HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-DEC-24 9ML9 TITLE CRYSTAL STRUCTURE OF THE SARS-COV-2 RBD IN COMPLEX WITH THE RABBIT TITLE 2 M8B-C9 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: M8B-C9 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: M8B-C9 LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: SARS-COV-2, 2019-NCOV, COVID-19 VIRUS; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 12 ORGANISM_COMMON: RABBIT; SOURCE 13 ORGANISM_TAXID: 9986; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 19 ORGANISM_COMMON: RABBIT; SOURCE 20 ORGANISM_TAXID: 9986; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNE SYSTEM, NEUTRALIZING ANTIBODY, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR C.FAN,P.J.BJORKMAN REVDAT 1 04-JUN-25 9ML9 0 JRNL AUTH C.FAN,J.R.KEEFFE,K.E.MALECEK,A.A.COHEN,A.P.WEST JR., JRNL AUTH 2 V.A.BAHARANI,A.V.RORICK,H.GAO,P.N.P.GNANAPRAGASAM,S.RHO, JRNL AUTH 3 J.ALVAREZ,L.N.SEGOVIA,T.HATZIIOANNOU,P.D.BIENIASZ, JRNL AUTH 4 P.J.BJORKMAN JRNL TITL CROSS-REACTIVE SARBECOVIRUS ANTIBODIES INDUCED BY MOSAIC RBD JRNL TITL 2 NANOPARTICLES. JRNL REF PROC.NATL.ACAD.SCI.USA V. 122 37122 2025 JRNL REFN ESSN 1091-6490 JRNL PMID 40402246 JRNL DOI 10.1073/PNAS.2501637122 REMARK 2 REMARK 2 RESOLUTION. 2.59 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 2.59 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 24625 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 : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 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 37.9900 - 6.2400 0.97 1631 145 0.1851 0.2052 REMARK 3 2 6.2400 - 4.9600 0.99 1649 146 0.1954 0.2197 REMARK 3 3 4.9600 - 4.3300 1.00 1646 145 0.1711 0.1926 REMARK 3 4 4.3300 - 3.9400 1.00 1641 145 0.2061 0.2544 REMARK 3 5 3.9300 - 3.6500 0.99 1636 145 0.2356 0.2549 REMARK 3 6 3.6500 - 3.4400 0.97 1581 139 0.2570 0.3062 REMARK 3 7 3.4400 - 3.2700 0.98 1623 143 0.2750 0.2795 REMARK 3 8 3.2700 - 3.1200 1.00 1622 143 0.2839 0.3244 REMARK 3 9 3.1200 - 3.0000 0.99 1621 144 0.2862 0.3237 REMARK 3 10 3.0000 - 2.9000 0.99 1620 143 0.3024 0.3936 REMARK 3 11 2.9000 - 2.8100 0.99 1635 143 0.3178 0.3738 REMARK 3 12 2.8100 - 2.7300 0.99 1622 144 0.3484 0.3496 REMARK 3 13 2.7300 - 2.6600 0.99 1629 144 0.3368 0.3846 REMARK 3 14 2.6600 - 2.5900 0.91 1470 130 0.3594 0.4278 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) : 0.401 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.684 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 70.34 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.94 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 : 0.003 5067 REMARK 3 ANGLE : 0.543 6899 REMARK 3 CHIRALITY : 0.044 768 REMARK 3 PLANARITY : 0.004 880 REMARK 3 DIHEDRAL : 5.040 725 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 9ML9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290168. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-FEB-24 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24650 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560 REMARK 200 RESOLUTION RANGE LOW (A) : 37.990 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.08200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5 REMARK 200 DATA REDUNDANCY IN SHELL : 7.10 REMARK 200 R MERGE FOR SHELL (I) : 0.98300 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 (%): 56.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2% V/V 1,4-DIOXANE 0.1M TRIS PH 8.0 REMARK 280 15% (W/V) PEG 3,350, VAPOR DIFFUSION, TEMPERATURE 297K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 54.07950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.59700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 54.07950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 63.59700 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ARG A 328 REMARK 465 PHE A 329 REMARK 465 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LEU A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 HIS A 538 REMARK 465 HIS A 539 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 ALA L 0 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD1 