HEADER TRANSCRIPTION 27-APR-21 7OCJ TITLE CRYSTAL STRUCTURE OF E.COLI LEXA IN COMPLEX WITH NANOBODY TITLE 2 NBSOS2(NB14509) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NBSOS2 (14509); COMPND 3 CHAIN: G, E, B, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LEXA REPRESSOR; COMPND 7 CHAIN: A, C, D, F; COMPND 8 EC: 3.4.21.88; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: MISSING RESIDUES ARE NOT VISIBLE IN THE ELECTRON COMPND 11 DENSITY MAPS SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 8 ORGANISM_TAXID: 562; SOURCE 9 GENE: LEXA, EAMG_02325; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TRANSCRIPTIONAL REPRESSOR DNA BINDING AUTOPROTEOLYSIS NANOBODIES, KEYWDS 2 TRANSCRIPTION EXPDTA X-RAY DIFFRACTION AUTHOR L.MASO,F.VASCON,M.CHINELLATO,E.PARDON,J.STEYAERT,A.ANGELINI,D.TONDI, AUTHOR 2 L.CENDRON JRNL AUTH L.MASO,F.VASCON,M.CHINELLATO,F.GOORMAGHTIGH,P.BELLIO, JRNL AUTH 2 E.CAMPAGNARO,L.VAN MELDEREN,M.RUZZENE,E.PARDON,A.ANGELINI, JRNL AUTH 3 G.CELENZA,J.STEYAERT,D.TONDI,L.CENDRON JRNL TITL NANOBODIES TARGETING LEXA AUTOCLEAVAGE DISCLOSE A NOVEL JRNL TITL 2 SUPPRESSION STRATEGY OF SOS-RESPONSE PATHWAY. JRNL REF STRUCTURE 2022 JRNL REFN ISSN 0969-2126 JRNL PMID 36240773 JRNL DOI 10.1016/J.STR.2022.09.004 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18.2 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.25 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 3 NUMBER OF REFLECTIONS : 28566 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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) : NULL 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) : 47.61 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 : 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: NULL REMARK 4 REMARK 4 7OCJ 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_1292115478. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-APR-21 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 : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96546 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28568 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 48.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 7.400 REMARK 200 R MERGE (I) : 0.12600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.73000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1JHF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.27 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1 M SODIUM REMARK 280 ACETATE PH 4.5, 30 % W/V PEG8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.50067 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.25033 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 48.25033 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 96.50067 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A, C, 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: 2 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: 5960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, 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 MET A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 LYS A 2 REMARK 465 ALA A 3 REMARK 465 LEU A 4 REMARK 465 THR A 5 REMARK 465 ALA A 6 REMARK 465 ARG A 7 REMARK 465 GLN A 8 REMARK 465 GLN A 9 REMARK 465 GLU A 10 REMARK 465 VAL A 11 REMARK 465 PHE A 12 REMARK 465 ASP A 13 REMARK 465 LEU A 14 REMARK 465 ILE A 15 REMARK 465 ARG A 16 REMARK 465 ASP A 17 REMARK 465 HIS A 18 REMARK 465 ILE A 19 REMARK 465 SER A 20 REMARK 465 GLN A 21 REMARK 465 THR A 22 REMARK 465 GLY A 23 REMARK 465 MET A 24 REMARK 465 PRO A 25 REMARK 465 PRO A 26 REMARK 465 THR A 27 REMARK 465 ARG A 28 REMARK 465 ALA A 29 REMARK 