HEADER VIRAL PROTEIN 28-SEP-22 8EN4 TITLE STRUCTURE OF GII.4 NOROVIRUS IN COMPLEX WITH NANOBODY 53 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VP1; COMPND 3 CHAIN: B, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 53; COMPND 7 CHAIN: C, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOROVIRUS; SOURCE 3 ORGANISM_TAXID: 142786; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 8 ORGANISM_TAXID: 30538; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NOROVIRUS, NANOBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.KHER,C.SABIN,A.KOROMYSLOVA,M.PANCERA,G.HANSMAN JRNL AUTH G.KHER,C.SABIN,A.KOROMYSLOVA,M.PANCERA,G.HANSMAN JRNL TITL STRUCTURE OF GII.4 NOROVIRUS IN COMPLEX WITH NANOBODY 53 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.04 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 46628 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.290 REMARK 3 FREE R VALUE TEST SET COUNT : 3837 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 6.8900 - 5.4800 1.00 3168 143 0.1675 0.1793 REMARK 3 2 5.4700 - 4.7800 0.99 3174 143 0.1575 0.1710 REMARK 3 3 4.7800 - 4.3500 1.00 3168 140 0.1490 0.1751 REMARK 3 4 4.3500 - 4.0300 1.00 3173 144 0.1636 0.2262 REMARK 3 5 4.0300 - 3.8000 1.00 3194 141 0.1886 0.2104 REMARK 3 6 3.8000 - 3.6100 1.00 3144 143 0.2072 0.2723 REMARK 3 7 3.6100 - 3.4500 0.99 3175 144 0.2279 0.2267 REMARK 3 8 3.4500 - 3.3200 0.99 3161 140 0.2279 0.2671 REMARK 3 9 3.3200 - 3.2000 0.99 3135 149 0.2403 0.2492 REMARK 3 10 3.2000 - 3.1000 1.00 3180 137 0.2445 0.2709 REMARK 3 11 3.1000 - 3.0100 1.00 3170 145 0.2507 0.2828 REMARK 3 12 3.0100 - 2.9300 0.99 3187 149 0.2610 0.3066 REMARK 3 13 2.9300 - 2.8600 0.99 3145 128 0.2790 0.3253 REMARK 3 14 2.8600 - 2.8000 0.99 3120 149 0.2782 0.3383 REMARK 3 15 2.8000 - 2.7400 0.99 3207 144 0.2793 0.2903 REMARK 3 16 2.7400 - 2.6800 1.00 3168 136 0.2705 0.3412 REMARK 3 17 2.6800 - 2.6300 0.99 3210 136 0.2809 0.3027 REMARK 3 18 2.6300 - 2.5900 1.00 3174 142 0.2712 0.3885 REMARK 3 19 2.5900 - 2.5400 1.00 3112 140 0.2806 0.2998 REMARK 3 20 2.5400 - 2.5000 1.00 3204 140 0.2906 0.3411 REMARK 3 21 2.5000 - 2.4600 1.00 3152 148 0.2854 0.3532 REMARK 3 22 2.4600 - 2.4300 1.00 3201 129 0.2940 0.3310 REMARK 3 23 2.4300 - 2.3900 0.99 3164 163 0.3177 0.3528 REMARK 3 24 2.3900 - 2.3600 1.00 3149 136 0.3099 0.3416 REMARK 3 25 2.3600 - 2.3300 1.00 3210 143 0.3366 0.3949 REMARK 3 26 2.3300 - 2.3000 1.00 3132 150 0.3491 0.3906 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.630 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.19 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 8EN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000267282. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-OCT-20 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 : BL14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.918400 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46757 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 54.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.00 REMARK 200 R MERGE FOR SHELL (I) : 0.43200 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: 4OOS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.23 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.08 M SODIUM REMARK 280 ACETATE, AND 20% [V/V] GLYCEROL, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 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 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 54.20550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.64600 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.08800 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.20550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.64600 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.08800 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.20550 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 68.64600 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.08800 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.20550 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 68.64600 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.08800 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 APPLY THE FOLLOWING TO CHAINS: B, C, D, A 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 HIS C 119 REMARK 465 HIS