HEADER VIRAL PROTEIN 28-SEP-22 8EMY TITLE STRUCTURE OF GII.4 NOROVIRUS IN COMPLEX WITH NANOBODY 82 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GII.4 P DOMAIN; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 82; COMPND 7 CHAIN: G, H, I, J, K, L; 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.4 NOROVIRUS IN COMPLEX WITH NANOBODY 82 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.70 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) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.39 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 377871 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.177 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.530 REMARK 3 FREE R VALUE TEST SET COUNT : 3843 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 61.3900 - 5.1000 0.98 27641 149 0.1506 0.1728 REMARK 3 2 5.1000 - 4.0500 0.99 27988 151 0.1293 0.1183 REMARK 3 3 4.0500 - 3.5400 0.98 27559 144 0.1558 0.2040 REMARK 3 4 3.5400 - 3.2100 0.98 27761 146 0.1728 0.1902 REMARK 3 5 3.2100 - 2.9800 0.99 27726 150 0.1767 0.1820 REMARK 3 6 2.9800 - 2.8100 0.99 27900 147 0.1864 0.2323 REMARK 3 7 2.8100 - 2.6700 0.98 27680 150 0.1846 0.2135 REMARK 3 8 2.6700 - 2.5500 0.98 27713 149 0.1892 0.1941 REMARK 3 9 2.5500 - 2.4500 0.99 27856 149 0.1845 0.2031 REMARK 3 10 2.4500 - 2.3700 0.99 27916 148 0.1842 0.2031 REMARK 3 11 2.3700 - 2.2900 0.99 27981 148 0.1818 0.2148 REMARK 3 12 2.2900 - 2.2300 0.90 25473 129 0.2099 0.2418 REMARK 3 13 2.2300 - 2.1700 0.99 27718 147 0.1828 0.2270 REMARK 3 14 2.1700 - 2.1200 0.98 27579 146 0.1826 0.1812 REMARK 3 15 2.1200 - 2.0700 0.94 26541 141 0.1964 0.2015 REMARK 3 16 2.0700 - 2.0200 0.93 26013 139 0.1981 0.2335 REMARK 3 17 2.0200 - 1.9800 0.98 27484 148 0.1845 0.2559 REMARK 3 18 1.9800 - 1.9500 0.97 27491 147 0.1997 0.2525 REMARK 3 19 1.9500 - 1.9100 0.90 25216 133 0.2714 0.3454 REMARK 3 20 1.9100 - 1.8800 0.96 26936 149 0.2362 0.3171 REMARK 3 21 1.8800 - 1.8500 0.98 27605 146 0.2102 0.2655 REMARK 3 22 1.8500 - 1.8200 0.98 27613 145 0.1911 0.2208 REMARK 3 23 1.8200 - 1.7900 0.98 27481 146 0.1984 0.1989 REMARK 3 24 1.7900 - 1.7700 0.93 26239 137 0.2018 0.1765 REMARK 3 25 1.7700 - 1.7400 0.85 23968 129 0.2098 0.2316 REMARK 3 26 1.7400 - 1.7200 0.79 22410 116 0.2339 0.2660 REMARK 3 27 1.7200 - 1.7000 0.75 21096 114 0.2614 0.3320 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) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.950 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.38 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 8EMY 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_1000267285. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-SEP-19 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) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 380256 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 117.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.38800 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 (%): 61.16 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5% [W/V] PEG 6000 AND 0.1M HEPES [PH REMARK 280 7.0], VAPOR DIFFUSION, 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 60.51050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.98450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.22950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.98450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.51050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.22950 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, 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 HIS J 117 REMARK 465 HIS J 118 REMARK 465 HIS J 119 REMARK 