HEADER SIGNALING PROTEIN 21-OCT-22 8BE5 TITLE CRYSTAL STRUCTURE OF SOS1-KRASG12V-NANOBODY22-NANOBODY75 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SON OF SEVENLESS HOMOLOG 1; COMPND 3 CHAIN: AAZA; COMPND 4 SYNONYM: SOS-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY75; COMPND 8 CHAIN: C; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ISOFORM 2B OF GTPASE KRAS; COMPND 12 CHAIN: R; COMPND 13 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS; COMPND 14 EC: 3.6.5.2; COMPND 15 ENGINEERED: YES; COMPND 16 MUTATION: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: NANOBODY22; COMPND 19 CHAIN: N; COMPND 20 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: SOS1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; 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_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: KRAS, KRAS2, RASK2; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 22 ORGANISM_TAXID: 9844; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, STABILIZER, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.FISCHER,A.WOHLKONIG,J.STEYAERT JRNL AUTH B.FISCHER,A.WOHLKONIG,J.STEYAERT JRNL TITL CHILL & DISCO TO DISCOVER NANOBODIES THAT MODULATE JRNL TITL 2 PROTEIN-PROTEIN INTERACTIONS AND TUNE THE SOS-RAS NUCLEOTIDE JRNL TITL 3 EXCHANGE RATE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.13 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.13 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 28506 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.278 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1426 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 29.9100 - 6.7300 1.00 2916 154 0.2019 0.2539 REMARK 3 2 6.7300 - 5.3500 1.00 2777 146 0.2470 0.2984 REMARK 3 3 5.3500 - 4.6800 1.00 2747 145 0.1977 0.2435 REMARK 3 4 4.6800 - 4.2500 1.00 2716 143 0.1849 0.2465 REMARK 3 5 4.2500 - 3.9500 1.00 2697 142 0.2115 0.2653 REMARK 3 6 3.9500 - 3.7100 1.00 2680 141 0.2335 0.2872 REMARK 3 7 3.7100 - 3.5300 1.00 2678 141 0.2787 0.3244 REMARK 3 8 3.5300 - 3.3700 1.00 2668 140 0.2825 0.3625 REMARK 3 9 3.3700 - 3.2400 1.00 2675 141 0.3008 0.3470 REMARK 3 10 3.2400 - 3.1300 0.95 2526 133 0.3854 0.3959 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) : 0.514 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.540 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 99.89 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.56 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 : 0.011 6553 REMARK 3 ANGLE : 1.381 8854 REMARK 3 CHIRALITY : 0.080 978 REMARK 3 PLANARITY : 0.012 1138 REMARK 3 DIHEDRAL : 16.855 2482 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 8BE5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292126210. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-DEC-17 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 : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96858 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28523 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.130 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 10.