HEADER IMMUNE SYSTEM/TRANSFERASE 10-SEP-24 9DL0 TITLE CRYSTAL STRUCTURE OF A SYNTHETIC FAB (R3H8) IN COMPLEX WITH THE FRB TITLE 2 DOMAIN OF MTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB HEAVY CHAIN; COMPND 3 CHAIN: A, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SERINE/THREONINE-PROTEIN KINASE MTOR; COMPND 7 CHAIN: G, I; COMPND 8 SYNONYM: FK506-BINDING PROTEIN 12-RAPAMYCIN COMPLEX-ASSOCIATED COMPND 9 PROTEIN 1,FKBP12-RAPAMYCIN COMPLEX-ASSOCIATED PROTEIN,MAMMALIAN COMPND 10 TARGET OF RAPAMYCIN,MTOR,MECHANISTIC TARGET OF RAPAMYCIN,RAPAMYCIN COMPND 11 AND FKBP12 TARGET 1,RAPAMYCIN TARGET PROTEIN 1; COMPND 12 EC: 2.7.11.1; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: FAB LIGHT CHAIN; COMPND 16 CHAIN: Y, Z; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1; 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, IMMUNE SYSTEM, IMMUNE KEYWDS 2 SYSTEM-TRANSFERASE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.M.O'LEARY,T.SLEZAK,A.A.KOSSIAKOFF REVDAT 1 11-JUN-25 9DL0 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. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 3 NUMBER OF REFLECTIONS : 81284 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.207 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.234 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160 REMARK 3 FREE R VALUE TEST SET COUNT : 4198 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 56.3100 - 6.2100 1.00 2966 131 0.1809 0.2018 REMARK 3 2 6.2100 - 4.9300 1.00 2798 161 0.1745 0.1820 REMARK 3 3 4.9300 - 4.3100 1.00 2775 165 0.1421 0.1707 REMARK 3 4 4.3100 - 3.9100 0.99 2748 151 0.1621 0.1740 REMARK 3 5 3.9100 - 3.6300 0.77 2116 106 0.1763 0.2336 REMARK 3 6 3.6300 - 3.4200 1.00 2738 152 0.1848 0.2096 REMARK 3 7 3.4200 - 3.2500 1.00 2728 159 0.2019 0.2244 REMARK 3 8 3.2500 - 3.1100 1.00 2756 140 0.2078 0.2216 REMARK 3 9 3.1100 - 2.9900 1.00 2713 156 0.2112 0.2430 REMARK 3 10 2.9900 - 2.8800 1.00 2731 142 0.2342 0.2616 REMARK 3 11 2.8800 - 2.7900 1.00 2698 161 0.2243 0.2809 REMARK 3 12 2.7900 - 2.7100 1.00 2734 131 0.2169 0.2781 REMARK 3 13 2.7100 - 2.6400 1.00 2713 147 0.2212 0.2649 REMARK 3 14 2.6400 - 2.5800 1.00 2692 154 0.2161 0.2747 REMARK 3 15 2.5800 - 2.5200 1.00 2714 143 0.2249 0.2952 REMARK 3 16 2.5200 - 2.4700 1.00 2703 128 0.2346 0.3245 REMARK 3 17 2.4700 - 2.4200 1.00 2725 145 0.2404 0.2333 REMARK 3 18 2.4200 - 2.3700 1.00 2693 145 0.2384 0.3107 REMARK 3 19 2.3700 - 2.3300 1.00 2698 167 0.2760 0.2829 REMARK 3 20 2.3300 - 2.2900 1.00 2681 134 0.2812 0.3075 REMARK 3 21 2.2900 - 2.2700 0.50 671 33 0.4782 0.6710 REMARK 3 22 2.2300 - 2.2200 0.73 852 52 0.4238 0.4433 REMARK 3 23 2.2200 - 2.1900 0.99 2681 120 0.2872 0.3282 REMARK 3 24 2.1900 - 2.1500 1.00 2704 136 0.2733 0.2829 REMARK 3 25 2.1500 - 2.1300 1.00 2710 143 0.2892 0.3239 REMARK 3 26 2.1300 - 2.1000 1.00 2683 145 0.3085 0.3565 REMARK 3 27 2.1000 - 2.0700 1.00 2697 158 0.3103 0.3941 REMARK 3 28 2.0700 - 2.0500 1.00 2620 181 0.3116 0.3319 REMARK 3 29 2.0500 - 2.0200 1.00 2690 149 0.3316 0.3672 REMARK 3 30 2.0200 - 2.0000 1.00 2658 163 0.3280 0.3681 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) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.210 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 : 0.008 NULL REMARK 3 ANGLE : 1.014 NULL REMARK 3 CHIRALITY : 0.061 1240 REMARK 3 PLANARITY : 0.007 1434 REMARK 3 DIHEDRAL : 18.143 2961 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 34.1836 -29.4808 -23.5179 REMARK 3 T TENSOR REMARK 3 T11: 0.2196 T22: 0.2343 REMARK 3 T33: 0.2510 T12: 0.0007 REMARK 3 T13: -0.0038 T23: 0.0107 REMARK 3 L TENSOR REMARK 3 L11: 0.0863 L22: 0.0551 REMARK 3 L33: 0.3561 L12: 0.0272 REMARK 3 L13: 0.0233 L23: -0.0028 REMARK 3 S TENSOR REMARK 3 S11: 0.0020 S12: 0.0211 S13: 0.0320 REMARK 3 S21: -0.0146 S22: -0.0014 S23: 0.0374 REMARK 3 S31: -0.0204 S32: -0.0128 S33: -0.0000 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 9DL0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288292. 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 : 82556 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 110.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07 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 (%): 55.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5 4% PEG 400 2.2 M REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 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+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,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 43.80650 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.53950 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.80650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.53950 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, Y REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I, Z 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 Z 342 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 141 REMARK 465 LYS A 142 REMARK 465 SER A 143 REMARK 465 THR A 144 REMARK 465 SER A 145 REMARK 465 GLY A 146 REMARK 465 SER G 2020 REMARK 465 LYS G 2113 REMARK 465 GLY G 2114 REMARK 465 GLY G 2115 REMARK 465 GLY G 2116 REMARK 465 GLY G 2117 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 LYS G2095 CG CD CE NZ 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 LYS A 46 -162.54 -124.58 REMARK 500 ASP A 157 73.44 62.74 REMARK 500 PRO A 215 -18.57 -47.81 REMARK 500 LYS H 46 -165.03 -121.54 REMARK 500 LYS H 142 34.45 -89.19 REMARK 500 SER H 143 57.97 -152.61 REMARK 500 ASP H 157 74.08 63.66 REMARK 500 SER Y 31 64.42 37.39 REMARK 500 SER Y 32 -2.06 61.95 REMARK 500 ALA Y 52 -43.95 71.28 REMARK 500 SER Y 78 79.08 -155.80 REMARK 500 ALA Y 85 170.88 174.83 REMARK 500 ASN Y 153 -4.50 67.55 REMARK 500 SER Z 31 64.49 35.49 REMARK 500 SER Z 32 -0.08 63.44 REMARK 500 ALA Z 52 -42.53 70.40 REMARK 500 SER Z 78 82.94 -151.89 REMARK 500 ALA Z 85 170.18 176.32 REMARK 500 ASN Z 153 -3.29 68.24 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 