465 HIS J 120 REMARK 465 HIS J 121 REMARK 465 HIS J 122 REMARK 465 HIS L 118 REMARK 465 HIS L 119 REMARK 465 HIS L 120 REMARK 465 HIS L 121 REMARK 465 HIS L 122 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 HIS L 117 CG ND1 CD2 CE1 NE2 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 CYS J 96 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 CYS K 96 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 CYS L 96 CA - CB - SG ANGL. DEV. = 8.7 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 21.04 -144.97 REMARK 500 GLN A 260 50.89 -145.15 REMARK 500 ARG A 373 -15.60 -151.20 REMARK 500 VAL A 386 -53.06 -123.25 REMARK 500 SER A 442 143.14 -179.66 REMARK 500 VAL A 521 -167.23 -128.45 REMARK 500 ARG B 373 -5.94 -154.61 REMARK 500 VAL B 386 -54.69 -122.13 REMARK 500 SER B 442 143.67 -179.17 REMARK 500 VAL B 521 -161.17 -128.84 REMARK 500 SER C 254 14.80 -142.18 REMARK 500 GLN C 260 50.05 -143.09 REMARK 500 ARG C 373 -10.80 -157.07 REMARK 500 VAL C 386 -53.51 -122.89 REMARK 500 SER C 442 144.11 -176.39 REMARK 500 SER C 519 146.47 -174.43 REMARK 500 SER D 254 17.11 -140.94 REMARK 500 GLN D 260 50.49 -140.97 REMARK 500 ARG D 373 -11.14 -150.28 REMARK 500 VAL D 386 -50.97 -123.76 REMARK 500 SER D 442 145.20 -174.86 REMARK 500 SER D 519 143.87 -175.81 REMARK 500 SER E 254 19.75 -142.20 REMARK 500 GLN E 260 51.72 -141.69 REMARK 500 ARG E 373 -13.79 -156.23 REMARK 500 VAL E 386 -50.56 -121.86 REMARK 500 SER E 442 144.58 -177.07 REMARK 500 VAL E 521 -167.98 -128.84 REMARK 500 ALA F 319 167.96 179.46 REMARK 500 ARG F 373 -21.17 -150.66 REMARK 500 VAL F 386 -52.57 -120.36 REMARK 500 ASP F 391 104.65 -57.11 REMARK 500 SER F 442 140.97 -177.35 REMARK 500 PHE G 29 -64.84 60.86 REMARK 500 ALA G 92 168.86 177.58 REMARK 500 ALA G 101 -120.96 58.45 REMARK 500 HIS G 118 32.20 -140.86 REMARK 500 PHE H 29 -66.60 63.85 REMARK 500 ALA H 92 171.17 178.52 REMARK 500 ALA H 101 -117.47 51.53 REMARK 500 PHE I 29 -65.31 64.59 REMARK 500 ALA I 92 167.41 176.26 REMARK 500 ALA I 101 -118.25 54.77 REMARK 500 PHE J 29 -63.47 62.75 REMARK 500 ALA J 92 171.65 176.53 REMARK 500 ALA J 101 -115.80 54.88 REMARK 500 PHE K 29 -67.43 65.67 REMARK 500 ALA K 92 165.44 173.40 REMARK 500 ALA K 101 -119.56 56.86 REMARK 500 PHE L 29 -66.60 62.93 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. 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 D 964 DISTANCE = 6.64 ANGSTROMS DBREF 8EMY A 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY B 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY C 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY D 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY E 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY F 224 530 UNP K4LM89 K4LM89_9CALI 224 530 DBREF 8EMY G 1 122 PDB 8EMY 8EMY 1 122 DBREF 8EMY H 1 122 PDB 8EMY 8EMY 1 122 DBREF 8EMY I 1 122 PDB 8EMY 8EMY 1 122 DBREF 8EMY J 1 122 PDB 8EMY 8EMY 1 122 DBREF 8EMY K 1 122 PDB 8EMY 8EMY 1 122 DBREF 8EMY L 1 122 PDB 8EMY 8EMY 1 122 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 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 C 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 C 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 C 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 C 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 C 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 C 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 C 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 C 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 C 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 C 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 