HEADER IMMUNE SYSTEM 19-JUN-24 9II9 TITLE CRYSTAL STRUCTURE OF SARS-COV-2 NEUTRALIZING ANTIBODY K4-66 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIGEN-BINDING FRAGMENTS (FABS); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: MISSING RESIDUES OF CHAIN C WERE NOT MODELED DUE TO COMPND 6 WEAK ELECTRON DENSITY.; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ANTIGEN-BINDING FRAGMENTS (FABS); COMPND 9 CHAIN: B, D; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: C-TERMINAL REGION OF CHAIN B WERE NOT MODELED DUE TO COMPND 12 WEAK ELECTRON DENSITY. MISSING RESIDUES OF CHAIN D WERE NOT MODELED COMPND 13 DUE TO WEAK ELECTRON DENSITY. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIGEN-BINDING FRAGMENTS (FABS), IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.K.KIMURA,T.HASHIGUCHI REVDAT 1 06-NOV-24 9II9 0 JRNL AUTH T.K.KIMURA,T.HASHIGUCHI JRNL TITL INDUCTION OF IGHV3-53 PUBLIC ANTIBODIES WITH BROADLY JRNL TITL 2 NEUTRALIZING ACTIVITY AGAINST SARS-COV-2 INCLUDING OMICRON JRNL TITL 3 SUBVARIANTS IN A DELTA BREAKTHROUGH INFECTION CASE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.90 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.41 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 38453 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.264 REMARK 3 R VALUE (WORKING SET) : 0.262 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180 REMARK 3 FREE R VALUE TEST SET COUNT : 1992 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 49.4100 - 6.9800 1.00 2813 143 0.2516 0.2154 REMARK 3 2 6.9800 - 5.5500 1.00 2684 134 0.2849 0.3005 REMARK 3 3 5.5500 - 4.8500 1.00 2636 141 0.2325 0.2806 REMARK 3 4 4.8400 - 4.4000 1.00 2618 145 0.2173 0.2512 REMARK 3 5 4.4000 - 4.0900 1.00 2588 148 0.2222 0.2557 REMARK 3 6 4.0900 - 3.8500 1.00 2624 123 0.2493 0.2918 REMARK 3 7 3.8500 - 3.6500 1.00 2587 139 0.2485 0.2971 REMARK 3 8 3.6500 - 3.4900 1.00 2576 145 0.3064 0.3487 REMARK 3 9 3.4900 - 3.3600 1.00 2543 148 0.2945 0.3112 REMARK 3 10 3.3600 - 3.2400 1.00 2591 135 0.2948 0.3525 REMARK 3 11 3.2400 - 3.1400 1.00 2538 138 0.2785 0.3472 REMARK 3 12 3.1400 - 3.0500 1.00 2575 143 0.3311 0.3632 REMARK 3 13 3.0500 - 2.9700 1.00 2535 156 0.3741 0.4218 REMARK 3 14 2.9700 - 2.9000 1.00 2553 154 0.4190 0.4617 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) : 0.533 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.624 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 80.55 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.98 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 5900 REMARK 3 ANGLE : 0.606 8091 REMARK 3 CHIRALITY : 0.044 953 REMARK 3 PLANARITY : 0.005 1070 REMARK 3 DIHEDRAL : 4.942 887 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9II9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300048636. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JAN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0-7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 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 : ADDREF REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41387 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830 REMARK 200 RESOLUTION RANGE LOW (A) : 49.410 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 81.