HEADER PROTEIN BINDING 22-APR-25 9OBN TITLE CRYSTAL STRUCTURE OF MALARIA TRANSMISSION-BLOCKING ANTIGEN PFS48/45 C- TITLE 2 TERMINAL DOMAIN IN COMPLEX WITH NANOBODY B2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAMETOCYTE SURFACE PROTEIN P45/48; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY B2; COMPND 8 CHAIN: E, H, G, F; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 3 ORGANISM_TAXID: 36329; SOURCE 4 STRAIN: ISOLATE 3D7; SOURCE 5 VARIANT: 6C.MAGE1; SOURCE 6 GENE: PF45/48, PFS45-48, PFS45/48, PF13_0247, PF3D7_1346700; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 13 ORGANISM_TAXID: 30538; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: WK6 KEYWDS TRANSMISSION-BLOCKING, NANOBODY, 6-CYSTEINE, MALARIA, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR F.M.T.LYONS,M.H.DIETRICH,W.H.THAM REVDAT 1 21-JAN-26 9OBN 0 JRNL AUTH F.M.T.LYONS,M.GABRIELA,L.J.CHAN,J.TONG,A.ADAIR,M.H.DIETRICH, JRNL AUTH 2 W.H.THAM JRNL TITL NANOBODIES TARGETING PFS48/45 BLOCK PLASMODIUM FALCIPARUM JRNL TITL 2 TRANSMISSION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 42408 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.211 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 2116 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 47.5400 - 6.1600 0.99 2909 153 0.2201 0.2427 REMARK 3 2 6.1600 - 4.8900 1.00 2757 143 0.1964 0.1978 REMARK 3 3 4.8900 - 4.2700 1.00 2719 142 0.1612 0.1937 REMARK 3 4 4.2700 - 3.8800 1.00 2695 142 0.1711 0.2274 REMARK 3 5 3.8800 - 3.6100 1.00 2687 142 0.1862 0.2095 REMARK 3 6 3.6100 - 3.3900 1.00 2666 138 0.1962 0.2831 REMARK 3 7 3.3900 - 3.2200 1.00 2696 142 0.2079 0.2617 REMARK 3 8 3.2200 - 3.0800 1.00 2664 141 0.2280 0.2820 REMARK 3 9 3.0800 - 2.9600 1.00 2628 137 0.2340 0.3228 REMARK 3 10 2.9600 - 2.8600 1.00 2672 141 0.2445 0.3156 REMARK 3 11 2.8600 - 2.7700 1.00 2628 138 0.2463 0.3266 REMARK 3 12 2.7700 - 2.6900 1.00 2674 141 0.2518 0.3439 REMARK 3 13 2.6900 - 2.6200 1.00 2638 139 0.2657 0.3167 REMARK 3 14 2.6200 - 2.5600 1.00 2650 139 0.2772 0.3360 REMARK 3 15 2.5600 - 2.5000 1.00 2609 138 0.2998 0.3540 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) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.280 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 8095 REMARK 3 ANGLE : 0.652 11013 REMARK 3 CHIRALITY : 0.048 1221 REMARK 3 PLANARITY : 0.005 1425 REMARK 3 DIHEDRAL : 13.311 2781 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 9OBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295210. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUL-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.953732 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 : 42503 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 47.540 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 10.50 REMARK 200 R MERGE (I) : 0.24800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.38700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE MONOHYDRATE, 0.1 REMARK 280 M BIS-TRIS PH 5.5, 25 %W/V PEG 3350, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,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 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.26100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 140.87700 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.26100 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 140.87700 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H 