C 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 C 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 C 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 C 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 C 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 C 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 C 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 C 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 C 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 C 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 C 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 C 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 C 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 C 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 D 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 D 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 D 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 D 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 D 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 D 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 D 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 D 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 D 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 D 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 D 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 D 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 D 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 D 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 D 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 D 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 D 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 D 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 D 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 D 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 D 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 D 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 D 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 D 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 E 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 E 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 E 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 E 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 E 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 E 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 E 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 E 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 E 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 E 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 E 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 E 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 E 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 E 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 E 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 E 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 E 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 E 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 E 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 E 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 E 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 E 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 E 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 E 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 F 307 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 F 307 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 F 307 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 F 307 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 F 307 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 F 307 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 F 307 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 F 307 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 F 307 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 F 307 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 F 307 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 F 307 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 F 307 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 F 307 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 F 307 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 F 307 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 F 307 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 F 307 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 F 307 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 F 307 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 F 307 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 F 307 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 F 307 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 F 307 GLN PHE TYR THR LEU ALA PRO MET SEQRES 1 G 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 G 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 G 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 G 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 G 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 G 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 G 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 G 122 HIS HIS HIS HIS HIS SEQRES 1 H 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 H 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 H 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 H 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 H 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 H 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 H 122 HIS HIS HIS HIS HIS SEQRES 1 I 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 I 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 I 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 I 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 I 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 I 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 I 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 I 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 I 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 I 122 HIS HIS HIS HIS HIS SEQRES 1 J 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 J 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 J 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 J 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 J 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 J 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 J 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 J 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 J 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 J 122 HIS HIS HIS HIS HIS SEQRES 1 K 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 K 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 K 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 K 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 K 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 K 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 K 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 K 122 HIS HIS HIS HIS HIS SEQRES 1 L 122 