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.5800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0-7.5, 16.5-19.0% REMARK 280 POLYETHYLENE GLYCOL 20000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.46500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 73.72500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 73.72500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.73250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 73.72500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 73.72500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.19750 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 73.72500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 73.72500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 38.73250 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 73.72500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 73.72500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.19750 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.46500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19100 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20500 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 GLU B 227 REMARK 465 CYS B 228 REMARK 465 GLU C 1 REMARK 465 SER C 135 REMARK 465 GLY C 149 REMARK 465 THR C 150 REMARK 465 GLY C 154 REMARK 465 SER C 202 REMARK 465 SER C 203 REMARK 465 PRO C 228 REMARK 465 LYS C 229 REMARK 465 ALA D 198 REMARK 465 ASP D 199 REMARK 465 ARG D 225 REMARK 465 GLY D 226 REMARK 465 GLU D 227 REMARK 465 CYS D 228 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 1 CG CD OE1 OE2 REMARK 470 ILE A 29 CG1 CG2 CD1 REMARK 470 VAL A 30 CG1 CG2 REMARK 470 SER A 35 OG REMARK 470 ARG A 36 CG CD NE CZ NH1 NH2 REMARK 470 SER A 58 OG REMARK 470 SER A 142 OG REMARK 470 SER A 143 OG REMARK 470 LYS A 144 CG CD CE NZ REMARK 470 SER A 145 OG REMARK 470 THR A 146 OG1 CG2 REMARK 470 SER A 147 OG REMARK 470 THR A 150 OG1 CG2 REMARK 470 SER A 176 OG REMARK 470 SER A 201 OG REMARK 470 SER A 203 OG REMARK 470 THR A 206 OG1 CG2 REMARK 470 GLN A 207 CG CD OE1 NE2 REMARK 470 THR A 208 OG1 CG2 REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 LYS A 229 CG CD CE NZ REMARK 470 SER B 59 OG REMARK 470 GLU B 137 CG CD OE1 OE2 REMARK 470 LYS B 183 CG CD CE NZ REMARK 470 LYS B 202 CG CD CE NZ REMARK 470 SER B 216 OG REMARK 470 PHE B 223 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 LEU C 4 CG CD1 CD2 REMARK 470 VAL C 5 CG1 CG2 REMARK 470 GLU C 6 CG CD OE1 OE2 REMARK 470 SER C 7 OG REMARK 470 LEU C 12 CG CD1 CD2 REMARK 470 VAL C 13 CG1 CG2 REMARK 470 GLN C 14 CG CD OE1 NE2 REMARK 470 SER C 18 OG REMARK 470 LEU C 19 CG CD1 CD2 REMARK 470 ARG C 20 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 21 CG CD1 CD2 REMARK 470 SER C 22 OG REMARK 470 SER C 26 OG REMARK 470 ILE C 28 CG1 CG2 CD1 REMARK 470 ILE C 29 CG1 CG2 CD1 REMARK 470 VAL C 