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 GLY A 429 REMARK 465 GLY A 430 REMARK 465 SER A 431 REMARK 465 GLU A 432 REMARK 465 ASN A 433 REMARK 465 LEU A 434 REMARK 465 TYR A 435 REMARK 465 PHE A 436 REMARK 465 GLN A 437 REMARK 465 GLU B 288 REMARK 465 THR B 289 REMARK 465 GLY B 290 REMARK 465 GLU B 291 REMARK 465 GLY B 429 REMARK 465 GLY B 430 REMARK 465 SER B 431 REMARK 465 GLU B 432 REMARK 465 ASN B 433 REMARK 465 LEU B 434 REMARK 465 TYR B 435 REMARK 465 PHE B 436 REMARK 465 GLN B 437 REMARK 465 GLU C 360 REMARK 465 SER C 361 REMARK 465 GLU C 362 REMARK 465 GLU C 363 REMARK 465 LEU C 364 REMARK 465 GLY C 429 REMARK 465 GLY C 430 REMARK 465 SER C 431 REMARK 465 GLU C 432 REMARK 465 ASN C 433 REMARK 465 LEU C 434 REMARK 465 TYR C 435 REMARK 465 PHE C 436 REMARK 465 GLN C 437 REMARK 465 GLU D 288 REMARK 465 GLU D 360 REMARK 465 SER D 361 REMARK 465 GLU D 362 REMARK 465 GLU D 363 REMARK 465 LEU D 364 REMARK 465 GLU D 365 REMARK 465 GLY D 429 REMARK 465 GLY D 430 REMARK 465 SER D 431 REMARK 465 GLU D 432 REMARK 465 ASN D 433 REMARK 465 LEU D 434 REMARK 465 TYR D 435 REMARK 465 PHE D 436 REMARK 465 GLN D 437 REMARK 465 HIS H 128 REMARK 465 HIS H 129 REMARK 465 HIS H 130 REMARK 465 HIS H 131 REMARK 465 HIS G 129 REMARK 465 HIS G 130 REMARK 465 HIS G 131 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 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 288 CG CD OE1 OE2 REMARK 470 LYS A 335 CE NZ REMARK 470 GLU A 360 CD OE1 OE2 REMARK 470 SER A 361 OG REMARK 470 GLU A 362 CG CD OE1 OE2 REMARK 470 GLU A 363 CG CD OE1 OE2 REMARK 470 LEU A 364 CG CD1 CD2 REMARK 470 GLU A 365 OE1 OE2 REMARK 470 LYS A 392 NZ REMARK 470 LYS A 413 CE NZ REMARK 470 LYS A 414 CE NZ REMARK 470 LYS A 416 CG CD CE NZ REMARK 470 LYS B 293 CG CD CE NZ REMARK 470 LYS B 307 CG CD CE NZ REMARK 470 LYS B 335 CG CD CE NZ REMARK 470 GLU B 360 CG CD OE1 OE2 REMARK 470 SER B 361 OG REMARK 470 GLU B 362 CG CD OE1 OE2 REMARK 470 GLU B 363 CG CD OE1 OE2 REMARK 470 LEU B 364 CG CD1 CD2 REMARK 470 ASP B 380 OD1 OD2 REMARK 470 GLU B 382 CD OE1 OE2 REMARK 470 LYS B 404 CG CD CE NZ REMARK 470 LYS B 414 CE NZ REMARK 470 LYS B 416 CE NZ REMARK 470 LYS C 292 CG CD CE NZ REMARK 470 LYS C 293 CG CD CE NZ REMARK 470 GLN C 358 CG CD OE1 NE2 REMARK 470 GLU C 365 CG CD OE1 OE2 REMARK 470 SER C 367 OG REMARK 470 ASP C 380 CG OD1 OD2 REMARK 470 LYS C 404 CG CD CE NZ REMARK 470 LYS C 416 CG CD CE NZ REMARK 470 THR D 289 OG1 CG2 REMARK 470 LYS D 292 CG CD CE NZ REMARK 470 LYS D 293 CG CD CE NZ REMARK 470 LYS D 335 CG CD CE NZ REMARK 470 PHE D 354 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN D 358 CD OE1 NE2 REMARK 470 SER D 367 OG REMARK 470 ASN D 368 CG OD1 ND2 REMARK 470 ILE D 378 CG1 CG2 CD1 REMARK 470 ASP D 380 CG OD1 OD2 REMARK 470 LYS D 404 CG CD CE NZ REMARK 470 LYS D 413 CG CD CE NZ REMARK 470 LYS D 414 CE NZ REMARK 470 LYS D 416 NZ REMARK 470 ILE D 425 CG2 CD1 REMARK 470 GLN E 1 CG CD OE1 NE2 REMARK 470 SER E 25 OG REMARK 470 ARG E 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 31 CG CD CE NZ REMARK 470 LYS E 43 CE NZ REMARK 470 HIS E 131 CG ND1 CD2 CE1 NE2 REMARK 470 GLN H 1 CD OE1 NE2 REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 ARG H 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 31 CE NZ REMARK 470 LYS H 43 CE NZ REMARK 470 LYS H 76 CD CE NZ REMARK 470 HIS H 127 CG ND1 CD2 CE1 NE2 REMARK 470 LEU G 11 CG CD1 CD2 REMARK 470 ARG G 