Z 392 DISTANCE = 6.31 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9DBO RELATED DB: PDB REMARK 900 9DBO CONTAINS THE SAME ANTIGEN COMPLEXED WITH ANOTHER UNIQUE REMARK 900 SYNTHETIC FAB (R3E9) DBREF 9DL0 A 4 227 PDB 9DL0 9DL0 4 227 DBREF 9DL0 G 2021 2113 UNP P42345 MTOR_HUMAN 2021 2113 DBREF 9DL0 H 4 227 PDB 9DL0 9DL0 4 227 DBREF 9DL0 I 2021 2113 UNP P42345 MTOR_HUMAN 2021 2113 DBREF 9DL0 Y 2 213 PDB 9DL0 9DL0 2 213 DBREF 9DL0 Z 2 213 PDB 9DL0 9DL0 2 213 SEQADV 9DL0 SER G 2020 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY G 2114 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY G 2115 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY G 2116 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY G 2117 UNP P42345 EXPRESSION TAG SEQADV 9DL0 SER I 2020 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY I 2114 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY I 2115 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY I 2116 UNP P42345 EXPRESSION TAG SEQADV 9DL0 GLY I 2117 UNP P42345 EXPRESSION TAG SEQRES 1 A 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 224 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 224 PHE ASN PHE SER SER SER TYR ILE HIS TRP VAL ARG GLN SEQRES 4 A 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 A 224 SER SER SER GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 A 224 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 A 224 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 224 ALA VAL TYR TYR CYS ALA ARG PHE SER TYR MET SER GLY SEQRES 9 A 224 SER VAL PHE TRP ALA LEU ASP TYR TRP GLY GLN GLY THR SEQRES 10 A 224 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 A 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 A 224 GLU PRO LYS SEQRES 1 G 98 SER ILE LEU TRP HIS GLU MET TRP HIS GLU GLY LEU GLU SEQRES 2 G 98 GLU ALA SER ARG LEU TYR PHE GLY GLU ARG ASN VAL LYS SEQRES 3 G 98 GLY MET PHE GLU VAL LEU GLU PRO LEU HIS ALA MET MET SEQRES 4 G 98 GLU ARG GLY PRO GLN THR LEU LYS GLU THR SER PHE ASN SEQRES 5 G 98 GLN ALA TYR GLY ARG ASP LEU MET GLU ALA GLN GLU TRP SEQRES 6 G 98 CYS ARG LYS TYR MET LYS SER GLY ASN VAL LYS ASP LEU SEQRES 7 G 98 THR GLN ALA TRP ASP LEU TYR TYR HIS VAL PHE ARG ARG SEQRES 8 G 98 ILE SER LYS GLY GLY GLY GLY 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 PHE SER SER SER TYR ILE HIS TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 224 SER SER SER GLY SER 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 PHE SER TYR MET SER GLY SEQRES 9 H 224 SER VAL PHE TRP ALA 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 I 98 SER ILE LEU TRP HIS GLU MET TRP HIS GLU GLY LEU GLU SEQRES 2 I 98 GLU ALA SER ARG LEU TYR PHE GLY GLU ARG ASN VAL LYS SEQRES 3 I 98 GLY MET PHE GLU VAL LEU GLU PRO LEU HIS ALA MET MET SEQRES 4 I 98 GLU ARG GLY PRO GLN THR LEU LYS GLU THR SER PHE ASN SEQRES 5 I 98 GLN ALA TYR GLY ARG ASP LEU MET GLU ALA GLN GLU TRP SEQRES 6 I 98 CYS ARG LYS TYR MET LYS SER GLY ASN VAL LYS ASP LEU SEQRES 7 I 98 