HEADER ANTIVIRAL PROTEIN 02-MAR-22 7X4I TITLE CRYSTAL STRUCTURE OF NANOBODY ASA3 IN COMPLEX WITH DIMER SARS-COV-1 TITLE 2 RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY ASA3; COMPND 8 CHAIN: E, F, G, H; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS; SOURCE 3 ORGANISM_TAXID: 2901879; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTT5; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 11 ORGANISM_TAXID: 30538; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PTT5 KEYWDS NANOBODY, SARS-COV-1, RBD, ANTIVIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.MA,W.H.ZENG,T.C.JIN REVDAT 1 11-JAN-23 7X4I 0 JRNL AUTH H.MA,X.ZHANG,W.ZENG,J.ZHOU,X.CHI,S.CHEN,P.ZHENG,M.WANG,Y.WU, JRNL AUTH 2 D.ZHAO,F.GONG,H.LIN,H.SUN,C.YU,Z.SHI,X.HU,H.ZHANG,T.JIN, JRNL AUTH 3 S.CHIU JRNL TITL A BISPECIFIC NANOBODY DIMER BROADLY NEUTRALIZES SARS-COV-1 & JRNL TITL 2 2 VARIANTS OF CONCERN AND OFFERS SUBSTANTIAL PROTECTION JRNL TITL 3 AGAINST OMICRON VIA LOW-DOSE INTRANASAL ADMINISTRATION. JRNL REF CELL DISCOV V. 8 132 2022 JRNL REFN ESSN 2056-5968 JRNL PMID 36494344 JRNL DOI 10.1038/S41421-022-00497-W REMARK 2 REMARK 2 RESOLUTION. 3.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_2481 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) : 3.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 24538 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.270 REMARK 3 R VALUE (WORKING SET) : 0.267 REMARK 3 FREE R VALUE : 0.321 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 1213 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 75.5190 - 7.0299 0.98 2726 140 0.2485 0.2649 REMARK 3 2 7.0299 - 5.5804 0.99 2638 139 0.2648 0.3196 REMARK 3 3 5.5804 - 4.8751 0.99 2591 135 0.2448 0.3167 REMARK 3 4 4.8751 - 4.4294 0.99 2592 124 0.2328 0.3429 REMARK 3 5 4.4294 - 4.1120 0.99 2600 116 0.2525 0.3254 REMARK 3 6 4.1120 - 3.8696 0.99 2558 131 0.2692 0.3031 REMARK 3 7 3.8696 - 3.6758 0.99 2554 145 0.3050 0.3340 REMARK 3 8 3.6758 - 3.5158 0.99 2541 133 0.3329 0.3726 REMARK 3 9 3.5158 - 3.3804 0.99 2525 150 0.3748 0.4454 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) : 0.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.340 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 85.05 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 100.6 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 : 0.005 10081 REMARK 3 ANGLE : 0.731 13740 REMARK 3 CHIRALITY : 0.047 1433 REMARK 3 PLANARITY : 0.006 1785 REMARK 3 DIHEDRAL : 4.759 6726 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 0.1381 0.2249 -1.3622 REMARK 3 T TENSOR REMARK 3 T11: 0.4785 T22: 0.6257 REMARK 3 T33: 0.6501 T12: 0.0109 REMARK 3 T13: 0.0091 T23: -0.0120 REMARK 3 L TENSOR REMARK 3 L11: 0.9885 L22: 1.3874 REMARK 3 L33: 0.6370 L12: -0.0322 REMARK 3 L13: 0.1396 L23: 0.0295 REMARK 3 S TENSOR REMARK 3 S11: 0.1321 S12: -0.0094 S13: 0.0293 REMARK 3 S21: -0.0404 S22: -0.0725 S23: -0.1557 REMARK 3 S31: 0.1258 S32: 0.1041 S33: -0.0589 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 320:425 OR RESID REMARK 3 427:513)) REMARK 3 SELECTION : (CHAIN B AND (RESID 320 OR (RESID 321 AND REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR REMARK 3 NAME CB )) OR RESID 322:425 OR RESID 427: REMARK 3 500 OR RESID 509:513)) REMARK 3 ATOM PAIRS NUMBER : 3501 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 320:425 OR RESID REMARK 3 427:513)) REMARK 3 SELECTION : (CHAIN C AND (RESID 320 OR (RESID 321 AND REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR REMARK 3 NAME CB )) OR RESID 322:425 OR RESID 427: REMARK 3 500 OR RESID 509:513)) REMARK 3 ATOM PAIRS NUMBER : 3501 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 320:425 OR RESID REMARK 3 427:513)) REMARK 3 SELECTION : (CHAIN D AND (RESID 320 OR (RESID 321 AND REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR REMARK 3 NAME CB )) OR RESID 322:425 OR RESID 427: REMARK 3 500 OR RESID 509:513)) REMARK 3 ATOM PAIRS NUMBER : 3501 REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN E AND (RESID 1:24 OR RESID 26:31 REMARK 3 OR (RESID 32:33 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 34:38 OR RESID 40:114 OR RESID 116:121)) REMARK 3 SELECTION : (CHAIN F AND (RESID 1:24 OR RESID 26:31 REMARK 3 OR (RESID 32:33 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 34:38 OR RESID 40:114 OR RESID 116:121)) REMARK 3 ATOM PAIRS NUMBER : 2071 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: (CHAIN E AND (RESID 1:24 OR RESID 26:31 REMARK 3 OR (RESID 32:33 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 34:38 OR RESID 40:114 OR RESID 116:121)) REMARK 3 SELECTION : (CHAIN G AND (RESID 1:24 OR RESID 26:31 REMARK 3 OR (RESID 32:33 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 34:38 OR RESID 40:114 OR RESID 116:121)) REMARK 3 ATOM PAIRS NUMBER : 2071 REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: (CHAIN E AND (RESID 1:24 OR RESID 26:31 REMARK 3 OR (RESID 32:33 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 34:38 OR RESID 40:114 OR RESID 116:121)) REMARK 3 SELECTION : (CHAIN H AND (RESID 1:24 OR RESID 26:38 REMARK 3 OR RESID 40:114 OR RESID 116:121)) REMARK 3 ATOM PAIRS NUMBER : 2071 REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7X4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-22. REMARK 100 THE DEPOSITION ID IS D_1300028016. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-21 REMARK 200 TEMPERATURE (KELVIN) : 190 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL02U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97911 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 : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24667 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.380 REMARK 200 RESOLUTION RANGE LOW (A) : 151.040 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 