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.6500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32 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: PHENIX REMARK 200 STARTING MODEL: 1BKD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 0.1 M SODIUM CITRATE, PH REMARK 280 5.5 AND 0.2 M SODIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 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 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+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 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 62.04000 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 204.40750 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 62.04000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 204.40750 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 62.04000 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 204.40750 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 62.04000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 204.40750 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 62.04000 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 204.40750 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 62.04000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 204.40750 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 62.04000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 204.40750 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 62.04000 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 62.04000 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 204.40750 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAZA, C, R, N 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 MET A 543 REMARK 465 GLY A 544 REMARK 465 SER A 545 REMARK 465 SER A 546 REMARK 465 HIS A 547 REMARK 465 HIS A 548 REMARK 465 HIS A 549 REMARK 465 HIS A 550 REMARK 465 HIS A 551 REMARK 465 HIS A 552 REMARK 465 SER A 553 REMARK 465 SER A 554 REMARK 465 GLY A 555 REMARK 465 LEU A 556 REMARK 465 VAL A 557 REMARK 465 PRO A 558 REMARK 465 ARG A 559 REMARK 465 GLY A 560 REMARK 465 SER A 561 REMARK 465 HIS A 562 REMARK 465 MET A 563 REMARK 465 GLU A 564 REMARK 465 GLU A 565 REMARK 465 GLN A 566 REMARK 465 MET A 567 REMARK 465 ARG A 568 REMARK 465 LEU A 569 REMARK 465 MET A 592 REMARK 465 GLN A 593 REMARK 465 PRO A 594 REMARK 465 LYS A 595 REMARK 465 GLU A 654 REMARK 465 PRO A 655 REMARK 465 THR A 656 REMARK 465 GLU A 657 REMARK 465 ALA A 658 REMARK 465 ASP A 659 REMARK 465 ARG A 660 REMARK 465 ILE A 661 REMARK 465 ALA A 662 REMARK 465 ILE A 663 REMARK 465 GLU A 664 REMARK 465 ASN A 665 REMARK 465 GLY A 666 REMARK 465 ASP A 667 REMARK 465 GLN A 668 REMARK 465 PRO A 669 REMARK 465 LEU A 670 REMARK 465 ARG A 744 REMARK 465 ASP A 745 REMARK 465 ASN A 746 REMARK 465 GLY A 747 REMARK 465 PRO A 748 REMARK 465 GLY A 749 REMARK 465 HIS A 750 REMARK 465 ASN