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 31 CG CD CE NZ REMARK 470 LYS G 43 CD CE NZ REMARK 470 GLU G 44 CG CD OE1 OE2 REMARK 470 LYS G 76 CD CE NZ REMARK 470 HIS G 126 CG ND1 CD2 CE1 NE2 REMARK 470 HIS G 128 CG ND1 CD2 CE1 NE2 REMARK 470 GLN F 1 CG CD OE1 NE2 REMARK 470 GLN F 3 CG CD OE1 NE2 REMARK 470 ARG F 27 CG CD NE CZ NH1 NH2 REMARK 470 LYS F 31 CE NZ REMARK 470 LYS F 43 CD CE NZ REMARK 470 LYS F 76 NZ REMARK 470 GLN F 117 CD OE1 NE2 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 O HOH G 211 O HOH G 246 2.03 REMARK 500 O HOH G 208 O HOH G 238 2.12 REMARK 500 O HOH F 326 O HOH F 332 2.17 REMARK 500 O HOH B 537 O HOH B 538 2.19 REMARK 500 O HOH G 237 O HOH G 243 2.19 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 B 518 O HOH G 205 3454 2.11 REMARK 500 O HOH C 546 O HOH G 247 3554 2.17 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 ASN A 337 54.36 -152.04 REMARK 500 PRO A 350 -151.68 -79.35 REMARK 500 PRO A 366 108.97 -56.16 REMARK 500 ASP A 415 -125.62 55.10 REMARK 500 ASN B 337 53.62 -152.05 REMARK 500 PRO B 350 -150.61 -79.86 REMARK 500 PRO B 359 21.74 -76.25 REMARK 500 GLU B 360 1.18 -67.80 REMARK 500 ASP B 380 60.30 -100.20 REMARK 500 ASP B 415 -126.68 54.97 REMARK 500 ASN C 337 54.84 -152.60 REMARK 500 PRO C 350 -151.75 -79.60 REMARK 500 ASP C 415 -125.84 54.57 REMARK 500 ASN D 337 52.55 -150.63 REMARK 500 PRO D 350 -153.99 -78.90 REMARK 500 ASN D 368 130.16 -175.58 REMARK 500 ASP D 380 10.66 55.01 REMARK 500 ASP D 415 -127.49 55.88 REMARK 500 HIS G 127 15.40 55.62 REMARK 500 REMARK 500 REMARK: NULL DBREF 9OBN A 291 428 UNP Q8I6T1 P4548_PLAF7 291 428 DBREF 9OBN B 291 428 UNP Q8I6T1 P4548_PLAF7 291 428 DBREF 9OBN C 291 428 UNP Q8I6T1 P4548_PLAF7 291 428 DBREF 9OBN D 291 428 UNP Q8I6T1 P4548_PLAF7 291 428 DBREF 9OBN E 1 131 PDB 9OBN 9OBN 1 131 DBREF 9OBN H 1 131 PDB 9OBN 9OBN 1 131 DBREF 9OBN G 1 131 PDB 9OBN 9OBN 1 131 DBREF 9OBN F 1 131 PDB 9OBN 9OBN 1 131 SEQADV 9OBN GLU A 288 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN THR A 289 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY A 290 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR A 308 UNP Q8I6T1 HIS 308 ENGINEERED MUTATION SEQADV 9OBN LEU A 397 UNP Q8I6T1 GLY 397 ENGINEERED MUTATION SEQADV 9OBN VAL A 402 UNP Q8I6T1 ILE 402 ENGINEERED MUTATION SEQADV 9OBN GLY A 429 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY A 430 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN SER A 431 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU A 432 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN ASN A 433 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN LEU A 434 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR A 435 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN PHE A 436 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLN A 437 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU B 288 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN THR B 289 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY B 290 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR B 308 UNP Q8I6T1 HIS 308 ENGINEERED MUTATION SEQADV 9OBN LEU B 397 UNP Q8I6T1 GLY 397 ENGINEERED MUTATION SEQADV 9OBN VAL B 402 UNP Q8I6T1 ILE 402 ENGINEERED MUTATION SEQADV 9OBN GLY B 429 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY B 430 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN SER B 431 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU B 432 