7.030 REMARK 200 R MERGE (I) : 0.20000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.38 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4 REMARK 200 DATA REDUNDANCY IN SHELL : 7.47 REMARK 200 R MERGE FOR SHELL (I) : 1.33400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.300 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: 7LM9, 70LZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(V/V) PEG 400, 0.1 M LITHIUM REMARK 280 CHLORIDE, 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 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 50.85100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.51850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.00300 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.51850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.85100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.00300 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: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H 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 PHE A 501 REMARK 465 GLU A 502 REMARK 465 LEU A 503 REMARK 465 LEU A 504 REMARK 465 ASN A 505 REMARK 465 ALA A 506 REMARK 465 PRO A 507 REMARK 465 ALA A 508 REMARK 465 LYS A 514 REMARK 465 LEU A 515 REMARK 465 SER A 516 REMARK 465 THR A 517 REMARK 465 ASP A 518 REMARK 465 LEU A 519 REMARK 465 ILE A 520 REMARK 465 LYS A 521 REMARK 465 ASN A 522 REMARK 465 GLN A 523 REMARK 465 LYS B 514 REMARK 465 LEU B 515 REMARK 465 SER B 516 REMARK 465 THR B 517 REMARK 465 ASP B 518 REMARK 465 LEU B 519 REMARK 465 ILE B 520 REMARK 465 LYS B 521 REMARK 465 ASN B 522 REMARK 465 GLN B 523 REMARK 465 GLU C 502 REMARK 465 LEU C 503 REMARK 465 LEU C 504 REMARK 465 ASN C 505 REMARK 465 ALA C 506 REMARK 465 PRO C 507 REMARK 465 LYS C 514 REMARK 465 LEU C 515 REMARK 465 SER C 516 REMARK 465 THR C 517 REMARK 465 ASP C 518 REMARK 465 LEU C 519 REMARK 465 ILE C 520 REMARK 465 LYS C 521 REMARK 465 ASN C 522 REMARK 465 GLN C 523 REMARK 465 PHE D 501 REMARK 465 GLU D 502 REMARK 465 LEU D 503 REMARK 465 LEU D 504 REMARK 465 ASN D 505 REMARK 465 ALA D 506 REMARK 465 PRO D 507 REMARK 465 LYS D 514 REMARK 465 LEU D 515 REMARK 465 SER D 516 REMARK 465 THR D 517 REMARK 465 ASP D 518 REMARK 465 LEU D 519 REMARK 465 ILE D 520 REMARK 465 LYS D 521 REMARK 465 ASN D 522 REMARK 465 GLN D 523 REMARK 465 SER H 122 REMARK 465 SER H 123 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 ASN A 321 CG OD1 ND2 REMARK 470 GLN G 115 CB CG CD OE1 NE2 REMARK 470 TYR H 32 CG CD1 CD2 CE1 CE2 CZ OH 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 OH TYR D 440 NE2 GLN F 115 2.13 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 ALA A 339 40.17 -105.40 REMARK 500 ASP A 415 30.33 -92.13 REMARK 500 ALA B 398 149.98 -170.29 REMARK 500 ASN C 473 23.31 46.57 REMARK 500 PRO D 470 40.88 -81.41 REMARK 500 SER E 25 -60.84 -96.46 REMARK 500 SER