30 CG1 CG2 REMARK 470 SER C 35 OG REMARK 470 ARG C 36 CG CD NE CZ NH1 NH2 REMARK 470 ASN C 37 CG OD1 ND2 REMARK 470 TYR C 38 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 MET C 39 CG SD CE REMARK 470 THR C 40 OG1 CG2 REMARK 470 TRP C 41 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 41 CZ3 CH2 REMARK 470 VAL C 42 CG1 CG2 REMARK 470 ARG C 43 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 44 CG CD OE1 NE2 REMARK 470 LYS C 48 CG CD CE NZ REMARK 470 GLU C 51 CG CD OE1 OE2 REMARK 470 VAL C 55 CG1 CG2 REMARK 470 ILE C 56 CG1 CG2 CD1 REMARK 470 TYR C 57 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP C 69 CG OD1 OD2 REMARK 470 VAL C 71 CG1 CG2 REMARK 470 LYS C 72 CG CD CE NZ REMARK 470 ARG C 75 CG CD NE CZ NH1 NH2 REMARK 470 PHE C 76 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR C 78 OG1 CG2 REMARK 470 SER C 79 OG REMARK 470 ARG C 80 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 82 CG OD1 OD2 REMARK 470 THR C 86 OG1 CG2 REMARK 470 LEU C 87 CG CD1 CD2 REMARK 470 TYR C 88 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU C 89 CG CD1 CD2 REMARK 470 GLN C 90 CG CD OE1 NE2 REMARK 470 MET C 91 CG SD CE REMARK 470 ASN C 92 CG OD1 ND2 REMARK 470 ARG C 95 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 97 CG OD1 OD2 REMARK 470 HIS C 110 CG ND1 CD2 CE1 NE2 REMARK 470 ARG C 113 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 114 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 120 CG CD OE1 NE2 REMARK 470 VAL C 126 CG1 CG2 REMARK 470 SER C 127 OG REMARK 470 SER C 128 OG REMARK 470 SER C 130 OG REMARK 470 THR C 131 OG1 CG2 REMARK 470 LYS C 132 CG CD CE NZ REMARK 470 PRO C 134 CG CD REMARK 470 VAL C 136 CG1 CG2 REMARK 470 PHE C 137 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS C 144 CG CD CE NZ REMARK 470 LEU C 153 CG CD1 CD2 REMARK 470 LEU C 156 CG CD1 CD2 REMARK 470 VAL C 157 CG1 CG2 REMARK 470 LYS C 158 CG CD CE NZ REMARK 470 ASP C 159 CG OD1 OD2 REMARK 470 TYR C 160 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE C 161 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU C 163 CG CD OE1 OE2 REMARK 470 THR C 166 OG1 CG2 REMARK 470 VAL C 167 CG1 CG2 REMARK 470 SER C 168 OG REMARK 470 ASN C 170 CG OD1 ND2 REMARK 470 LEU C 185 CG CD1 CD2 REMARK 470 GLN C 186 CG CD OE1 NE2 REMARK 470 SER C 187 OG REMARK 470 SER C 188 OG REMARK 470 LEU C 190 CG CD1 CD2 REMARK 470 TYR C 191 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER C 192 OG REMARK 470 LEU C 193 CG CD1 CD2 REMARK 470 SER C 194 OG REMARK 470 SER C 195 OG REMARK 470 VAL C 196 CG1 CG2 REMARK 470 VAL C 199 CG1 CG2 REMARK 470 SER C 201 OG REMARK 470 LEU C 204 CG CD1 CD2 REMARK 470 THR C 206 OG1 CG2 REMARK 470 GLN C 207 CG CD OE1 NE2 REMARK 470 THR C 208 OG1 CG2 REMARK 470 TYR C 209 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE C 210 CG1 CG2 CD1 REMARK 470 ASN C 212 CG OD1 ND2 REMARK 470 VAL C 213 CG1 CG2 REMARK 470 ASN C 214 CG OD1 ND2 REMARK 470 HIS C 215 CG ND1 CD2 CE1 NE2 REMARK 470 LYS C 216 CG CD CE NZ REMARK 470 SER C 218 OG REMARK 470 ASN C 219 CG OD1 ND2 REMARK 470 THR