A 751 REMARK 465 ASN A 1044 REMARK 465 PRO A 1045 REMARK 465 ARG A 1046 REMARK 465 PRO A 1047 REMARK 465 GLY A 1048 REMARK 465 THR A 1049 REMARK 465 GLN C 1 REMARK 465 LEU C 11 REMARK 465 VAL C 12 REMARK 465 GLN C 13 REMARK 465 ALA C 14 REMARK 465 GLY C 15 REMARK 465 GLY C 16 REMARK 465 SER C 17 REMARK 465 LEU C 18 REMARK 465 ASN C 27 REMARK 465 GLN C 39 REMARK 465 THR C 40 REMARK 465 PRO C 41 REMARK 465 GLY C 42 REMARK 465 VAL C 68 REMARK 465 LYS C 69 REMARK 465 GLY C 70 REMARK 465 ARG C 71 REMARK 465 PHE C 72 REMARK 465 THR C 73 REMARK 465 ILE C 74 REMARK 465 SER C 75 REMARK 465 GLY C 76 REMARK 465 ASP C 77 REMARK 465 ASN C 78 REMARK 465 ALA C 79 REMARK 465 LYS C 80 REMARK 465 ASN C 81 REMARK 465 THR C 82 REMARK 465 VAL C 83 REMARK 465 TYR C 84 REMARK 465 LEU C 85 REMARK 465 GLN C 86 REMARK 465 MET C 87 REMARK 465 SER C 88 REMARK 465 SER C 89 REMARK 465 LEU C 90 REMARK 465 LYS C 91 REMARK 465 PRO C 92 REMARK 465 GLU C 93 REMARK 465 ASP C 94 REMARK 465 THR C 95 REMARK 465 VAL C 124 REMARK 465 SER C 125 REMARK 465 SER C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 HIS C 131 REMARK 465 HIS C 132 REMARK 465 GLU C 133 REMARK 465 PRO C 134 REMARK 465 GLU C 135 REMARK 465 ALA C 136 REMARK 465 MET R -20 REMARK 465 GLY R -19 REMARK 465 SER R -18 REMARK 465 SER R -17 REMARK 465 HIS R -16 REMARK 465 HIS R -15 REMARK 465 HIS R -14 REMARK 465 HIS R -13 REMARK 465 HIS R -12 REMARK 465 HIS R -11 REMARK 465 SER R -10 REMARK 465 SER R -9 REMARK 465 GLY R -8 REMARK 465 GLU R -7 REMARK 465 ASN R -6 REMARK 465 LEU R -5 REMARK 465 TYR R -4 REMARK 465 PHE R -3 REMARK 465 GLN R -2 REMARK 465 GLY R -1 REMARK 465 SER R 0 REMARK 465 ASN R 26 REMARK 465 HIS R 27 REMARK 465 PHE R 28 REMARK 465 VAL R 29 REMARK 465 ASP R 30 REMARK 465 LYS R 165 REMARK 465 HIS R 166 REMARK 465 LYS R 167 REMARK 465 GLU R 168 REMARK 465 LYS R 169 REMARK 465 GLN N 1 REMARK 465 VAL N 2 REMARK 465 GLY N 26 REMARK 465 ASP N 27 REMARK 465 ILE N 28 REMARK 465 VAL N 29 REMARK 465 HIS N 116 REMARK 465 HIS N 117 REMARK 465 HIS N 118 REMARK 465 HIS N 119 REMARK 465 HIS N 120 REMARK 465 GLU N 121 REMARK 465 PRO N 122 REMARK 465 GLU N 123 REMARK 465 ALA N 124 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 SERZA 582 166.55 179.68 REMARK 500 ILEZA 598 120.07 -170.15 REMARK 500 PHEZA 677 33.77 -63.56 REMARK 500 ARGZA 678 -45.77 -153.41 REMARK 500 TYRZA 681 -88.34 -112.26 REMARK 500 HISZA 700 39.16 -140.55 REMARK 500 LYSZA 724 1.39 -64.31 REMARK 500 LYSZA 727 11.15 -62.84 REMARK 500 LYSZA 741 39.40 -96.12 REMARK 500 SERZA 756 -167.14 -107.14 REMARK 500 ILEZA 765 -61.08 -109.31 REMARK 500 HISZA 770 69.15 -112.75 REMARK 500 SERZA 807 24.98 47.98 REMARK 500 HISZA 951 -2.05 69.39 REMARK 500 GLUZA1017 86.64 -157.77 REMARK 500 PROZA1021 -71.92 -59.31 REMARK 500 LEUZA1035 70.07 -107.70 REMARK 500 PROZA1042 -158.06 -79.67 REMARK 500 SER C 7 -164.23 -162.30 REMARK 500 CYS C 22 41.64 -152.50 REMARK 500 ALA C 49 138.91 -172.38 REMARK 500 SER C 54 101.44 60.80 REMARK 500 VAL C 65 -62.01 -92.76 