ASP A 364 OG SER A 366 2.11 REMARK 500 O LYS H 13 OG1 THR H 16 2.16 REMARK 500 NE2 GLN A 409 O HOH A 701 2.17 REMARK 500 REMARK 500 REMARK: NULL 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 ALA A 352 41.17 -105.76 REMARK 500 ASP A 405 0.32 -64.58 REMARK 500 ALA A 411 147.14 -170.83 REMARK 500 THR A 470 53.60 37.50 REMARK 500 ASP H 10 -179.97 -170.74 REMARK 500 SER L 30 -130.09 58.37 REMARK 500 ALA L 51 -10.59 72.97 REMARK 500 SER L 52 -3.45 -143.03 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ML9 A 328 533 UNP P0DTC2 SPIKE_SARS2 328 533 DBREF 9ML9 H 2 220 PDB 9ML9 9ML9 2 220 DBREF 9ML9 L 0 214 PDB 9ML9 9ML9 0 214 SEQADV 9ML9 HIS A 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML9 HIS A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML9 HIS A 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML9 HIS A 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML9 HIS A 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML9 HIS A 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 212 ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU SEQRES 2 A 212 VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP SEQRES 3 A 212 ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER SEQRES 4 A 212 VAL LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS SEQRES 5 A 212 TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE SEQRES 6 A 212 THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP SEQRES 7 A 212 GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE SEQRES 8 A 212 ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY SEQRES 9 A 212 CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS SEQRES 10 A 212 VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG SEQRES 11 A 212 LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR SEQRES 12 A 212 GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL SEQRES 13 A 212 GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY SEQRES 14 A 212 PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG SEQRES 15 A 212 VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA SEQRES 16 A 212 THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU HIS HIS SEQRES 17 A 212 HIS HIS HIS HIS SEQRES 1 H 236 GLN SER LEU GLU GLU SER GLY GLY ASP LEU VAL LYS PRO SEQRES 2 H 236 GLY THR SER LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 H 236 SER PHE SER HIS ASN TYR VAL MET CYS TRP VAL ARG GLN SEQRES 4 H 236 ALA PRO GLY LYS GLY LEU GLU CYS VAL ALA CYS ILE TYR SEQRES 5 H 236 PHE GLY PHE GLY ASP THR TYR TYR ALA SER TRP ALA LYS SEQRES 6 H 236 GLY ARG ILE THR ILE SER LYS THR SER SER THR THR VAL SEQRES 7 H 236 THR LEU GLN MET THR SER LEU THR ALA ALA ASP THR ALA SEQRES 8 H 236 THR TYR PHE CYS ALA ARG ALA LEU GLY TYR TYR ILE TYR SEQRES 9 H 236 GLY ASP ALA GLY ASP ILE TYR ILE ALA ASP TYR PHE LYS SEQRES 10 H 236 LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER GLY SEQRES 11 H 236 GLN PRO LYS ALA PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 236 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 236 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 236 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 236 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 236 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 236 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 236 LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP LYS SEQRES 19 H 236 THR HIS SEQRES 1 L 217 ALA ASP ILE VAL MET THR GLN THR PRO ALA SER VAL GLU SEQRES 2 L 217 ALA ALA VAL GLY GLY THR VAL THR ILE LYS CYS GLN ALA SEQRES 3 L 217 SER GLN SER ILE SER LYS TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 217 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE PHE GLU ALA SEQRES 5 L 217 SER THR LEU GLU SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 L 217 ARG GLY SER GLY THR GLU PHE THR LEU THR ILE SER ASP SEQRES 7 L 217 LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN GLY SEQRES 8 L 217 TYR TYR TYR SER SER HIS SER TYR VAL PHE GLY GLY GLY SEQRES 9 L 217 THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG A 601 14 HET TRS A 602 8 HET TRS A 603 8 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 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 HETSYN TRS TRIS BUFFER FORMUL 4 NAG C8 H15 N O6 FORMUL 5 TRS 2(C4 H12 N O3 1+) FORMUL 7 HOH *23(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 TYR A 365 ASN A 370 1 6 HELIX 3 AA3 THR A 385 LEU A 390 1 6 HELIX 4 AA4 ASP A 405 ILE A 410 5 6 HELIX 5 AA5 GLY A 416 ASN A 422 1 7 HELIX 6 AA6 SER A 438 SER A 443 1 6 HELIX 7 AA7 GLY A 502 TYR A 505 5 4 HELIX 8 AA8 THR H 83 THR H 87 5 5 HELIX 9 AA9 SER H 127 LYS H 129 5 3 HELIX 10 AB1 SER H 156 ALA H 158 5 3 HELIX 11 AB2 SER H 187 LEU H 189 5 3 HELIX 12 AB3 LYS H 201 ASN H 204 5 4 HELIX 13 AB4 GLU L 79 ALA L 83 5 5 HELIX 14 AB5 SER L 121 SER L 127 1 7 HELIX 15 AB6 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O TYR A 508 N ILE A 402 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N LYS A 378 O VAL A 433 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 LEU A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 4 SER H 3 SER H 7 0 SHEET 2 AA5 4 LEU H 18 SER H 25 -1 O THR H 23 N GLU H 5 SHEET 3 AA5 4 THR H 76 MET H 81 -1 O LEU H 79 N LEU H 20 SHEET 4 AA5 4 ILE H 67 LYS H 71 -1 N THR H 68 O GLN H 80 SHEET 1 AA6 6 LEU H 11 VAL H 12 0 SHEET 2 AA6 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA6 6 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA6 6 TYR H 33 GLN H 39 -1 N VAL H 37 O PHE H 91 SHEET 5 AA6 6 LEU H 45 TYR H 52 -1 O VAL H 48 N TRP H 36 SHEET 6 AA6 6 ASP H 56 TYR H 59 -1 O TYR H 58 N CYS H 50 SHEET 1 AA7 4 LEU H 11 VAL H 12 0 SHEET 2 AA7 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 4 ALA H 88 LEU H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 4 LEU H 102 TRP H 103 -1 O LEU H 102 N ARG H 94 SHEET 1 AA8 2 TYR H 98 TYR H 100A 0 SHEET 2 AA8 2 ASP H 100F ILE H 100I-1 O ILE H 100I N TYR H 98 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AA9 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA9 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB1 4 THR H 131 SER H 132 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB1 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB2 3 THR H 151 TRP H 154 0 SHEET 2 AB2 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB2 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AB3 4 MET L 4 THR L 7 0 SHEET 2 AB3 4 VAL L 19 ALA L 25 -1 O LYS L 22 N THR L 7 SHEET 3 AB3 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N LYS L 63 O THR L 74 SHEET 1 AB4 6 SER L 10 ALA L 14 0 SHEET 2 AB4 6 THR L 102 LYS L 107 1 O VAL L 105 N VAL L 11 SHEET 3 AB4 6 THR L 85 TYR L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AB4 6 LYS L 45 PHE L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB4 6 THR L 53 LEU L 54 -1 O THR L 53 N PHE L 49 SHEET 1 AB5 4 SER L 10 ALA L 14 0 SHEET 2 AB5 4 THR L 102 LYS L 107 1 O VAL L 105 N VAL L 11 SHEET 3 AB5 4 THR L 85 TYR L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AB5 4 SER L 95B PHE L 98 -1 O VAL L 97 N GLY L 90 SHEET 1 AB6 4 SER L 114 PHE L 118 0 SHEET 2 AB6 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB6 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB6 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB7 4 ALA L 153 LEU L 154 0 SHEET 2 AB7 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB7 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB7 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.03 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.03 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 6 CYS H 35A CYS H 50 1555 1555 2.03 SSBOND 7 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 9 CYS L 134 CYS L 194 1555 1555 2.03 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -4.72 CISPEP 2 GLU H 148 PRO H 149 0 1.75 CISPEP 3 THR L 7 PRO L 8 0 -4.80 CISPEP 4 TYR L 140 PRO L 141 0 1.48 CRYST1 108.159 127.194 75.431 90.00 127.72 90.00 C 1 2 1 4 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 0.009246 0.000000 0.007151 0.00000 SCALE2 0.000000 0.007862 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016760 0.00000