C 220 OG1 CG2 REMARK 470 LYS C 221 CG CD CE NZ REMARK 470 VAL C 222 CG1 CG2 REMARK 470 ASP C 223 CG OD1 OD2 REMARK 470 LYS C 224 CG CD CE NZ REMARK 470 LYS C 225 CG CD CE NZ REMARK 470 VAL C 226 CG1 CG2 REMARK 470 GLU C 227 CG CD OE1 OE2 REMARK 470 ASP D 1 CG OD1 OD2 REMARK 470 ILE D 29 CG1 CG2 CD1 REMARK 470 LYS D 31 CG CD CE NZ REMARK 470 SER D 59 OG REMARK 470 THR D 63 OG1 CG2 REMARK 470 GLN D 100 CG CD OE1 NE2 REMARK 470 SER D 101 OG REMARK 470 ASP D 102 CG OD1 OD2 REMARK 470 ASN D 103 CG OD1 ND2 REMARK 470 LEU D 108 CG CD1 CD2 REMARK 470 GLN D 114 CG CD OE1 NE2 REMARK 470 ILE D 131 CG1 CG2 CD1 REMARK 470 PHE D 132 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU D 137 CG CD OE1 OE2 REMARK 470 GLN D 138 CG CD OE1 NE2 REMARK 470 LEU D 139 CG CD1 CD2 REMARK 470 LYS D 140 CG CD CE NZ REMARK 470 SER D 141 OG REMARK 470 SER D 145 OG REMARK 470 VAL D 146 CG1 CG2 REMARK 470 VAL D 147 CG1 CG2 REMARK 470 LEU D 149 CG CD1 CD2 REMARK 470 ARG D 156 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 157 CG CD OE1 OE2 REMARK 470 LYS D 159 CG CD CE NZ REMARK 470 VAL D 160 CG1 CG2 REMARK 470 GLN D 161 CG CD OE1 NE2 REMARK 470 TRP D 162 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 162 CZ3 CH2 REMARK 470 LYS D 163 CG CD CE NZ REMARK 470 VAL D 164 CG1 CG2 REMARK 470 ASP D 165 CG OD1 OD2 REMARK 470 ASN D 166 CG OD1 ND2 REMARK 470 LEU D 168 CG CD1 CD2 REMARK 470 GLN D 169 CG CD OE1 NE2 REMARK 470 SER D 170 OG REMARK 470 ASN D 172 CG OD1 ND2 REMARK 470 SER D 173 OG REMARK 470 GLN D 174 CG CD OE1 NE2 REMARK 470 GLU D 175 CG CD OE1 OE2 REMARK 470 SER D 176 OG REMARK 470 THR D 178 OG1 CG2 REMARK 470 ASP D 181 CG OD1 OD2 REMARK 470 LYS D 183 CG CD CE NZ REMARK 470 LEU D 189 CG CD1 CD2 REMARK 470 SER D 190 OG REMARK 470 THR D 194 OG1 CG2 REMARK 470 LEU D 195 CG CD1 CD2 REMARK 470 SER D 196 OG REMARK 470 LYS D 197 CG CD CE NZ REMARK 470 TYR D 200 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D 201 CG CD OE1 OE2 REMARK 470 LYS D 202 CG CD CE NZ REMARK 470 HIS D 203 CG ND1 CD2 CE1 NE2 REMARK 470 LYS D 204 CG CD CE NZ REMARK 470 VAL D 205 CG1 CG2 REMARK 470 TYR D 206 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D 209 CG CD OE1 OE2 REMARK 470 VAL D 210 CG1 CG2 REMARK 470 LEU D 215 CG CD1 CD2 REMARK 470 SER D 216 OG REMARK 470 LEU D 217 CG CD1 CD2 REMARK 470 LYS D 221 CG CD CE NZ REMARK 470 SER D 222 OG REMARK 470 PHE D 223 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN D 224 CG OD1 ND2 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 ARG A 113 -166.88 -129.37 REMARK 500 ASP A 159 75.53 62.56 REMARK 500 SER A 203 16.43 59.64 REMARK 500 ASN B 30 -122.73 59.73 REMARK 500 ALA B 51 -42.42 72.11 REMARK 500 ASN B 152 107.08 -31.70 REMARK 500 ASP B 184 -30.68 -132.67 REMARK 500 LYS B 204 -53.88 -126.28 REMARK 500 GLN C 3 115.09 -163.36 REMARK 500 SER C 35 -12.78 65.02 REMARK 500 VAL C 53 -80.90 -117.08 REMARK 500 SER C 145 -122.66 48.21 REMARK 500 THR C 146 -130.39 45.65 REMARK 500 SER C 147 85.29 -177.30 REMARK 500 LYS C 158 -67.05 -99.57 REMARK 500 ASP C 159 -72.37 -60.19 REMARK 500 TYR C 160 81.80 52.99 REMARK 500 GLN C 186 -159.26 -91.98 REMARK 500 THR C 208 45.40 -86.77 REMARK 500 TYR C 209 99.94 -64.42 REMARK 500 PRO C 217 41.85 -104.78 REMARK 500 THR C 220 68.28 -156.86 REMARK 500 GLN D 27 -156.38 -119.77 REMARK 500 ASN D 30 -125.08 57.31 REMARK 500 TYR D 32 57.46 -111.71 REMARK 500 ALA D 51 -51.12 67.94 REMARK 500 GLN D 99 114.35 -162.29 REMARK 500 ASN D 151 -72.97 -75.24 REMARK 500 LEU D 168 100.36 -161.18 REMARK 500 HIS D 203 36.75 99.