465 GLU A 30 REMARK 465 ILE A 31 REMARK 465 ALA A 32 REMARK 465 GLN A 33 REMARK 465 ARG A 34 REMARK 465 LEU A 35 REMARK 465 GLY A 36 REMARK 465 PHE A 37 REMARK 465 ARG A 38 REMARK 465 SER A 39 REMARK 465 PRO A 40 REMARK 465 ASN A 41 REMARK 465 ALA A 42 REMARK 465 ALA A 43 REMARK 465 GLU A 44 REMARK 465 GLU A 45 REMARK 465 HIS A 46 REMARK 465 LEU A 47 REMARK 465 LYS A 48 REMARK 465 ALA A 49 REMARK 465 LEU A 50 REMARK 465 ALA A 51 REMARK 465 ARG A 52 REMARK 465 LYS A 53 REMARK 465 GLY A 54 REMARK 465 VAL A 55 REMARK 465 ILE A 56 REMARK 465 GLU A 57 REMARK 465 ILE A 58 REMARK 465 VAL A 59 REMARK 465 SER A 60 REMARK 465 GLY A 61 REMARK 465 ALA A 62 REMARK 465 SER A 63 REMARK 465 ARG A 64 REMARK 465 GLY A 65 REMARK 465 ILE A 66 REMARK 465 ARG A 67 REMARK 465 LEU A 68 REMARK 465 LEU A 69 REMARK 465 GLN A 70 REMARK 465 GLU A 71 REMARK 465 GLU A 72 REMARK 465 GLU A 73 REMARK 465 MET C -19 REMARK 465 GLY C -18 REMARK 465 SER C -17 REMARK 465 SER C -16 REMARK 465 HIS C -15 REMARK 465 HIS C -14 REMARK 465 HIS C -13 REMARK 465 HIS C -12 REMARK 465 HIS C -11 REMARK 465 HIS C -10 REMARK 465 SER C -9 REMARK 465 SER C -8 REMARK 465 GLY C -7 REMARK 465 LEU C -6 REMARK 465 VAL C -5 REMARK 465 PRO C -4 REMARK 465 ARG C -3 REMARK 465 GLY C -2 REMARK 465 SER C -1 REMARK 465 HIS C 0 REMARK 465 MET C 1 REMARK 465 LYS C 2 REMARK 465 ALA C 3 REMARK 465 LEU C 4 REMARK 465 THR C 5 REMARK 465 ALA C 6 REMARK 465 ARG C 7 REMARK 465 GLN C 8 REMARK 465 GLN C 9 REMARK 465 GLU C 10 REMARK 465 VAL C 11 REMARK 465 PHE C 12 REMARK 465 ASP C 13 REMARK 465 LEU C 14 REMARK 465 ILE C 15 REMARK 465 ARG C 16 REMARK 465 ASP C 17 REMARK 465 HIS C 18 REMARK 465 ILE C 19 REMARK 465 SER C 20 REMARK 465 GLN C 21 REMARK 465 THR C 22 REMARK 465 GLY C 23 REMARK 465 MET C 24 REMARK 465 PRO C 25 REMARK 465 PRO C 26 REMARK 465 THR C 27 REMARK 465 ARG C 28 REMARK 465 ALA C 29 REMARK 465 GLU C 30 REMARK 465 ILE C 31 REMARK 465 ALA C 32 REMARK 465 GLN C 33 REMARK 465 ARG C 34 REMARK 465 LEU C 35 REMARK 465 GLY C 36 REMARK 465 PHE C 37 REMARK 465 ARG C 38 REMARK 465 SER C 39 REMARK 465 PRO C 40 REMARK 465 ASN C 41 REMARK 465 ALA C 42 REMARK 465 ALA C 43 REMARK 465 GLU C 44 REMARK 465 GLU C 45 REMARK 465 HIS C 46 REMARK 465 LEU C 47 REMARK 465 LYS C 48 REMARK 465 ALA C 49 REMARK 465 LEU C 50 REMARK 465 ALA C 51 REMARK 465 ARG C 52 REMARK 465 LYS C 53 REMARK 465 GLY C 54 REMARK 465 VAL C 55 REMARK 465 ILE C 56 REMARK 465 GLU C 57 REMARK 465 ILE C 58 REMARK 465 VAL C 59 REMARK 465 SER C 60 REMARK 465 GLY C 61 REMARK 465 ALA C 62 REMARK 465 SER C 63 REMARK 465 ARG C 64 REMARK 465 GLY C 65 REMARK 465 ILE C 66 REMARK 465 ARG C 67 REMARK 465 LEU C 68 REMARK 465 LEU C 69 REMARK 465 GLN C 70 REMARK 465 GLU C 71 REMARK 465 GLU C 72 REMARK 465 MET D -19 REMARK 465 GLY D -18 REMARK 465 SER D -17 REMARK 465 SER D -16 REMARK 465 HIS D -15 REMARK 465 HIS D -14 REMARK 465 HIS D -13 REMARK 465 HIS D -12 REMARK 465 HIS D -11 REMARK 465 HIS D -10 REMARK 465 SER D -9 REMARK 465 SER D -8 REMARK 465 GLY D -7 REMARK 465 LEU D -6 REMARK 465 VAL D -5 REMARK 465 PRO D -4 REMARK 465 ARG D -3 REMARK 465 GLY D -2 REMARK 465 SER D -1 REMARK 465 HIS D 0 REMARK 465 MET D 1 REMARK 465 LYS D 2 REMARK 465 ALA D 3 REMARK 465 LEU D 4 REMARK 465 THR D 5 REMARK 465 ALA D 6 REMARK 465 ARG D 7 REMARK 465 GLN D 8 REMARK 465 GLN D 9 REMARK 465 GLU D 10 REMARK 465 VAL D 11 REMARK 465 PHE D 12 REMARK 465 ASP D 13 REMARK 465 LEU D 14 REMARK 465 ILE D 15 REMARK 465 ARG D 16 REMARK 465 ASP D 17 REMARK 465 HIS D 18 REMARK 465 ILE D 19 REMARK 465 SER D 20 REMARK 465 GLN D 21 REMARK 465 THR D 22 REMARK 465 GLY D 23 REMARK 465 MET D 24 REMARK 465 PRO D 25 REMARK 465 PRO D 