HEADER TRANSFERASE/IMMUNE SYSTEM 19-JAN-26 10GH TITLE CRYO-EM STRUCTURE OF RECEPTOR TYROSINE KINASE ROS1 IN COMPLEX WITH TITLE 2 FAB-RX5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTO-ONCOGENE C-ROS,PROTO-ONCOGENE C-ROS-1,RECEPTOR COMPND 5 TYROSINE KINASE C-ROS ONCOGENE 1,C-ROS RECEPTOR TYROSINE KINASE; COMPND 6 EC: 2.7.10.1; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: FAB-RX5 LIGHT CHAIN; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: FAB-RX5 HEAVY CHAIN; COMPND 14 CHAIN: C; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: ROS1, ROS, ROS-1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RECEPTOR TYROSINE KINASE, ROS1 EXTRACELLULAR BENT-OVER CONFORMATION, KEYWDS 2 INHIBITORY FAB-RX5, TRANSFERASE-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR H.LI,D.KLEIN REVDAT 1 25-FEB-26 10GH 0 JRNL AUTH H.LI,D.KLEIN JRNL TITL CLUSTERING AND A CONFORMATIONAL SWITCH DRIVE ACTIVATION OF JRNL TITL 2 THE MAMMALIAN RECEPTOR TYROSINE KINASE ROS1 JRNL REF TO BE PUBLISHED JRNL REFN JRNL DOI 10.1038/S41467-026-69630-7 REMARK 2 REMARK 2 RESOLUTION. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.060 REMARK 3 NUMBER OF PARTICLES : 166992 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 10GH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-26. REMARK 100 THE DEPOSITION ID IS D_1000304330. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : RECEPTOR TYROSINE KINASE ROS1 REMARK 245 IN COMPLEX WITH FAB-RX5 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 SER A 135 -134.44 50.63 REMARK 500 PRO A 218 42.02 -79.12 REMARK 500 SER A 251 -156.26 -150.75 REMARK 500 GLU A 299 55.02 37.86 REMARK 500 LYS A 308 -107.70 54.20 REMARK 500 ASN A 406 29.15 -142.99 REMARK 500 ALA A 420 71.58 53.62 REMARK 500 ARG A 452 -95.11 55.92 REMARK 500 SER A 495 -164.79 -78.93 REMARK 500 PHE A 512 46.78 -140.25 REMARK 500 ASN A 516 55.76 -99.05 REMARK 500 ASN A 517 -6.54 67.62 REMARK 500 ASP A 531 -71.40 -94.47 REMARK 500 SER A 532 -16.97 -146.39 REMARK 500 PHE A 550 160.46 65.24 REMARK 500 LEU A 616 69.60 62.39 REMARK 500 GLU A 617 -84.74 106.85 REMARK 500 ILE A 618 59.76 34.58 REMARK 500 ASN A 624 60.48 60.17 REMARK 500 THR A 628 35.33 -99.00 REMARK 500 GLU A 679 43.86 -85.24 REMARK 500 CYS A 688 58.95 -94.10 REMARK 500 MET A 730 48.32 -82.65 REMARK 500 ASP A 731 -173.80 -173.63 REMARK 500 TYR A 803 16.13 -140.18 REMARK 500 ARG A 859 -135.41 56.63 REMARK 500 TRP A 861 142.81 -171.13 REMARK 500 ALA A 872 -4.17 68.06 REMARK 500 SER A 