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN ASN B 433 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN LEU B 434 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR B 435 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN PHE B 436 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLN B 437 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU C 288 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN THR C 289 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY C 290 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR C 308 UNP Q8I6T1 HIS 308 ENGINEERED MUTATION SEQADV 9OBN LEU C 397 UNP Q8I6T1 GLY 397 ENGINEERED MUTATION SEQADV 9OBN VAL C 402 UNP Q8I6T1 ILE 402 ENGINEERED MUTATION SEQADV 9OBN GLY C 429 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY C 430 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN SER C 431 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU C 432 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN ASN C 433 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN LEU C 434 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR C 435 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN PHE C 436 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLN C 437 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU D 288 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN THR D 289 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY D 290 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR D 308 UNP Q8I6T1 HIS 308 ENGINEERED MUTATION SEQADV 9OBN LEU D 397 UNP Q8I6T1 GLY 397 ENGINEERED MUTATION SEQADV 9OBN VAL D 402 UNP Q8I6T1 ILE 402 ENGINEERED MUTATION SEQADV 9OBN GLY D 429 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLY D 430 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN SER D 431 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLU D 432 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN ASN D 433 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN LEU D 434 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN TYR D 435 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN PHE D 436 UNP Q8I6T1 EXPRESSION TAG SEQADV 9OBN GLN D 437 UNP Q8I6T1 EXPRESSION TAG SEQRES 1 A 150 GLU THR GLY GLU LYS LYS VAL ILE HIS GLY CYS ASN PHE SEQRES 2 A 150 SER SER ASN VAL SER SER LYS TYR THR PHE THR ASP SER SEQRES 3 A 150 LEU ASP ILE SER LEU VAL ASP ASP SER ALA HIS ILE SER SEQRES 4 A 150 CYS ASN VAL HIS LEU SER GLU PRO LYS TYR ASN HIS LEU SEQRES 5 A 150 VAL GLY LEU ASN CYS PRO GLY ASP ILE ILE PRO ASP CYS SEQRES 6 A 150 PHE PHE GLN VAL TYR GLN PRO GLU SER GLU GLU LEU GLU SEQRES 7 A 150 PRO SER ASN ILE VAL TYR LEU ASP SER GLN ILE ASN ILE SEQRES 8 A 150 GLY ASP ILE GLU TYR TYR GLU ASP ALA GLU GLY ASP ASP SEQRES 9 A 150 LYS ILE LYS LEU PHE LEU ILE VAL GLY SER VAL PRO LYS SEQRES 10 A 150 THR THR SER PHE THR CYS ILE CYS LYS LYS ASP LYS LYS SEQRES 11 A 150 SER ALA TYR MET THR VAL THR ILE ASP SER ALA GLY GLY SEQRES 12 A 150 SER GLU ASN LEU TYR PHE GLN SEQRES 1 B 150 GLU THR GLY GLU LYS LYS VAL ILE HIS GLY CYS ASN PHE SEQRES 2 B 150 SER SER ASN VAL SER SER LYS TYR THR PHE THR ASP SER SEQRES 3 B 150 LEU ASP ILE SER LEU VAL ASP ASP SER ALA HIS ILE SER SEQRES 4 B 150 CYS ASN VAL HIS LEU SER GLU PRO LYS TYR ASN HIS LEU SEQRES 5 B 150 VAL GLY LEU ASN CYS PRO GLY ASP ILE ILE PRO ASP CYS SEQRES 6 B 150 PHE PHE GLN VAL TYR GLN PRO GLU SER GLU GLU LEU GLU SEQRES 7 B 150 PRO SER ASN