEQRES 4 H 213 PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR PRO SEQRES 5 H 213 GLY ASN SER ASP ALA THR TYR ASN GLN LYS PHE LYS GLY SEQRES 6 H 213 LYS ALA LYS LEU THR ALA VAL THR SER ALA ASN THR ALA SEQRES 7 H 213 TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER ALA SEQRES 8 H 213 VAL TYR TYR CYS THR ASN TYR PHE ASP GLN TRP GLY GLN SEQRES 9 H 213 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR ALA SEQRES 10 H 213 PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SEQRES 11 H 213 THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY SEQRES 12 H 213 TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SEQRES 13 H 213 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 14 H 213 GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL SEQRES 15 H 213 THR SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN SEQRES 16 H 213 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS SEQRES 17 H 213 ILE GLU PRO ALA ALA SEQRES 1 L 212 THR THR VAL THR GLN THR PRO SER SER MET TYR ALA SER SEQRES 2 L 212 LEU GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER GLN SEQRES 3 L 212 ASP ILE ASN SER TYR LEU ASN TRP PHE GLN LEU LYS PRO SEQRES 4 L 212 GLY LYS SER PRO LYS THR LEU ILE TYR ARG ALA ASN ARG SEQRES 5 L 212 LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 6 L 212 SER GLY GLN ASP TYR SER LEU THR ILE SER SER LEU GLU SEQRES 7 L 212 TYR GLU ASP MET GLY ILE TYR TYR CYS LEU GLN TYR ASP SEQRES 8 L 212 GLU LEU TYR THR PHE GLY GLY GLY THR LYS LEU GLU MET SEQRES 9 L 212 LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO SEQRES 10 L 212 PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL SEQRES 11 L 212 VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN SEQRES 12 L 212 VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY SEQRES 13 L 212 VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER SEQRES 14 L 212 THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP SEQRES 15 L 212 GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR SEQRES 16 L 212 HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN SEQRES 17 L 212 ARG ASN GLU CYS SEQRES 1 P 9 GLU GLU PHE GLY ARG ALA PHE SER PHE HELIX 1 AA1 GLY A 56 ASN A 86 1 31 HELIX 2 AA2 ALA A 139 ALA A 149 1 11 HELIX 3 AA3 ARG A 151 GLY A 162 1 12 HELIX 4 AA4 GLY A 162 GLY A 175 1 14 HELIX 5 AA5 GLY C 56 ASN C 86 1 31 HELIX 6 AA6 ALA C 139 ALA C 149 1 11 HELIX 7 AA7 ARG C 151 GLY C 162 1 12 HELIX 8 AA8 GLY C 162 GLY C 175 1 14 HELIX 9 AA9 SER F 28 TYR F 32 5 5 HELIX 10 AB1 THR F 87 SER F 91 5 5 HELIX 11 AB2 PRO F 126 ASP F 130 5 5 HELIX 12 AB3 SER F 156 SER F 158 5 3 HELIX 13 AB4 GLU G 79 MET G 83 5 5 HELIX 14 AB5 SER G 120 THR G 125 1 6 HELIX 15 AB6 LYS G 182 GLU G 186 1 5 HELIX 16 AB7 SER H 28 TYR H 32 5 5 HELIX 17 AB8 THR H 87 SER H 91 5 5 HELIX 18 AB9 PRO H 126 ASP H 130 5 5 HELIX 19 AC1 SER H 156 SER H 158 5 3 HELIX 20 AC2 GLU L 79 MET L 83 5 5 HELIX 21 AC3 SER L 120 SER L 126 1 7 HELIX 22 AC4 LYS L 182 ARG L 187 1 6 SHEET 1 AA1 8 GLU A 46 PRO A 47 0 SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31 SHEET 4 AA1 8 HIS A 3 MET A 12 -1 N ARG A 6 O TYR A 27 SHEET 5 AA1 8 ILE A 94 VAL A 103 -1 O VAL A 103 N HIS A 3 SHEET 6 AA1 8 LEU A 109 TYR A 118 -1 O GLN A 115 N MET A 98 SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O ILE A 124 N TYR A 116 SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125 SHEET 1 AA2 4 LYS A 186 PRO A 193 0 SHEET 2 AA2 4 VAL A 199 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA2 4 PHE A 241 VAL A 249 -1 O VAL A 249 N VAL A 199 SHEET 4 AA2 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 AA3 4 LYS A 186 PRO A 193 0 SHEET 2 AA3 4 VAL A 199 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA3 4 PHE A 241 VAL A 249 -1 O VAL A 249 N VAL A 199 SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 AA4 4 GLU A 222 ASP A 223 0 SHEET 2 AA4 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222 SHEET 3 AA4 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216 SHEET 4 AA4 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259 SHEET 1 AA5 4 LYS B 6 SER B 11 0 SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21 SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AA6 4 LYS B 6 SER B 11 0 SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21 SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AA7 4 GLU B 44 ARG B 45 0 SHEET 2 AA7 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AA7 4 TYR B 78 HIS B 84 -1 O ASN B 83 N GLU B 36 SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 AA8 8 GLU C 46 PRO C 47 0 SHEET 2 AA8 8 THR C 31 ASP C 37 -1 N ARG C 35 O GLU C 46 SHEET 3 AA8 8 ARG C 21 VAL C 28 -1 N VAL C 28 O THR C 31 SHEET 4 AA8 8 HIS C 3 MET C 12 -1 N ARG C 6 O TYR C 27 SHEET 5 AA8 8 ILE C 94 VAL C 103 -1 O ARG C 97 N TYR C 9 SHEET 6 AA8 8 LEU C 109 TYR C 118 -1 O GLN C 115 N MET C 98 SHEET 7 AA8 8 LYS C 121 LEU C 126 -1 O ILE C 124 N TYR C 116 SHEET 8 AA8 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125 SHEET 1 AA9 4 LYS C 186 PRO C 193 0 SHEET 2 AA9 4 GLU C 198 PHE C 208 -1 O TRP C 204 N HIS C 188 SHEET 3 AA9 4 PHE C 241 PRO C 250 -1 O VAL C 249 N VAL C 199 SHEET 4 AA9 4 GLU C 229 LEU C 230 -1 N GLU C 229 O ALA C 246 SHEET 1 AB1 4 LYS C 186 PRO C 193 0 SHEET 2 AB1 4 GLU C 198 PHE C 208 -1 O TRP C 204 N HIS C 188 SHEET 3 AB1 4 PHE C 241 PRO C 250 -1 O VAL C 249 N VAL C 199 SHEET 4 AB1 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242 SHEET 1 AB2 3 GLU C 222 ASP C 223 0 SHEET 2 AB2 3 ILE C 213 ARG C 219 -1 N ARG C 219 O GLU C 222 SHEET 3 AB2 3 TYR C 257 HIS C 263 -1 O THR C 258 N GLN C 218 SHEET 1 AB3 4 LYS D 6 SER D 11 0 SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O SER D 28 N LYS D 6 SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O PHE D 70 N ASN D 21 SHEET 4 AB3 4 GLU D 50 HIS D 51 -1 N GLU D 50 O TYR D 67 SHEET 1 AB4 4 LYS D 6 SER D 11 0 SHEET 2 AB4 4 ASN D 21 PHE D 30 -1 O SER D 28 N LYS D 6 SHEET 3 AB4 4 PHE D 62 PHE D 70 -1 O PHE D 70 N ASN D 21 SHEET 4 AB4 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63 SHEET 1 AB5 4 GLU D 44 ARG D 45 0 SHEET 2 AB5 4 ILE D 35 LYS D 41 -1 N LYS D 41 O GLU D 44 SHEET 3 AB5 4 TYR D 78 HIS D 84 -1 O ARG D 81 N ASP D 38 SHEET 4 AB5 4 LYS D 91 LYS D 94 -1 O LYS D 91 N VAL D 82 SHEET 1 AB6 2 LEU F 4 GLN F 6 0 SHEET 2 AB6 2 CYS F 