E 53 92.65 -69.83 REMARK 500 LEU E 99 57.53 -112.85 REMARK 500 HIS F 31 74.99 -105.55 REMARK 500 ASP F 52 -179.50 -68.29 REMARK 500 LEU F 99 59.04 -101.13 REMARK 500 ASP F 111 -16.51 81.68 REMARK 500 SER G 29 -32.77 -38.02 REMARK 500 HIS G 31 78.36 -103.05 REMARK 500 LEU G 99 61.38 -101.33 REMARK 500 PHE H 27 65.97 -103.53 REMARK 500 HIS H 31 71.83 -104.83 REMARK 500 LEU H 99 62.39 -101.09 REMARK 500 REMARK 500 REMARK: NULL DBREF 7X4I A 320 523 UNP Q19QX0 Q19QX0_SARS 320 523 DBREF 7X4I B 320 523 UNP Q19QX0 Q19QX0_SARS 320 523 DBREF 7X4I C 320 523 UNP Q19QX0 Q19QX0_SARS 320 523 DBREF 7X4I D 320 523 UNP Q19QX0 Q19QX0_SARS 320 523 DBREF 7X4I E 1 123 PDB 7X4I 7X4I 1 123 DBREF 7X4I F 1 123 PDB 7X4I 7X4I 1 123 DBREF 7X4I G 1 123 PDB 7X4I 7X4I 1 123 DBREF 7X4I H 1 123 PDB 7X4I 7X4I 1 123 SEQRES 1 A 204 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 A 204 LYS PHE PRO SER VAL TYR ALA TRP GLU ARG LYS LYS ILE SEQRES 3 A 204 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 A 204 THR PHE PHE SER THR PHE LYS CYS TYR GLY VAL SER ALA SEQRES 5 A 204 THR LYS LEU ASN ASP LEU CYS PHE SER ASN VAL TYR ALA SEQRES 6 A 204 ASP SER PHE VAL VAL LYS GLY ASP ASP VAL ARG GLN ILE SEQRES 7 A 204 ALA PRO GLY GLN THR GLY VAL ILE ALA ASP TYR ASN TYR SEQRES 8 A 204 LYS LEU PRO ASP ASP PHE MET GLY CYS VAL LEU ALA TRP SEQRES 9 A 204 ASN THR ARG ASN ILE ASP ALA THR SER THR GLY ASN HIS SEQRES 10 A 204 ASN TYR LYS TYR ARG TYR LEU ARG HIS GLY LYS LEU ARG SEQRES 11 A 204 PRO PHE GLU ARG ASP ILE SER ASN VAL PRO PHE SER PRO SEQRES 12 A 204 ASP GLY LYS PRO CYS THR PRO PRO ALA LEU ASN CYS TYR SEQRES 13 A 204 TRP PRO LEU ASN ASP TYR GLY PHE TYR THR THR THR GLY SEQRES 14 A 204 ILE GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 A 204 GLU LEU LEU ASN ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 16 A 204 LEU SER THR ASP LEU ILE LYS ASN GLN SEQRES 1 B 204 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 B 204 LYS PHE PRO SER VAL TYR ALA TRP GLU ARG LYS LYS ILE SEQRES 3 B 204 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 B 204 THR PHE PHE SER THR PHE LYS CYS TYR GLY VAL SER ALA SEQRES 5 B 204 THR LYS LEU ASN ASP LEU CYS PHE SER ASN VAL TYR ALA SEQRES 6 B 204 ASP SER PHE VAL VAL LYS GLY ASP ASP VAL ARG GLN ILE SEQRES 7 B 204 ALA PRO GLY GLN THR GLY VAL ILE ALA ASP TYR ASN TYR SEQRES 8 B 204 LYS LEU PRO ASP ASP PHE MET GLY CYS VAL LEU ALA TRP SEQRES 9 B 204 ASN THR ARG ASN ILE ASP ALA THR SER THR GLY ASN HIS SEQRES 10 B 204 ASN TYR LYS TYR ARG TYR LEU ARG HIS GLY LYS LEU ARG SEQRES 11 B 204 PRO PHE GLU ARG ASP ILE SER ASN VAL PRO PHE SER PRO SEQRES 12 B 204 ASP GLY LYS PRO CYS THR PRO PRO ALA LEU ASN CYS TYR SEQRES 13 B 204 TRP PRO LEU ASN ASP TYR GLY PHE TYR THR THR THR GLY SEQRES 14 B 204 ILE GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 B 204 GLU LEU LEU ASN ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 16 B 204 LEU SER