C 120 REMARK 465 HIS C 121 REMARK 465 HIS C 122 REMARK 465 GLY D 109 REMARK 465 THR D 110 REMARK 465 GLN D 111 REMARK 465 VAL D 112 REMARK 465 THR D 113 REMARK 465 VAL D 114 REMARK 465 SER D 115 REMARK 465 SER D 116 REMARK 465 HIS D 117 REMARK 465 HIS D 118 REMARK 465 HIS D 119 REMARK 465 HIS D 120 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 THR A 224 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 GLN B 277 -164.04 -119.08 REMARK 500 ARG B 373 4.31 -163.58 REMARK 500 VAL B 386 -52.59 -127.32 REMARK 500 SER D 84 77.35 51.65 REMARK 500 PRO A 243 64.10 -69.35 REMARK 500 ARG A 373 -8.17 -140.73 REMARK 500 VAL A 386 -53.36 -120.98 REMARK 500 SER A 442 140.00 -170.15 REMARK 500 ASP A 518 -68.26 -99.38 REMARK 500 REMARK 500 REMARK: NULL DBREF 8EN4 B 224 531 UNP K4LM89 K4LM89_9CALI 224 531 DBREF 8EN4 C 1 122 PDB 8EN4 8EN4 1 122 DBREF 8EN4 D 1 122 PDB 8EN4 8EN4 1 122 DBREF 8EN4 A 224 531 UNP K4LM89 K4LM89_9CALI 224 531 SEQRES 1 B 308 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 B 308 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 B 308 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 B 308 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 B 308 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 B 308 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 B 308 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 B 308 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 B 308 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 B 308 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 B 308 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 B 308 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 B 308 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 B 308 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 B 308 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 B 308 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 B 308 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 B 308 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 B 308 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 B 308 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 B 308 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 B 308 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 B 308 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 B 308 GLN PHE TYR THR LEU ALA PRO MET GLY SEQRES 1 C 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 122 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 122 ASP ILE PHE SER ILE TYR LEU MET GLY TRP TYR ARG GLN SEQRES 4 C 122 SER PRO GLY LYS GLN ARG GLU LEU VAL ALA THR ILE THR SEQRES 5 C 122 SER SER GLY GLU THR LYS HIS VAL TYR SER VAL LYS GLY SEQRES 6 C 122 ARG PHE THR ILE SER ARG GLU ASN ALA LYS ASN ALA TRP SEQRES 7 C 122 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY SEQRES 8 C 122 VAL TYR TYR CYS HIS ALA VAL THR GLY VAL ILE ALA SER SEQRES 9 C 122 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 C 122 HIS HIS HIS HIS HIS SEQRES 1 D 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 122 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 122 ASP ILE PHE SER ILE TYR LEU MET GLY TRP TYR ARG GLN SEQRES 4 D 122 SER PRO GLY LYS GLN ARG GLU LEU VAL ALA THR ILE THR SEQRES 5 D 122 SER SER GLY GLU THR LYS HIS VAL TYR SER VAL LYS GLY SEQRES 6 D 122 ARG PHE THR ILE SER ARG GLU ASN ALA LYS ASN ALA TRP SEQRES 7 D 122 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY SEQRES 8 D 122 VAL TYR TYR CYS HIS ALA VAL THR GLY VAL ILE ALA SER SEQRES 9 D 122 SER TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 D 122 HIS HIS HIS HIS HIS SEQRES 1 A 308 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 A 308 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 A 308 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 A 308 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 A 308 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 A 308 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 A 308 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 A 308 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 A 308 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 A 308 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 A 308 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 A 308 