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR C 146 SER C 147 143.12 REMARK 500 LYS C 216 PRO C 217 148.29 REMARK 500 LYS D 202 HIS D 203 -149.63 REMARK 500 REMARK 500 REMARK: NULL DBREF 9II9 A 1 229 PDB 9II9 9II9 1 229 DBREF 9II9 B 1 228 PDB 9II9 9II9 1 228 DBREF 9II9 C 1 229 PDB 9II9 9II9 1 229 DBREF 9II9 D 1 228 PDB 9II9 9II9 1 228 SEQRES 1 A 218 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 218 ILE ILE VAL SER ARG ASN TYR MET THR TRP VAL ARG GLN SEQRES 4 A 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 A 218 SER GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 A 218 ARG PHE THR THR SER ARG ASP ASP SER LYS ASN THR LEU SEQRES 7 A 218 TYR LEU GLN MET ASN SER LEU ARG GLY ASP ASP THR ALA SEQRES 8 A 218 VAL TYR TYR CYS ALA ARG ASP PRO PRO HIS ARG ARG GLY SEQRES 9 A 218 SER TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 A 218 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 A 218 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 A 218 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 A 218 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 A 218 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 A 218 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 A 218 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 A 218 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 B 214 ASP ILE LEU MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 B 214 GLN ASP ILE ASN LYS TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 B 214 GLY SER GLY THR ASP PHE SER PHE THR ILE SER SER LEU SEQRES 7 B 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 B 214 ASP ASN LEU PRO PRO THR PHE GLY GLN GLY THR ASN VAL SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER LEU PRO VAL THR LYS SER SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS SEQRES 1 C 218 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 218 ILE ILE VAL SER ARG ASN TYR MET THR TRP VAL ARG GLN SEQRES 4 C 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 C 218 SER GLY GLY THR THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 218 ARG PHE THR THR SER ARG ASP ASP SER LYS ASN THR LEU SEQRES 7 C 218 TYR LEU GLN MET ASN SER LEU ARG GLY ASP ASP THR ALA SEQRES 8 C 218 VAL TYR TYR CYS ALA ARG ASP PRO PRO HIS ARG ARG GLY SEQRES 9 C 218 SER TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 C 218 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 C 218 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 C 218 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 C 218 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 C 218 