875 149.85 67.56 REMARK 500 PRO A 916 46.01 -81.14 REMARK 500 ASN A 935 59.61 -95.43 REMARK 500 VAL A 942 -65.22 37.30 REMARK 500 TYR A1019 47.75 -82.81 REMARK 500 ASP B 28 38.50 -99.86 REMARK 500 SER B 57 -136.67 52.95 REMARK 500 ALA B 78 -4.06 67.32 REMARK 500 TYR B 121 56.75 -91.69 REMARK 500 ASN B 165 -165.44 -78.66 REMARK 500 VAL C 74 -57.16 -122.51 REMARK 500 SER C 82 16.97 57.00 REMARK 500 TYR C 130 30.17 -141.28 REMARK 500 SER C 147 176.77 62.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG D 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45172 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RECEPTOR TYROSINE KINASE ROS1 IN COMPLEX WITH REMARK 900 FAB-RX5 REMARK 900 RELATED ID: EMD-75151 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RECEPTOR TYROSINE KINASE ROS1 IN COMPLEX WITH REMARK 900 FAB-RX5 DBREF 10GH A 28 1033 UNP Q78DX7 ROS1_MOUSE 28 1033 DBREF 10GH B 24 253 PDB 10GH 10GH 24 253 DBREF 10GH C 24 261 PDB 10GH 10GH 24 261 SEQRES 1 A 1006 SER THR VAL LEU SER SER CYS LEU THR SER CYS VAL THR SEQRES 2 A 1006 ASN LEU GLY ARG GLN LEU ASP SER GLY THR ARG TYR ASN SEQRES 3 A 1006 LEU SER GLU ALA CYS ILE HIS GLY CYS GLN PHE TRP ASN SEQRES 4 A 1006 SER VAL ASP GLN GLU THR CYS ALA LEU LYS CYS ASN ASP SEQRES 5 A 1006 THR TYR ALA THR ILE CYS GLU ARG GLU SER CYS GLU VAL SEQRES 6 A 1006 GLY CYS SER ASN ALA GLU GLY SER TYR GLU GLU GLU VAL SEQRES 7 A 1006 LEU GLU SER THR GLU LEU PRO THR ALA PRO PHE ALA SER SEQRES 8 A 1006 SER ILE GLY SER HIS GLY VAL THR LEU ARG TRP ASN PRO SEQRES 9 A 1006 ALA ASN ILE SER GLY VAL LYS TYR ILE ILE GLN TRP LYS SEQRES 10 A 1006 TYR ALA GLN LEU PRO GLY SER TRP THR PHE THR GLU THR SEQRES 11 A 1006 VAL SER LYS LEU SER TYR THR VAL GLU PRO LEU HIS PRO SEQRES 12 A 1006 PHE THR GLU TYR ILE PHE ARG VAL VAL TRP ILE PHE THR SEQRES 13 A 1006 ALA GLN LEU HIS LEU TYR SER PRO PRO SER PRO SER TYR SEQRES 14 A 1006 ARG THR HIS PRO TYR GLY VAL PRO GLU THR ALA PRO LEU SEQRES 15 A 1006 ILE LEU ASN MET GLU SER TRP SER PRO ASP THR VAL GLU SEQRES 16 A 1006 VAL SER TRP ALA PRO PRO HIS PHE PRO GLY GLY PRO ILE SEQRES 17 A 1006 LEU GLY TYR ASN LEU ARG LEU ILE SER LYS ASN GLN LYS SEQRES 18 A 1006 LEU ASP SER GLY THR GLN ARG THR SER PHE GLN PHE TYR SEQRES 19 A 1006 SER THR LEU PRO ASN THR THR TYR ARG PHE SER ILE ALA SEQRES 20 A 1006 ALA VAL ASN GLU VAL GLY GLU GLY PRO GLU ALA GLU SER SEQRES 21 A 1006 THR VAL THR THR PRO SER PRO SER VAL GLN GLU GLU GLU SEQRES 22 A 1006 GLN TRP LEU PHE LEU SER ARG LYS THR SER LEU ARG LYS