ILE VAL TYR LEU ASP SER GLN ILE ASN ILE SEQRES 8 B 150 GLY ASP ILE GLU TYR TYR GLU ASP ALA GLU GLY ASP ASP SEQRES 9 B 150 LYS ILE LYS LEU PHE LEU ILE VAL GLY SER VAL PRO LYS SEQRES 10 B 150 THR THR SER PHE THR CYS ILE CYS LYS LYS ASP LYS LYS SEQRES 11 B 150 SER ALA TYR MET THR VAL THR ILE ASP SER ALA GLY GLY SEQRES 12 B 150 SER GLU ASN LEU TYR PHE GLN SEQRES 1 C 150 GLU THR GLY GLU LYS LYS VAL ILE HIS GLY CYS ASN PHE SEQRES 2 C 150 SER SER ASN VAL SER SER LYS TYR THR PHE THR ASP SER SEQRES 3 C 150 LEU ASP ILE SER LEU VAL ASP ASP SER ALA HIS ILE SER SEQRES 4 C 150 CYS ASN VAL HIS LEU SER GLU PRO LYS TYR ASN HIS LEU SEQRES 5 C 150 VAL GLY LEU ASN CYS PRO GLY ASP ILE ILE PRO ASP CYS SEQRES 6 C 150 PHE PHE GLN VAL TYR GLN PRO GLU SER GLU GLU LEU GLU SEQRES 7 C 150 PRO SER ASN ILE VAL TYR LEU ASP SER GLN ILE ASN ILE SEQRES 8 C 150 GLY ASP ILE GLU TYR TYR GLU ASP ALA GLU GLY ASP ASP SEQRES 9 C 150 LYS ILE LYS LEU PHE LEU ILE VAL GLY SER VAL PRO LYS SEQRES 10 C 150 THR THR SER PHE THR CYS ILE CYS LYS LYS ASP LYS LYS SEQRES 11 C 150 SER ALA TYR MET THR VAL THR ILE ASP SER ALA GLY GLY SEQRES 12 C 150 SER GLU ASN LEU TYR PHE GLN SEQRES 1 D 150 GLU THR GLY GLU LYS LYS VAL ILE HIS GLY CYS ASN PHE SEQRES 2 D 150 SER SER ASN VAL SER SER LYS TYR THR PHE THR ASP SER SEQRES 3 D 150 LEU ASP ILE SER LEU VAL ASP ASP SER ALA HIS ILE SER SEQRES 4 D 150 CYS ASN VAL HIS LEU SER GLU PRO LYS TYR ASN HIS LEU SEQRES 5 D 150 VAL GLY LEU ASN CYS PRO GLY ASP ILE ILE PRO ASP CYS SEQRES 6 D 150 PHE PHE GLN VAL TYR GLN PRO GLU SER GLU GLU LEU GLU SEQRES 7 D 150 PRO SER ASN ILE VAL TYR LEU ASP SER GLN ILE ASN ILE SEQRES 8 D 150 GLY ASP ILE GLU TYR TYR GLU ASP ALA GLU GLY ASP ASP SEQRES 9 D 150 LYS ILE LYS LEU PHE LEU ILE VAL GLY SER VAL PRO LYS SEQRES 10 D 150 THR THR SER PHE THR CYS ILE CYS LYS LYS ASP LYS LYS SEQRES 11 D 150 SER ALA TYR MET THR VAL THR ILE ASP SER ALA GLY GLY SEQRES 12 D 150 SER GLU ASN LEU TYR PHE GLN SEQRES 1 E 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 131 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 131 ARG THR PHE SER LYS TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 E 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 E 131 GLY ALA GLY GLY ALA THR VAL HIS ALA ALA PRO VAL LYS SEQRES 6 E 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 E 131 GLY TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 E 131 ALA VAL TYR TYR CYS ALA GLN THR GLY SER THR GLY TRP SEQRES 9 E 131 PRO ALA GLY ARG THR TYR THR TYR ASP TYR TRP GLY GLN SEQRES 10 E 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 E 131 HIS SEQRES 1 H 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 131 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 131 ARG THR PHE SER LYS TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 H 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 H 131 GLY ALA GLY GLY ALA THR VAL HIS ALA ALA PRO VAL LYS SEQRES 6 H 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 H 131 GLY TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 H 131 ALA VAL TYR TYR CYS ALA GLN THR GLY SER THR GLY TRP SEQRES 9 H 131 PRO ALA GLY ARG THR TYR THR TYR ASP TYR TRP GLY GLN SEQRES 10 H 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 H 131 HIS SEQRES 1 G 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 131 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 131 ARG THR PHE SER LYS TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 G 