22 ALA F 24 -1 O LYS F 23 N GLU F 5 SHEET 1 AB7 6 VAL F 10 ALA F 12 0 SHEET 2 AB7 6 THR F 107 VAL F 111 1 O THR F 108 N VAL F 10 SHEET 3 AB7 6 ALA F 92 ASN F 98 -1 N TYR F 94 O THR F 107 SHEET 4 AB7 6 MET F 34 GLN F 39 -1 N VAL F 37 O TYR F 95 SHEET 5 AB7 6 LEU F 45 TYR F 52 -1 O GLU F 46 N LYS F 38 SHEET 6 AB7 6 ASP F 57 TYR F 60 -1 O THR F 59 N ALA F 50 SHEET 1 AB8 3 VAL F 18 MET F 20 0 SHEET 2 AB8 3 THR F 78 LEU F 83 -1 O MET F 81 N MET F 20 SHEET 3 AB8 3 ALA F 68 VAL F 73 -1 N VAL F 73 O THR F 78 SHEET 1 AB9 4 SER F 120 LEU F 124 0 SHEET 2 AB9 4 SER F 135 TYR F 145 -1 O LYS F 143 N SER F 120 SHEET 3 AB9 4 LEU F 174 THR F 184 -1 O LEU F 177 N VAL F 142 SHEET 4 AB9 4 VAL F 163 GLN F 171 -1 N GLN F 171 O LEU F 174 SHEET 1 AC1 3 THR F 151 TRP F 154 0 SHEET 2 AC1 3 ILE F 193 HIS F 199 -1 O ALA F 198 N THR F 151 SHEET 3 AC1 3 THR F 204 ILE F 210 -1 O LYS F 208 N CYS F 195 SHEET 1 AC2 4 VAL G 4 THR G 7 0 SHEET 2 AC2 4 VAL G 19 ALA G 25 -1 O LYS G 24 N THR G 5 SHEET 3 AC2 4 ASP G 70 ILE G 75 -1 O LEU G 73 N ILE G 21 SHEET 4 AC2 4 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AC3 6 SER G 10 ALA G 13 0 SHEET 2 AC3 6 THR G 101 MET G 105 1 O LYS G 102 N MET G 11 SHEET 3 AC3 6 GLY G 84 GLN G 90 -1 N GLY G 84 O LEU G 103 SHEET 4 AC3 6 LEU G 33 LEU G 38 -1 N PHE G 36 O TYR G 87 SHEET 5 AC3 6 LYS G 45 TYR G 49 -1 O LYS G 45 N GLN G 37 SHEET 6 AC3 6 ARG G 53 LEU G 54 -1 O ARG G 53 N TYR G 49 SHEET 1 AC4 4 SER G 10 ALA G 13 0 SHEET 2 AC4 4 THR G 101 MET G 105 1 O LYS G 102 N MET G 11 SHEET 3 AC4 4 GLY G 84 GLN G 90 -1 N GLY G 84 O LEU G 103 SHEET 4 AC4 4 THR G 96 PHE G 97 -1 O THR G 96 N GLN G 90 SHEET 1 AC5 4 THR G 113 PHE G 117 0 SHEET 2 AC5 4 GLY G 128 PHE G 138 -1 O PHE G 134 N SER G 115 SHEET 3 AC5 4 TYR G 172 THR G 181 -1 O TYR G 172 N PHE G 138 SHEET 4 AC5 4 VAL G 158 TRP G 162 -1 N LEU G 159 O THR G 177 SHEET 1 AC6 4 SER G 152 ARG G 154 0 SHEET 2 AC6 4 ASN G 144 ILE G 149 -1 N ILE G 149 O SER G 152 SHEET 3 AC6 4 TYR G 191 THR G 196 -1 O THR G 196 N ASN G 144 SHEET 4 AC6 4 ILE G 204 PHE G 208 -1 O ILE G 204 N ALA G 195 SHEET 1 AC7 2 LEU H 4 GLN H 6 0 SHEET 2 AC7 2 CYS H 22 ALA H 24 -1 O LYS H 23 N GLU H 5 SHEET 1 AC8 6 VAL H 10 ALA H 12 0 SHEET 2 AC8 6 THR H 107 VAL H 111 1 O THR H 108 N VAL H 10 SHEET 3 AC8 6 ALA H 92 ASN H 98 -1 N TYR H 94 O THR H 107 SHEET 4 AC8 6 MET H 34 GLN H 39 -1 N HIS H 35 O THR H 97 SHEET 5 AC8 6 LEU H 45 TYR H 52 -1 O GLU H 46 N LYS H 38 SHEET 6 AC8 6 ASP H 57 TYR H 60 -1 O THR H 59 N ALA H 50 SHEET 1 AC9 3 VAL H 18 MET H 20 0 SHEET 2 AC9 3 THR H 78 LEU H 83 -1 O MET H 81 N MET H 20 SHEET 3 AC9 3 ALA H 68 VAL H 73 -1 N VAL H 73 O THR H 78 SHEET 1 AD1 4 SER H 120 LEU H 124 0 SHEET 2 AD1 4 VAL H 136 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AD1 4 LEU H 174 VAL H 183 -1 O VAL H 183 N VAL H 136 SHEET 4 AD1 4 HIS H 164 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 AD2 3 THR H 151 TRP H 154 0 SHEET 2 AD2 3 THR H 194 HIS H 199 -1 O ALA H 198 N THR H 151 SHEET 3 AD2 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 AD3 4 VAL L 4 THR L 7 0 SHEET 2 AD3 4 VAL L 19 ALA L 25 -1 O THR L 22 N THR L 7 SHEET 3 