THR ASP LEU ILE LYS ASN GLN SEQRES 1 C 204 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 C 204 LYS PHE PRO SER VAL TYR ALA TRP GLU ARG LYS LYS ILE SEQRES 3 C 204 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 C 204 THR PHE PHE SER THR PHE LYS CYS TYR GLY VAL SER ALA SEQRES 5 C 204 THR LYS LEU ASN ASP LEU CYS PHE SER ASN VAL TYR ALA SEQRES 6 C 204 ASP SER PHE VAL VAL LYS GLY ASP ASP VAL ARG GLN ILE SEQRES 7 C 204 ALA PRO GLY GLN THR GLY VAL ILE ALA ASP TYR ASN TYR SEQRES 8 C 204 LYS LEU PRO ASP ASP PHE MET GLY CYS VAL LEU ALA TRP SEQRES 9 C 204 ASN THR ARG ASN ILE ASP ALA THR SER THR GLY ASN HIS SEQRES 10 C 204 ASN TYR LYS TYR ARG TYR LEU ARG HIS GLY LYS LEU ARG SEQRES 11 C 204 PRO PHE GLU ARG ASP ILE SER ASN VAL PRO PHE SER PRO SEQRES 12 C 204 ASP GLY LYS PRO CYS THR PRO PRO ALA LEU ASN CYS TYR SEQRES 13 C 204 TRP PRO LEU ASN ASP TYR GLY PHE TYR THR THR THR GLY SEQRES 14 C 204 ILE GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 C 204 GLU LEU LEU ASN ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 16 C 204 LEU SER THR ASP LEU ILE LYS ASN GLN SEQRES 1 D 204 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 D 204 LYS PHE PRO SER VAL TYR ALA TRP GLU ARG LYS LYS ILE SEQRES 3 D 204 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 D 204 THR PHE PHE SER THR PHE LYS CYS TYR GLY VAL SER ALA SEQRES 5 D 204 THR LYS LEU ASN ASP LEU CYS PHE SER ASN VAL TYR ALA SEQRES 6 D 204 ASP SER PHE VAL VAL LYS GLY ASP ASP VAL ARG GLN ILE SEQRES 7 D 204 ALA PRO GLY GLN THR GLY VAL ILE ALA ASP TYR ASN TYR SEQRES 8 D 204 LYS LEU PRO ASP ASP PHE MET GLY CYS VAL LEU ALA TRP SEQRES 9 D 204 ASN THR ARG ASN ILE ASP ALA THR SER THR GLY ASN HIS SEQRES 10 D 204 ASN TYR LYS TYR ARG TYR LEU ARG HIS GLY LYS LEU ARG SEQRES 11 D 204 PRO PHE GLU ARG ASP ILE SER ASN VAL PRO PHE SER PRO SEQRES 12 D 204 ASP GLY LYS PRO CYS THR PRO PRO ALA LEU ASN CYS TYR SEQRES 13 D 204 TRP PRO LEU ASN ASP TYR GLY PHE TYR THR THR THR GLY SEQRES 14 D 204 ILE GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 15 D 204 GLU LEU LEU ASN ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 16 D 204 LEU SER THR ASP LEU ILE LYS ASN GLN SEQRES 1 E 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 123 PHE THR SER ASP HIS TYR ALA LEU ALA TRP PHE ARG GLN SEQRES 4 E 123 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE ASP SEQRES 5 E 123 SER ASP GLY ASN PRO PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 E 123 ARG PHE THR GLY SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 E 123 TYR LEU GLN MET ASN SER LEU LYS LEU GLU ASP THR ALA SEQRES 8 E 123 VAL TYR TYR CYS ALA ALA GLY LEU TRP TYR GLY ARG SER SEQRES 9 E 123 LEU ASN SER PHE ASP TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 E 123 GLN VAL THR VAL SER SER SEQRES 1 F 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 123 PHE THR SER ASP HIS TYR ALA LEU ALA TRP PHE ARG GLN SEQRES 4 