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 G 131 GLY ALA GLY GLY ALA THR VAL HIS ALA ALA PRO VAL LYS SEQRES 6 G 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 G 131 GLY TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 G 131 ALA VAL TYR TYR CYS ALA GLN THR GLY SER THR GLY TRP SEQRES 9 G 131 PRO ALA GLY ARG THR TYR THR TYR ASP TYR TRP GLY GLN SEQRES 10 G 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 G 131 HIS SEQRES 1 F 131 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 131 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 131 ARG THR PHE SER LYS TYR ALA MET ALA TRP PHE ARG GLN SEQRES 4 F 131 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER SEQRES 5 F 131 GLY ALA GLY GLY ALA THR VAL HIS ALA ALA PRO VAL LYS SEQRES 6 F 131 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN MET SEQRES 7 F 131 GLY TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 F 131 ALA VAL TYR TYR CYS ALA GLN THR GLY SER THR GLY TRP SEQRES 9 F 131 PRO ALA GLY ARG THR TYR THR TYR ASP TYR TRP GLY GLN SEQRES 10 F 131 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 11 F 131 HIS HET SO4 D 501 5 HET SO4 E 201 5 HET EPE E 202 15 HET EPE F 201 15 HETNAM SO4 SULFATE ION HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN EPE HEPES FORMUL 9 SO4 2(O4 S 2-) FORMUL 11 EPE 2(C8 H18 N2 O4 S) FORMUL 13 HOH *383(H2 O) HELIX 1 AA1 ASP A 315 VAL A 319 5 5 HELIX 2 AA2 LEU A 372 ASN A 377 1 6 HELIX 3 AA3 ASP B 315 VAL B 319 5 5 HELIX 4 AA4 LEU B 372 ASN B 377 1 6 HELIX 5 AA5 ASP C 315 VAL C 319 5 5 HELIX 6 AA6 LEU C 372 ASN C 377 1 6 HELIX 7 AA7 ASP D 315 VAL D 319 5 5 HELIX 8 AA8 LEU D 372 ASN D 377 1 6 HELIX 9 AA9 GLY E 26 TYR E 32 5 7 HELIX 10 AB1 LYS E 87 THR E 91 5 5 HELIX 11 AB2 GLY E 103 GLY E 107 5 5 HELIX 12 AB3 ARG E 108 TYR E 112 5 5 HELIX 13 AB4 GLY H 26 TYR H 32 5 7 HELIX 14 AB5 LYS H 87 THR H 91 5 5 HELIX 15 AB6 GLY H 103 GLY H 107 5 5 HELIX 16 AB7 ARG H 108 TYR H 112 5 5 HELIX 17 AB8 GLY G 26 TYR G 32 5 7 HELIX 18 AB9 ASN G 74 LYS G 76 5 3 HELIX 19 AC1 LYS G 87 THR G 91 5 5 HELIX 20 AC2 GLY G 103 GLY G 107 5 5 HELIX 21 AC3 ARG G 108 TYR G 112 5 5 HELIX 22 AC4 GLY F 26 TYR F 32 5 7 HELIX 23 AC5 ALA F 62 LYS F 65 5 4 HELIX 24 AC6 LYS F 87 THR F 91 5 5 HELIX 25 AC7 GLY F 103 GLY F 107 5 5 HELIX 26 AC8 ARG F 108 TYR F 112 5 5 SHEET 1 AA1 5 PHE A 310 SER A 313 0 SHEET 2 AA1 5 ILE A 295 ASN A 299 1 N ASN A 299 O ASP A 312 SHEET 3 AA1 5 TYR A 336 CYS A 344 1 O LEU A 339 N HIS A 296 SHEET 4 AA1 5 ASP A 391 GLY A 400 -1 O LYS A 392 N CYS A 344 SHEET 5 AA1 5 ASP A 380 GLU A 388 -1 N TYR A 384 O LEU A 395 SHEET 1 AA210 ASP A 347 ILE A 349 0 SHEET 2 AA210 THR A 406 LYS A 414 -1 O LYS A 413 N ASP A 347 SHEET 3 AA210 LYS A 417 ILE A 425 -1 O MET A 421 N CYS A 410 SHEET 4 AA210 HIS A 324 LEU A 331 1 N LEU A 331 O THR A 424 SHEET 5 AA210 ALA G 57 HIS G 60 -1 O HIS G 60 N HIS A 324 SHEET 6 AA210 GLU G 46 ILE G 51 -1 N ALA G 50 O VAL G 59 SHEET 7 AA210 ALA G 33 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 8 AA210 ALA G 92 THR G 99 -1 O TYR G 95 N PHE G 37 SHEET 9 AA210 THR G 119 SER G 124 -1 O THR G 119 N TYR G 94 SHEET 10 AA210 GLY G 10 GLN G 13 1 N VAL G 12 O THR G 122 SHEET 1 AA3 9 ASP A 347 ILE A 349 0 SHEET 2 AA3 9 THR A 406 LYS A 414 -1 O LYS A 413 N ASP A 347 SHEET 3 AA3 9 LYS A 417 ILE A 425 -1 O MET A 421 N CYS A 410 SHEET 4 AA3 9 HIS A 324 LEU A 331 1 N LEU A 331 O THR A 424 SHEET 5 AA3 9 ALA G 57 HIS G 60 -1 O HIS G 60 N HIS A 324 SHEET 