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 C 218 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 C 218 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 C 218 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 D 214 ASP ILE LEU MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 D 214 GLN ASP ILE ASN LYS TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 D 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR ASP PHE SER PHE THR ILE SER SER LEU SEQRES 7 D 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 D 214 ASP ASN LEU PRO PRO THR PHE GLY GLN GLY THR ASN VAL SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER LEU PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS HELIX 1 AA1 ASP A 69 LYS A 72 5 4 HELIX 2 AA2 ARG A 95 THR A 99 5 5 HELIX 3 AA3 GLN B 89 VAL B 93 5 5 HELIX 4 AA4 SER B 135 SER B 141 1 7 HELIX 5 AA5 LYS B 197 LYS B 202 1 6 HELIX 6 AA6 ARG C 95 THR C 99 5 5 HELIX 7 AA7 SER C 171 ALA C 173 5 3 HELIX 8 AA8 SER D 135 LYS D 140 1 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 19 SER A 26 -1 O SER A 22 N SER A 7 SHEET 3 AA1 4 THR A 86 MET A 91 -1 O MET A 91 N LEU A 19 SHEET 4 AA1 4 PHE A 76 ASP A 81 -1 N SER A 79 O TYR A 88 SHEET 1 AA2 6 LEU A 12 VAL A 13 0 SHEET 2 AA2 6 THR A 122 VAL A 126 1 O THR A 125 N VAL A 13 SHEET 3 AA2 6 ALA A 100 ARG A 106 -1 N TYR A 102 O THR A 122 SHEET 4 AA2 6 MET A 39 GLN A 44 -1 N VAL A 42 O TYR A 103 SHEET 5 AA2 6 LEU A 50 ILE A 56 -1 O SER A 54 N TRP A 41 SHEET 6 AA2 6 THR A 65 TYR A 67 -1 O TYR A 66 N VAL A 55 SHEET 1 AA3 4 LEU A 12 VAL A 13 0 SHEET 2 AA3 4 THR A 122 VAL A 126 1 O THR A 125 N VAL A 13 SHEET 3 AA3 4 ALA A 100 ARG A 106 -1 N TYR A 102 O THR A 122 SHEET 4 AA3 4 TYR A 117 TRP A 118 -1 O TYR A 117 N ARG A 106 SHEET 1 AA4 4 SER A 135 LEU A 139 0 SHEET 2 AA4 4 THR A 150 TYR A 160 -1 O GLY A 154 N LEU A 139 SHEET 3 AA4 4 TYR A 191 PRO A 200 -1 O VAL A 199 N ALA A 151 SHEET 4 AA4 4 VAL A 178 THR A 180 -1 N HIS A 179 O VAL A 196 SHEET 1 AA5 4 SER A 135 LEU A 139 0 SHEET 2 AA5 4 THR A 150 TYR A 160 -1 O GLY A 154 N LEU A 139 SHEET 3 AA5 4 TYR A 191 PRO A 200 -1 O VAL A 199 N ALA A 151 SHEET 4 AA5 4 VAL A 184 LEU A 185 -1 N VAL A 184 O SER A 192 SHEET 1 AA6 3 THR A 166 TRP A 169 0 SHEET 2 AA6 3 ILE A 210 ASN A 214 -1 O ASN A 212 N SER A 168 SHEET 3 AA6 3 THR A 220 LYS A 224 -1 O LYS A 221 N VAL A 213 SHEET 1 AA7 4 MET B 4 SER B 7 0 SHEET 2 AA7 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7 SHEET 3 AA7 4 ASP B 80 ILE B 85 -1 O PHE B 83 N ILE B 21 SHEET 4 AA7 4 PHE B 70 SER B 77 -1 N SER B 71 O THR B 84 SHEET 1 AA8 6 SER B 10 SER B 14 0 SHEET 2 AA8 6 THR B 116 LYS B 121 1 O GLU B 119 N LEU B 11 SHEET 3 AA8 6 ALA B 94 GLN B 100 -1 N TYR B 96 O THR B 116 SHEET 4 AA8 6 LEU B 33 GLN B 38 -1 N ASN B 34 O GLN B 99 SHEET 5 AA8 6 LYS B 45 TYR B 49 -1 O ILE B 48 N TRP B 35 SHEET 6 AA8 6 ASN B 60 LEU B 61 -1 O ASN B 60 N TYR B 49 SHEET 1 AA9 4 SER B 10 SER B 14 0 SHEET 2 AA9 4 THR B 116 LYS B 121 1 O GLU B 119 N LEU B 11 SHEET 3 AA9 4 ALA B 94 GLN B 100 -1 N TYR B 96 O THR B 116 SHEET 4 AA9 4 THR B 111 PHE B 112 -1 O