F 123 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE ASP SEQRES 5 F 123 SER ASP GLY ASN PRO PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 F 123 ARG PHE THR GLY SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 F 123 TYR LEU GLN MET ASN SER LEU LYS LEU GLU ASP THR ALA SEQRES 8 F 123 VAL TYR TYR CYS ALA ALA GLY LEU TRP TYR GLY ARG SER SEQRES 9 F 123 LEU ASN SER PHE ASP TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 F 123 GLN VAL THR VAL SER SER SEQRES 1 G 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 123 PHE THR SER ASP HIS TYR ALA LEU ALA TRP PHE ARG GLN SEQRES 4 G 123 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE ASP SEQRES 5 G 123 SER ASP GLY ASN PRO PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 G 123 ARG PHE THR GLY SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 G 123 TYR LEU GLN MET ASN SER LEU LYS LEU GLU ASP THR ALA SEQRES 8 G 123 VAL TYR TYR CYS ALA ALA GLY LEU TRP TYR GLY ARG SER SEQRES 9 G 123 LEU ASN SER PHE ASP TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 G 123 GLN VAL THR VAL SER SER SEQRES 1 H 123 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 123 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 123 PHE THR SER ASP HIS TYR ALA LEU ALA TRP PHE ARG GLN SEQRES 4 H 123 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE ASP SEQRES 5 H 123 SER ASP GLY ASN PRO PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 123 ARG PHE THR GLY SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 H 123 TYR LEU GLN MET ASN SER LEU LYS LEU GLU ASP THR ALA SEQRES 8 H 123 VAL TYR TYR CYS ALA ALA GLY LEU TRP TYR GLY ARG SER SEQRES 9 H 123 LEU ASN SER PHE ASP TYR ASP TYR TRP GLY GLN GLY THR SEQRES 10 H 123 GLN VAL THR VAL SER SER HELIX 1 AA1 PHE A 325 ASN A 330 1 6 HELIX 2 AA2 TYR A 352 ASN A 357 1 6 HELIX 3 AA3 THR A 372 LEU A 377 5 6 HELIX 4 AA4 ASP A 392 VAL A 394 5 3 HELIX 5 AA5 GLY A 403 ASN A 409 1 7 HELIX 6 AA6 THR A 425 ALA A 430 1 6 HELIX 7 AA7 GLY A 488 TYR A 491 5 4 HELIX 8 AA8 PHE B 325 ASN B 330 1 6 HELIX 9 AA9 TYR B 352 ASN B 357 1 6 HELIX 10 AB1 SER B 370 ASN B 375 1 6 HELIX 11 AB2 ASP B 392 VAL B 394 5 3 HELIX 12 AB3 GLY B 403 ASN B 409 1 7 HELIX 13 AB4 THR B 425 ALA B 430 1 6 HELIX 14 AB5 PHE C 325 ASN C 330 1 6 HELIX 15 AB6 TYR C 352 ASN C 357 1 6 HELIX 16 AB7 THR C 372 LEU C 377 5 6 HELIX 17 AB8 ASP C 392 VAL C 394 5 3 HELIX 18 AB9 GLY C 403 ASN C 409 1 7 HELIX 19 AC1 THR C 425 ALA C 430 1 6 HELIX 20 AC2 PHE D 325 ASN D 330 1 6 HELIX 21 AC3 TYR D 352 ASN D 357 1 6 HELIX 22 AC4 SER D 370 LEU D 377 5 8 HELIX 23 AC5 ASP D 392 VAL D 394 5 3 HELIX 24 AC6 GLY D 403 ASN D 409 1 7 HELIX 25 AC7 THR D 425 ALA D 430 1 6 HELIX 26 AC8 ASP E 61 LYS E 64 5 4 HELIX 27 AC9 ASN E 106 TYR E 110 5 5 HELIX 28 AD1 ASN F 106 TYR F 110 5 5 HELIX 29 AD2 ASN G 106 TYR G 110 5 5 SHEET 1 AA1 5 GLU A 341 ILE A 345 0 SHEET 2 AA1 5 VAL A 382 LYS A 390 -1 O SER