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 L 122 PRO GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 L 122 PHE THR PHE GLY GLY TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 L 122 ALA PRO GLY LYS GLY PRO GLU TRP VAL SER SER ILE ASN SEQRES 5 L 122 SER GLY GLY ASP ILE THR ASN TYR ALA THR SER VAL LYS SEQRES 6 L 122 GLY ARG PHE SER ILE SER ARG ASP ASN PRO SER LYS THR SEQRES 7 L 122 LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SER SEQRES 8 L 122 ALA VAL TYR TYR CYS LYS THR GLN LEU ALA ASN ARG ASP SEQRES 9 L 122 TYR ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 10 L 122 HIS HIS HIS HIS HIS HET EDO A 601 4 HET EDO A 602 4 HET EDO A 603 10 HET EDO A 604 10 HET EDO A 605 10 HET EDO A 606 4 HET EDO B 601 4 HET EDO B 602 10 HET EDO B 603 10 HET EDO B 604 10 HET EDO B 605 10 HET EDO C 601 4 HET EDO C 602 4 HET EDO C 603 4 HET EDO C 604 4 HET EDO C 605 10 HET EDO C 606 4 HET EDO D 601 4 HET EDO D 602 4 HET EDO D 603 4 HET EDO D 604 4 HET EDO D 605 4 HET EDO D 606 10 HET EDO D 607 10 HET EDO E 601 4 HET EDO E 602 10 HET EDO E 603 10 HET EDO E 604 10 HET EDO E 605 10 HET EDO F 601 4 HET EDO F 602 4 HET EDO F 603 10 HET EDO F 604 10 HET EDO F 605 4 HET EDO K 201 10 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 13 EDO 35(C2 H6 O2) FORMUL 48 HOH *2317(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 THR B 233 MET B 237 5 5 HELIX 6 AA6 SER B 279 ILE B 283 5 5 HELIX 7 AA7 PRO B 360 LEU B 362 5 3 HELIX 8 AA8 PRO B 454 ALA B 465 1 12 HELIX 9 AA9 THR C 233 MET C 237 5 5 HELIX 10 AB1 SER C 279 ILE C 283 5 5 HELIX 11 AB2 ALA C 359 LEU C 362 5 4 HELIX 12 AB3 PRO C 454 ALA C 465 1 12 HELIX 13 AB4 THR D 233 MET D 237 5 5 HELIX 14 AB5 SER D 279 ILE D 283 5 5 HELIX 15 AB6 ALA D 359 LEU D 362 5 4 HELIX 16 AB7 PRO D 454 ALA D 465 1 12 HELIX 17 AB8 THR E 233 MET E 237 5 5 HELIX 18 AB9 SER E 279 ILE E 283 5 5 HELIX 19 AC1 ALA E 359 LEU E 362 5 4 HELIX 20 AC2 PRO E 454 ALA E 465 1 12 HELIX 21 AC3 SER F 279 ILE F 283 5 5 HELIX 22 AC4 PRO F 360 LEU F 362 5 3 HELIX 23 AC5 PRO F 454 ALA F 465 1 12 HELIX 24 AC6 THR G 62 LYS G 65 5 4 HELIX 25 AC7 ARG G 87 SER G 91 5 5 HELIX 26 AC8 ARG H 87 SER H 91 5 5 HELIX 27 AC9 ARG I 87 SER I 91 5 5 HELIX 28 AD1 THR J 62 LYS J 65 5 4 HELIX 29 AD2 ARG J 87 SER J 91 5 5 HELIX 30 AD3 THR K 62 LYS K 65 5 4 HELIX 31 AD4 ARG K 87 SER K 91 5 5 HELIX 32 AD5 THR L 62 LYS L 65 5 4 HELIX 33 AD6 ARG L 87 SER L 91 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 491 N ALA A 473 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 THR A 384 N VAL A 333 SHEET 7 AA214 GLY A 440 GLY A 443 1 O CYS A 441 N VAL A 388 SHEET 8 AA214 PHE D 286 HIS D 292 0 SHEET 9 AA214 ASN D 298 LEU D 303 -1 O THR D 300 N THR D 291 SHEET 10 AA214 LYS D 329 THR D 337 0 SHEET 11 AA214 THR D 344 TYR D 352 -1 O ALA D 349 N GLY D 332 SHEET 12 AA214 ARG D 364 THR D 369 -1 O GLU D 368 N THR D 350 SHEET 13 AA214 THR D 381 ILE D 389 -1 O LYS D 382 N THR D 335 SHEET 14 AA214 GLY D 440 GLY D 443 1 O CYS D 441 N VAL D 388 SHEET 1 AA3 8 LYS B 248 GLY B 252 0 SHEET 2 AA3 8 GLU B 429 THR B 437 -1 O PHE B 433 N PHE B 250 SHEET 3 AA3 8 ASP B 448 CYS B 451 -1 O CYS B 451 N PHE B 434 SHEET 4 AA3 8 VAL B 472 VAL B 478 0 SHEET 5 AA3 8 VAL B 485 HIS B 492 -1 O LEU B 486 N PHE B 477 SHEET 6 AA3 8 TYR B 496 ALA B 500 -1 O TYR B 496 N HIS B 492 SHEET 7 AA3 8 HIS B 505 ASP B 506 -1 O HIS B 505 N THR B 251 SHEET 8 AA3 8 TYR B 514 VAL B 521 -1 O SER B 519 N LEU B 474 SHEET 1 AA415 PHE B 286 HIS B 292 0 SHEET 2 AA415 ASN B 298 LEU B 303 -1 O ASN B 302 N ASP B 289 SHEET 3 AA415 LYS B 329 THR B 337 0 SHEET 4 AA415 THR B 344 TYR B 352 -1 O ALA B 349 N GLY B 332 SHEET 5 