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 A 308 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 A 308 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 A 308 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 A 308 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 A 308 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 A 308 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 A 308 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 A 308 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 A 308 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 A 308 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 A 308 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 A 308 GLN PHE TYR THR LEU ALA PRO MET GLY HET EDO C 201 4 HET EDO C 202 4 HET EDO A 601 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 EDO 3(C2 H6 O2) FORMUL 8 HOH *113(H2 O) HELIX 1 AA1 PRO B 454 ALA B 465 1 12 HELIX 2 AA2 ILE C 28 ILE C 31 5 4 HELIX 3 AA3 TYR C 61 LYS C 64 5 4 HELIX 4 AA4 LYS C 86 THR C 90 5 5 HELIX 5 AA5 ASP D 27 ILE D 31 5 5 HELIX 6 AA6 TYR D 61 LYS D 64 5 4 HELIX 7 AA7 LYS D 86 THR D 90 5 5 HELIX 8 AA8 THR A 233 MET A 237 5 5 HELIX 9 AA9 ALA A 359 LEU A 362 5 4 HELIX 10 AB1 PRO A 454 ALA A 465 1 12 SHEET 1 AA1 8 LYS B 248 GLY B 252 0 SHEET 2 AA1 8 GLU B 429 THR B 437 -1 O PHE B 433 N PHE B 250 SHEET 3 AA1 8 ASP B 448 CYS B 451 -1 O LEU B 449 N SER B 436 SHEET 4 AA1 8 VAL B 472 VAL B 478 0 SHEET 5 AA1 8 VAL B 485 HIS B 492 -1 O LEU B 486 N PHE B 477 SHEET 6 AA1 8 TYR B 496 ALA B 500 -1 O TYR B 496 N HIS B 492 SHEET 7 AA1 8 HIS B 505 LEU B 507 -1 O LEU B 507 N LEU B 249 SHEET 8 AA1 8 TYR B 514 VAL B 521 -1 O SER B 519 N LEU B 474 SHEET 1 AA214 PHE B 286 THR B 291 0 SHEET 2 AA214 ASN B 298 LEU B 303 -1 O THR B 300 N THR B 291 SHEET 3 AA214 LYS B 329 THR B 337 0 SHEET 4 AA214 THR B 344 TYR B 352 -1 O HIS B 347 N LEU B 334 SHEET 5 AA214 ARG B 364 THR B 369 -1 O GLU B 368 N THR B 350 SHEET 6 AA214 THR B 381 ILE B 389 -1 O GLY B 387 N GLN B 331 SHEET 7 AA214 GLY B 440 GLY B 443 1 O CYS B 441 N VAL B 388 SHEET 8 AA214 PHE A 286 HIS A 292 0 SHEET 9 AA214 ASN A 298 LEU A 303 -1 O THR A 300 N THR A 291 SHEET 10 AA214 LYS A 329 THR A 337 0 SHEET 11 AA214 THR A 344 TYR A 352 -1 O ALA A 349 N GLY A 332 SHEET 12 AA214 ARG A 364 THR A 369 -1 O GLU A 368 N THR A 350 SHEET 13 AA214 THR A 381 ILE A 389 -1 O LYS A 382 N THR A 335 SHEET 14 AA214 GLY A 440 GLY A 443 1 O CYS A 441 N VAL A 388 SHEET 1 AA3 4 VAL C 2 SER C 7 0 SHEET 2 AA3 4 LEU C 18 GLY C 26 -1 O ALA C 23 N GLN C 5 SHEET 3 AA3 4 ALA C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA3 4 PHE C 67 ARG C 71 -1 N SER C 70 O TYR C 79 SHEET 1 AA4 7 GLY C 10 VAL C 12 0 SHEET 2 AA4 7 LEU C 33 GLN C 39 0 SHEET 3 AA4 7 ARG C 45 THR C 52 -1 O ILE C 51 N MET C 34 SHEET 4 AA4 7 THR C 57 HIS C 59 -1 O LYS C 58 N THR C 50 SHEET 5 AA4 7 GLY C 91 VAL C 98 -1 O TYR C 94 N TYR C 37 SHEET 6 AA4 7 SER C 104 TRP C 106 -1 O SER C 105 N ALA C 97 SHEET 7 AA4 7 THR C 110 VAL C 114 -1 O THR C 110 N TYR C 93 SHEET 1 AA5 4 GLN D 3 SER D 7 0 SHEET 2 AA5 4 SER D 17 SER D 25 -1 O ALA D 23 N GLN D 5 SHEET 3 AA5 4 ALA D 77 ASN D 83 -1 O MET D 82 N LEU D 18 SHEET 4 AA5 4 PHE D 67 ARG D 71 -1 N SER D 70 O TYR D 79 SHEET 1 AA6 5 THR D 57 HIS D 59 0 SHEET 2 AA6 5 GLU D 46 THR D 52 -1 N THR D 50 O LYS D 58 SHEET 3 AA6 5 LEU D 33 GLN D 39 -1 N MET D 34 O ILE D 51 SHEET 4 AA6 5 VAL D 92 VAL D 98 -1 O TYR D 94 N TYR D 37 SHEET 5 AA6 5 SER D 104 TRP D 106 -1 O SER D 105 N ALA D 97 SHEET 1 AA7 8 LYS A 248 GLY A 252 0 SHEET 2 AA7 8 GLU A 429 THR A 437 -1 O PHE A 433 N PHE A 250 SHEET 3 AA7 8 ASP A 448 CYS A 451 -1 O CYS A 451 N PHE A 434 SHEET 4 AA7 8 VAL A 472 VAL A 478 0 SHEET 5 AA7 8 VAL A 485 HIS A 492 -1 O LEU A 491 N ALA A 473 SHEET 6 AA7 8 TYR A 496 ALA A 500 -1 O TYR A 496 N HIS A 492 SHEET 7 AA7 8 HIS A 505 LEU A 507 -1 O HIS A 505 N THR A 251 SHEET 8 AA7 8 TYR A 514 VAL A 521 -1 O ASP A 518 N LEU A 474 SSBOND 1 CYS C 22 CYS C 95 1555 1555 2.04 SSBOND 2 CYS D 22 CYS D 95 1555 1555 2.04 CISPEP 1 GLU B 399 PRO B 400 0 -3.40 CISPEP 2 GLU A 399 PRO A 400 0 -3.62 CRYST1 108.411 137.292 140.176 90.00 90.00 90.00 I 2 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 0.009224 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007284 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007134 0.00000