THR GLN ALA TRP ASP LEU TYR TYR HIS VAL PHE ARG ARG SEQRES 8 I 98 ILE SER LYS GLY GLY GLY GLY SEQRES 1 Y 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 Y 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 Y 212 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 Y 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 Y 212 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 Y 212 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 Y 212 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 Y 212 SER TRP PHE PRO ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 Y 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 Y 212 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 Y 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 Y 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 Y 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 Y 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 Y 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 Y 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 Y 212 PHE ASN ARG GLY SEQRES 1 Z 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 Z 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 Z 212 GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 Z 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 Z 212 SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 Z 212 ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 Z 212 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 Z 212 SER TRP PHE PRO ILE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 Z 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 Z 212 PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR ALA SEQRES 11 Z 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 Z 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 Z 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 Z 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 Z 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 Z 212 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 Z 212 PHE ASN ARG GLY FORMUL 7 HOH *373(H2 O) HELIX 1 AA1 ASN A 31 SER A 34 5 4 HELIX 2 AA2 THR A 77 LYS A 79 5 3 HELIX 3 AA3 ARG A 90 THR A 94 5 5 HELIX 4 AA4 SER A 169 ALA A 171 5 3 HELIX 5 AA5 SER A 200 LEU A 202 5 3 HELIX 6 AA6 LYS A 214 ASN A 217 5 4 HELIX 7 AA7 LEU G 2022 GLY G 2040 1 19 HELIX 8 AA8 ASN G 2043 GLY G 2061 1 19 HELIX 9 AA9 THR G 2064 GLY G 2092 1 29 HELIX 10 AB1 ASN G 2093 SER G 2112 1 20 HELIX 11 AB2 ASN H 31 SER H 34 5 4 HELIX 12 AB3 THR H 77 LYS H 79 5 3 HELIX 13 AB4 ARG H 90 THR H 94 5 5 HELIX 14 AB5 SER H 169 ALA H 171 5 3 HELIX 15 AB6 SER H 200 LEU H 202 5 3 HELIX 16 AB7 LYS H 214 ASN H 217 5 4 HELIX 17 AB8 LEU I 2022 GLY I 2040 1 19 HELIX 18 AB9 ASN I 2043 ARG I 2060 1 18 HELIX 19 AC1 THR I 2064 GLY I 2092 1 29 HELIX 20 AC2 ASN I 2093 GLY I 2115 1 23 HELIX 21 AC3 GLN Y 80 PHE Y 84 5 5 HELIX 22 AC4 SER Y 122 LYS Y 127 1 6 HELIX 23 AC5 LYS Y 184 LYS Y 189 1 6 HELIX 24 AC6 GLN Z 80 PHE Z 84 5 5 HELIX 25 AC7 SER Z 122 