HEADER VIRAL PROTEIN 14-JAN-17 5MV2 TITLE CRYSTAL STRUCTURE OF THE E PROTEIN OF THE JAPANESE ENCEPHALITIS LIVE TITLE 2 ATTENUATED VACCINE VIRUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: E PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: JAPANESE ENCEPHALITIS VIRUS (STRAIN SA-14); SOURCE 3 ORGANISM_TAXID: 11073; SOURCE 4 STRAIN: SA-14; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS VIRAL ENVELOPE GLYCOPROTEIN, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR X.LIU,X.ZHAO,R.NA,L.LI,E.WARKENTIN,J.WITT,X.LU,Y.WEI,G.PENG,Y.LI, AUTHOR 2 J.WANG REVDAT 4 13-NOV-24 5MV2 1 REMARK REVDAT 3 17-JAN-24 5MV2 1 REMARK REVDAT 2 27-FEB-19 5MV2 1 JRNL REVDAT 1 23-MAY-18 5MV2 0 JRNL AUTH X.LIU,X.ZHAO,R.NA,L.LI,E.WARKENTIN,J.WITT,X.LU,Y.YU,Y.WEI, JRNL AUTH 2 G.PENG,Y.LI,J.WANG JRNL TITL THE STRUCTURE DIFFERENCES OF JAPANESE ENCEPHALITIS VIRUS JRNL TITL 2 SA14 AND SA14-14-2 E PROTEINS ELUCIDATE THE VIRULENCE JRNL TITL 3 ATTENUATION MECHANISM. JRNL REF PROTEIN CELL V. 10 149 2019 JRNL REFN ESSN 1674-8018 JRNL PMID 29752689 JRNL DOI 10.1007/S13238-018-0551-6 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 28165 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1409 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 19.9451 - 4.5086 0.99 2747 145 0.1574 0.1858 REMARK 3 2 4.5086 - 3.5854 1.00 2710 143 0.1450 0.1897 REMARK 3 3 3.5854 - 3.1342 1.00 2687 141 0.1586 0.1735 REMARK 3 4 3.1342 - 2.8485 1.00 2673 141 0.1758 0.2348 REMARK 3 5 2.8485 - 2.6448 0.99 2676 141 0.2058 0.2736 REMARK 3 6 2.6448 - 2.4892 0.99 2664 140 0.2294 0.2817 REMARK 3 7 2.4892 - 2.3647 0.99 2642 139 0.2561 0.3384 REMARK 3 8 2.3647 - 2.2619 0.99 2646 139 0.2460 0.3106 REMARK 3 9 2.2619 - 2.1750 0.99 2674 141 0.2526 0.3003 REMARK 3 10 2.1750 - 2.1000 0.99 2637 139 0.2752 0.3309 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.470 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.012 3177 REMARK 3 ANGLE : 1.185 4310 REMARK 3 CHIRALITY : 0.073 479 REMARK 3 PLANARITY : 0.008 555 REMARK 3 DIHEDRAL : 14.401 1876 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID -9 THROUGH 163 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.0745 -9.2902 40.0781 REMARK 3 T TENSOR REMARK 3 T11: 0.3673 T22: 0.3756 REMARK 3 T33: 0.3309 T12: -0.0032 REMARK 3 T13: -0.0408 T23: 0.0293 REMARK 3 L TENSOR REMARK 3 L11: 2.9895 L22: 0.0727 REMARK 3 L33: 0.6806 L12: -0.2045 REMARK 3 L13: 1.3022 L23: -0.0037 REMARK 3 S TENSOR REMARK 3 S11: -0.0165 S12: -0.2453 S13: -0.0258 REMARK 3 S21: 0.0470 S22: 0.0095 S23: -0.0081 REMARK 3 S31: -0.0049 S32: -0.0447 S33: -0.0381 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 265 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.2138 -12.4066 43.5263 REMARK 3 T TENSOR REMARK 3 T11: 0.3808 T22: 0.3319 REMARK 3 T33: 0.2899 T12: -0.0139 REMARK 3 T13: 0.0231 T23: 0.0236 REMARK 3 L TENSOR REMARK 3 L11: 6.4043 L22: 0.3934 REMARK 3 