SEQRES 23 A 1006 ARG SER LEU LYS TYR LEU VAL ASP GLU ALA HIS CYS LEU SEQRES 24 A 1006 TRP SER ASP ALA ILE HIS HIS ASN ILE THR GLY ILE SER SEQRES 25 A 1006 VAL TYR ALA GLN GLN GLN VAL VAL TYR PHE SER GLU GLY SEQRES 26 A 1006 THR VAL ILE TRP MET LYS GLY ALA ALA ASN MET SER ASP SEQRES 27 A 1006 VAL SER ASP LEU ARG ILE PHE TYR GLN GLY SER GLY LEU SEQRES 28 A 1006 VAL SER SER ILE SER ILE ASP TRP LEU TYR GLN ARG MET SEQRES 29 A 1006 TYR PHE ILE MET ASP LYS LEU VAL TYR VAL CYS GLU LEU SEQRES 30 A 1006 LYS ASN CYS SER ASN LEU GLU GLU ILE THR PRO PHE SER SEQRES 31 A 1006 LEU ILE ALA PRO GLN LYS VAL VAL VAL ASP SER TYR ASN SEQRES 32 A 1006 GLY TYR LEU PHE TYR LEU LEU ARG ASP GLY ILE TYR ARG SEQRES 33 A 1006 VAL ASN LEU PRO LEU PRO SER GLY ARG ASP THR LYS ALA SEQRES 34 A 1006 VAL ARG ILE VAL GLU SER GLY THR LEU LYS ASP PHE ALA SEQRES 35 A 1006 VAL LYS PRO GLN SER LYS ARG ILE ILE TYR PHE ASN ASP SEQRES 36 A 1006 THR MET GLN LEU PHE MET SER THR PHE LEU ASP GLY SER SEQRES 37 A 1006 ALA PHE HIS ARG VAL LEU PRO TRP VAL PRO LEU VAL THR SEQRES 38 A 1006 VAL LYS SER PHE ALA CYS GLU ASN ASN ASP PHE LEU ILE SEQRES 39 A 1006 THR ASP GLY LYS ALA ILE PHE GLN GLN ASP SER LEU SER SEQRES 40 A 1006 PHE ASN GLU PHE ILE VAL GLY CYS ASP LEU SER HIS ILE SEQRES 41 A 1006 GLU GLU PHE GLY PHE GLY ASN LEU VAL ILE PHE GLY SER SEQRES 42 A 1006 SER VAL GLN SER TYR PRO LEU PRO GLY HIS PRO GLN GLU SEQRES 43 A 1006 VAL SER VAL LEU PHE GLY SER ARG GLU ALA LEU ILE GLN SEQRES 44 A 1006 TRP THR PRO PRO ALA LEU ALA ILE GLY ALA SER PRO SER SEQRES 45 A 1006 ALA TRP GLN ASN TRP THR TYR GLU VAL LYS VAL TYR SER SEQRES 46 A 1006 GLN ASP ILE LEU GLU ILE THR GLN VAL PHE SER ASN ILE SEQRES 47 A 1006 SER GLY THR MET LEU ASN VAL PRO GLU LEU GLN SER SER SEQRES 48 A 1006 THR LYS TYR THR VAL SER VAL ARG ALA SER SER PRO LYS SEQRES 49 A 1006 GLY PRO GLY PRO TRP SER ALA PRO SER VAL GLY THR THR SEQRES 50 A 1006 LEU VAL PRO ALA THR GLU PRO PRO PHE ILE MET ALA VAL SEQRES 51 A 1006 LYS GLU ASP GLY LEU TRP SER LYS PRO LEU CYS SER PHE SEQRES 52 A 1006 GLY PRO GLY GLU PHE LEU SER SER ASP VAL GLY ASN VAL SEQRES 53 A 1006 SER ASP MET ASP TRP TYR ASN ASN SER LEU TYR TYR SER SEQRES 54 A 1006 ASP THR LYS GLY ASN VAL TYR VAL ARG PRO LEU ASN GLY SEQRES 55 A 1006 MET ASP ILE SER GLU ASN TYR HIS ILE PRO SER ILE VAL SEQRES 56 A 1006 GLY ALA GLY ALA LEU ALA PHE GLU TRP LEU GLY HIS PHE SEQRES 57 A 1006 LEU TYR TRP ALA GLY LYS THR TYR VAL ILE GLN ARG GLN SEQRES 58 A 1006 SER VAL LEU THR GLY HIS THR ASP ILE VAL THR HIS VAL