REMARK 500 ASP C 66 70.28 -157.47 REMARK 500 LEU C 102 109.52 -163.16 REMARK 500 PRO C 108 -7.78 -59.66 REMARK 500 THR C 120 56.58 -147.00 REMARK 500 ASP R 38 -8.60 -59.03 REMARK 500 ASP R 92 0.01 -66.47 REMARK 500 ASP R 105 65.94 76.56 REMARK 500 PRO R 121 -169.17 -101.61 REMARK 500 LYS R 147 20.58 -60.94 REMARK 500 THR R 148 -1.31 -155.91 REMARK 500 ARG R 149 8.40 53.49 REMARK 500 SER N 17 58.36 -145.63 REMARK 500 PRO N 53 -15.42 -49.93 REMARK 500 SER N 56 -164.03 -166.64 REMARK 500 ASN N 73 -36.63 -39.13 REMARK 500 LYS N 76 69.42 -51.43 REMARK 500 GLN N 99 -64.40 -108.17 REMARK 500 REMARK 500 REMARK: NULL DBREF 8BE5ZA 564 1049 UNP Q07889 SOS1_HUMAN 564 1049 DBREF 8BE5 C 1 136 PDB 8BE5 8BE5 1 136 DBREF 8BE5 R 1 169 UNP P01116-2 RASK_HUMAN 1 169 DBREF 8BE5 N 1 124 PDB 8BE5 8BE5 1 124 SEQADV 8BE5 METZA 543 UNP Q07889 INITIATING METHIONINE SEQADV 8BE5 GLYZA 544 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 SERZA 545 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 SERZA 546 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 547 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 548 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 549 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 550 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 551 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 552 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 SERZA 553 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 SERZA 554 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 GLYZA 555 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 LEUZA 556 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 VALZA 557 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 PROZA 558 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 ARGZA 559 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 GLYZA 560 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 SERZA 561 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 HISZA 562 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 METZA 563 UNP Q07889 EXPRESSION TAG SEQADV 8BE5 MET R -20 UNP P01116-2 INITIATING METHIONINE SEQADV 8BE5 GLY R -19 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 SER R -18 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 SER R -17 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -16 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -15 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -14 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -13 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -12 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 HIS R -11 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 SER R -10 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 SER R -9 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 GLY R -8 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 GLU R -7 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 ASN R -6 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 