L33: 0.9491 L12: 0.6021 REMARK 3 L13: 1.4349 L23: 0.1651 REMARK 3 S TENSOR REMARK 3 S11: 0.0352 S12: -0.4667 S13: -0.2259 REMARK 3 S21: 0.0917 S22: -0.0357 S23: -0.0011 REMARK 3 S31: 0.0756 S32: -0.0348 S33: -0.0414 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 266 THROUGH 312 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5943 -11.4541 27.5494 REMARK 3 T TENSOR REMARK 3 T11: 0.3613 T22: 0.3933 REMARK 3 T33: 0.4756 T12: -0.0233 REMARK 3 T13: -0.0470 T23: 0.0098 REMARK 3 L TENSOR REMARK 3 L11: 1.6053 L22: 0.1241 REMARK 3 L33: 2.3884 L12: -0.4416 REMARK 3 L13: 1.0475 L23: -0.2229 REMARK 3 S TENSOR REMARK 3 S11: -0.0685 S12: -0.2794 S13: -0.1895 REMARK 3 S21: -0.0175 S22: 0.1690 S23: 0.2052 REMARK 3 S31: -0.1931 S32: -0.4363 S33: -0.0503 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 400 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.2773 -13.4375 8.2609 REMARK 3 T TENSOR REMARK 3 T11: 0.3409 T22: 0.3548 REMARK 3 T33: 0.3943 T12: -0.0008 REMARK 3 T13: -0.1125 T23: -0.0754 REMARK 3 L TENSOR REMARK 3 L11: 3.2269 L22: 2.0553 REMARK 3 L33: 5.2105 L12: 0.4552 REMARK 3 L13: 1.2371 L23: -0.7759 REMARK 3 S TENSOR REMARK 3 S11: -0.0601 S12: 0.3008 S13: -0.4135 REMARK 3 S21: -0.1558 S22: 0.0950 S23: 0.2401 REMARK 3 S31: 0.1421 S32: -0.5165 S33: -0.0876 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 5MV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-17. REMARK 100 THE DEPOSITION ID IS D_1200002796. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-SEP-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.9 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97621 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28195 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.14400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 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: 5MV1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRI-NA CITRATE, PH 7.9, 18% PEG REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 65.30000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.95000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.30000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.95000 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 401 REMARK 465 THR A 402 REMARK 465 LEU A 403 REMARK 465 GLY A 404 REMARK 465 LYS A 405 REMARK 465 ALA A 406 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 O HOH A 686 O HOH A 696 1.86 REMARK 500 O HOH A 514 O HOH A 689 1.89 REMARK 500 O HOH A 651 O HOH A 722 1.92 REMARK 500 N GLU A -9 O HOH A 501 2.00 REMARK 500 O HOH A 632 O HOH A 672 2.00 REMARK 500 O HOH A 691 O HOH A 726 2.00 REMARK 500 OE2 GLU A 55 O HOH A 502 2.07 REMARK 500 NE ARG A 193 O HOH A 503 2.12 REMARK 500 O ASN A 367 O HOH A 504 2.14 REMARK 500 O HOH A 704 O HOH A 726 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 609 O HOH A 729 2656 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 