HEADER TRANSFERASE/IMMUNE SYSTEM 23-AUG-24 9DBO TITLE CRYSTAL STRUCTURE OF A SYNTHETIC FAB (R3E9) IN COMPLEX WITH THE FRB TITLE 2 DOMAIN OF MTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR; COMPND 3 CHAIN: C; COMPND 4 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED COMPND 5 PROTEIN 1,FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN,MAMMALIAN COMPND 6 TARGET OF RAPAMYCIN,MTOR,MECHANISTIC TARGET OF RAPAMYCIN,RAPAMYCIN COMPND 7 AND FKBP12 TARGET 1,RAPAMYCIN TARGET PROTEIN 1; COMPND 8 EC: 2.7.11.1; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: FAB HEAVY CHAIN; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: FAB LIGHT CHAIN; COMPND 16 CHAIN: L; COMPND 17 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: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS KINASE, INHIBITOR, ANTIBODY, SIGNALING PROTEIN, TRANSFERASE-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.M.O'LEARY,T.SLEZAK,A.A.KOSSIAKOFF REVDAT 1 11-JUN-25 9DBO 0 JRNL AUTH K.M.O'LEARY,T.SLEZAK,A.A.KOSSIAKOFF JRNL TITL CONFORMATION-SPECIFIC SYNTHETIC INTRABODIES MODULATE MTOR JRNL TITL 2 SIGNALING WITH SUBCELLULAR SPATIAL RESOLUTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX V1.21.1 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.10 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 71645 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3812 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.074 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.15000 REMARK 3 B22 (A**2) : 0.85000 REMARK 3 B33 (A**2) : -1.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.33000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN REMARK 3 THE INPUT REMARK 4 REMARK 4 9DBO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287798. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-APR-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75458 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550 REMARK 200 RESOLUTION RANGE LOW (A) : 45.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE DIHYDRATE 16% REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 495 LIES ON A SPECIAL POSITION. REMARK 375 HOH L 505 LIES ON A SPECIAL POSITION. 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 PHE H 106 -164.43 70.60 REMARK 500 PHE H 108 -29.87 71.75 REMARK 500 ASP H 157 64.88 68.55 REMARK 500 SER L 31 -134.95 48.85 REMARK 500 ALA L 52 -36.57 67.56 REMARK 500 ASN L 139 61.14 61.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C2300 DISTANCE = 6.90 ANGSTROMS REMARK 525 HOH H 523 DISTANCE = 5.82 ANGSTROMS REMARK 525 HOH H 524 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH H 525 DISTANCE = 6.32 ANGSTROMS REMARK 525 HOH H 526 DISTANCE = 6.85 ANGSTROMS DBREF 9DBO C 2021 2113 UNP P42345 MTOR_HUMAN 2021 2113 DBREF 9DBO H 4 227 PDB 9DBO 9DBO 4 227 DBREF 9DBO L 2 213 PDB 9DBO 9DBO 2 213 SEQRES 1 C 93 ILE LEU TRP HIS GLU MET TRP HIS GLU GLY LEU GLU GLU SEQRES 2 C 93 ALA SER ARG LEU TYR PHE GLY GLU ARG ASN VAL LYS GLY SEQRES 3 C 93 MET PHE GLU VAL LEU GLU PRO LEU HIS ALA MET MET GLU SEQRES 4 C 93 ARG GLY PRO GLN THR LEU LYS GLU THR SER PHE ASN GLN SEQRES 5 C 93 ALA TYR GLY ARG ASP LEU MET GLU ALA GLN GLU TRP CYS SEQRES 6 C 93 ARG LYS TYR MET LYS SER GLY ASN VAL LYS ASP LEU THR SEQRES 7 C 93 GLN ALA TRP ASP LEU TYR TYR HIS VAL PHE ARG ARG ILE SEQRES 8 C 93 SER LYS SEQRES 1 H 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 224 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 224 PHE ASN VAL TYR SER TYR SER ILE HIS TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE TYR SEQRES 5 H 224 PRO SER SER GLY TYR THR SER TYR ALA ASP SER VAL LYS SEQRES 6 H 224 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 H 224 