A 386 N GLU A 341 SHEET 3 AA1 5 PRO A 493 LEU A 499 -1 O TYR A 494 N VAL A 389 SHEET 4 AA1 5 GLY A 418 ALA A 422 -1 N CYS A 419 O LEU A 499 SHEET 5 AA1 5 THR A 363 TYR A 367 -1 N LYS A 365 O VAL A 420 SHEET 1 AA2 2 LYS A 439 ARG A 441 0 SHEET 2 AA2 2 LEU A 478 ASP A 480 -1 O ASN A 479 N TYR A 440 SHEET 1 AA3 6 GLU B 341 ILE B 345 0 SHEET 2 AA3 6 VAL B 382 LYS B 390 -1 O VAL B 382 N ILE B 345 SHEET 3 AA3 6 PRO B 493 SER B 500 -1 O SER B 500 N TYR B 383 SHEET 4 AA3 6 GLY B 418 ALA B 422 -1 N CYS B 419 O LEU B 499 SHEET 5 AA3 6 THR B 363 TYR B 367 -1 N TYR B 367 O GLY B 418 SHEET 6 AA3 6 ARG F 103 SER F 104 -1 O ARG F 103 N PHE B 364 SHEET 1 AA4 2 CYS B 348 VAL B 349 0 SHEET 2 AA4 2 VAL B 510 CYS B 511 1 O CYS B 511 N CYS B 348 SHEET 1 AA5 2 LYS B 439 ARG B 441 0 SHEET 2 AA5 2 LEU B 478 ASP B 480 -1 O ASN B 479 N TYR B 440 SHEET 1 AA6 6 GLU C 341 ILE C 345 0 SHEET 2 AA6 6 VAL C 382 LYS C 390 -1 O VAL C 382 N ILE C 345 SHEET 3 AA6 6 PRO C 493 SER C 500 -1 O TYR C 494 N VAL C 389 SHEET 4 AA6 6 GLY C 418 ALA C 422 -1 N LEU C 421 O VAL C 497 SHEET 5 AA6 6 THR C 363 TYR C 367 -1 N LYS C 365 O VAL C 420 SHEET 6 AA6 6 ARG G 103 SER G 104 -1 O ARG G 103 N PHE C 364 SHEET 1 AA7 2 CYS C 348 VAL C 349 0 SHEET 2 AA7 2 VAL C 510 CYS C 511 1 O CYS C 511 N CYS C 348 SHEET 1 AA8 2 LYS C 439 ARG C 441 0 SHEET 2 AA8 2 LEU C 478 ASP C 480 -1 O ASN C 479 N TYR C 440 SHEET 1 AA9 6 GLU D 341 ILE D 345 0 SHEET 2 AA9 6 VAL D 382 LYS D 390 -1 O VAL D 382 N ILE D 345 SHEET 3 AA9 6 PRO D 493 SER D 500 -1 O TYR D 494 N VAL D 389 SHEET 4 AA9 6 GLY D 418 ALA D 422 -1 N CYS D 419 O LEU D 499 SHEET 5 AA9 6 THR D 363 TYR D 367 -1 N LYS D 365 O VAL D 420 SHEET 6 AA9 6 ARG E 103 SER E 104 -1 O ARG E 103 N PHE D 364 SHEET 1 AB1 2 CYS D 348 VAL D 349 0 SHEET 2 AB1 2 VAL D 510 CYS D 511 1 O CYS D 511 N CYS D 348 SHEET 1 AB2 2 LYS D 439 ARG D 441 0 SHEET 2 AB2 2 LEU D 478 ASP D 480 -1 O ASN D 479 N TYR D 440 SHEET 1 AB3 4 LEU E 4 SER E 7 0 SHEET 2 AB3 4 LEU E 18 ALA E 24 -1 O SER E 21 N SER E 7 SHEET 3 AB3 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AB3 4 PHE E 67 ARG E 71 -1 N THR E 68 O GLN E 81 SHEET 1 AB4 6 LEU E 11 VAL E 12 0 SHEET 2 AB4 6 THR E 117 VAL E 121 1 O THR E 120 N VAL E 12 SHEET 3 AB4 6 ALA E 91 ALA E 96 -1 N TYR E 93 O THR E 117 SHEET 4 AB4 6 LEU E 34 GLN E 39 -1 N PHE E 37 O TYR E 94 SHEET 5 AB4 6 GLU E 46 ILE E 51 -1 O ILE E 51 N LEU E 34 SHEET 6 AB4 6 PRO E 57 TYR E 59 -1 O PHE E 58 N CYS E 50 SHEET 1 AB5 4 LEU F 4 SER F 7 0 SHEET 2 AB5 4 LEU F 18 ALA F 24 -1 O SER F 21 N SER F 7 SHEET 3 AB5 4 THR F 77 MET F 82 -1 O MET F 82 N LEU F 18 SHEET 4 AB5 4 PHE F 67 ARG F 71 -1 N THR F 68 O GLN F 81 SHEET 1 AB6 6 LEU F 11 VAL F 12 0 SHEET 2 AB6 6 THR F 117 VAL F 121 1 O THR F 120 N VAL F 12 SHEET 3 AB6 6 ALA F 91 GLY F 98 -1 N TYR F 93 O THR F 117 SHEET 4 AB6 6 ALA F 33 GLN F 39 -1 N PHE F 37 O TYR F 94 SHEET 5 AB6 6 GLU F 46 ILE F 51 -1 O SER F 49 