76 -8.46 67.07 REMARK 500 SER A 230 83.35 -156.09 REMARK 500 ALA A 247 -86.82 38.90 REMARK 500 TYR A 274 58.07 -149.67 REMARK 500 THR A 299 1.05 -66.24 REMARK 500 REMARK 500 REMARK: NULL DBREF 5MV2 A 1 406 UNP Q8QQT1 Q8QQT1_JAEV1 1 406 SEQADV 5MV2 GLU A -9 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 ASN A -8 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 LEU A -7 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 TYR A -6 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 PHE A -5 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 GLN A -4 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 GLY A -3 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 GLY A -2 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 ILE A -1 UNP Q8QQT1 EXPRESSION TAG SEQADV 5MV2 HIS A 0 UNP Q8QQT1 EXPRESSION TAG SEQRES 1 A 416 GLU ASN LEU TYR PHE GLN GLY GLY ILE HIS PHE ASN CYS SEQRES 2 A 416 LEU GLY MET GLY ASN ARG ASP PHE ILE GLU GLY ALA SER SEQRES 3 A 416 GLY ALA THR TRP VAL ASP LEU VAL LEU GLU GLY ASP SER SEQRES 4 A 416 CYS LEU THR ILE MET ALA ASN ASP LYS PRO THR LEU ASP SEQRES 5 A 416 VAL ARG MET ILE ASN ILE GLU ALA SER GLN LEU ALA GLU SEQRES 6 A 416 VAL ARG SER TYR CYS TYR HIS ALA SER VAL THR ASP ILE SEQRES 7 A 416 SER THR VAL ALA ARG CYS PRO THR THR GLY GLU ALA HIS SEQRES 8 A 416 ASN GLU LYS ARG ALA ASP SER SER TYR VAL CYS LYS GLN SEQRES 9 A 416 GLY PHE THR ASP ARG GLY TRP GLY ASN GLY CYS GLY PHE SEQRES 10 A 416 PHE GLY LYS GLY SER ILE ASP THR CYS ALA LYS PHE SER SEQRES 11 A 416 CYS THR SER LYS ALA ILE GLY ARG THR ILE GLN PRO GLU SEQRES 12 A 416 ASN ILE LYS TYR LYS VAL GLY ILE PHE VAL HIS GLY THR SEQRES 13 A 416 THR THR SER GLU ASN HIS GLY ASN TYR SER ALA GLN VAL SEQRES 14 A 416 GLY ALA SER GLN ALA ALA LYS PHE THR VAL THR PRO ASN SEQRES 15 A 416 ALA PRO SER VAL ALA LEU LYS LEU GLY ASP TYR GLY GLU SEQRES 16 A 416 VAL THR LEU ASP CYS GLU PRO ARG SER GLY LEU ASN THR SEQRES 17 A 416 GLU ALA PHE TYR VAL MET THR VAL GLY SER LYS SER PHE SEQRES 18 A 416 LEU VAL HIS ARG GLU TRP PHE HIS ASP LEU ALA LEU PRO SEQRES 19 A 416 TRP THR SER PRO SER SER THR ALA TRP ARG ASN ARG GLU SEQRES 20 A 416 LEU LEU MET GLU PHE GLU GLY ALA HIS ALA THR LYS GLN SEQRES 21 A 416 SER VAL VAL ALA LEU GLY SER GLN GLU GLY GLY LEU HIS SEQRES 22 A 416 HIS ALA LEU ALA GLY ALA ILE VAL VAL GLU TYR SER SER SEQRES 23 A 416 SER VAL MET LEU THR SER GLY HIS LEU LYS CYS ARG LEU SEQRES 24 A 416 LYS MET ASP LYS LEU ALA LEU LYS GLY THR THR TYR GLY SEQRES 25 A 416 MET CYS THR GLU LYS PHE SER PHE ALA LYS ASN PRO VAL SEQRES 26 A 416 ASP THR GLY HIS GLY THR VAL VAL ILE GLU LEU SER TYR SEQRES 27 A 416 SER GLY SER ASP GLY PRO CYS LYS ILE PRO ILE VAL SER SEQRES 28 A 416 VAL ALA SER LEU ASN ASP MET THR PRO VAL GLY ARG LEU SEQRES 29 A 416 VAL THR VAL ASN PRO PHE VAL ALA THR SER SER ALA ASN SEQRES 30 A 416 SER LYS VAL LEU VAL GLU MET GLU PRO PRO PHE GLY ASP SEQRES 31 A 416 SER