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA ARG GLY THR TYR TYR PHE TYR SEQRES 9 H 224 PHE MET SER TRP GLY LEU ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 224 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 224 GLU PRO LYS SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 212 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 212 PHE SER SER LEU PHE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 212 PHE ASN ARG GLY FORMUL 4 HOH *548(H2 O) HELIX 1 AA1 LEU C 2022 ARG C 2042 1 21 HELIX 2 AA2 ASN C 2043 ARG C 2060 1 18 HELIX 3 AA3 THR C 2064 GLY C 2092 1 29 HELIX 4 AA4 ASN C 2093 LYS C 2113 1 21 HELIX 5 AA5 ASN H 31 TYR H 35 5 5 HELIX 6 AA6 THR H 77 LYS H 79 5 3 HELIX 7 AA7 ARG H 90 THR H 94 5 5 HELIX 8 AA8 SER H 140 LYS H 142 5 3 HELIX 9 AA9 SER H 169 ALA H 171 5 3 HELIX 10 AB1 SER H 200 LEU H 202 5 3 HELIX 11 AB2 LYS H 214 ASN H 217 5 4 HELIX 12 AB3 GLN L 80 PHE L 84 5 5 HELIX 13 AB4 SER L 122 SER L 128 1 7 HELIX 14 AB5 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 4 GLN H 6 SER H 10 0 SHEET 2 AA1 4 LEU H 21 SER H 28 -1 O ALA H 26 N VAL H 8 SHEET 3 AA1 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21 SHEET 4 AA1 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA2 6 GLY H 13 VAL H 15 0 SHEET 2 AA2 6 THR H 120 VAL H 124 1 O THR H 123 N GLY H 13 SHEET 3 AA2 6 ALA H 95 PHE H 106 -1 N ALA H 95 O VAL H 122 SHEET 4 AA2 6 SER H 36 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA2 6 LEU H 48 TYR H 55 -1 O GLU H 49 N ARG H 41 SHEET 6 AA2 6 TYR H 60 TYR H 63 -1 O TYR H 60 N TYR H 55 SHEET 1 AA3 4 GLY H 13 VAL H 15 0 SHEET 2 AA3 4 THR H 120 VAL H 124 1 O THR H 123 N GLY H 13 SHEET 3 AA3 4 ALA H 95 PHE H 106 -1 N ALA H 95 O VAL H 122 SHEET 4 AA3 4 SER H 110 TRP H 116 -1 O SER H 110 N TYR H 105 SHEET 1 AA4 4 SER H 133 LEU H 137 0 SHEET 2 AA4 4 THR H 148 TYR H 158 -1 O LEU H 154 N PHE H 135 SHEET 3 AA4 4 TYR H 189 PRO H 198 -1 O LEU H 191 N VAL H 155 SHEET 4 AA4 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194 SHEET 1 AA5 4 THR H 144 SER H 145 0 SHEET 2 AA5 4 THR H 148 TYR H 158 -1 O THR H 148 N SER H 145 SHEET 3 AA5 4 TYR H 189 PRO H 198 -1 O LEU H 191 N VAL H 155 SHEET 4 AA5 4 VAL H 182 LEU H 183 -1 N VAL H 182 O SER H 190 SHEET 1 AA6 3 THR H 164 TRP H 167 0 SHEET 2 AA6 3 ILE H 208 HIS H 213 -1 O ASN H 210 N SER H 166 SHEET 3 AA6 3 THR H 218 LYS H 223 -1 O VAL H 220 N VAL H 211 SHEET 1 AA7 4 MET L 5 SER L 8 0 SHEET 2 AA7 4 VAL L 20 ALA L 26 -1 O THR L 23 N SER L 8 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 SER L 11 ALA L 14 0 SHEET 2 AA8 6 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA8 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA8 6 VAL L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA8 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36 SHEET 6 AA8 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50 SHEET 1 AA9 4 SER L 11 ALA L 14 0 SHEET 2 AA9 4 THR L 103 ILE L 107 1 O GLU L 106 N LEU L 12 SHEET 3 AA9 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O LEU L 136 N PHE L 117 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O SER L 178 N CYS L 135 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS H 25 CYS H 99 1555 1555 2.04 SSBOND 2 CYS H 153 CYS H 209 1555 1555 2.08 SSBOND 3 CYS L 24 CYS L 89 1555 1555 2.06 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.02 CISPEP 1 PHE H 159 PRO H 160 0 -9.91 CISPEP 2 GLU H 161 PRO H 162 0 -2.98 CISPEP 3 SER L 8 PRO L 9 0 -7.50 CISPEP 4 TYR L 141 PRO L 142 0 2.11 CRYST1 45.055 69.732 89.413 90.00 90.12 90.00 P 1 2 1 2 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 0.022195 0.000000 0.000046 0.00000 SCALE2 0.000000 0.014341 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011184 0.00000