LEU R -5 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 TYR R -4 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 PHE R -3 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 GLN R -2 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 GLY R -1 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 SER R 0 UNP P01116-2 EXPRESSION TAG SEQADV 8BE5 VAL R 12 UNP P01116-2 GLY 12 ENGINEERED MUTATION SEQRES 1ZA 507 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2ZA 507 LEU VAL PRO ARG GLY SER HIS MET GLU GLU GLN MET ARG SEQRES 3ZA 507 LEU PRO SER ALA ASP VAL TYR ARG PHE ALA GLU PRO ASP SEQRES 4ZA 507 SER GLU GLU ASN ILE ILE PHE GLU GLU ASN MET GLN PRO SEQRES 5ZA 507 LYS ALA GLY ILE PRO ILE ILE LYS ALA GLY THR VAL ILE SEQRES 6ZA 507 LYS LEU ILE GLU ARG LEU THR TYR HIS MET TYR ALA ASP SEQRES 7ZA 507 PRO ASN PHE VAL ARG THR PHE LEU THR THR TYR ARG SER SEQRES 8ZA 507 PHE CYS LYS PRO GLN GLU LEU LEU SER LEU ILE ILE GLU SEQRES 9ZA 507 ARG PHE GLU ILE PRO GLU PRO GLU PRO THR GLU ALA ASP SEQRES 10ZA 507 ARG ILE ALA ILE GLU ASN GLY ASP GLN PRO LEU SER ALA SEQRES 11ZA 507 GLU LEU LYS ARG PHE ARG LYS GLU TYR ILE GLN PRO VAL SEQRES 12ZA 507 GLN LEU ARG VAL LEU ASN VAL CYS ARG HIS TRP VAL GLU SEQRES 13ZA 507 HIS HIS PHE TYR ASP PHE GLU ARG ASP ALA TYR LEU LEU SEQRES 14ZA 507 GLN ARG MET GLU GLU PHE ILE GLY THR VAL ARG GLY LYS SEQRES 15ZA 507 ALA MET LYS LYS TRP VAL GLU SER ILE THR LYS ILE ILE SEQRES 16ZA 507 GLN ARG LYS LYS ILE ALA ARG ASP ASN GLY PRO GLY HIS SEQRES 17ZA 507 ASN ILE THR PHE GLN SER SER PRO PRO THR VAL GLU TRP SEQRES 18ZA 507 HIS ILE SER ARG PRO GLY HIS ILE GLU THR PHE ASP LEU SEQRES 19ZA 507 LEU THR LEU HIS PRO ILE GLU ILE ALA ARG GLN LEU THR SEQRES 20ZA 507 LEU LEU GLU SER ASP LEU TYR ARG ALA VAL GLN PRO SER SEQRES 21ZA 507 GLU LEU VAL GLY SER VAL TRP THR LYS GLU ASP LYS GLU SEQRES 22ZA 507 ILE ASN SER PRO ASN LEU LEU LYS MET ILE ARG HIS THR SEQRES 23ZA 507 THR ASN LEU THR LEU TRP PHE GLU LYS CYS ILE VAL GLU SEQRES 24ZA 507 THR GLU ASN LEU GLU GLU ARG VAL ALA VAL VAL SER ARG SEQRES 25ZA 507 ILE ILE GLU ILE LEU GLN VAL PHE GLN GLU LEU ASN ASN SEQRES 26ZA 507 PHE ASN GLY VAL LEU GLU VAL VAL SER ALA MET ASN SER SEQRES 27ZA 507 SER PRO VAL TYR ARG LEU ASP HIS THR PHE GLU GLN ILE SEQRES 28ZA 507 PRO SER ARG GLN LYS LYS ILE LEU GLU GLU ALA HIS GLU SEQRES 29ZA 507 LEU SER GLU ASP HIS TYR LYS LYS TYR LEU ALA LYS LEU SEQRES 30ZA 507 ARG SER ILE ASN PRO PRO CYS VAL PRO PHE PHE GLY ILE SEQRES 31ZA 507 TYR LEU THR ASN ILE LEU LYS THR GLU GLU GLY ASN PRO SEQRES 32ZA 507 GLU VAL LEU LYS ARG HIS GLY LYS GLU LEU ILE ASN PHE SEQRES 33ZA 507 SER LYS ARG ARG LYS VAL ALA GLU ILE THR GLY GLU ILE SEQRES 34ZA 507 GLN GLN TYR GLN ASN GLN PRO TYR CYS LEU ARG VAL GLU SEQRES 35ZA 507 SER ASP ILE LYS ARG PHE PHE GLU ASN LEU ASN PRO MET SEQRES 36ZA 507 GLY ASN SER MET GLU LYS GLU PHE THR ASP TYR LEU PHE SEQRES 37ZA 507 ASN LYS SER LEU GLU ILE GLU PRO ARG ASN PRO LYS PRO SEQRES 38ZA 507 LEU PRO ARG PHE PRO LYS LYS TYR SER TYR PRO