SEQRES 59 A 1006 LYS LEU LEU VAL ASN ASP MET ALA VAL ASP SER VAL GLY SEQRES 60 A 1006 GLY TYR LEU TYR TRP THR THR LEU TYR SER VAL GLU SER SEQRES 61 A 1006 THR ARG LEU ASN GLY GLU SER SER LEU VAL LEU GLN ALA SEQRES 62 A 1006 GLN PRO TRP LEU SER GLY LYS LYS VAL ILE ALA LEU THR SEQRES 63 A 1006 LEU ASP LEU SER ASP GLY LEU LEU TYR TRP LEU VAL GLN SEQRES 64 A 1006 ASP ASN GLN CYS ILE HIS LEU TYR THR ALA VAL LEU ARG SEQRES 65 A 1006 GLY TRP SER GLY GLY ASP ALA THR ILE THR GLU PHE ALA SEQRES 66 A 1006 ALA TRP SER THR SER GLU ILE SER GLN ASN ALA LEU MET SEQRES 67 A 1006 TYR TYR SER GLY ARG LEU PHE TRP ILE ASN GLY PHE ARG SEQRES 68 A 1006 ILE ILE THR ALA GLN GLU ILE GLY GLN ARG THR SER VAL SEQRES 69 A 1006 SER VAL SER GLU PRO ALA LYS PHE ASN GLN PHE THR ILE SEQRES 70 A 1006 ILE GLN THR SER LEU LYS PRO LEU PRO GLY ASN PHE SER SEQRES 71 A 1006 SER THR PRO LYS VAL ILE PRO ASP PRO VAL GLN GLU SER SEQRES 72 A 1006 SER PHE ARG ILE GLU GLY HIS THR SER SER PHE GLN ILE SEQRES 73 A 1006 LEU TRP ASN GLU PRO PRO ALA VAL ASP TRP GLY ILE VAL SEQRES 74 A 1006 PHE TYR SER VAL GLU PHE SER THR HIS SER LYS PHE LEU SEQRES 75 A 1006 ILE ILE GLU GLN GLN SER LEU PRO ILE PHE THR VAL GLU SEQRES 76 A 1006 GLY LEU GLU PRO TYR THR LEU PHE ASN LEU SER VAL THR SEQRES 77 A 1006 PRO TYR THR TYR TRP GLY LYS GLY GLN LYS THR SER LEU SEQRES 78 A 1006 SER PHE ARG ALA PRO SEQRES 1 B 230 SER MET ALA SER ASP ILE GLN MET THR GLN SER PRO SER SEQRES 2 B 230 SER LEU SER ALA SER VAL GLY ASP ARG VAL THR ILE THR SEQRES 3 B 230 CYS ARG ALA SER GLN SER VAL SER SER ALA VAL ALA TRP SEQRES 4 B 230 TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE SEQRES 5 B 230 TYR SER ALA SER SER LEU TYR SER GLY VAL PRO SER ARG SEQRES 6 B 230 PHE SER GLY SER ARG SER GLY THR ASP PHE THR LEU THR SEQRES 7 B 230 ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR SEQRES 8 B 230 CYS GLN GLN TYR TYR ALA TYR SER LEU PHE THR PHE GLY SEQRES 9 B 230 GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 B 230 PRO SER VAL PHE ILE PHE PRO PRO SER ASP SER GLN LEU SEQRES 11 B 230 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 B 230 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 B 230 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 B 230 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 B 230 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 B 230 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 B 230 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS GLY GLY SEQRES 18 B 230 SER ASP