AD3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AD3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AD4 6 SER L 10 ALA L 13 0 SHEET 2 AD4 6 THR L 101 MET L 105 1 O GLU L 104 N ALA L 13 SHEET 3 AD4 6 ILE L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AD4 6 LEU L 33 LEU L 38 -1 N LEU L 38 O ILE L 85 SHEET 5 AD4 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AD4 6 ARG L 53 LEU L 54 -1 O ARG L 53 N TYR L 49 SHEET 1 AD5 4 SER L 10 ALA L 13 0 SHEET 2 AD5 4 THR L 101 MET L 105 1 O GLU L 104 N ALA L 13 SHEET 3 AD5 4 ILE L 85 GLN L 90 -1 N TYR L 86 O THR L 101 SHEET 4 AD5 4 THR L 96 PHE L 97 -1 O THR L 96 N GLN L 90 SHEET 1 AD6 4 THR L 113 PHE L 117 0 SHEET 2 AD6 4 GLY L 128 PHE L 138 -1 O PHE L 134 N SER L 115 SHEET 3 AD6 4 TYR L 172 THR L 181 -1 O MET L 174 N LEU L 135 SHEET 4 AD6 4 VAL L 158 TRP L 162 -1 N SER L 161 O SER L 175 SHEET 1 AD7 4 SER L 152 ARG L 154 0 SHEET 2 AD7 4 ILE L 143 ILE L 149 -1 N ILE L 149 O SER L 152 SHEET 3 AD7 4 TYR L 191 HIS L 197 -1 O THR L 196 N ASN L 144 SHEET 4 AD7 4 ILE L 204 PHE L 208 -1 O PHE L 208 N TYR L 191 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.02 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04 SSBOND 4 CYS C 101 CYS C 164 1555 1555 2.04 SSBOND 5 CYS C 203 CYS C 259 1555 1555 2.03 SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.04 SSBOND 7 CYS F 22 CYS F 96 1555 1555 2.03 SSBOND 8 CYS F 140 CYS F 195 1555 1555 2.04 SSBOND 9 CYS G 23 CYS G 88 1555 1555 2.02 SSBOND 10 CYS G 133 CYS G 193 1555 1555 2.03 SSBOND 11 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 12 CYS H 140 CYS H 195 1555 1555 2.04 SSBOND 13 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 14 CYS L 133 CYS L 193 1555 1555 2.04 CISPEP 1 TYR A 209 PRO A 210 0 -1.07 CISPEP 2 HIS B 31 PRO B 32 0 -0.60 CISPEP 3 TYR C 209 PRO C 210 0 -0.50 CISPEP 4 HIS D 31 PRO D 32 0 0.21 CISPEP 5 PHE F 146 PRO F 147 0 -1.72 CISPEP 6 GLU F 148 PRO F 149 0 2.94 CISPEP 7 TRP F 188 PRO F 189 0 -0.60 CISPEP 8 THR G 7 PRO G 8 0 -5.37 CISPEP 9 TYR G 139 PRO G 140 0 3.41 CISPEP 10 PHE H 146 PRO H 147 0 -1.89 CISPEP 11 GLU H 148 PRO H 149 0 2.78 CISPEP 12 TRP H 188 PRO H 189 0 0.59 CISPEP 13 THR L 7 PRO L 8 0 -4.72 CISPEP 14 TYR L 139 PRO L 140 0 3.26 CRYST1 89.500 92.840 229.810 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 0.011173 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010771 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004351 0.00000 MTRIX1 1 0.786625 -0.148375 -0.599338 88.01785 1 MTRIX2 1 0.182954 0.983116 -0.003260 -4.12709 1 MTRIX3 1 0.589702 -0.107087 0.800490 -95.93693 1 MTRIX1 2 0.819067 -0.124727 -0.559975 82.32322 1 MTRIX2 2 0.161495 0.986737 0.016435 -4.33191 1 MTRIX3 2 0.550498 -0.103895 0.828346 -95.38500 1 MTRIX1 3 0.754196 0.073067 0.652572 -3.12878 1 MTRIX2 3 -0.098824 0.995101 0.002795 4.38355 1 MTRIX3 3 -0.649171 -0.066597 0.757722 135.99665 1 MTRIX1 4 -0.764532 -0.179992 0.618946 106.39510 1 MTRIX2 4 0.146147 -0.983619 -0.105519 77.45790 1 MTRIX3 4 0.627800 0.009785 0.778314 -98.92907 1 MTRIX1 5 -0.780181 -0.151979 0.606812 108.03735 1 MTRIX2 5 0.136384 -0.988028 -0.072107 76.39347 1 MTRIX3 5 0.610506 0.026503 0.791568 -98.34364 1