26 REMARK 465 THR D 27 REMARK 465 ARG D 28 REMARK 465 ALA D 29 REMARK 465 GLU D 30 REMARK 465 ILE D 31 REMARK 465 ALA D 32 REMARK 465 GLN D 33 REMARK 465 ARG D 34 REMARK 465 LEU D 35 REMARK 465 GLY D 36 REMARK 465 PHE D 37 REMARK 465 ARG D 38 REMARK 465 SER D 39 REMARK 465 PRO D 40 REMARK 465 ASN D 41 REMARK 465 ALA D 42 REMARK 465 ALA D 43 REMARK 465 GLU D 44 REMARK 465 GLU D 45 REMARK 465 HIS D 46 REMARK 465 LEU D 47 REMARK 465 LYS D 48 REMARK 465 ALA D 49 REMARK 465 LEU D 50 REMARK 465 ALA D 51 REMARK 465 ARG D 52 REMARK 465 LYS D 53 REMARK 465 GLY D 54 REMARK 465 VAL D 55 REMARK 465 ILE D 56 REMARK 465 GLU D 57 REMARK 465 ILE D 58 REMARK 465 VAL D 59 REMARK 465 SER D 60 REMARK 465 GLY D 61 REMARK 465 ALA D 62 REMARK 465 SER D 63 REMARK 465 ARG D 64 REMARK 465 GLY D 65 REMARK 465 ILE D 66 REMARK 465 ARG D 67 REMARK 465 LEU D 68 REMARK 465 LEU D 69 REMARK 465 GLN D 70 REMARK 465 GLU D 71 REMARK 465 GLU D 72 REMARK 465 MET F -19 REMARK 465 GLY F -18 REMARK 465 SER F -17 REMARK 465 SER F -16 REMARK 465 HIS F -15 REMARK 465 HIS F -14 REMARK 465 HIS F -13 REMARK 465 HIS F -12 REMARK 465 HIS F -11 REMARK 465 HIS F -10 REMARK 465 SER F -9 REMARK 465 SER F -8 REMARK 465 GLY F -7 REMARK 465 LEU F -6 REMARK 465 VAL F -5 REMARK 465 PRO F -4 REMARK 465 ARG F -3 REMARK 465 GLY F -2 REMARK 465 SER F -1 REMARK 465 HIS F 0 REMARK 465 MET F 1 REMARK 465 LYS F 2 REMARK 465 ALA F 3 REMARK 465 LEU F 4 REMARK 465 THR F 5 REMARK 465 ALA F 6 REMARK 465 ARG F 7 REMARK 465 GLN F 8 REMARK 465 GLN F 9 REMARK 465 GLU F 10 REMARK 465 VAL F 11 REMARK 465 PHE F 12 REMARK 465 ASP F 13 REMARK 465 LEU F 14 REMARK 465 ILE F 15 REMARK 465 ARG F 16 REMARK 465 ASP F 17 REMARK 465 HIS F 18 REMARK 465 ILE F 19 REMARK 465 SER F 20 REMARK 465 GLN F 21 REMARK 465 THR F 22 REMARK 465 GLY F 23 REMARK 465 MET F 24 REMARK 465 PRO F 25 REMARK 465 PRO F 26 REMARK 465 THR F 27 REMARK 465 ARG F 28 REMARK 465 ALA F 29 REMARK 465 GLU F 30 REMARK 465 ILE F 31 REMARK 465 ALA F 32 REMARK 465 GLN F 33 REMARK 465 ARG F 34 REMARK 465 LEU F 35 REMARK 465 GLY F 36 REMARK 465 PHE F 37 REMARK 465 ARG F 38 REMARK 465 SER F 39 REMARK 465 PRO F 40 REMARK 465 ASN F 41 REMARK 465 ALA F 42 REMARK 465 ALA F 43 REMARK 465 GLU F 44 REMARK 465 GLU F 45 REMARK 465 HIS F 46 REMARK 465 LEU F 47 REMARK 465 LYS F 48 REMARK 465 ALA F 49 REMARK 465 LEU F 50 REMARK 465 ALA F 51 REMARK 465 ARG F 52 REMARK 465 LYS F 53 REMARK 465 GLY F 54 REMARK 465 VAL F 55 REMARK 465 ILE F 56 REMARK 465 GLU F 57 REMARK 465 ILE F 58 REMARK 465 VAL F 59 REMARK 465 SER F 60 REMARK 465 GLY F 61 REMARK 465 ALA F 62 REMARK 465 SER F 63 REMARK 465 ARG F 64 REMARK 465 GLY F 65 REMARK 465 ILE F 66 REMARK 465 ARG F 67 REMARK 465 LEU F 68 REMARK 465 LEU F 69 REMARK 465 GLN F 70 REMARK 465 GLU F 71 REMARK 465 GLY H 15 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 VAL G 48 -62.00 -105.11 REMARK 500 ASN G 76 35.98 71.25 REMARK 500 LEU A 89 33.40 -85.25 REMARK 500 GLU A 152 105.27 -161.14 REMARK 500 GLN A 161 79.48 -157.32 REMARK 500 ASN A 171 113.02 -161.93 REMARK 500 GLU C 170 62.84 -109.53 REMARK 500 ASN C 171 109.46 -172.44 REMARK 500 LEU C 181 1.26 -69.54 REMARK 500 ALA E 74 -169.63 -74.96 REMARK 500 ALA E 91 177.43 178.07 REMARK 500 SER E 114 -167.75 -101.81 REMARK 500 VAL B 48 -62.79 -95.47 REMARK 500 LYS B 75 -64.34 71.54 REMARK 500 ASN B 76 39.92 -88.26 REMARK 500 ALA B 91 171.34 179.80 REMARK 500 LEU B 100 23.82 48.78 REMARK 500 SER B 114 -160.22 -121.40 REMARK 500 GLU D 74 91.07 -170.04 REMARK 500 LEU D 89 45.70 -100.71 REMARK 500 ASN D 171 102.97 -162.47 REMARK 500 LEU F 89 40.94 -97.65 REMARK 500 GLU F 170 52.64 -116.15 REMARK 500 LEU F 181 4.13 -65.28 REMARK 500 VAL H 48 -64.10 -90.01 REMARK 500 ALA H 91 -168.61 -178.10 REMARK 500 LEU H 100 29.22 49.