TYR LYS ASP ASP ASP ASP LYS SEQRES 1 C 238 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 C 238 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 C 238 ALA SER GLY PHE ASN LEU SER SER SER SER MET HIS TRP SEQRES 4 C 238 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 C 238 TYR ILE TYR PRO TYR SER SER SER THR SER TYR ALA ASP SEQRES 6 C 238 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 C 238 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 C 238 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR TRP SEQRES 9 C 238 GLY TYR TYR GLY LEU ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 C 238 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 238 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 238 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 238 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 238 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 238 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 238 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 238 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 238 PRO LYS SER CYS ASP LYS THR HIS THR SER ARG HIS HIS SEQRES 19 C 238 HIS HIS HIS HIS HET NAG E 1 14 HET NAG E 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG A1101 14 HET NAG A1102 14 HET NAG A1103 14 HET NAG A1104 14 HET NAG A1105 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 11(C8 H15 N O6) HELIX 1 AA1 SER A 28 LEU A 42 1 15 HELIX 2 AA2 GLY A 43 GLN A 45 5 3 HELIX 3 AA3 ASN A 53 VAL A 68 1 16 HELIX 4 AA4 THR A 72 TYR A 81 1 10 HELIX 5 AA5 THR A 83 SER A 108 1 26 HELIX 6 AA6 PRO A 822 GLY A 826 5 5 HELIX 7 AA7 GLN A 926 LYS A 930 5 5 HELIX 8 AA8 GLN A 948 PHE A 952 5 5 HELIX 9 AA9 HIS A 957 SER A 960 5 4 HELIX 10 AB1 GLN B 106 PHE B 110 5 5 HELIX 11 AB2 SER B 149 GLY B 156 1 8 HELIX 12 AB3 VAL B 178 ALA B 181 5 4 HELIX 13 AB4 SER B 210 HIS B 217 1 8 HELIX 14 AB5 ARG B 239 GLY B 243 1 5 HELIX 15 AB6 ASP B 249 LYS B 253 5 5 HELIX 16 AB7 ASN C 54 SER C 56 5 3 HELIX 17 AB8 ARG C 113 THR C 117 5 5 HELIX 18 AB9 SER C 159 LYS C 161 5 3 HELIX 19 AC1 SER C 188 ALA C 190 5 3 HELIX 20 AC2 SER C 219 LEU C 221 5 3 SHEET 1 AA1 3 PHE A 116 GLY A 121 0 SHEET 2 AA1 3 GLY A 124 ARG A 128 -1 O ARG A 128 N PHE A 116 SHEET 3 AA1 3 SER A 162 VAL A 165 -1 O TYR A 163 N LEU A 127 SHEET 1 AA2 3 LYS A 138 TYR A 145 0 SHEET 2 AA2 3 GLU A 173 ILE A 181 -1 O ILE A 175 N LYS A 144 SHEET 3 AA2 3 HIS A 187 TYR A 189 -1 O LEU A 188 N TRP A 180 SHEET 1 AA3 3 LYS A 138 TYR A 145 0 SHEET 