LYS Z 127 1 6 HELIX 26 AC8 LYS Z 184 LYS Z 189 1 6 SHEET 1 AA1 4 GLN A 6 SER A 10 0 SHEET 2 AA1 4 LEU A 21 SER A 28 -1 O SER A 24 N SER A 10 SHEET 3 AA1 4 THR A 81 MET A 86 -1 O MET A 86 N LEU A 21 SHEET 4 AA1 4 PHE A 71 ASP A 76 -1 N THR A 72 O GLN A 85 SHEET 1 AA2 6 GLY A 13 VAL A 15 0 SHEET 2 AA2 6 THR A 120 VAL A 124 1 O THR A 123 N VAL A 15 SHEET 3 AA2 6 ALA A 95 TYR A 104 -1 N ALA A 95 O VAL A 122 SHEET 4 AA2 6 TYR A 36 GLN A 42 -1 N VAL A 40 O TYR A 98 SHEET 5 AA2 6 GLU A 49 SER A 55 -1 O GLU A 49 N ARG A 41 SHEET 6 AA2 6 THR A 61 TYR A 63 -1 O SER A 62 N SER A 53 SHEET 1 AA3 4 GLY A 13 VAL A 15 0 SHEET 2 AA3 4 THR A 120 VAL A 124 1 O THR A 123 N VAL A 15 SHEET 3 AA3 4 ALA A 95 TYR A 104 -1 N ALA A 95 O VAL A 122 SHEET 4 AA3 4 TRP A 111 TRP A 116 -1 O TYR A 115 N ARG A 101 SHEET 1 AA4 4 SER A 133 LEU A 137 0 SHEET 2 AA4 4 THR A 148 TYR A 158 -1 O GLY A 152 N LEU A 137 SHEET 3 AA4 4 TYR A 189 PRO A 198 -1 O LEU A 191 N VAL A 155 SHEET 4 AA4 4 VAL A 176 THR A 178 -1 N HIS A 177 O VAL A 194 SHEET 1 AA5 4 SER A 133 LEU A 137 0 SHEET 2 AA5 4 THR A 148 TYR A 158 -1 O GLY A 152 N LEU A 137 SHEET 3 AA5 4 TYR A 189 PRO A 198 -1 O LEU A 191 N VAL A 155 SHEET 4 AA5 4 VAL A 182 LEU A 183 -1 N VAL A 182 O SER A 190 SHEET 1 AA6 3 THR A 164 TRP A 167 0 SHEET 2 AA6 3 TYR A 207 HIS A 213 -1 O ASN A 210 N SER A 166 SHEET 3 AA6 3 THR A 218 VAL A 224 -1 O VAL A 224 N TYR A 207 SHEET 1 AA7 4 GLN H 6 SER H 10 0 SHEET 2 AA7 4 LEU H 21 SER H 28 -1 O SER H 24 N SER H 10 SHEET 3 AA7 4 THR H 81 MET H 86 -1 O LEU H 84 N LEU H 23 SHEET 4 AA7 4 PHE H 71 ASP H 76 -1 N THR H 72 O GLN H 85 SHEET 1 AA8 6 GLY H 13 VAL H 15 0 SHEET 2 AA8 6 THR H 120 VAL H 124 1 O THR H 123 N VAL H 15 SHEET 3 AA8 6 ALA H 95 TYR H 104 -1 N ALA H 95 O VAL H 122 SHEET 4 AA8 6 TYR H 36 GLN H 42 -1 N VAL H 40 O TYR H 98 SHEET 5 AA8 6 LEU H 48 SER H 55 -1 O ALA H 52 N TRP H 39 SHEET 6 AA8 6 THR H 61 TYR H 63 -1 O SER H 62 N SER H 53 SHEET 1 AA9 4 GLY H 13 VAL H 15 0 SHEET 2 AA9 4 THR H 120 VAL H 124 1 O THR H 123 N VAL H 15 SHEET 3 AA9 4 ALA H 95 TYR H 104 -1 N ALA H 95 O VAL H 122 SHEET 4 AA9 4 TRP H 111 TRP H 116 -1 O ALA H 112 N SER H 103 SHEET 1 AB1 4 SER H 133 LEU H 137 0 SHEET 2 AB1 4 THR H 148 TYR H 158 -1 O GLY H 152 N LEU H 137 SHEET 3 AB1 4 TYR H 189 PRO H 198 -1 O VAL H 197 N ALA H 149 SHEET 4 AB1 4 VAL H 176 THR H 178 -1 N HIS H 177 O VAL H 194 SHEET 1 AB2 4 SER H 133 LEU H 137 0 SHEET 2 AB2 4 THR H 148 TYR H 158 -1 O GLY H 152 N LEU H 137 SHEET 3 AB2 4 TYR H 189 PRO H 198 -1 O VAL H 197 N ALA H 149 SHEET 4 AB2 4 VAL H 182 LEU H 183 -1 N VAL H 182 O SER H 190 SHEET 1 AB3 3 THR H 164 TRP H 167 0 SHEET 2 AB3 3 TYR H 207 HIS H 213 -1 O ASN H 210 N SER H 166 SHEET 3 AB3 3 THR H 218 VAL H 224 -1 O VAL H 220 N VAL H 211 SHEET 1 AB4 4 MET Y 5 SER Y 8 0 SHEET 2 AB4 4 VAL Y 20 ALA Y 26 -1 O THR Y 23 N SER Y 8 SHEET 3 AB4 4 ASP Y 71 ILE Y 76 -1 O LEU Y 74 N ILE Y 22 SHEET 4 AB4 4 PHE Y 63 SER Y 68 -1 N SER Y 68 O ASP Y 71 SHEET 1 AB5 6 SER Y 11 SER Y 15 0 SHEET 2 AB5 6 THR Y 103 LYS