HEADER VIRAL PROTEIN 28-SEP-22 8EN1 TITLE STRUCTURE OF GII.4 NOROVIRUS IN COMPLEX WITH NANOBODY 30 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GII.4 P DOMAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY 30; 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.4 NOROVIRUS IN COMPLEX WITH NANOBODY 30 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 34056 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.860 REMARK 3 FREE R VALUE TEST SET COUNT : 3844 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 57.7500 - 7.2000 0.98 2271 135 0.1837 0.2315 REMARK 3 2 7.1900 - 5.7100 0.99 2288 144 0.1839 0.2183 REMARK 3 3 5.7100 - 4.9900 0.99 2328 154 0.1714 0.1873 REMARK 3 4 4.9900 - 4.5400 0.98 2220 140 0.1480 0.2512 REMARK 3 5 4.5300 - 4.2100 0.98 2265 148 0.1475 0.2218 REMARK 3 6 4.2100 - 3.9600 0.99 2329 141 0.1635 0.2301 REMARK 3 7 3.9600 - 3.7600 0.99 2263 146 0.1784 0.2187 REMARK 3 8 3.7600 - 3.6000 0.99 2317 142 0.1963 0.2562 REMARK 3 9 3.6000 - 3.4600 1.00 2282 137 0.1915 0.2464 REMARK 3 10 3.4600 - 3.3400 1.00 2335 146 0.2111 0.2605 REMARK 3 11 3.3400 - 3.2400 1.00 2294 143 0.2030 0.2513 REMARK 3 12 3.2400 - 3.1400 0.97 2230 134 0.2087 0.3016 REMARK 3 13 3.1400 - 3.0600 0.97 2269 151 0.2254 0.2710 REMARK 3 14 3.0600 - 2.9900 0.99 2295 148 0.2289 0.2401 REMARK 3 15 2.9900 - 2.9200 0.99 2294 137 0.2478 0.3391 REMARK 3 16 2.9200 - 2.8600 0.99 2273 145 0.2466 0.2970 REMARK 3 17 2.8600 - 2.8000 1.00 2311 136 0.2517 0.3116 REMARK 3 18 2.8000 - 2.7500 0.99 2320 133 0.2481 0.3419 REMARK 3 19 2.7500 - 2.7000 1.00 2306 156 0.2681 0.2839 REMARK 3 20 2.7000 - 2.6500 1.00 2316 142 0.2629 0.3734 REMARK 3 21 2.6500 - 2.6100 0.99 2289 135 0.2680 0.2655 REMARK 3 22 2.6100 - 2.5700 0.99 2261 151 0.2621 0.3300 REMARK 3 23 2.5700 - 2.5300 1.00 2350 133 0.2659 0.3770 REMARK 3 24 2.5300 - 2.5000 0.99 2285 145 0.2634 0.2454 REMARK 3 25 2.5000 - 2.4600 0.99 2295 148 0.2672 0.3485 REMARK 3 26 2.4600 - 2.4300 0.97 2226 129 0.2732 0.3198 REMARK 3 27 2.4300 - 2.4000 0.97 2230 145 0.2973 0.3627 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.000 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.33 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 8EN1 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_1000267421. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-OCT-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 : ESRF REMARK 200 BEAMLINE : ID13 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626 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 : XIA2 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34103 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 57.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.16700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : 0.55400 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: 4X7E REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: (0.2 M CALCIUM CHLORIDE AND 20% [W/V] REMARK 280 PEG3350), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2 REMARK 290 4555 -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 47.05230 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.22150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.53377 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 47.05230 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.22150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 59.53377 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, B, C, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 701 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 702 LIES ON A SPECIAL POSITION. 