2 AA3 3 GLU A 173 ILE A 181 -1 O ILE A 175 N LYS A 144 SHEET 3 AA3 3 TYR A 196 ARG A 197 -1 O TYR A 196 N TYR A 174 SHEET 1 AA4 3 LEU A 209 SER A 217 0 SHEET 2 AA4 3 THR A 220 ALA A 226 -1 O SER A 224 N ASN A 212 SHEET 3 AA4 3 SER A 257 TYR A 261 -1 O PHE A 258 N VAL A 223 SHEET 1 AA5 4 ILE A 235 TYR A 238 0 SHEET 2 AA5 4 THR A 268 ASN A 277 -1 O VAL A 276 N GLY A 237 SHEET 3 AA5 4 ARG A 241 ILE A 243 -1 N ILE A 243 O ARG A 270 SHEET 4 AA5 4 LYS A 248 ASP A 250 -1 O LEU A 249 N LEU A 242 SHEET 1 AA6 3 ILE A 235 TYR A 238 0 SHEET 2 AA6 3 THR A 268 ASN A 277 -1 O VAL A 276 N GLY A 237 SHEET 3 AA6 3 GLU A 281 THR A 290 -1 O SER A 287 N PHE A 271 SHEET 1 AA7 3 SER A 310 SER A 315 0 SHEET 2 AA7 3 TRP A 302 ARG A 307 -1 N LEU A 303 O ARG A 314 SHEET 3 AA7 3 VAL A 556 PHE A 558 -1 O PHE A 558 N TRP A 302 SHEET 1 AA8 4 ILE A 335 TYR A 341 0 SHEET 2 AA8 4 VAL A 346 GLU A 351 -1 O VAL A 346 N TYR A 341 SHEET 3 AA8 4 VAL A 354 GLY A 359 -1 O TRP A 356 N PHE A 349 SHEET 4 AA8 4 ARG A 370 TYR A 373 -1 O PHE A 372 N ILE A 355 SHEET 1 AA9 4 VAL A 379 ASP A 385 0 SHEET 2 AA9 4 ARG A 390 MET A 395 -1 O ILE A 394 N SER A 380 SHEET 3 AA9 4 VAL A 399 GLU A 403 -1 O TYR A 400 N PHE A 393 SHEET 4 AA9 4 GLU A 411 GLU A 412 -1 O GLU A 411 N VAL A 401 SHEET 1 AB1 4 VAL A 426 ASP A 427 0 SHEET 2 AB1 4 TYR A 432 LEU A 436 -1 O TYR A 432 N ASP A 427 SHEET 3 AB1 4 GLY A 440 ASN A 445 -1 O TYR A 442 N TYR A 435 SHEET 4 AB1 4 VAL A 457 GLU A 461 -1 O VAL A 457 N ARG A 443 SHEET 1 AB2 4 PHE A 468 LYS A 471 0 SHEET 2 AB2 4 ARG A 476 PHE A 480 -1 O ILE A 478 N ALA A 469 SHEET 3 AB2 4 PHE A 487 PHE A 491 -1 O THR A 490 N ILE A 477 SHEET 4 AB2 4 HIS A 498 ARG A 499 -1 O HIS A 498 N SER A 489 SHEET 1 AB3 3 PHE A 519 THR A 522 0 SHEET 2 AB3 3 ILE A 527 GLN A 530 -1 O PHE A 528 N ILE A 521 SHEET 3 AB3 3 PHE A 535 PHE A 538 -1 O PHE A 538 N ILE A 527 SHEET 1 AB4 3 GLN A 572 PHE A 578 0 SHEET 2 AB4 3 ALA A 583 THR A 588 -1 O THR A 588 N GLN A 572 SHEET 3 AB4 3 MET A 629 VAL A 632 -1 O LEU A 630 N ILE A 585 SHEET 1 AB5 4 GLN A 620 ILE A 625 0 SHEET 2 AB5 4 THR A 605 TYR A 611 -1 N TYR A 606 O ILE A 625 SHEET 3 AB5 4 LYS A 640 SER A 648 -1 O SER A 648 N THR A 605 SHEET 4 AB5 4 PRO A 653 TRP A 656 -1 O GLY A 654 N ALA A 647 SHEET 1 AB6 4 GLN A 620 ILE A 625 0 SHEET 2 AB6 4 THR A 605 TYR A 611 -1 N TYR A 606 O ILE A 625 SHEET 3 AB6 4 LYS A 640 SER A 648 -1 O SER A 648 N THR A 605 SHEET 4 AB6 4 SER A 660 THR A 663 -1 O GLY A 662 N TYR A 641 SHEET 1 AB7 3 GLY A 681 PRO A 686 0 SHEET 