N TRP F 36 SHEET 6 AB6 6 PRO F 57 TYR F 59 -1 O PHE F 58 N CYS F 50 SHEET 1 AB7 4 LEU F 11 VAL F 12 0 SHEET 2 AB7 4 THR F 117 VAL F 121 1 O THR F 120 N VAL F 12 SHEET 3 AB7 4 ALA F 91 GLY F 98 -1 N TYR F 93 O THR F 117 SHEET 4 AB7 4 TYR F 112 TRP F 113 -1 O TYR F 112 N ALA F 97 SHEET 1 AB8 4 LEU G 4 SER G 7 0 SHEET 2 AB8 4 LEU G 18 ALA G 24 -1 O SER G 21 N SER G 7 SHEET 3 AB8 4 THR G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 4 AB8 4 PHE G 67 ARG G 71 -1 N SER G 70 O TYR G 79 SHEET 1 AB9 5 PRO G 57 TYR G 59 0 SHEET 2 AB9 5 GLU G 46 ILE G 51 -1 N CYS G 50 O PHE G 58 SHEET 3 AB9 5 ALA G 33 GLN G 39 -1 N TRP G 36 O SER G 49 SHEET 4 AB9 5 ALA G 91 GLY G 98 -1 O TYR G 94 N PHE G 37 SHEET 5 AB9 5 TYR G 112 TRP G 113 -1 O TYR G 112 N ALA G 97 SHEET 1 AC1 5 PRO G 57 TYR G 59 0 SHEET 2 AC1 5 GLU G 46 ILE G 51 -1 N CYS G 50 O PHE G 58 SHEET 3 AC1 5 ALA G 33 GLN G 39 -1 N TRP G 36 O SER G 49 SHEET 4 AC1 5 ALA G 91 GLY G 98 -1 O TYR G 94 N PHE G 37 SHEET 5 AC1 5 THR G 117 VAL G 119 -1 O THR G 117 N TYR G 93 SHEET 1 AC2 4 LEU H 4 SER H 7 0 SHEET 2 AC2 4 LEU H 18 ALA H 24 -1 O SER H 21 N SER H 7 SHEET 3 AC2 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AC2 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AC3 5 PRO H 57 TYR H 59 0 SHEET 2 AC3 5 GLU H 46 ILE H 51 -1 N CYS H 50 O PHE H 58 SHEET 3 AC3 5 ALA H 33 GLN H 39 -1 N TRP H 36 O SER H 49 SHEET 4 AC3 5 ALA H 91 GLY H 98 -1 O TYR H 94 N PHE H 37 SHEET 5 AC3 5 TYR H 112 TRP H 113 -1 O TYR H 112 N ALA H 97 SHEET 1 AC4 5 PRO H 57 TYR H 59 0 SHEET 2 AC4 5 GLU H 46 ILE H 51 -1 N CYS H 50 O PHE H 58 SHEET 3 AC4 5 ALA H 33 GLN H 39 -1 N TRP H 36 O SER H 49 SHEET 4 AC4 5 ALA H 91 GLY H 98 -1 O TYR H 94 N PHE H 37 SHEET 5 AC4 5 THR H 117 VAL H 119 -1 O THR H 117 N TYR H 93 SSBOND 1 CYS A 323 CYS A 348 1555 1555 2.03 SSBOND 2 CYS A 366 CYS A 419 1555 1555 2.04 SSBOND 3 CYS A 378 CYS A 511 1555 1555 2.04 SSBOND 4 CYS A 467 CYS A 474 1555 1555 2.04 SSBOND 5 CYS B 323 CYS B 348 1555 1555 2.04 SSBOND 6 CYS B 366 CYS B 419 1555 1555 2.05 SSBOND 7 CYS B 378 CYS B 511 1555 1555 2.04 SSBOND 8 CYS B 467 CYS B 474 1555 1555 2.05 SSBOND 9 CYS C 323 CYS C 348 1555 1555 2.04 SSBOND 10 CYS C 366 CYS C 419 1555 1555 2.04 SSBOND 11 CYS C 378 CYS C 511 1555 1555 2.03 SSBOND 12 CYS C 467 CYS C 474 1555 1555 2.05 SSBOND 13 CYS D 323 CYS D 348 1555 1555 2.04 SSBOND 14 CYS D 366 CYS D 419 1555 1555 2.04 SSBOND 15 CYS D 378 CYS D 511 1555 1555 2.04 SSBOND 16 CYS D 467 CYS D 474 1555 1555 2.04 SSBOND 17 CYS E 22 CYS E 95 1555 1555 2.05 SSBOND 18 CYS F 22 CYS F 95 1555 1555 2.05 SSBOND 19 CYS G 22 CYS G 95 1555 1555 2.04 SSBOND 20 CYS H 22 CYS H 95 1555 1555 2.04 CRYST1 101.702 112.006 151.037 90.00 90.00 90.00 P 21 21 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.009833 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008928 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006621 0.00000