HEADER VIRAL PROTEIN 28-SEP-22 8EN6 TITLE STRUCTURE OF GII.17 NOROVIRUS IN COMPLEX WITH NANOBODY 76 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GII.17 P DOMAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 76; 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, INHIBITOR, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.KHER,C.SABIN,M.PANCERA,A.KOROMYSLOVA,G.HANSMAN JRNL AUTH G.KHER,C.SABIN,M.PANCERA,A.KOROMYSLOVA,G.HANSMAN JRNL TITL STRUCTURE OF GII.17 NOROVIRUS IN COMPLEX WITH NANOBODY 76 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.60 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 150255 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 7305 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 64.3100 - 4.9700 0.98 5045 215 0.1686 0.1779 REMARK 3 2 4.9700 - 3.9500 1.00 4890 273 0.1395 0.1571 REMARK 3 3 3.9500 - 3.4500 1.00 4880 221 0.1597 0.1625 REMARK 3 4 3.4500 - 3.1300 0.99 4787 249 0.1682 0.1876 REMARK 3 5 3.1300 - 2.9100 1.00 4852 234 0.1716 0.1797 REMARK 3 6 2.9100 - 2.7400 1.00 4800 227 0.1768 0.1937 REMARK 3 7 2.7400 - 2.6000 1.00 4766 275 0.1752 0.2069 REMARK 3 8 2.6000 - 2.4900 1.00 4762 252 0.1783 0.2027 REMARK 3 9 2.4900 - 2.3900 1.00 4757 258 0.1750 0.2034 REMARK 3 10 2.3900 - 2.3100 1.00 4780 239 0.1754 0.2132 REMARK 3 11 2.3100 - 2.2400 1.00 4724 274 0.1709 0.2058 REMARK 3 12 2.2400 - 2.1700 1.00 4748 253 0.1648 0.1887 REMARK 3 13 2.1700 - 2.1100 1.00 4744 270 0.1677 0.1779 REMARK 3 14 2.1100 - 2.0600 1.00 4739 256 0.1622 0.1823 REMARK 3 15 2.0600 - 2.0200 1.00 4728 243 0.1621 0.1932 REMARK 3 16 2.0200 - 1.9700 1.00 4735 260 0.1623 0.1714 REMARK 3 17 1.9700 - 1.9300 1.00 4735 254 0.1685 0.2064 REMARK 3 18 1.9300 - 1.9000 1.00 4755 225 0.1815 0.2147 REMARK 3 19 1.9000 - 1.8600 1.00 4695 272 0.1877 0.2321 REMARK 3 20 1.8600 - 1.8300 1.00 4754 240 0.1908 0.2033 REMARK 3 21 1.8300 - 1.8000 0.99 4688 238 0.1892 0.2319 REMARK 3 22 1.8000 - 1.7700 0.99 4682 241 0.1917 0.2053 REMARK 3 23 1.7700 - 1.7500 0.99 4756 225 0.1907 0.2102 REMARK 3 24 1.7500 - 1.7200 1.00 4733 226 0.1943 0.2182 REMARK 3 25 1.7200 - 1.7000 1.00 4686 234 0.1968 0.2284 REMARK 3 26 1.7000 - 1.6800 1.00 4753 239 0.2025 0.2290 REMARK 3 27 1.6800 - 1.6600 1.00 4746 213 0.2042 0.2293 REMARK 3 28 1.6600 - 1.6400 1.00 4737 232 0.2173 0.2518 REMARK 3 29 1.6400 - 1.6200 1.00 4688 240 0.2225 0.2683 REMARK 3 30 1.6200 - 1.6000 1.00 4805 227 0.2315 0.2465 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) : 0.140 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.310 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 11.67 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.69 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 8EN6 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_1000267284. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-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) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 171712 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530 REMARK 200 RESOLUTION RANGE LOW (A) : 87.370 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.08300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.75100 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 (%): 59.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 17% [W/V] PEG4000, 0.0095 M HEPES [PH REMARK 280 7.5], 8.5% [V/V] ISOPROPANOL, AND 15% GLYCEROL, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 37.20600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.90800 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.85300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.90800 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.20600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.85300 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D 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 D 121 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 O3 GOL A 602 O2 GOL A 604 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP B 269 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES 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 SER A 254 19.25 -142.16 REMARK 500 GLN A 260 50.49 -140.46 REMARK 500 ALA A 359 58.56 -141.86 REMARK 500 ARG A 373 -12.12 -144.77 REMARK 500 VAL A 386 -52.65 -120.76 REMARK 500 ALA C 91 166.03 175.49 REMARK 500 HIS C 120 4.27 -64.85 REMARK 500 GLN B 260 51.36 -140.43 REMARK 500 ALA B 359 56.96 -143.14 REMARK 500 ARG B 373 -9.94 -151.59 REMARK 500 VAL B 386 -51.87 -120.93 REMARK 500 ASN D 76 51.94 39.83 REMARK 500 SER D 119 30.22 -99.