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7BG2 RELATED DB: PDB REMARK 900 7BG2 CONTAINS THE SAME LEXA DIMER IN COMPLEX WITH A DIFFERENT NB REMARK 900 RELATED ID: 7B5G RELATED DB: PDB REMARK 900 7B5G CONTAINS THE SAME LEXA DIMER IN COMPLEX WITH A DIFFERENT NB DBREF 7OCJ G 1 115 PDB 7OCJ 7OCJ 1 115 DBREF1 7OCJ A 1 202 UNP A0A1X3HXW2_ECOLX DBREF2 7OCJ A A0A1X3HXW2 1 202 DBREF1 7OCJ C 1 202 UNP A0A1X3HXW2_ECOLX DBREF2 7OCJ C A0A1X3HXW2 1 202 DBREF 7OCJ E 1 115 PDB 7OCJ 7OCJ 1 115 DBREF 7OCJ B 1 115 PDB 7OCJ 7OCJ 1 115 DBREF1 7OCJ D 1 202 UNP A0A1X3HXW2_ECOLX DBREF2 7OCJ D A0A1X3HXW2 1 202 DBREF1 7OCJ F 1 202 UNP A0A1X3HXW2_ECOLX DBREF2 7OCJ F A0A1X3HXW2 1 202 DBREF 7OCJ H 1 115 PDB 7OCJ 7OCJ 1 115 SEQADV 7OCJ MET A -19 UNP A0A1X3HXW INITIATING METHIONINE SEQADV 7OCJ GLY A -18 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER A -17 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER A -16 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -15 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -14 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -13 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -12 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -11 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A -10 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER A -9 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER A -8 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY A -7 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ LEU A -6 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ VAL A -5 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ PRO A -4 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ ARG A -3 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY A -2 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER A -1 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS A 0 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ MET C -19 UNP A0A1X3HXW INITIATING METHIONINE SEQADV 7OCJ GLY C -18 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER C -17 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER C -16 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -15 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -14 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -13 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -12 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -11 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C -10 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER C -9 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER C -8 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY C -7 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ LEU C -6 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ VAL C -5 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ PRO C -4 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ ARG C -3 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY C -2 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER C -1 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS C 0 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ MET D -19 UNP A0A1X3HXW INITIATING METHIONINE SEQADV 7OCJ GLY D -18 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER D -17 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER D -16 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -15 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -14 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -13 