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 GLY A 531 REMARK 465 ASN A 532 REMARK 465 GLY A 533 REMARK 465 THR A 534 REMARK 465 GLY A 535 REMARK 465 ARG A 536 REMARK 465 ARG A 537 REMARK 465 ARG A 538 REMARK 465 ALA A 539 REMARK 465 VAL A 540 REMARK 465 GLY B 531 REMARK 465 ASN B 532 REMARK 465 GLY B 533 REMARK 465 THR B 534 REMARK 465 GLY B 535 REMARK 465 ARG B 536 REMARK 465 ARG B 537 REMARK 465 ARG B 538 REMARK 465 ALA B 539 REMARK 465 VAL B 540 REMARK 465 HIS C 135 REMARK 465 HIS D 130 REMARK 465 HIS D 131 REMARK 465 HIS D 132 REMARK 465 HIS D 133 REMARK 465 HIS D 134 REMARK 465 HIS D 135 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 OG SER B 470 O VAL B 521 2.16 REMARK 500 OG SER D 25 O HOH D 201 2.18 REMARK 500 NZ LYS B 329 OD1 ASP B 391 2.18 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 ASN A 282 40.49 -89.51 REMARK 500 ASP A 341 4.01 -151.87 REMARK 500 ARG A 373 -28.58 -153.18 REMARK 500 VAL A 386 -54.12 -120.17 REMARK 500 ASP A 391 -169.36 -127.04 REMARK 500 THR A 425 -64.34 -106.90 REMARK 500 SER A 442 144.66 -174.21 REMARK 500 GLN B 260 59.66 -141.18 REMARK 500 ASN B 282 40.31 -93.67 REMARK 500 THR B 369 -166.46 -113.12 REMARK 500 ARG B 373 -32.07 -156.27 REMARK 500 VAL B 386 -54.48 -121.77 REMARK 500 GLN B 390 109.27 -168.70 REMARK 500 ASP B 391 25.47 -148.94 REMARK 500 THR B 394 -136.93 42.17 REMARK 500 THR B 395 -29.74 -36.97 REMARK 500 HIS B 396 136.82 -38.01 REMARK 500 SER B 442 143.95 -171.03 REMARK 500 THR B 502 28.83 -153.05 REMARK 500 VAL C 48 -56.48 -120.16 REMARK 500 VAL D 48 -56.78 -121.95 REMARK 500 REMARK 500 REMARK: NULL DBREF 8EN1 A 224 540 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN1 B 224 540 UNP K4LM89 K4LM89_9CALI 224 540 DBREF 8EN1 C 1 135 PDB 8EN1 8EN1 1 135 DBREF 8EN1 D 1 135 PDB 8EN1 8EN1 1 135 SEQRES 1 A 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 A 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 A 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 A 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 A 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 A 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 A 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 A 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 A 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 A 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 A 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 A 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 A 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 A 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 A 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 A 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 A 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 A 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 A 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 A 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 A 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 