TYR ILE VAL VAL GLY ARG GLY ASP LYS GLN ILE ASN SEQRES 32 A 416 HIS HIS TRP HIS LYS ALA GLY SER THR LEU GLY LYS ALA FORMUL 2 HOH *236(H2 O) HELIX 1 AA1 ASN A -8 GLN A -4 5 5 HELIX 2 AA2 ASN A 82 ASP A 87 5 6 HELIX 3 AA3 GLY A 100 GLY A 104 5 5 HELIX 4 AA4 GLN A 131 GLU A 133 5 3 HELIX 5 AA5 ASN A 154 ALA A 161 1 8 HELIX 6 AA6 GLY A 181 TYR A 183 5 3 HELIX 7 AA7 PRO A 192 LEU A 196 5 5 HELIX 8 AA8 ASN A 197 GLU A 199 5 3 HELIX 9 AA9 ARG A 215 ASP A 220 1 6 HELIX 10 AB1 ASN A 235 LEU A 238 5 4 HELIX 11 AB2 GLN A 258 LEU A 266 1 9 SHEET 1 AA1 5 ASP A 10 GLY A 14 0 SHEET 2 AA1 5 LEU A 31 ALA A 35 1 O THR A 32 N ILE A 12 SHEET 3 AA1 5 LEU A 41 ALA A 50 -1 O LEU A 41 N ILE A 33 SHEET 4 AA1 5 ILE A 135 VAL A 143 -1 O LYS A 138 N ILE A 46 SHEET 5 AA1 5 ALA A 164 VAL A 169 -1 O VAL A 169 N TYR A 137 SHEET 1 AA2 4 ASP A 10 GLY A 14 0 SHEET 2 AA2 4 LEU A 31 ALA A 35 1 O THR A 32 N ILE A 12 SHEET 3 AA2 4 LEU A 41 ALA A 50 -1 O LEU A 41 N ILE A 33 SHEET 4 AA2 4 MET A 279 THR A 281 -1 O MET A 279 N ALA A 50 SHEET 1 AA3 4 TRP A 20 GLU A 26 0 SHEET 2 AA3 4 HIS A 284 LYS A 290 -1 O LEU A 289 N VAL A 21 SHEET 3 AA3 4 GLU A 185 CYS A 190 -1 N THR A 187 O LYS A 290 SHEET 4 AA3 4 SER A 175 LYS A 179 -1 N VAL A 176 O LEU A 188 SHEET 1 AA4 5 TYR A 90 ARG A 99 0 SHEET 2 AA4 5 GLY A 109 THR A 129 -1 O GLY A 109 N ARG A 99 SHEET 3 AA4 5 ALA A 54 ALA A 72 -1 N VAL A 56 O GLY A 127 SHEET 4 AA4 5 TRP A 225 SER A 227 -1 O THR A 226 N SER A 58 SHEET 5 AA4 5 SER A 230 ARG A 234 -1 O ARG A 234 N TRP A 225 SHEET 1 AA5 5 TYR A 90 ARG A 99 0 SHEET 2 AA5 5 GLY A 109 THR A 129 -1 O GLY A 109 N ARG A 99 SHEET 3 AA5 5 PHE A 201 VAL A 206 -1 O VAL A 203 N ARG A 128 SHEET 4 AA5 5 LYS A 209 HIS A 214 -1 O LYS A 209 N VAL A 206 SHEET 5 AA5 5 ILE A 270 VAL A 272 -1 O ILE A 270 N LEU A 212 SHEET 1 AA6 2 MET A 240 PHE A 242 0 SHEET 2 AA6 2 VAL A 252 ALA A 254 -1 O VAL A 253 N GLU A 241 SHEET 1 AA7 4 PHE A 308 ASP A 316 0 SHEET 2 AA7 4 VAL A 322 TYR A 328 -1 O SER A 327 N SER A 309 SHEET 3 AA7 4 SER A 368 GLU A 375 -1 O VAL A 370 N LEU A 326 SHEET 4 AA7 4 ARG A 353 LEU A 354 -1 N ARG A 353 O GLU A 375 SHEET 1 AA8 2 CYS A 335 LYS A 336 0 SHEET 2 AA8 2 PHE A 360 VAL A 361 -1 O VAL A 361 N CYS A 335 SHEET 1 AA9 4 PRO A 350 VAL A 351 0 SHEET 2 AA9 4 ILE A 339 VAL A 342 -1 N SER A 341 O VAL A 351 SHEET 3 AA9 4 GLY A 379 VAL A 385 -1 O VAL A 384 N VAL A 340 SHEET 4 AA9 4 ILE A 392 LYS A 398 -1 O ILE A 392 N VAL A 385 SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.09 SSBOND 2 CYS A 74 CYS A 105 1555 1555 2.10 SSBOND 3 CYS A 92 CYS A 116 1555 1555 2.01 SSBOND 4 CYS A 190 CYS A 287 1555 1555 2.07 SSBOND 5 CYS A 304 CYS A 335 1555 1555 2.09 CISPEP 1 GLY A 333 PRO A 334 0 1.23 CRYST1 130.600 55.900 90.100 90.00 132.10 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.007657 0.000000 0.006919 0.00000 SCALE2 0.000000 0.017889 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014958 0.00000