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -12 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -11 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D -10 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER D -9 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER D -8 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY D -7 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ LEU D -6 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ VAL D -5 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ PRO D -4 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ ARG D -3 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY D -2 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER D -1 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS D 0 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ MET F -19 UNP A0A1X3HXW INITIATING METHIONINE SEQADV 7OCJ GLY F -18 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER F -17 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER F -16 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -15 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -14 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -13 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -12 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -11 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F -10 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER F -9 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER F -8 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY F -7 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ LEU F -6 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ VAL F -5 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ PRO F -4 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ ARG F -3 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ GLY F -2 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ SER F -1 UNP A0A1X3HXW EXPRESSION TAG SEQADV 7OCJ HIS F 0 UNP A0A1X3HXW EXPRESSION TAG SEQRES 1 G 115 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 115 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 115 SER ILE ARG SER LEU ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 G 115 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 G 115 SER ARG GLY SER THR ARG TYR GLY ASP PHE VAL LYS GLY SEQRES 6 G 115 ARG PHE THR ILE SER ARG GLY ASN ALA LYS ASN THR VAL SEQRES 7 G 115 TYR LEU GLN MET ASN SER LEU SER VAL GLU ASP THR ALA SEQRES 8 G 115 VAL TYR TYR CYS LYS GLN THR GLN LEU GLY TYR ASP TYR SEQRES 9 G 115 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 A 222 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 222 LEU VAL PRO ARG GLY SER HIS MET LYS ALA LEU THR ALA SEQRES 3 A 222 ARG GLN GLN GLU VAL PHE ASP LEU ILE ARG ASP HIS ILE SEQRES 4 A 222 SER GLN THR GLY MET PRO PRO THR ARG ALA GLU ILE ALA SEQRES 5 A 222 GLN ARG LEU GLY PHE ARG SER PRO ASN ALA ALA GLU GLU SEQRES 6 A 222 HIS LEU LYS ALA LEU ALA ARG LYS GLY VAL ILE GLU ILE SEQRES 7 A 222 VAL SER GLY ALA SER ARG GLY ILE ARG LEU LEU GLN GLU SEQRES 8 A 222 GLU GLU GLU GLY LEU PRO LEU VAL GLY ARG VAL ALA ALA SEQRES 9 A 222 GLY GLU PRO LEU LEU ALA GLN GLN HIS ILE GLU GLY HIS SEQRES 10 A 222 TYR GLN VAL ASP PRO SER LEU PHE LYS PRO ASN ALA ASP SEQRES 11 A 222 PHE LEU LEU ARG VAL SER GLY MET SER MET LYS ASP ILE SEQRES 12 A 222 GLY ILE MET ASP GLY ASP LEU LEU ALA VAL HIS LYS THR SEQRES 13 A 222 GLN ASP VAL ARG ASN GLY GLN VAL VAL VAL ALA ARG ILE SEQRES 14 A 222 ASP ASP GLU VAL THR VAL LYS ARG LEU LYS LYS GLN GLY SEQRES 15 A 222 ASN LYS VAL GLU LEU LEU PRO GLU ASN SER GLU PHE LYS SEQRES 16 A 222 PRO ILE VAL VAL ASP LEU ARG GLN GLN SER