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B1004 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH B1005 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH D 446 DISTANCE = 5.83 ANGSTROMS DBREF 8EN6 A 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EN6 C 1 121 PDB 8EN6 8EN6 1 121 DBREF 8EN6 B 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EN6 D 1 121 PDB 8EN6 8EN6 1 121 SEQRES 1 A 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 A 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 A 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 A 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 A 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 A 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 A 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 A 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 A 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 A 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 A 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 A 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 A 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 A 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 A 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 A 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 A 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 A 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 A 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 A 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 A 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 A 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 A 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 A 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 C 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 121 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 121 THR ILE PHE SER ILE ASP ALA PHE GLY TRP TYR ARG GLN SEQRES 4 C 121 ALA PRO GLY LYS GLN ARG GLU TRP VAL ALA GLY ILE THR SEQRES 5 C 121 SER GLY SER SER THR ILE TYR ALA ASP PHE VAL LYS GLY SEQRES 6 C 121 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 C 121 PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 121 VAL TYR TYR CYS ASN ARG ALA LYS PRO PRO THR TYR TYR SEQRES 9 C 121 SER LEU GLU PRO TRP GLY LYS GLY THR GLN VAL THR VAL SEQRES 10 C 121 SER SER HIS HIS SEQRES 1 B 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 B 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 B 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 B 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 B 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 B 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 B 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 B 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 B 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 B 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 B 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 B 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 B 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 B 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 B 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 B 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 B 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 B 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 B 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 B 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 B 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 B 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 B 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 B 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 D 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 121 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 121 THR ILE PHE SER ILE ASP ALA PHE GLY TRP TYR ARG GLN SEQRES 4 D 121 ALA PRO GLY LYS GLN ARG GLU TRP VAL ALA GLY ILE THR SEQRES 5 D 121 SER GLY SER SER THR ILE TYR ALA ASP PHE VAL LYS GLY SEQRES 6 D 121 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 D 121 PHE LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 121 VAL TYR TYR CYS ASN ARG ALA LYS PRO PRO THR TYR TYR SEQRES 9 D 121 SER LEU GLU PRO TRP GLY LYS GLY THR GLN VAL