6 AA3 9 GLU G 46 ILE G 51 -1 N ALA G 50 O VAL G 59 SHEET 7 AA3 9 ALA G 33 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 8 AA3 9 ALA G 92 THR G 99 -1 O TYR G 95 N PHE G 37 SHEET 9 AA3 9 TYR G 114 TRP G 115 -1 O TYR G 114 N GLN G 98 SHEET 1 AA4 2 GLN A 355 TYR A 357 0 SHEET 2 AA4 2 ILE A 369 TYR A 371 -1 O VAL A 370 N VAL A 356 SHEET 1 AA5 5 TYR B 308 SER B 313 0 SHEET 2 AA5 5 LYS B 293 ASN B 299 1 N LYS B 293 O THR B 309 SHEET 3 AA5 5 TYR B 336 CYS B 344 1 O LEU B 339 N HIS B 296 SHEET 4 AA5 5 ASP B 391 GLY B 400 -1 O LYS B 392 N CYS B 344 SHEET 5 AA5 5 ILE B 381 GLU B 388 -1 N TYR B 384 O LEU B 395 SHEET 1 AA610 ASP B 347 ILE B 349 0 SHEET 2 AA610 THR B 406 LYS B 414 -1 O LYS B 413 N ASP B 347 SHEET 3 AA610 LYS B 417 ILE B 425 -1 O ALA B 419 N CYS B 412 SHEET 4 AA610 HIS B 324 LEU B 331 1 N CYS B 327 O THR B 422 SHEET 5 AA610 ALA E 57 HIS E 60 -1 O HIS E 60 N HIS B 324 SHEET 6 AA610 GLU E 46 ILE E 51 -1 N ALA E 50 O VAL E 59 SHEET 7 AA610 ALA E 33 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 8 AA610 ALA E 92 THR E 99 -1 O TYR E 95 N PHE E 37 SHEET 9 AA610 THR E 119 SER E 124 -1 O THR E 119 N TYR E 94 SHEET 10 AA610 LEU E 11 GLN E 13 1 N VAL E 12 O SER E 124 SHEET 1 AA7 9 ASP B 347 ILE B 349 0 SHEET 2 AA7 9 THR B 406 LYS B 414 -1 O LYS B 413 N ASP B 347 SHEET 3 AA7 9 LYS B 417 ILE B 425 -1 O ALA B 419 N CYS B 412 SHEET 4 AA7 9 HIS B 324 LEU B 331 1 N CYS B 327 O THR B 422 SHEET 5 AA7 9 ALA E 57 HIS E 60 -1 O HIS E 60 N HIS B 324 SHEET 6 AA7 9 GLU E 46 ILE E 51 -1 N ALA E 50 O VAL E 59 SHEET 7 AA7 9 ALA E 33 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 8 AA7 9 ALA E 92 THR E 99 -1 O TYR E 95 N PHE E 37 SHEET 9 AA7 9 TYR E 114 TRP E 115 -1 O TYR E 114 N GLN E 98 SHEET 1 AA8 2 GLN B 355 TYR B 357 0 SHEET 2 AA8 2 ILE B 369 TYR B 371 -1 O VAL B 370 N VAL B 356 SHEET 1 AA9 5 THR C 309 SER C 313 0 SHEET 2 AA9 5 VAL C 294 ASN C 299 1 N ILE C 295 O THR C 309 SHEET 3 AA9 5 TYR C 336 CYS C 344 1 O LEU C 339 N HIS C 296 SHEET 4 AA9 5 ASP C 391 GLY C 400 -1 O LYS C 392 N CYS C 344 SHEET 5 AA9 5 ILE C 381 GLU C 388 -1 N GLU C 382 O LEU C 397 SHEET 1 AB110 ASP C 347 ILE C 349 0 SHEET 2 AB110 THR C 406 LYS C 414 -1 O LYS C 413 N ASP C 347 SHEET 3 AB110 LYS C 417 ILE C 425 -1 O MET C 421 N CYS C 410 SHEET 4 AB110 HIS C 324 LEU C 331 1 N LEU C 331 O THR C 424 SHEET 5 AB110 ALA F 57 HIS F 60 -1 O HIS F 60 N HIS C 324 SHEET 6 AB110 GLU F 46 ILE F 51 -1 N ALA F 50 O VAL F 59 SHEET 7 AB110 ALA F 33 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 8 AB110 ALA F 92 THR F 99 -1 O TYR F 95 N PHE F 37 SHEET 9 AB110 THR F 119 SER F 124 -1 O THR F 119 N TYR F 94 SHEET 10 AB110 GLY F 10 GLN F 13 1 N VAL F 12 O SER F 124 SHEET 1 AB2 9 ASP C 347 ILE C 349 0 SHEET 2 AB2 9 THR C 406 LYS C 414 -1 O LYS C 413 N ASP C 347 SHEET 3 AB2 9 LYS C 417 ILE C 425 -1 O MET C 421 N CYS C 410 SHEET 4 AB2 9 HIS C 324 LEU C 331 1 N LEU C 331 O THR C 424 SHEET 5 AB2 9 ALA F 57 HIS F 60 -1 O HIS F 60 N HIS C 324 SHEET 6 AB2 9 GLU F 46 ILE F 51 -1 N ALA F 50 O VAL F 59 SHEET 7 AB2 9 ALA F 33 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 8 AB2 9 ALA F 92 THR F 99 -1 O TYR F 95 N PHE F 37 SHEET 9 AB2 9 TYR F 114 TRP F 115 -1 O TYR F 114 N GLN F 98 SHEET 1 AB3 2 GLN C 355 TYR C 357 0 SHEET 2 AB3 2 ILE C 369 TYR C 371 -1 O VAL C 370 N VAL C 356 SHEET 1 AB4 5 THR D 309 SER D 313 0 SHEET 2 AB4 5 VAL D 294 ASN D 299 1 N ILE D 295 O THR D 309 SHEET 3 AB4 5 TYR D 336 CYS D 344 1 O