PHE THR ILE SEQRES 17 A 222 GLU GLY LEU ALA VAL GLY VAL ILE ARG ASN GLY ASP TRP SEQRES 18 A 222 LEU SEQRES 1 C 222 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 C 222 LEU VAL PRO ARG GLY SER HIS MET LYS ALA LEU THR ALA SEQRES 3 C 222 ARG GLN GLN GLU VAL PHE ASP LEU ILE ARG ASP HIS ILE SEQRES 4 C 222 SER GLN THR GLY MET PRO PRO THR ARG ALA GLU ILE ALA SEQRES 5 C 222 GLN ARG LEU GLY PHE ARG SER PRO ASN ALA ALA GLU GLU SEQRES 6 C 222 HIS LEU LYS ALA LEU ALA ARG LYS GLY VAL ILE GLU ILE SEQRES 7 C 222 VAL SER GLY ALA SER ARG GLY ILE ARG LEU LEU GLN GLU SEQRES 8 C 222 GLU GLU GLU GLY LEU PRO LEU VAL GLY ARG VAL ALA ALA SEQRES 9 C 222 GLY GLU PRO LEU LEU ALA GLN GLN HIS ILE GLU GLY HIS SEQRES 10 C 222 TYR GLN VAL ASP PRO SER LEU PHE LYS PRO ASN ALA ASP SEQRES 11 C 222 PHE LEU LEU ARG VAL SER GLY MET SER MET LYS ASP ILE SEQRES 12 C 222 GLY ILE MET ASP GLY ASP LEU LEU ALA VAL HIS LYS THR SEQRES 13 C 222 GLN ASP VAL ARG ASN GLY GLN VAL VAL VAL ALA ARG ILE SEQRES 14 C 222 ASP ASP GLU VAL THR VAL LYS ARG LEU LYS LYS GLN GLY SEQRES 15 C 222 ASN LYS VAL GLU LEU LEU PRO GLU ASN SER GLU PHE LYS SEQRES 16 C 222 PRO ILE VAL VAL ASP LEU ARG GLN GLN SER PHE THR ILE SEQRES 17 C 222 GLU GLY LEU ALA VAL GLY VAL ILE ARG ASN GLY ASP TRP SEQRES 18 C 222 LEU SEQRES 1 E 115 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 115 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 115 SER ILE ARG SER LEU ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 E 115 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 E 115 SER ARG GLY SER THR ARG TYR GLY ASP PHE VAL LYS GLY SEQRES 6 E 115 ARG PHE THR ILE SER ARG GLY ASN ALA LYS ASN THR VAL SEQRES 7 E 115 TYR LEU GLN MET ASN SER LEU SER VAL GLU ASP THR ALA SEQRES 8 E 115 VAL TYR TYR CYS LYS GLN THR GLN LEU GLY TYR ASP TYR SEQRES 9 E 115 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 B 115 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 115 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 115 SER ILE ARG SER LEU ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 B 115 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 B 115 SER ARG GLY SER THR ARG TYR GLY ASP PHE VAL LYS GLY SEQRES 6 B 115 ARG PHE THR ILE SER ARG GLY ASN ALA LYS ASN THR VAL SEQRES 7 B 115 TYR LEU GLN MET ASN SER LEU SER VAL GLU ASP THR ALA SEQRES 8 B 115 VAL TYR TYR CYS LYS GLN THR GLN LEU GLY TYR ASP TYR SEQRES 9 B 115 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 D 222 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 D 222 LEU VAL PRO ARG GLY SER HIS MET LYS ALA LEU THR ALA SEQRES 3 D 222 ARG GLN GLN GLU VAL PHE ASP LEU ILE ARG ASP HIS ILE SEQRES 4 D 222 SER GLN THR GLY MET PRO PRO THR ARG ALA GLU ILE ALA SEQRES 5 D 222 GLN ARG LEU GLY PHE ARG SER PRO ASN ALA ALA GLU GLU SEQRES 6 D 222 HIS LEU LYS ALA LEU ALA ARG LYS GLY VAL ILE GLU ILE SEQRES 7 D 222 VAL SER GLY ALA SER ARG GLY ILE ARG LEU LEU GLN GLU SEQRES 8 D 222 GLU GLU GLU GLY LEU PRO LEU VAL GLY ARG VAL ALA ALA SEQRES 9 D 222 GLY GLU PRO LEU LEU ALA GLN GLN HIS ILE GLU GLY HIS SEQRES 10 D 222 TYR GLN VAL ASP PRO SER LEU PHE LYS PRO ASN ALA ASP SEQRES 11 D 222 PHE LEU LEU ARG VAL SER GLY MET SER MET LYS ASP ILE SEQRES 12 D 222 GLY ILE MET ASP GLY ASP LEU LEU ALA VAL HIS LYS THR SEQRES 13 D 222 GLN ASP VAL ARG ASN GLY GLN VAL VAL VAL ALA ARG ILE SEQRES 14 D 222 ASP ASP GLU VAL THR VAL LYS ARG LEU LYS LYS GLN GLY SEQRES 15 D 222 ASN LYS VAL GLU LEU LEU PRO GLU ASN SER GLU PHE LYS SEQRES 16 D 222 PRO ILE VAL VAL ASP LEU ARG GLN GLN SER PHE THR ILE SEQRES 17 D 222 GLU GLY LEU ALA VAL GLY VAL ILE ARG ASN GLY ASP TRP SEQRES 18 D 222 LEU SEQRES 1 F 222 