A 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 A 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 A 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 A 317 ARG ARG ARG ALA VAL SEQRES 1 B 317 THR LYS PRO PHE SER VAL PRO VAL LEU THR VAL GLU GLU SEQRES 2 B 317 MET THR ASN SER ARG PHE PRO ILE PRO LEU GLU LYS LEU SEQRES 3 B 317 PHE THR GLY PRO SER SER ALA PHE VAL VAL GLN PRO GLN SEQRES 4 B 317 ASN GLY ARG CYS THR THR ASP GLY VAL LEU LEU GLY THR SEQRES 5 B 317 THR GLN LEU SER PRO VAL ASN ILE CYS THR PHE ARG GLY SEQRES 6 B 317 ASP VAL THR HIS ILE THR GLY SER ARG ASN TYR THR MET SEQRES 7 B 317 ASN LEU ALA SER GLN ASN TRP ASN ASP TYR ASP PRO THR SEQRES 8 B 317 GLU GLU ILE PRO ALA PRO LEU GLY THR PRO ASP PHE VAL SEQRES 9 B 317 GLY LYS ILE GLN GLY VAL LEU THR GLN THR THR ARG THR SEQRES 10 B 317 ASP GLY SER THR ARG GLY HIS LYS ALA THR VAL TYR THR SEQRES 11 B 317 GLY SER ALA ASP PHE ALA PRO LYS LEU GLY ARG VAL GLN SEQRES 12 B 317 PHE GLU THR ASP THR ASP ARG ASP PHE GLU ALA ASN GLN SEQRES 13 B 317 ASN THR LYS PHE THR PRO VAL GLY VAL ILE GLN ASP GLY SEQRES 14 B 317 GLY THR THR HIS ARG ASN GLU PRO GLN GLN TRP VAL LEU SEQRES 15 B 317 PRO SER TYR SER GLY ARG ASN THR HIS ASN VAL HIS LEU SEQRES 16 B 317 ALA PRO ALA VAL ALA PRO THR PHE PRO GLY GLU GLN LEU SEQRES 17 B 317 LEU PHE PHE ARG SER THR MET PRO GLY CYS SER GLY TYR SEQRES 18 B 317 PRO ASN MET ASP LEU ASP CYS LEU LEU PRO GLN GLU TRP SEQRES 19 B 317 VAL GLN TYR PHE TYR GLN GLU ALA ALA PRO ALA GLN SER SEQRES 20 B 317 ASP VAL ALA LEU LEU ARG PHE VAL ASN PRO ASP THR GLY SEQRES 21 B 317 ARG VAL LEU PHE GLU CYS LYS LEU HIS LYS SER GLY TYR SEQRES 22 B 317 VAL THR VAL ALA HIS THR GLY GLN HIS ASP LEU VAL ILE SEQRES 23 B 317 PRO PRO ASN GLY TYR PHE ARG PHE ASP SER TRP VAL ASN SEQRES 24 B 317 GLN PHE TYR THR LEU ALA PRO MET GLY ASN GLY THR GLY SEQRES 25 B 317 ARG ARG ARG ALA VAL SEQRES 1 C 135 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 135 ALA GLY GLY SER LEU ASN LEU ALA CYS VAL SER SER GLY SEQRES 3 C 135 ARG THR PHE SER THR TRP LEU MET GLY TRP PHE ARG GLN SEQRES 4 C 135 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE ASP SEQRES 5 C 135 TRP ARG SER SER SER THR THR TYR ALA ASP SER VAL LYS SEQRES 6 C 135 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 135 MET TYR LEU GLN MET THR GLY LEU LYS PRO GLU ASP THR SEQRES 8 C 135 ALA VAL TYR TYR CYS ALA SER ASP ARG ASP HIS TYR SER SEQRES 9 C 135 GLY THR TYR TYR GLY ARG ARG PHE VAL GLU GLU TYR ASP SEQRES 10 C 135 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 11 C 135 HIS HIS HIS HIS HIS SEQRES 1 D 135 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 135 ALA GLY GLY SER LEU ASN LEU ALA CYS VAL SER SER GLY SEQRES 3 D 135 ARG THR PHE SER THR TRP LEU MET GLY TRP PHE ARG GLN SEQRES 4 D 135 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE ASP SEQRES 5 D 135 TRP ARG SER SER SER THR THR TYR ALA ASP SER VAL LYS SEQRES 6 D 135 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 135 MET TYR LEU GLN MET THR GLY LEU LYS PRO GLU ASP THR SEQRES 8 D 135 ALA VAL TYR TYR CYS ALA SER ASP ARG ASP HIS TYR SER SEQRES 9 D 135 GLY THR TYR TYR GLY ARG ARG PHE VAL GLU GLU TYR ASP SEQRES 10 D 135 TYR TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS SEQRES 11 D 135 HIS HIS HIS HIS