Y 108 1 O LYS Y 108 N ALA Y 14 SHEET 3 AB5 6 ALA Y 85 GLN Y 91 -1 N ALA Y 85 O VAL Y 105 SHEET 4 AB5 6 VAL Y 34 GLN Y 39 -1 N GLN Y 39 O THR Y 86 SHEET 5 AB5 6 LYS Y 46 TYR Y 50 -1 O LEU Y 48 N TRP Y 36 SHEET 6 AB5 6 SER Y 54 LEU Y 55 -1 O SER Y 54 N TYR Y 50 SHEET 1 AB6 4 SER Y 11 SER Y 15 0 SHEET 2 AB6 4 THR Y 103 LYS Y 108 1 O LYS Y 108 N ALA Y 14 SHEET 3 AB6 4 ALA Y 85 GLN Y 91 -1 N ALA Y 85 O VAL Y 105 SHEET 4 AB6 4 THR Y 98 PHE Y 99 -1 O THR Y 98 N GLN Y 91 SHEET 1 AB7 4 SER Y 115 PHE Y 119 0 SHEET 2 AB7 4 THR Y 130 PHE Y 140 -1 O LEU Y 136 N PHE Y 117 SHEET 3 AB7 4 TYR Y 174 SER Y 183 -1 O LEU Y 180 N VAL Y 133 SHEET 4 AB7 4 SER Y 160 VAL Y 164 -1 N SER Y 163 O SER Y 177 SHEET 1 AB8 4 ALA Y 154 LEU Y 155 0 SHEET 2 AB8 4 LYS Y 146 VAL Y 151 -1 N VAL Y 151 O ALA Y 154 SHEET 3 AB8 4 VAL Y 192 THR Y 198 -1 O GLU Y 196 N GLN Y 148 SHEET 4 AB8 4 VAL Y 206 ASN Y 211 -1 O VAL Y 206 N VAL Y 197 SHEET 1 AB9 4 MET Z 5 SER Z 8 0 SHEET 2 AB9 4 VAL Z 20 ALA Z 26 -1 O ARG Z 25 N THR Z 6 SHEET 3 AB9 4 ASP Z 71 ILE Z 76 -1 O LEU Z 74 N ILE Z 22 SHEET 4 AB9 4 PHE Z 63 SER Z 68 -1 N SER Z 68 O ASP Z 71 SHEET 1 AC1 6 SER Z 11 SER Z 15 0 SHEET 2 AC1 6 THR Z 103 LYS Z 108 1 O LYS Z 108 N ALA Z 14 SHEET 3 AC1 6 ALA Z 85 GLN Z 91 -1 N ALA Z 85 O VAL Z 105 SHEET 4 AC1 6 VAL Z 34 GLN Z 39 -1 N GLN Z 39 O THR Z 86 SHEET 5 AC1 6 LYS Z 46 TYR Z 50 -1 O LEU Z 48 N TRP Z 36 SHEET 6 AC1 6 SER Z 54 LEU Z 55 -1 O SER Z 54 N TYR Z 50 SHEET 1 AC2 4 SER Z 11 SER Z 15 0 SHEET 2 AC2 4 THR Z 103 LYS Z 108 1 O LYS Z 108 N ALA Z 14 SHEET 3 AC2 4 ALA Z 85 GLN Z 91 -1 N ALA Z 85 O VAL Z 105 SHEET 4 AC2 4 THR Z 98 PHE Z 99 -1 O THR Z 98 N GLN Z 91 SHEET 1 AC3 4 SER Z 115 PHE Z 119 0 SHEET 2 AC3 4 THR Z 130 PHE Z 140 -1 O LEU Z 136 N PHE Z 117 SHEET 3 AC3 4 TYR Z 174 SER Z 183 -1 O LEU Z 180 N VAL Z 133 SHEET 4 AC3 4 SER Z 160 VAL Z 164 -1 N GLN Z 161 O THR Z 179 SHEET 1 AC4 4 ALA Z 154 LEU Z 155 0 SHEET 2 AC4 4 LYS Z 146 VAL Z 151 -1 N VAL Z 151 O ALA Z 154 SHEET 3 AC4 4 VAL Z 192 THR Z 198 -1 O THR Z 198 N LYS Z 146 SHEET 4 AC4 4 VAL Z 206 ASN Z 211 -1 O VAL Z 206 N VAL Z 197 SSBOND 1 CYS A 25 CYS A 99 1555 1555 2.08 SSBOND 2 CYS A 153 CYS A 209 1555 1555 2.06 SSBOND 3 CYS H 25 CYS H 99 1555 1555 2.07 SSBOND 4 CYS H 153 CYS H 209 1555 1555 2.07 SSBOND 5 CYS Y 24 CYS Y 89 1555 1555 2.10 SSBOND 6 CYS Y 135 CYS Y 195 1555 1555 2.07 SSBOND 7 CYS Z 24 CYS Z 89 1555 1555 2.12 SSBOND 8 CYS Z 135 CYS Z 195 1555 1555 2.08 CISPEP 1 PHE A 159 PRO A 160 0 -3.16 CISPEP 2 GLU A 161 PRO A 162 0 0.18 CISPEP 3 PHE H 159 PRO H 160 0 -5.25 CISPEP 4 GLU H 161 PRO H 162 0 0.68 CISPEP 5 SER Y 8 PRO Y 9 0 -2.53 CISPEP 6 PHE Y 95 PRO Y 96 0 -5.14 CISPEP 7 TYR Y 141 PRO Y 142 0 2.76 CISPEP 8 SER Z 8 PRO Z 9 0 -3.47 CISPEP 9 TYR Z 141 PRO Z 142 0 2.22 CRYST1 87.613 110.042 131.079 90.00 90.00 90.00 P 21 2 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 0.011414 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009087 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007629 0.00000