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 F 222 LEU VAL PRO ARG GLY SER HIS MET LYS ALA LEU THR ALA SEQRES 3 F 222 ARG GLN GLN GLU VAL PHE ASP LEU ILE ARG ASP HIS ILE SEQRES 4 F 222 SER GLN THR GLY MET PRO PRO THR ARG ALA GLU ILE ALA SEQRES 5 F 222 GLN ARG LEU GLY PHE ARG SER PRO ASN ALA ALA GLU GLU SEQRES 6 F 222 HIS LEU LYS ALA LEU ALA ARG LYS GLY VAL ILE GLU ILE SEQRES 7 F 222 VAL SER GLY ALA SER ARG GLY ILE ARG LEU LEU GLN GLU SEQRES 8 F 222 GLU GLU GLU GLY LEU PRO LEU VAL GLY ARG VAL ALA ALA SEQRES 9 F 222 GLY GLU PRO LEU LEU ALA GLN GLN HIS ILE GLU GLY HIS SEQRES 10 F 222 TYR GLN VAL ASP PRO SER LEU PHE LYS PRO ASN ALA ASP SEQRES 11 F 222 PHE LEU LEU ARG VAL SER GLY MET SER MET LYS ASP ILE SEQRES 12 F 222 GLY ILE MET ASP GLY ASP LEU LEU ALA VAL HIS LYS THR SEQRES 13 F 222 GLN ASP VAL ARG ASN GLY GLN VAL VAL VAL ALA ARG ILE SEQRES 14 F 222 ASP ASP GLU VAL THR VAL LYS ARG LEU LYS LYS GLN GLY SEQRES 15 F 222 ASN LYS VAL GLU LEU LEU PRO GLU ASN SER GLU PHE LYS SEQRES 16 F 222 PRO ILE VAL VAL ASP LEU ARG GLN GLN SER PHE THR ILE SEQRES 17 F 222 GLU GLY LEU ALA VAL GLY VAL ILE ARG ASN GLY ASP TRP SEQRES 18 F 222 LEU SEQRES 1 H 115 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 115 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 115 SER ILE ARG SER LEU ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 H 115 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 H 115 SER ARG GLY SER THR ARG TYR GLY ASP PHE VAL LYS GLY SEQRES 6 H 115 ARG PHE THR ILE SER ARG GLY ASN ALA LYS ASN THR VAL SEQRES 7 H 115 TYR LEU GLN MET ASN SER LEU SER VAL GLU ASP THR ALA SEQRES 8 H 115 VAL TYR TYR CYS LYS GLN THR GLN LEU GLY TYR ASP TYR SEQRES 9 H 115 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HET EDO A 301 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 9 EDO C2 H6 O2 FORMUL 10 HOH *46(H2 O) HELIX 1 AA1 SER G 86 THR G 90 5 5 HELIX 2 AA2 ASP A 101 PHE A 105 5 5 HELIX 3 AA3 MET A 120 GLY A 124 5 5 HELIX 4 AA4 ASP C 101 PHE C 105 5 5 HELIX 5 AA5 MET C 120 GLY C 124 5 5 HELIX 6 AA6 SER B 86 THR B 90 5 5 HELIX 7 AA7 ALA D 90 GLN D 92 5 3 HELIX 8 AA8 ASP D 101 PHE D 105 5 5 HELIX 9 AA9 MET D 120 GLY D 124 5 5 HELIX 10 AB1 ALA F 90 GLN F 92 5 3 HELIX 11 AB2 ASP F 101 PHE F 105 5 5 HELIX 12 AB3 MET F 120 GLY F 124 5 5 HELIX 13 AB4 SER H 86 THR H 90 5 5 SHEET 1 AA1 4 VAL G 2 SER G 7 0 SHEET 2 AA1 4 LEU G 18 GLY G 26 -1 O SER G 25 N GLN G 3 SHEET 3 AA1 4 THR G 77 MET G 82 -1 O LEU G 80 N LEU G 20 SHEET 4 AA1 4 PHE G 67 ARG G 71 -1 N THR G 68 O GLN G 81 SHEET 1 AA2 3 GLY G 10 GLN G 13 0 SHEET 2 AA2 3 GLN G 110 SER G 114 1 O THR G 112 N VAL G 12 SHEET 3 AA2 3 ALA G 91 VAL G 92 -1 N ALA G 91 O VAL G 111 SHEET 1 AA330 ALA G 33 GLN G 39 0 SHEET 2 AA330 ARG G 45 THR G 52 -1 O GLU G 46 N ARG G 38 SHEET 3 AA330 THR G 57 TYR G 59 -1 O ARG G 58 N ALA G 50 SHEET 4 AA330 CYS G 95 GLN G 99 -1 O LYS G 96 N GLY G 35 SHEET 5 AA330 TYR G 102 TRP G 105 -1 O TYR G 102 N GLN G 99 SHEET 6 AA330 LEU A 76 VAL A 79 0 SHEET 7 AA330 ILE A 94 TYR A 98 -1 O TYR A 98 N LEU A 76 SHEET 8 AA330 PHE A 111 ARG A 114 1 O LEU A 112 N PRO A 77 SHEET 9 AA330 LEU A 130 HIS A 134 -1 O LEU A 131 N LEU A 113 SHEET 10 AA330 VAL A 144 ILE A 149 0 SHEET 11 AA330 VAL A 153 LYS A 160 -1 O THR A 154 N ALA A 147 SHEET 12 AA330 VAL A 165 LEU A 168 -1 O GLU A 166 N LYS A 159 SHEET 13 AA330 ILE A 177 VAL A 178 -1 O ILE A 177 N LEU A 167 SHEET 14 AA330 PHE A 186 ARG A 197 -1 O GLY A 190 N VAL A 146 SHEET 15 AA330 LEU C 76 VAL C 79 0 SHEET 16 AA330 ILE C 94 TYR C 98 -1 O TYR C 98 N LEU C 76 SHEET 17 AA330 PHE C 111 ARG C 114 1 O LEU C 112 N VAL C 79 SHEET 18 AA330 LEU C 130 LYS C 135 -1 O VAL C 133 N PHE C 111 SHEET 19 AA330 VAL C 