2 AB7 3 PHE A 673 LYS A 678 -1 N ILE A 674 O LYS A 685 SHEET 3 AB7 3 ILE A 924 ILE A 925 -1 O ILE A 925 N PHE A 673 SHEET 1 AB8 4 VAL A 703 TRP A 708 0 SHEET 2 AB8 4 LEU A 713 ASP A 717 -1 O SER A 716 N SER A 704 SHEET 3 AB8 4 ASN A 721 ARG A 725 -1 O ASN A 721 N ASP A 717 SHEET 4 AB8 4 TYR A 736 VAL A 742 -1 O TYR A 736 N VAL A 724 SHEET 1 AB9 4 ALA A 746 GLU A 750 0 SHEET 2 AB9 4 PHE A 755 ALA A 759 -1 O PHE A 755 N GLU A 750 SHEET 3 AB9 4 VAL A 764 SER A 769 -1 O GLN A 768 N LEU A 756 SHEET 4 AB9 4 THR A 775 HIS A 780 -1 O VAL A 778 N ILE A 765 SHEET 1 AC1 4 VAL A 785 ASP A 791 0 SHEET 2 AC1 4 TYR A 796 THR A 801 -1 O THR A 800 N ASN A 786 SHEET 3 AC1 4 SER A 804 ARG A 809 -1 O THR A 808 N LEU A 797 SHEET 4 AC1 4 LEU A 816 GLN A 819 -1 O LEU A 816 N SER A 807 SHEET 1 AC2 3 LYS A 828 ASP A 835 0 SHEET 2 AC2 3 LEU A 840 GLN A 846 -1 O TYR A 842 N THR A 833 SHEET 3 AC2 3 ILE A 851 ALA A 856 -1 O HIS A 852 N VAL A 845 SHEET 1 AC3 4 ILE A 879 TYR A 887 0 SHEET 2 AC3 4 ARG A 890 ASN A 895 -1 O PHE A 892 N MET A 885 SHEET 3 AC3 4 ILE A 900 GLU A 904 -1 O GLN A 903 N LEU A 891 SHEET 4 AC3 4 VAL A 911 SER A 912 -1 O VAL A 911 N ALA A 902 SHEET 1 AC4 3 ARG A 953 GLU A 955 0 SHEET 2 AC4 3 GLN A 962 LEU A 964 -1 O LEU A 964 N ARG A 953 SHEET 3 AC4 3 ILE A 998 THR A1000 -1 O PHE A 999 N ILE A 963 SHEET 1 AC5 4 ILE A 991 GLN A 994 0 SHEET 2 AC5 4 PHE A 977 THR A 984 -1 N TYR A 978 O GLN A 994 SHEET 3 AC5 4 PHE A1010 THR A1018 -1 O SER A1013 N GLU A 981 SHEET 4 AC5 4 GLY A1021 LYS A1022 -1 O GLY A1021 N THR A1018 SHEET 1 AC6 4 ILE A 991 GLN A 994 0 SHEET 2 AC6 4 PHE A 977 THR A 984 -1 N TYR A 978 O GLN A 994 SHEET 3 AC6 4 PHE A1010 THR A1018 -1 O SER A1013 N GLU A 981 SHEET 4 AC6 4 LEU A1028 PHE A1030 -1 O PHE A1030 N PHE A1010 SHEET 1 AC7 4 MET B 31 SER B 34 0 SHEET 2 AC7 4 VAL B 46 ALA B 52 -1 O ARG B 51 N THR B 32 SHEET 3 AC7 4 ASP B 97 ILE B 102 -1 O PHE B 98 N CYS B 50 SHEET 4 AC7 4 PHE B 89 SER B 92 -1 N SER B 92 O THR B 99 SHEET 1 AC8 2 SER B 37 ALA B 40 0 SHEET 2 AC8 2 LYS B 131 ILE B 134 1 O GLU B 133 N ALA B 40 SHEET 1 AC9 3 LYS B 72 ILE B 75 0 SHEET 2 AC9 3 VAL B 60 GLN B 65 -1 N GLN B 64 O LYS B 72 SHEET 3 AC9 3 THR B 112 GLN B 117 -1 O GLN B 116 N ALA B 61 SHEET 1 AD1 3 VAL B 143 PHE B 146 0 SHEET 2 AD1 3 VAL B 160 LEU B 164 -1 O VAL B 161 N PHE B 146 SHEET 3 AD1 3 LEU B 203 LEU B 207 -1 O LEU B 203 N LEU B 164 SHEET 1 AD2 2 VAL B 174 TRP B 176 0 SHEET 2 AD2 2 CYS B 222 VAL B 224 -1 O GLU B 223 N GLN B 175 SHEET 1 AD3 2 VAL B 219 TYR B 