AA415 PHE B 358 ALA B 359 0 SHEET 6 AA415 ARG B 364 THR B 369 -1 O ARG B 364 N ALA B 359 SHEET 7 AA415 THR B 381 ILE B 389 -1 O THR B 384 N VAL B 333 SHEET 8 AA415 GLY B 440 GLY B 443 1 O CYS B 441 N VAL B 388 SHEET 9 AA415 PHE E 286 HIS E 292 0 SHEET 10 AA415 ASN E 298 LEU E 303 -1 O ASN E 302 N ASP E 289 SHEET 11 AA415 LYS E 329 THR E 337 0 SHEET 12 AA415 THR E 344 TYR E 352 -1 O ALA E 349 N GLY E 332 SHEET 13 AA415 ARG E 364 THR E 369 -1 O GLU E 368 N THR E 350 SHEET 14 AA415 THR E 381 ILE E 389 -1 O LYS E 382 N THR E 335 SHEET 15 AA415 GLY E 440 GLY E 443 1 O CYS E 441 N VAL E 388 SHEET 1 AA5 8 LYS C 248 GLY C 252 0 SHEET 2 AA5 8 GLU C 429 THR C 437 -1 O PHE C 433 N PHE C 250 SHEET 3 AA5 8 ASP C 448 CYS C 451 -1 O CYS C 451 N PHE C 434 SHEET 4 AA5 8 VAL C 472 VAL C 478 0 SHEET 5 AA5 8 VAL C 485 HIS C 492 -1 O LEU C 491 N ALA C 473 SHEET 6 AA5 8 TYR C 496 ALA C 500 -1 O TYR C 496 N HIS C 492 SHEET 7 AA5 8 HIS C 505 ASP C 506 -1 O HIS C 505 N THR C 251 SHEET 8 AA5 8 TYR C 514 VAL C 521 -1 O SER C 519 N LEU C 474 SHEET 1 AA615 PHE C 286 HIS C 292 0 SHEET 2 AA615 ASN C 298 LEU C 303 -1 O ASN C 302 N ASP C 289 SHEET 3 AA615 LYS C 329 THR C 337 0 SHEET 4 AA615 THR C 344 TYR C 352 -1 O HIS C 347 N LEU C 334 SHEET 5 AA615 ARG C 364 THR C 369 -1 O GLU C 368 N THR C 350 SHEET 6 AA615 THR C 381 ILE C 389 -1 O LYS C 382 N THR C 335 SHEET 7 AA615 GLY C 440 GLY C 443 1 O CYS C 441 N VAL C 388 SHEET 8 AA615 PHE F 286 HIS F 292 0 SHEET 9 AA615 ASN F 298 LEU F 303 -1 O ASN F 302 N ASP F 289 SHEET 10 AA615 LYS F 329 THR F 337 0 SHEET 11 AA615 THR F 344 TYR F 352 -1 O ALA F 349 N GLY F 332 SHEET 12 AA615 PHE F 358 ALA F 359 0 SHEET 13 AA615 ARG F 364 THR F 369 -1 O ARG F 364 N ALA F 359 SHEET 14 AA615 THR F 381 ILE F 389 -1 O THR F 384 N VAL F 333 SHEET 15 AA615 GLY F 440 GLY F 443 1 O CYS F 441 N VAL F 388 SHEET 1 AA7 8 LYS D 248 GLY D 252 0 SHEET 2 AA7 8 GLU D 429 THR D 437 -1 O PHE D 433 N PHE D 250 SHEET 3 AA7 8 ASP D 448 CYS D 451 -1 O CYS D 451 N PHE D 434 SHEET 4 AA7 8 VAL D 472 VAL D 478 0 SHEET 5 AA7 8 VAL D 485 HIS D 492 -1 O LEU D 491 N ALA D 473 SHEET 6 AA7 8 TYR D 496 ALA D 500 -1 O TYR D 496 N HIS D 492 SHEET 7 AA7 8 HIS D 505 ASP D 506 -1 O HIS D 505 N THR D 251 SHEET 8 AA7 8 TYR D 514 VAL D 521 -1 O SER D 519 N LEU D 474 SHEET 1 AA8 8 LYS E 248 GLY E 252 0 SHEET 2 AA8 8 GLU E 429 THR E 437 -1 O PHE E 433 N PHE E 250 SHEET 3 AA8 8 ASP E 448 CYS E 451 -1 O CYS E 451 N PHE E 434 SHEET 4 AA8 8 VAL E 472 VAL E 478 0 SHEET 5 AA8 8 VAL E 485 HIS E 492 -1 O LEU E 491 N ALA E 473 SHEET 6 AA8 8 TYR E 496 ALA E 500 -1 O TYR E 496 N HIS E 492 SHEET 7 AA8 8 HIS E 505 ASP E 506 -1 O HIS E 505 N THR E 251 SHEET 8 AA8 8 TYR E 514 VAL E 521 -1 O SER E 519 N LEU E 474 SHEET 1 AA9 8 LYS F 248 GLY F 252 0 SHEET 2 AA9 8 GLU F 429 THR F 437 -1 O PHE F 433 N PHE F 250 SHEET 3 AA9 8 ASP F 448 CYS F 451 -1 O CYS F 451 N PHE F 434 SHEET 4 AA9 8 VAL F 472 VAL F 478 0 SHEET 5 AA9 8 VAL F 485 HIS F 492 -1 O LEU F 491 N ALA F 473 SHEET 6 AA9 8 TYR F 496 ALA F 500 -1 O TYR F 496 N HIS F 492 SHEET 7 AA9 8 HIS F 505 ASP F 506 -1 O HIS F 505 N THR F 251 SHEET 8 AA9 8 TYR F 514 VAL F 521 -1 O SER F 519 N LEU F 474 SHEET 1 AB1 4 GLN G 3 SER G 7 0 SHEET 2 AB1 4 LEU G 18 SER G 25 -1 O ALA G 23 N GLN G 5 SHEET 3 AB1 4 THR G 78 MET G 83 -1 O MET G 83 N LEU G 18 SHEET 4 AB1 4 PHE G 68 ASP G 73 -1 N SER G 69 O GLN G 82 SHEET 1 AB2 7 GLY G 10 VAL G 12 0 SHEET 2 AB2 7 MET G 34 GLN G 39 0 SHEET 3 AB2 7 GLU G 46 ILE G 51 -1 O SER G 49 N TRP G 36 SHEET 4 AB2 7 THR G 58 TYR G 60 -1 O ASN G 59 N SER G 50 SHEET 5 AB2 7 ALA G 92 LEU G 100 -1 O TYR G 95 N VAL G 37 SHEET 6 AB2 7 ARG G 103 ARG G 106 -1 O