THR B 111 N GLN B 100 SHEET 1 AB1 4 VAL B 129 PHE B 132 0 SHEET 2 AB1 4 THR B 143 PHE B 153 -1 O LEU B 149 N PHE B 130 SHEET 3 AB1 4 TYR B 187 SER B 196 -1 O LEU B 189 N LEU B 150 SHEET 4 AB1 4 SER B 173 VAL B 177 -1 N GLN B 174 O THR B 192 SHEET 1 AB2 4 ALA B 167 LEU B 168 0 SHEET 2 AB2 4 LYS B 159 VAL B 164 -1 N VAL B 164 O ALA B 167 SHEET 3 AB2 4 VAL B 205 THR B 211 -1 O GLU B 209 N GLN B 161 SHEET 4 AB2 4 VAL B 219 ASN B 224 -1 O PHE B 223 N TYR B 206 SHEET 1 AB3 2 VAL C 5 SER C 7 0 SHEET 2 AB3 2 SER C 22 ALA C 24 -1 O SER C 22 N SER C 7 SHEET 1 AB4 3 SER C 18 ARG C 20 0 SHEET 2 AB4 3 LEU C 89 ASN C 92 -1 O MET C 91 N LEU C 19 SHEET 3 AB4 3 PHE C 76 THR C 78 -1 N THR C 77 O GLN C 90 SHEET 1 AB5 5 THR C 65 TYR C 67 0 SHEET 2 AB5 5 LEU C 50 ILE C 56 -1 N VAL C 55 O TYR C 66 SHEET 3 AB5 5 MET C 39 GLN C 44 -1 N ARG C 43 O GLU C 51 SHEET 4 AB5 5 ALA C 100 ARG C 106 -1 O TYR C 103 N VAL C 42 SHEET 5 AB5 5 THR C 122 VAL C 124 -1 O VAL C 124 N ALA C 100 SHEET 1 AB6 2 THR C 166 TRP C 169 0 SHEET 2 AB6 2 CYS C 211 ASN C 214 -1 O ASN C 212 N SER C 168 SHEET 1 AB7 2 VAL C 178 HIS C 179 0 SHEET 2 AB7 2 VAL C 196 VAL C 197 -1 O VAL C 196 N HIS C 179 SHEET 1 AB8 4 MET D 4 GLN D 6 0 SHEET 2 AB8 4 VAL D 19 ALA D 25 -1 O GLN D 24 N THR D 5 SHEET 3 AB8 4 ASP D 80 ILE D 85 -1 O ILE D 85 N VAL D 19 SHEET 4 AB8 4 PHE D 70 SER D 77 -1 N SER D 73 O SER D 82 SHEET 1 AB9 6 SER D 10 ALA D 13 0 SHEET 2 AB9 6 THR D 116 ILE D 120 1 O GLU D 119 N LEU D 11 SHEET 3 AB9 6 THR D 95 GLN D 100 -1 N TYR D 96 O THR D 116 SHEET 4 AB9 6 LEU D 33 GLN D 38 -1 N GLN D 38 O THR D 95 SHEET 5 AB9 6 PRO D 44 TYR D 49 -1 O ILE D 48 N TRP D 35 SHEET 6 AB9 6 ASN D 60 LEU D 61 -1 O ASN D 60 N TYR D 49 SHEET 1 AC1 4 SER D 10 ALA D 13 0 SHEET 2 AC1 4 THR D 116 ILE D 120 1 O GLU D 119 N LEU D 11 SHEET 3 AC1 4 THR D 95 GLN D 100 -1 N TYR D 96 O THR D 116 SHEET 4 AC1 4 THR D 111 PHE D 112 -1 O THR D 111 N GLN D 100 SHEET 1 AC2 4 VAL D 129 PHE D 132 0 SHEET 2 AC2 4 THR D 143 LEU D 150 -1 O LEU D 149 N PHE D 130 SHEET 3 AC2 4 LEU D 189 SER D 196 -1 O LEU D 195 N ALA D 144 SHEET 4 AC2 4 SER D 173 VAL D 177 -1 N GLN D 174 O THR D 192 SHEET 1 AC3 3 LYS D 159 TRP D 162 0 SHEET 2 AC3 3 CYS D 208 THR D 211 -1 O GLU D 209 N GLN D 161 SHEET 3 AC3 3 VAL D 219 THR D 220 -1 O VAL D 219 N VAL D 210 SSBOND 1 CYS A 23 CYS A 104 1555 1555 2.04 SSBOND 2 CYS A 155 CYS A 211 1555 1555 2.03 SSBOND 3 CYS B 23 CYS B 98 1555 1555 2.04 SSBOND 4 CYS B 148 CYS B 208 1555 1555 2.04 SSBOND 5 CYS C 23 CYS C 104 1555 1555 2.03 SSBOND 6 CYS C 155 CYS C 211 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 98 1555 1555 2.03 CISPEP 1 PHE A 161 PRO A 162 0 -3.76 CISPEP 2 GLU A 163 PRO A 164 0 -0.45 CISPEP 3 SER B 7 PRO B 8 0 -1.46 CISPEP 4 LEU B 108 PRO B 109 0 -2.35 CISPEP 5 TYR B 154 PRO B 155 0 2.07 CISPEP 6 TYR D 154 PRO D 155 0 -0.68 CRYST1 147.450 147.450 154.930 90.00 90.00 90.00 P 41 21 2 16 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 0.006782 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006782 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006455 0.00000