220 0 SHEET 2 AD3 2 PHE B 237 ASN B 238 -1 O PHE B 237 N TYR B 220 SHEET 1 AD4 4 GLN C 29 SER C 33 0 SHEET 2 AD4 4 LEU C 44 SER C 51 -1 O SER C 51 N GLN C 29 SHEET 3 AD4 4 THR C 104 MET C 109 -1 O LEU C 107 N LEU C 46 SHEET 4 AD4 4 PHE C 94 ASP C 99 -1 N SER C 97 O TYR C 106 SHEET 1 AD5 6 LEU C 37 VAL C 38 0 SHEET 2 AD5 6 THR C 139 VAL C 143 1 O THR C 142 N VAL C 38 SHEET 3 AD5 6 ALA C 118 TYR C 126 -1 N ALA C 118 O VAL C 141 SHEET 4 AD5 6 SER C 58 GLN C 65 -1 N VAL C 63 O TYR C 121 SHEET 5 AD5 6 LEU C 71 TYR C 78 -1 O GLU C 72 N ARG C 64 SHEET 6 AD5 6 SER C 83 TYR C 86 -1 O SER C 83 N TYR C 78 SHEET 1 AD6 4 LEU C 37 VAL C 38 0 SHEET 2 AD6 4 THR C 139 VAL C 143 1 O THR C 142 N VAL C 38 SHEET 3 AD6 4 ALA C 118 TYR C 126 -1 N ALA C 118 O VAL C 141 SHEET 4 AD6 4 TYR C 134 TRP C 135 -1 O TYR C 134 N ARG C 124 SHEET 1 AD7 4 SER C 152 LEU C 156 0 SHEET 2 AD7 4 THR C 167 TYR C 177 -1 O GLY C 171 N LEU C 156 SHEET 3 AD7 4 TYR C 208 PRO C 217 -1 O VAL C 216 N ALA C 168 SHEET 4 AD7 4 VAL C 195 THR C 197 -1 N HIS C 196 O VAL C 213 SHEET 1 AD8 4 THR C 163 SER C 164 0 SHEET 2 AD8 4 THR C 167 TYR C 177 -1 O THR C 167 N SER C 164 SHEET 3 AD8 4 TYR C 208 PRO C 217 -1 O VAL C 216 N ALA C 168 SHEET 4 AD8 4 VAL C 201 LEU C 202 -1 N VAL C 201 O SER C 209 SHEET 1 AD9 3 THR C 183 TRP C 186 0 SHEET 2 AD9 3 TYR C 226 HIS C 232 -1 O ASN C 229 N SER C 185 SHEET 3 AD9 3 THR C 237 VAL C 243 -1 O THR C 237 N HIS C 232 SSBOND 1 CYS A 34 CYS A 62 1555 1555 2.04 SSBOND 2 CYS A 38 CYS A 58 1555 1555 2.02 SSBOND 3 CYS A 73 CYS A 94 1555 1555 2.03 SSBOND 4 CYS A 77 CYS A 90 1555 1555 2.03 SSBOND 5 CYS A 325 CYS A 542 1555 1555 2.03 SSBOND 6 CYS A 402 CYS A 407 1555 1555 2.04 SSBOND 7 CYS B 50 CYS B 115 1555 1555 2.03 SSBOND 8 CYS B 162 CYS B 222 1555 1555 2.03 SSBOND 9 CYS B 242 CYS C 248 1555 1555 2.03 SSBOND 10 CYS C 48 CYS C 122 1555 1555 2.03 SSBOND 11 CYS C 172 CYS C 228 1555 1555 2.03 LINK ND2 ASN A 266 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 334 C1 NAG A1104 1555 1555 1.44 LINK ND2 ASN A 481 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN A 603 C1 NAG A1101 1555 1555 1.44 LINK ND2 ASN A 624 C1 NAG A1102 1555 1555 1.44 LINK ND2 ASN A 710 C1 NAG A1103 1555 1555 1.44 LINK ND2 ASN A1011 C1 NAG A1105 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 CISPEP 1 SER B 34 PRO B 35 0 -1.06 CISPEP 2 TYR B 168 PRO B 169 0 5.04 CISPEP 3 PHE C 178 PRO C 179 0 -2.57 CISPEP 4 GLU C 180 PRO C 181 0 -2.46 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000