LEU LYS SEQRES 39ZA 507 SER PRO GLY VAL ARG PRO SER ASN PRO ARG PRO GLY THR SEQRES 1 C 136 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 136 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 136 ASN ILE LEU PRO ILE ASN VAL MET GLY TRP TYR ARG GLN SEQRES 4 C 136 THR PRO GLY SER GLN ARG GLU LEU VAL ALA THR ILE VAL SEQRES 5 C 136 THR SER GLY GLY SER THR ALA GLY ASN THR ASN TYR VAL SEQRES 6 C 136 ASP SER VAL LYS GLY ARG PHE THR ILE SER GLY ASP ASN SEQRES 7 C 136 ALA LYS ASN THR VAL TYR LEU GLN MET SER SER LEU LYS SEQRES 8 C 136 PRO GLU ASP THR ALA VAL TYR TYR CYS ASN LEU LYS THR SEQRES 9 C 136 ARG ARG ALA PRO TRP ALA THR PRO ASN ASN TYR TRP GLY SEQRES 10 C 136 GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS SEQRES 11 C 136 HIS HIS GLU PRO GLU ALA SEQRES 1 R 190 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 R 190 GLU ASN LEU TYR PHE GLN GLY SER MET THR GLU TYR LYS SEQRES 3 R 190 LEU VAL VAL VAL GLY ALA VAL GLY VAL GLY LYS SER ALA SEQRES 4 R 190 LEU THR ILE GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU SEQRES 5 R 190 TYR ASP PRO THR ILE GLU ASP SER TYR ARG LYS GLN VAL SEQRES 6 R 190 VAL ILE ASP GLY GLU THR CYS LEU LEU ASP ILE LEU ASP SEQRES 7 R 190 THR ALA GLY GLN GLU GLU TYR SER ALA MET ARG ASP GLN SEQRES 8 R 190 TYR MET ARG THR GLY GLU GLY PHE LEU CYS VAL PHE ALA SEQRES 9 R 190 ILE ASN ASN THR LYS SER PHE GLU ASP ILE HIS HIS TYR SEQRES 10 R 190 ARG GLU GLN ILE LYS ARG VAL LYS ASP SER GLU ASP VAL SEQRES 11 R 190 PRO MET VAL LEU VAL GLY ASN LYS CYS ASP LEU PRO SER SEQRES 12 R 190 ARG THR VAL ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SEQRES 13 R 190 SER TYR GLY ILE PRO PHE ILE GLU THR SER ALA LYS THR SEQRES 14 R 190 ARG GLN GLY VAL ASP ASP ALA PHE TYR THR LEU VAL ARG SEQRES 15 R 190 GLU ILE ARG LYS HIS LYS GLU LYS SEQRES 1 N 124 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 124 ALA GLU GLY SER LEU ARG LEU SER CYS LEU VAL SER GLY SEQRES 3 N 124 ASP ILE VAL ARG SER ASN LEU MET GLY TRP TYR ARG GLN SEQRES 4 N 124 ALA PRO GLY LYS GLN ARG GLU PHE VAL ALA ARG ILE ASN SEQRES 5 N 124 PRO THR GLY SER ALA ASN TYR ALA ASP SER VAL ARG GLY SEQRES 6 N 124 ARG PHE THR ILE SER LYS ASP ASN SER LYS LYS THR LEU SEQRES 7 N 124 TYR LEU GLN MET GLY SER LEU GLN PRO GLU ASP THR ALA SEQRES 8 N 124 VAL TYR TYR CYS ARG LEU ILE GLN ASN ARG ASP TYR TRP SEQRES 9 N 124 GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS HIS SEQRES 10 N 124 HIS HIS HIS GLU PRO GLU ALA FORMUL 5 HOH *19(H2 O) HELIX 1 AA1 TYRZA 575 GLUZA 579 5 5 HELIX 2 AA2 THRZA 605 THRZA 614 1 10 HELIX 3 AA3 ASPZA 620 TYRZA 631 1 12 HELIX 4 AA4 ARGZA 632 PHEZA 634 5 3 HELIX 5 AA5 LYSZA 636 ARGZA 647 1 12 HELIX 6 AA6 LYSZA 675 GLUZA 680 1 6 HELIX 7 AA7 TYRZA 681 HISZA 700 1 20 HELIX 8 AA8 PHEZA 701 ARGZA 706 1 6 HELIX 9 AA9 ASPZA 707 VALZA 721 1 15 HELIX 10 AB1 LYSZA 728 LYSZA 741 1 14 HELIX 11 AB2 HISZA 770 PHEZA 774 5 5 HELIX 12 AB3 HISZA 780 ALAZA 798 1 19 HELIX 13 AB4 VALZA 799 LEUZA 804 5 6 HELIX 14 AB5 SERZA 807 LYSZA 811 5 5 HELIX 15 AB6 ASPZA 