144 ILE C 149 0 SHEET 20 AA330 GLU C 152 GLN C 161 -1 O THR C 154 N ALA C 147 SHEET 21 AA330 LYS C 164 LEU C 168 -1 O LEU C 168 N ARG C 157 SHEET 22 AA330 ILE C 177 ASP C 180 -1 O ILE C 177 N LEU C 167 SHEET 23 AA330 PHE C 186 ARG C 197 -1 O THR C 187 N ARG C 148 SHEET 24 AA330 GLY E 10 GLN E 13 0 SHEET 25 AA330 ALA E 33 GLN E 39 0 SHEET 26 AA330 GLU E 46 THR E 52 -1 O ILE E 51 N MET E 34 SHEET 27 AA330 THR E 57 TYR E 59 -1 O ARG E 58 N ALA E 50 SHEET 28 AA330 ALA E 91 GLN E 99 -1 O LYS E 96 N GLY E 35 SHEET 29 AA330 TYR E 102 TRP E 105 -1 O TYR E 104 N GLN E 97 SHEET 30 AA330 THR E 109 SER E 114 -1 O THR E 109 N TYR E 93 SHEET 1 AA4 4 VAL E 2 GLY E 8 0 SHEET 2 AA4 4 LEU E 18 GLY E 26 -1 O ALA E 23 N VAL E 5 SHEET 3 AA4 4 THR E 77 MET E 82 -1 O LEU E 80 N LEU E 20 SHEET 4 AA4 4 PHE E 67 SER E 70 -1 N SER E 70 O TYR E 79 SHEET 1 AA5 4 VAL B 2 SER B 7 0 SHEET 2 AA5 4 SER B 17 GLY B 26 -1 O SER B 25 N GLN B 3 SHEET 3 AA5 4 THR B 77 ASN B 83 -1 O MET B 82 N LEU B 18 SHEET 4 AA5 4 PHE B 67 ARG B 71 -1 N THR B 68 O GLN B 81 SHEET 1 AA6 7 GLY B 10 GLN B 13 0 SHEET 2 AA6 7 ALA B 33 GLN B 39 0 SHEET 3 AA6 7 GLU B 46 THR B 52 -1 O GLU B 46 N ARG B 38 SHEET 4 AA6 7 THR B 57 TYR B 59 -1 O ARG B 58 N ALA B 50 SHEET 5 AA6 7 ALA B 91 GLN B 99 -1 O LYS B 96 N GLY B 35 SHEET 6 AA6 7 TYR B 102 TRP B 105 -1 O TYR B 102 N GLN B 99 SHEET 7 AA6 7 THR B 109 SER B 114 -1 O THR B 109 N TYR B 93 SHEET 1 AA725 LEU D 76 VAL D 79 0 SHEET 2 AA725 ILE D 94 TYR D 98 -1 O GLY D 96 N LEU D 78 SHEET 3 AA725 PHE D 111 ARG D 114 1 O LEU D 112 N VAL D 79 SHEET 4 AA725 LEU D 130 HIS D 134 -1 O LEU D 131 N LEU D 113 SHEET 5 AA725 VAL D 144 ILE D 149 0 SHEET 6 AA725 VAL D 153 GLN D 161 -1 O THR D 154 N ALA D 147 SHEET 7 AA725 LYS D 164 LEU D 168 -1 O LEU D 168 N ARG D 157 SHEET 8 AA725 ILE D 177 ASP D 180 -1 O ILE D 177 N LEU D 167 SHEET 9 AA725 PHE D 186 ARG D 197 -1 O GLU D 189 N VAL D 146 SHEET 10 AA725 LEU F 76 VAL F 79 0 SHEET 11 AA725 ILE F 94 TYR F 98 -1 O TYR F 98 N LEU F 76 SHEET 12 AA725 PHE F 111 ARG F 114 1 O LEU F 112 N VAL F 79 SHEET 13 AA725 LEU F 130 LYS F 135 -1 O LEU F 131 N LEU F 113 SHEET 14 AA725 VAL F 144 ILE F 149 0 SHEET 15 AA725 VAL F 153 LYS F 159 -1 O LYS F 156 N VAL F 145 SHEET 16 AA725 LYS F 164 LEU F 168 -1 O GLU F 166 N LYS F 159 SHEET 17 AA725 ILE F 177 ASP F 180 -1 O VAL F 179 N VAL F 165 SHEET 18 AA725 PHE F 186 ARG F 197 -1 O THR F 187 N ARG F 148 SHEET 19 AA725 GLY H 10 GLN H 13 0 SHEET 20 AA725 ALA H 33 GLN H 39 0 SHEET 21 AA725 ARG H 45 THR H 52 -1 O GLU H 46 N ARG H 38 SHEET 22 AA725 THR H 57 TYR H 59 -1 O ARG H 58 N ALA H 50 SHEET 23 AA725 ALA H 91 GLN H 99 -1 O LYS H 96 N GLY H 35 SHEET 24 AA725 TYR H 102 TYR H 104 -1 O TYR H 102 N GLN H 99 SHEET 25 AA725 GLN H 110 SER H 114 -1 O VAL H 111 N ALA H 91 SHEET 1 AA8 2 VAL H 2 GLN H 3 0 SHEET 2 AA8 2 SER H 25 GLY H 26 -1 O SER H 25 N GLN H 3 SHEET 1 AA9 4 GLU H 6 GLY H 8 0 SHEET 2 AA9 4 LEU H 18 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AA9 4 THR H 77 MET H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 AA9 4 PHE H 67 ARG H 71 -1 N THR H 68 O GLN H 81 SSBOND 1 CYS G 22 CYS G 95 1555 1555 2.04 SSBOND 2 CYS E 22 CYS E 95 1555 1555 2.01 SSBOND 3 CYS B 22 CYS B 95 1555 1555 2.02 SSBOND 4 CYS H 22 CYS H 95 1555 1555 2.01 CISPEP 1 LYS A 106 PRO A 107 0 -4.83 CISPEP 2 LYS C 106 PRO C 107 0 -6.27 CISPEP 3 LYS D 106 PRO D 107 0 -8.28 CISPEP 4 LYS F 106 PRO F 107 0 -7.26 CRYST1 112.672 112.672 144.751 90.00 90.00 120.00 P 32 2 1 24 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 0.008875 0.005124 0.000000 0.00000 SCALE2 0.000000 0.010248 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006908 0.00000