LEU D 339 N HIS D 296 SHEET 4 AB4 5 ASP D 391 GLY D 400 -1 O LYS D 392 N CYS D 344 SHEET 5 AB4 5 GLU D 382 GLU D 388 -1 N GLU D 382 O LEU D 397 SHEET 1 AB510 ASP D 347 ILE D 349 0 SHEET 2 AB510 THR D 406 LYS D 414 -1 O ILE D 411 N ILE D 349 SHEET 3 AB510 LYS D 417 ILE D 425 -1 O MET D 421 N CYS D 410 SHEET 4 AB510 HIS D 324 LEU D 331 1 N LEU D 331 O THR D 424 SHEET 5 AB510 ALA H 57 HIS H 60 -1 O HIS H 60 N HIS D 324 SHEET 6 AB510 GLU H 46 ILE H 51 -1 N ALA H 50 O VAL H 59 SHEET 7 AB510 ALA H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 8 AB510 ALA H 92 THR H 99 -1 O TYR H 95 N PHE H 37 SHEET 9 AB510 THR H 119 SER H 124 -1 O THR H 119 N TYR H 94 SHEET 10 AB510 GLY H 10 GLN H 13 1 N VAL H 12 O SER H 124 SHEET 1 AB6 9 ASP D 347 ILE D 349 0 SHEET 2 AB6 9 THR D 406 LYS D 414 -1 O ILE D 411 N ILE D 349 SHEET 3 AB6 9 LYS D 417 ILE D 425 -1 O MET D 421 N CYS D 410 SHEET 4 AB6 9 HIS D 324 LEU D 331 1 N LEU D 331 O THR D 424 SHEET 5 AB6 9 ALA H 57 HIS H 60 -1 O HIS H 60 N HIS D 324 SHEET 6 AB6 9 GLU H 46 ILE H 51 -1 N ALA H 50 O VAL H 59 SHEET 7 AB6 9 ALA H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 8 AB6 9 ALA H 92 THR H 99 -1 O TYR H 95 N PHE H 37 SHEET 9 AB6 9 TYR H 114 TRP H 115 -1 O TYR H 114 N GLN H 98 SHEET 1 AB7 2 GLN D 355 TYR D 357 0 SHEET 2 AB7 2 ILE D 369 TYR D 371 -1 O VAL D 370 N VAL D 356 SHEET 1 AB8 4 GLN E 3 SER E 7 0 SHEET 2 AB8 4 LEU E 18 SER E 25 -1 O ALA E 23 N GLN E 5 SHEET 3 AB8 4 MET E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AB8 4 PHE E 68 ASP E 73 -1 N ASP E 73 O MET E 78 SHEET 1 AB9 4 LEU H 4 SER H 7 0 SHEET 2 AB9 4 LEU H 18 ALA H 24 -1 O ALA H 23 N GLN H 5 SHEET 3 AB9 4 MET H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB9 4 PHE H 68 ASP H 73 -1 N ASP H 73 O MET H 78 SHEET 1 AC1 4 GLN G 3 SER G 7 0 SHEET 2 AC1 4 LEU G 18 SER G 25 -1 O ALA G 23 N GLN G 5 SHEET 3 AC1 4 MET G 78 MET G 83 -1 O MET G 83 N LEU G 18 SHEET 4 AC1 4 PHE G 68 ASP G 73 -1 N THR G 69 O GLN G 82 SHEET 1 AC2 4 GLN F 3 SER F 7 0 SHEET 2 AC2 4 LEU F 18 SER F 25 -1 O ALA F 23 N GLN F 5 SHEET 3 AC2 4 MET F 78 MET F 83 -1 O GLY F 79 N CYS F 22 SHEET 4 AC2 4 PHE F 68 ASP F 73 -1 N ASP F 73 O MET F 78 SSBOND 1 CYS A 298 CYS A 327 1555 1555 2.04 SSBOND 2 CYS A 344 CYS A 412 1555 1555 2.03 SSBOND 3 CYS A 352 CYS A 410 1555 1555 2.04 SSBOND 4 CYS B 298 CYS B 327 1555 1555 2.01 SSBOND 5 CYS B 344 CYS B 412 1555 1555 2.04 SSBOND 6 CYS B 352 CYS B 410 1555 1555 2.04 SSBOND 7 CYS C 298 CYS C 327 1555 1555 2.04 SSBOND 8 CYS C 344 CYS C 412 1555 1555 2.03 SSBOND 9 CYS C 352 CYS C 410 1555 1555 2.04 SSBOND 10 CYS D 298 CYS D 327 1555 1555 2.03 SSBOND 11 CYS D 344 CYS D 412 1555 1555 2.04 SSBOND 12 CYS D 352 CYS D 410 1555 1555 2.04 SSBOND 13 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 14 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 15 CYS G 22 CYS G 96 1555 1555 2.04 SSBOND 16 CYS F 22 CYS F 96 1555 1555 2.03 CISPEP 1 ILE A 349 PRO A 350 0 -5.73 CISPEP 2 CYS A 352 PHE A 353 0 2.65 CISPEP 3 ILE B 349 PRO B 350 0 -5.71 CISPEP 4 CYS B 352 PHE B 353 0 2.19 CISPEP 5 ILE C 349 PRO C 350 0 -6.75 CISPEP 6 CYS C 352 PHE C 353 0 2.47 CISPEP 7 ILE D 349 PRO D 350 0 -5.75 CISPEP 8 CYS D 352 PHE D 353 0 2.11 CRYST1 47.690 88.522 281.754 90.00 90.00 90.00 P 2 21 21 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 0.020969 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011297 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003549 0.00000