813 SERZA 818 1 6 HELIX 16 AB7 SERZA 818 GLUZA 841 1 24 HELIX 17 AB8 ASNZA 844 LEUZA 865 1 22 HELIX 18 AB9 ASNZA 867 SERZA 880 1 14 HELIX 19 AC1 SERZA 880 ARGZA 885 1 6 HELIX 20 AC2 LEUZA 886 GLUZA 891 1 6 HELIX 21 AC3 PROZA 894 ILEZA 922 1 29 HELIX 22 AC4 PHEZA 930 GLYZA 943 1 14 HELIX 23 AC5 PHEZA 958 TYRZA 974 1 17 HELIX 24 AC6 GLUZA 984 ASNZA 993 1 10 HELIX 25 AC7 METZA 1001 GLUZA 1017 1 17 HELIX 26 AC8 GLY R 15 GLN R 25 1 11 HELIX 27 AC9 ILE R 36 SER R 39 5 4 HELIX 28 AD1 TYR R 64 ALA R 66 5 3 HELIX 29 AD2 MET R 67 THR R 74 1 8 HELIX 30 AD3 ASN R 86 ASP R 92 1 7 HELIX 31 AD4 ASP R 92 ASP R 105 1 14 HELIX 32 AD5 ASP R 126 GLY R 138 1 13 HELIX 33 AD6 LYS R 147 ARG R 149 5 3 HELIX 34 AD7 GLY R 151 ARG R 164 1 14 HELIX 35 AD8 ASP N 61 ARG N 64 5 4 SHEET 1 AA1 3 ILEZA 586 PHEZA 588 0 SHEET 2 AA1 3 ILEZA 601 GLYZA 604 -1 O LYSZA 602 N ILEZA 587 SHEET 3 AA1 3 ILEZA 956 ASNZA 957 -1 O ILEZA 956 N GLYZA 604 SHEET 1 AA2 2 LYSZA 949 ARGZA 950 0 SHEET 2 AA2 2 LYSZA 953 GLUZA 954 -1 O LYSZA 953 N ARGZA 950 SHEET 1 AA3 2 GLN C 3 LEU C 4 0 SHEET 2 AA3 2 ALA C 24 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 1 AA4 4 THR C 62 TYR C 64 0 SHEET 2 AA4 4 GLU C 46 THR C 53 -1 N THR C 50 O ASN C 63 SHEET 3 AA4 4 ILE C 31 ARG C 38 -1 N TRP C 36 O ALA C 49 SHEET 4 AA4 4 TYR C 99 CYS C 100 -1 O TYR C 99 N TYR C 37 SHEET 1 AA5 4 THR C 62 TYR C 64 0 SHEET 2 AA5 4 GLU C 46 THR C 53 -1 N THR C 50 O ASN C 63 SHEET 3 AA5 4 ILE C 31 ARG C 38 -1 N TRP C 36 O ALA C 49 SHEET 4 AA5 4 LYS C 103 ARG C 105 -1 O LYS C 103 N VAL C 33 SHEET 1 AA6 6 ARG R 41 ILE R 46 0 SHEET 2 AA6 6 GLU R 49 ASP R 57 -1 O LEU R 53 N LYS R 42 SHEET 3 AA6 6 THR R 2 GLY R 10 1 N LEU R 6 O LEU R 56 SHEET 4 AA6 6 GLY R 77 ALA R 83 1 O VAL R 81 N VAL R 9 SHEET 5 AA6 6 MET R 111 LYS R 117 1 O ASN R 116 N PHE R 82 SHEET 6 AA6 6 PHE R 141 SER R 145 1 O THR R 144 N GLY R 115 SHEET 1 AA7 2 VAL N 12 GLN N 13 0 SHEET 2 AA7 2 VAL N 112 SER N 113 1 O SER N 113 N VAL N 12 SHEET 1 AA8 3 ARG N 19 LEU N 20 0 SHEET 2 AA8 3 LEU N 78 MET N 82 -1 O LEU N 80 N LEU N 20 SHEET 3 AA8 3 PHE N 67 LYS N 71 -1 N THR N 68 O GLN N 81 SHEET 1 AA9 5 ALA N 57 TYR N 59 0 SHEET 2 AA9 5 GLU N 46 ILE N 51 -1 N ARG N 50 O ASN N 58 SHEET 3 AA9 5 LEU N 33 GLN N 39 -1 N TRP N 36 O ALA N 49 SHEET 4 AA9 5 ALA N 91 ILE N 98 -1 O TYR N 94 N TYR N 37 SHEET 5 AA9 5 ASP N 102 TYR N 103 -1 O TYR N 103 N LEU N 97 SHEET 1 AB1 5 ALA N 57 TYR N 59 0 SHEET 2 AB1 5 GLU N 46 ILE N 51 -1 N ARG N 50 O ASN N 58 SHEET 3 AB1 5 LEU N 33 GLN N 39 -1 N TRP N 36 O ALA N 49 SHEET 4 AB1 5 ALA N 91 ILE N 98 -1 O TYR N 94 N TYR N 37 SHEET 5 AB1 5 THR N 108 VAL N 110 -1 O THR N 108 N TYR N 93 SSBOND 1 CYS C 22 CYS C 100 1555 1555 2.02 SSBOND 2 CYS N 22 CYS N 95 1555 1555 2.01 CISPEP 1 PROZA 924 PROZA 925 0 23.26 CRYST1 124.080 124.080 408.815 90.00 90.00 90.00 I 4 2 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 0.008059 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008059 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002446 0.00000