THR VAL SEQRES 10 D 121 SER SER HIS HIS HET GOL A 601 6 HET GOL A 602 6 HET IPA A 603 4 HET GOL A 604 6 HET EDO A 605 4 HET EDO A 606 10 HET EDO A 607 10 HET GOL B 601 6 HET EDO B 602 4 HET DMS B 603 10 HET EDO B 604 10 HET EDO B 605 10 HET EDO D 201 4 HET GOL D 202 6 HET IPA D 203 4 HETNAM GOL GLYCEROL HETNAM IPA ISOPROPYL ALCOHOL HETNAM EDO 1,2-ETHANEDIOL HETNAM DMS DIMETHYL SULFOXIDE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN IPA 2-PROPANOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 GOL 5(C3 H8 O3) FORMUL 7 IPA 2(C3 H8 O) FORMUL 9 EDO 7(C2 H6 O2) FORMUL 14 DMS C2 H6 O S FORMUL 20 HOH *872(H2 O) HELIX 1 AA1 THR A 233 MET A 237 5 5 HELIX 2 AA2 SER A 279 ILE A 283 5 5 HELIX 3 AA3 ALA A 359 LEU A 362 5 4 HELIX 4 AA4 PRO A 454 ALA A 465 1 12 HELIX 5 AA5 ILE C 28 ASP C 32 5 5 HELIX 6 AA6 ASN C 73 LYS C 75 5 3 HELIX 7 AA7 LYS C 86 THR C 90 5 5 HELIX 8 AA8 THR B 233 MET B 237 5 5 HELIX 9 AA9 SER B 279 ILE B 283 5 5 HELIX 10 AB1 ALA B 359 LEU B 362 5 4 HELIX 11 AB2 PRO B 454 ALA B 465 1 12 HELIX 12 AB3 ILE D 28 ASP D 32 5 5 HELIX 13 AB4 ASP D 61 LYS D 64 5 4 HELIX 14 AB5 ASN D 73 LYS D 75 5 3 HELIX 15 AB6 LYS D 86 THR D 90 5 5 SHEET 1 AA1 8 LYS A 248 THR A 251 0 SHEET 2 AA1 8 GLU A 429 THR A 437 -1 O PHE A 433 N PHE A 250 SHEET 3 AA1 8 ASP A 448 CYS A 451 -1 O CYS A 451 N PHE A 434 SHEET 4 AA1 8 VAL A 472 VAL A 478 0 SHEET 5 AA1 8 VAL A 485 HIS A 492 -1 O LEU A 486 N PHE A 477 SHEET 6 AA1 8 TYR A 496 ALA A 500 -1 O TYR A 496 N HIS A 492 SHEET 7 AA1 8 HIS A 505 ASP A 506 -1 O HIS A 505 N THR A 251 SHEET 8 AA1 8 TYR A 514 VAL A 521 -1 O SER A 519 N LEU A 474 SHEET 1 AA214 PHE A 286 HIS A 292 0 SHEET 2 AA214 ASN A 298 LEU A 303 -1 O ASN A 302 N ASP A 289 SHEET 3 AA214 LYS A 329 THR A 337 0 SHEET 4 AA214 THR A 344 TYR A 352 -1 O ALA A 349 N GLY A 332 SHEET 5 AA214 ARG A 364 THR A 369 -1 O GLU A 368 N THR A 350 SHEET 6 AA214 THR A 381 ILE A 389 -1 O LYS A 382 N THR A 335 SHEET 7 AA214 GLY A 440 GLY A 443 1 O CYS A 441 N VAL A 388 SHEET 8 AA214 PHE B 286 THR B 291 0 SHEET 9 AA214 ASN B 298 LEU B 303 -1 O ASN B 302 N ASP B 289 SHEET 10 AA214 LYS B 329 THR B 337 0 SHEET 11 AA214 THR B 344 TYR B 352 -1 O ALA B 349 N GLY B 332 SHEET 12 AA214 ARG B 364 THR B 369 -1 O GLU B 368 N THR B 350 SHEET 13 AA214 THR B 381 ILE B 389 -1 O LYS B 382 N THR B 335 SHEET 14 AA214 GLY B 440 GLY B 443 1 O CYS B 441 N VAL B 388 SHEET 1 AA3 4 GLN C 3 SER C 7 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 AA3 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA3 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AA4 7 GLY C 10 GLN C 13 0 SHEET 2 AA4 7 ALA C 33 GLN C 39 0 SHEET 3 AA4 7 GLU C 46 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 4 AA4 7 THR C 57 TYR C 59 -1 O ILE C 58 N GLY C 50 SHEET 5 AA4 7 ALA C 91 LYS C 99 -1 O TYR C 94 N TYR C 37 SHEET 6 AA4 7 TYR C 104 SER C 105 -1 O TYR C 104 N LYS C 99 SHEET 7 AA4 7 THR C 113 SER C 118 -1 O VAL C 115 N ALA C 91 SHEET 1 AA5 8 LYS B 248 THR B 251 0 SHEET 2 AA5 8 GLU B 429 THR B 437 -1 O PHE B 433 N PHE B 250 SHEET 3 AA5 8 ASP B 448 CYS B 451 -1 O CYS B 451 N PHE B 434 SHEET 4 AA5 8 VAL B 472 VAL B 478 0 SHEET 5 AA5 8 VAL B 485 HIS B 492 -1 O LEU B 491 N ALA B 473 SHEET 6 AA5 8 TYR B 496 ALA B 500 -1 O TYR B 496 N HIS B 492 SHEET 7 AA5 8 HIS B 505 ASP B 506 -1 O HIS B 505 N THR B 251 SHEET 8 AA5 8 TYR B 514 VAL B 521 -1 O SER B 519 N LEU B 474 SHEET 1 AA6 4 GLN D 3 SER D 7 0 SHEET 2 AA6 4 LEU D 18 SER D 25 -1 O ALA D 23 N GLN D 5 SHEET 3 AA6 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AA6 4 PHE D 67 ASP D 72 -1 N THR D 68 O GLN D 81 SHEET 1 AA7 7 GLY D 10 GLN D 13 0 SHEET 2 AA7 7 ALA D 33 GLN D 39 0 SHEET 3 AA7 7 GLU D 46 ILE D 51 -1 O VAL D 48 N TRP D 36 SHEET 4 AA7 7 THR D 57 TYR D 59 -1 O ILE D 58 N GLY D 50 SHEET 5 AA7 7 ALA D 91 LYS D 99 -1 O TYR D 94 N TYR D 37 SHEET 6 AA7 7 TYR D 104 SER D 105 -1 O TYR D 104 N LYS D 99 SHEET 7 AA7 7 THR D 113 SER D 118 -1 O THR D 113 N TYR D 93 SSBOND 1 CYS C 22 CYS C 95 1555 1555 2.03 SSBOND 2 CYS D 22 CYS D 95 1555 1555 2.01 CISPEP 1 GLU A 399 PRO A 400 0 -9.30 CISPEP 2 PRO C 100 PRO C 101 0 5.27 CISPEP 3 GLU B 399 PRO B 400 0 -8.18 CISPEP 4 PRO D 100 PRO D 101 0 5.54 CRYST1 74.412 119.706 127.816 90.00 90.00 90.00 P 21 21 21 8 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 0.013439 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008354 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007824 0.00000