HIS FORMUL 5 HOH *273(H2 O) HELIX 1 AA1 THR A 233 MET A 237 5 5 HELIX 2 AA2 ALA A 359 LEU A 362 5 4 HELIX 3 AA3 PRO A 454 ALA A 465 1 12 HELIX 4 AA4 THR B 233 MET B 237 5 5 HELIX 5 AA5 ALA B 359 LEU B 362 5 4 HELIX 6 AA6 PRO B 454 ALA B 465 1 12 HELIX 7 AA7 ASN C 74 LYS C 76 5 3 HELIX 8 AA8 LYS C 87 THR C 91 5 5 HELIX 9 AA9 PHE C 112 TYR C 116 5 5 HELIX 10 AB1 ASP D 62 LYS D 65 5 4 HELIX 11 AB2 LYS D 87 THR D 91 5 5 HELIX 12 AB3 PHE D 112 TYR D 116 5 5 SHEET 1 AA1 8 LYS A 248 THR A 251 0 SHEET 2 AA1 8 GLN A 430 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 VAL A 499 -1 O TYR A 496 N HIS A 492 SHEET 7 AA1 8 LEU A 507 ILE A 509 -1 O ILE A 509 N LEU A 249 SHEET 8 AA1 8 TYR A 514 VAL A 521 -1 O VAL A 521 N VAL A 472 SHEET 1 AA214 PHE A 286 HIS A 292 0 SHEET 2 AA214 ASN A 298 ALA A 304 -1 O ALA A 304 N ARG A 287 SHEET 3 AA214 LYS A 329 THR A 337 0 SHEET 4 AA214 THR A 344 TYR A 352 -1 O HIS A 347 N LEU A 334 SHEET 5 AA214 ARG A 364 THR A 369 -1 O GLU A 368 N THR A 350 SHEET 6 AA214 ASN A 380 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 HIS B 292 0 SHEET 9 AA214 ASN B 298 ALA B 304 -1 O ALA B 304 N ARG B 287 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 ASN B 380 VAL B 388 -1 O GLY B 387 N GLN B 331 SHEET 14 AA214 SER B 442 GLY B 443 -1 O GLY B 443 N THR A 344 SHEET 1 AA3 8 LYS B 248 THR B 251 0 SHEET 2 AA3 8 GLN B 430 THR B 437 -1 O PHE B 433 N PHE B 250 SHEET 3 AA3 8 ASP B 448 CYS B 451 -1 O LEU B 449 N SER B 436 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 491 N ALA B 473 SHEET 6 AA3 8 TYR B 496 VAL B 499 -1 O TYR B 496 N HIS B 492 SHEET 7 AA3 8 LEU B 507 ILE B 509 -1 O ILE B 509 N LEU B 249 SHEET 8 AA3 8 TYR B 514 VAL B 521 -1 O TYR B 514 N VAL B 478 SHEET 1 AA4 4 VAL C 2 SER C 7 0 SHEET 2 AA4 4 LEU C 18 GLY C 26 -1 O VAL C 23 N GLN C 5 SHEET 3 AA4 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA4 4 THR C 69 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AA5 7 LEU C 11 GLN C 13 0 SHEET 2 AA5 7 LEU C 33 GLN C 39 0 SHEET 3 AA5 7 GLU C 46 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 4 AA5 7 THR C 58 TYR C 60 -1 O THR C 59 N SER C 50 SHEET 5 AA5 7 ALA C 92 ASP C 99 -1 O TYR C 95 N PHE C 37 SHEET 6 AA5 7 TYR C 118 TRP C 119 -1 O TYR C 118 N SER C 98 SHEET 7 AA5 7 THR C 123 SER C 128 -1 O THR C 123 N TYR C 94 SHEET 1 AA6 4 VAL D 2 SER D 7 0 SHEET 2 AA6 4 LEU D 18 GLY D 26 -1 O VAL D 23 N GLN D 5 SHEET 3 AA6 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA6 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA7 7 LEU D 11 GLN D 13 0 SHEET 2 AA7 7 LEU D 33 GLN D 39 0 SHEET 3 AA7 7 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 4 AA7 7 THR D 58 TYR D 60 -1 O THR D 59 N SER D 50 SHEET 5 AA7 7 ALA D 92 ASP D 99 -1 O ASP D 99 N LEU D 33 SHEET 6 AA7 7 TYR D 118 TRP D 119 -1 O TYR D 118 N SER D 98 SHEET 7 AA7 7 THR D 123 SER D 128 -1 O THR D 123 N TYR D 94 SSBOND 1 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 2 CYS D 22 CYS D 96 1555 1555 2.03 CISPEP 1 GLU A 399 PRO A 400 0 -2.94 CISPEP 2 GLU B 399 PRO B 400 0 -0.58 CRYST1 117.767 62.443 121.396 90.00 101.24 90.00 I 1 2 1 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 0.008491 0.000000 0.001687 0.00000 SCALE2 0.000000 0.016015 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008399 0.00000