ARG G 103 N LEU G 100 SHEET 7 AB2 7 THR G 110 VAL G 114 -1 O THR G 110 N TYR G 94 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AB3 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB3 4 SER H 69 ASP H 73 -1 N SER H 69 O GLN H 82 SHEET 1 AB4 7 GLY H 10 VAL H 12 0 SHEET 2 AB4 7 MET H 34 GLN H 39 0 SHEET 3 AB4 7 GLU H 46 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 4 AB4 7 THR H 58 TYR H 60 -1 O ASN H 59 N SER H 50 SHEET 5 AB4 7 ALA H 92 LEU H 100 -1 O TYR H 95 N VAL H 37 SHEET 6 AB4 7 ARG H 103 ARG H 106 -1 O ARG H 103 N LEU H 100 SHEET 7 AB4 7 THR H 110 VAL H 114 -1 O THR H 110 N TYR H 94 SHEET 1 AB5 4 GLN I 3 SER I 7 0 SHEET 2 AB5 4 LEU I 18 SER I 25 -1 O SER I 21 N SER I 7 SHEET 3 AB5 4 THR I 78 MET I 83 -1 O MET I 83 N LEU I 18 SHEET 4 AB5 4 PHE I 68 ASP I 73 -1 N SER I 69 O GLN I 82 SHEET 1 AB6 7 GLY I 10 VAL I 12 0 SHEET 2 AB6 7 MET I 34 GLN I 39 0 SHEET 3 AB6 7 PRO I 45 ILE I 51 -1 O GLU I 46 N ARG I 38 SHEET 4 AB6 7 THR I 58 TYR I 60 -1 O ASN I 59 N SER I 50 SHEET 5 AB6 7 ALA I 92 LEU I 100 -1 O TYR I 95 N VAL I 37 SHEET 6 AB6 7 ARG I 103 ARG I 106 -1 O ARG I 103 N LEU I 100 SHEET 7 AB6 7 THR I 110 VAL I 114 -1 O THR I 110 N TYR I 94 SHEET 1 AB7 4 GLN J 3 SER J 7 0 SHEET 2 AB7 4 LEU J 18 SER J 25 -1 O SER J 21 N SER J 7 SHEET 3 AB7 4 THR J 78 MET J 83 -1 O MET J 83 N LEU J 18 SHEET 4 AB7 4 PHE J 68 ASP J 73 -1 N SER J 69 O GLN J 82 SHEET 1 AB8 7 GLY J 10 VAL J 12 0 SHEET 2 AB8 7 MET J 34 GLN J 39 0 SHEET 3 AB8 7 GLU J 46 ILE J 51 -1 O GLU J 46 N ARG J 38 SHEET 4 AB8 7 THR J 58 TYR J 60 -1 O ASN J 59 N SER J 50 SHEET 5 AB8 7 ALA J 92 LEU J 100 -1 O TYR J 95 N VAL J 37 SHEET 6 AB8 7 ARG J 103 ARG J 106 -1 O ARG J 103 N LEU J 100 SHEET 7 AB8 7 THR J 110 VAL J 114 -1 O THR J 110 N TYR J 94 SHEET 1 AB9 4 GLN K 3 SER K 7 0 SHEET 2 AB9 4 LEU K 18 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AB9 4 THR K 78 MET K 83 -1 O MET K 83 N LEU K 18 SHEET 4 AB9 4 PHE K 68 ASP K 73 -1 N SER K 69 O GLN K 82 SHEET 1 AC1 7 LEU K 11 VAL K 12 0 SHEET 2 AC1 7 MET K 34 GLN K 39 0 SHEET 3 AC1 7 PRO K 45 ILE K 51 -1 O SER K 49 N TRP K 36 SHEET 4 AC1 7 THR K 58 TYR K 60 -1 O ASN K 59 N SER K 50 SHEET 5 AC1 7 ALA K 92 LEU K 100 -1 O TYR K 95 N VAL K 37 SHEET 6 AC1 7 ARG K 103 ARG K 106 -1 O ARG K 103 N LEU K 100 SHEET 7 AC1 7 THR K 110 VAL K 114 -1 O THR K 110 N TYR K 94 SHEET 1 AC2 4 GLN L 3 SER L 7 0 SHEET 2 AC2 4 LEU L 18 SER L 25 -1 O ALA L 23 N GLN L 5 SHEET 3 AC2 4 THR L 78 MET L 83 -1 O MET L 83 N LEU L 18 SHEET 4 AC2 4 PHE L 68 ASP L 73 -1 N SER L 69 O GLN L 82 SHEET 1 AC3 7 GLY L 10 VAL L 12 0 SHEET 2 AC3 7 MET L 34 GLN L 39 0 SHEET 3 AC3 7 GLU L 46 ILE L 51 -1 O GLU L 46 N ARG L 38 SHEET 4 AC3 7 THR L 58 TYR L 60 -1 O ASN L 59 N SER L 50 SHEET 5 AC3 7 ALA L 92 LEU L 100 -1 O TYR L 95 N VAL L 37 SHEET 6 AC3 7 ARG L 103 ARG L 106 -1 O ARG L 103 N LEU L 100 SHEET 7 AC3 7 THR L 110 VAL L 114 -1 O VAL L 112 N ALA L 92 SSBOND 1 CYS G 22 CYS G 96 1555 1555 2.07 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.06 SSBOND 3 CYS I 22 CYS I 96 1555 1555 2.05 SSBOND 4 CYS J 22 CYS J 96 1555 1555 2.06 SSBOND 5 CYS K 22 CYS K 96 1555 1555 2.08 SSBOND 6 CYS L 22 CYS L 96 1555 1555 2.08 CISPEP 1 GLU A 399 PRO A 400 0 -4.93 CISPEP 2 GLU B 399 PRO B 400 0 -4.26 CISPEP 3 GLU C 399 PRO C 400 0 -3.74 CISPEP 4 GLU D 399 PRO D 400 0 -0.71 CISPEP 5 GLU E 399 PRO E 400 0 -4.53 CISPEP 6 GLU F 399 PRO F 400 0 -6.09 CRYST1 121.021 142.459 207.969 90.00 90.00 90.00 P 21 21 21 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 0.008263 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007020 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004808 0.00000