HEADER VIRAL PROTEIN/IMMUNE SYSTEM 04-JUN-24 8ZRD TITLE THE COMPLEX STRUCTURE OF SARS-COV-2 RBD AND LLAMA SINGLE-DOMAIN TITLE 2 ANTIBODY S4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, E; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN (RBD); COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: LLAMA SINGLE-DOMAIN ANTIBODY S4; COMPND 8 CHAIN: C, D; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: BAC CLONING VECTOR 16-12-21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 2992794; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: BAC CLONING VECTOR 16-12-21; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 2992794 KEYWDS SARS-COV-2, LLAMA SINGLE-DOMAIN ANTIBODY, VIRAL PROTEIN/IMMUNE KEYWDS 2 SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.CHEN REVDAT 1 10-SEP-25 8ZRD 0 JRNL AUTH C.LIU,H.HADIATULLAH,Z.YUCHI JRNL TITL IDENTIFICATION OF A POTENT SARS-COV-2 NEUTRALIZING NANOBODY JRNL TITL 2 TARGETING THE RECEPTOR-BINDING DOMAIN OF THE SPIKE PROTEIN. JRNL REF INT.J.BIOL.MACROMOL. V. 281 36403 2024 JRNL REFN ISSN 0141-8130 JRNL PMID 39383917 JRNL DOI 10.1016/J.IJBIOMAC.2024.136403 REMARK 2 REMARK 2 RESOLUTION. 2.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.14_3247: ???) 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) : 2.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7 REMARK 3 NUMBER OF REFLECTIONS : 49004 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.240 REMARK 3 R VALUE (WORKING SET) : 0.235 REMARK 3 FREE R VALUE : 0.295 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.460 REMARK 3 FREE R VALUE TEST SET COUNT : 3657 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 27.8000 - 7.9828 0.88 1606 126 0.2047 0.2620 REMARK 3 2 7.9828 - 6.3606 1.00 1802 146 0.2245 0.2835 REMARK 3 3 6.3606 - 5.5637 1.00 1795 144 0.2089 0.2755 REMARK 3 4 5.5637 - 5.0583 1.00 1795 148 0.2061 0.2763 REMARK 3 5 5.0583 - 4.6975 1.00 1809 149 0.1947 0.2589 REMARK 3 6 4.6975 - 4.4217 1.00 1808 147 0.1848 0.2601 REMARK 3 7 4.4217 - 4.2010 1.00 1799 143 0.1924 0.2316 REMARK 3 8 4.2010 - 4.0187 1.00 1815 148 0.2046 0.2848 REMARK 3 9 4.0187 - 3.8644 0.83 1473 121 0.2433 0.2541 REMARK 3 10 3.8644 - 3.7314 1.00 1834 146 0.2499 0.3343 REMARK 3 11 3.7314 - 3.6149 0.70 1250 103 0.2686 0.3150 REMARK 3 12 3.6149 - 3.5118 1.00 1785 147 0.2670 0.3515 REMARK 3 13 3.5118 - 3.4195 0.74 1336 103 0.2878 0.3454 REMARK 3 14 3.4195 - 3.3362 1.00 1793 148 0.2941 0.3719 REMARK 3 15 3.3362 - 3.2605 1.00 1821 151 0.2854 0.3348 REMARK 3 16 3.2605 - 3.1912 1.00 1794 143 0.2843 0.3332 REMARK 3 17 3.1912 - 3.1275 1.00 1793 151 0.2901 0.3341 REMARK 3 18 3.1275 - 3.0685 1.00 1818 145 0.2891 0.3546 REMARK 3 19 3.0685 - 3.0138 1.00 1778 141 0.2831 0.3087 REMARK 3 20 3.0138 - 2.9628 1.00 1823 147 0.2985 0.3378 REMARK 3 21 2.9628 - 2.9150 1.00 1794 144 0.2974 0.3569 REMARK 3 22 2.9150 - 2.8702 1.00 1819 140 0.3240 0.3835 REMARK 3 23 2.8702 - 2.8280 1.00 1786 145 0.3259 0.3677 REMARK 3 24 2.8280 - 2.7882 1.00 1818 146 0.3354 0.4038 REMARK 3 25 2.7882 - 2.7506 1.00 1799 141 0.3582 0.3937 REMARK 3 26 2.7506 - 2.7150 1.00 1804 144 0.3701 0.4213 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) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.620 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 77.40 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 : 0.009 4898 REMARK 3 ANGLE : 1.027 6691 REMARK 3 CHIRALITY : 0.055 710 REMARK 3 PLANARITY : 0.006 881 REMARK 3 DIHEDRAL : 6.918 2779 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 8ZRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048384. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-SEP-22 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 : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 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 : AUTOXDS 2.3.79 REMARK 200 DATA SCALING SOFTWARE : AUTOXDS 2.3.79 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49004 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.715 REMARK 200 RESOLUTION RANGE LOW (A) : 27.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7 REMARK 200 DATA REDUNDANCY : 22.10 REMARK 200 R MERGE (I) : 0.13040 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.8300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.440 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX 1.14_3247 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRATE AT PH 5.0 AND 20% REMARK 280 PEG6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.83200 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 165.66400 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 124.24800 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 207.08000 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.41600 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.83200 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 165.66400 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 207.08000 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 124.24800 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 41.41600 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E 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 ALA A 316 REMARK 465 ASP A 317 REMARK 465 PRO A 318 REMARK 465 ARG A 319 REMARK 465 VAL A 320 REMARK 465 GLN A 321 REMARK 465 PRO A 322 REMARK 465 THR A 323 REMARK 465 GLU A 324 REMARK 465 SER A 325 REMARK 465 ILE A 326 REMARK 465 VAL A 327 REMARK 465 ARG A 328 REMARK 465 PHE A 329 REMARK 465 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 THR A 333 REMARK 465 ASN A 334 REMARK 465 CYS A 525 REMARK 465 GLY A 526 REMARK 465 PRO A 527 REMARK 465 LYS A 528 REMARK 465 LYS A 529 REMARK 465 HIS A 530 REMARK 465 HIS A 531 REMARK 465 HIS A 532 REMARK 465 HIS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 SER C 136 REMARK 465 LEU C 137 REMARK 465 GLU C 138 REMARK 465 HIS C 139 REMARK 465 HIS C 140 REMARK 465 HIS C 141 REMARK 465 HIS C 142 REMARK 465 HIS C 143 REMARK 465 HIS C 144 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 GLY D 67 REMARK 465 ARG D 68 REMARK 465 ASP D 103 REMARK 465 VAL D 104 REMARK 465 GLY D 105 REMARK 465 GLY D 106 REMARK 465 SER D 107 REMARK 465 TYR D 108 REMARK 465 LEU D 109 REMARK 465 TYR D 110 REMARK 465 THR D 111 REMARK 465 SER D 131 REMARK 465 SER D 132 REMARK 465 GLY D 133 REMARK 465 GLY D 134 REMARK 465 GLY D 135 REMARK 465 SER D 136 REMARK 465 LEU D 137 REMARK 465 GLU D 138 REMARK 465 HIS D 139 REMARK 465 HIS D 140 REMARK 465 HIS D 141 REMARK 465 HIS D 142 REMARK 465 HIS D 143 REMARK 465 HIS D 144 REMARK 465 ALA E 316 REMARK 465 ASP E 317 REMARK 465 PRO E 318 REMARK 465 ARG E 319 REMARK 465 VAL E 320 REMARK 465 GLN E 321 REMARK 465 PRO E 322 REMARK 465 THR E 323 REMARK 465 GLU E 324 REMARK 465 SER E 325 REMARK 465 ILE E 326 REMARK 465 VAL E 327 REMARK 465 ARG E 328 REMARK 465 PHE E 329 REMARK 465 PRO E 330 REMARK 465 ASN E 331 REMARK 465 ILE E 332 REMARK 465 ASN E 370 REMARK 465 SER E 371 REMARK 465 ALA E 372 REMARK 465 LYS E 528 REMARK 465 LYS E 529 REMARK 465 HIS E 530 REMARK 465 HIS E 531 REMARK 465 HIS E 532 REMARK 465 HIS E 533 REMARK 465 HIS E 534 REMARK 465 HIS E 535 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 LEU A 335 CG CD1 CD2 REMARK 470 GLU A 340 CG CD OE1 OE2 REMARK 470 LYS A 356 CG CD CE NZ REMARK 470 SER A 359 OG REMARK 470 VAL A 362 CG1 CG2 REMARK 470 LEU A 368 CG CD1 CD2 REMARK 470 SER A 373 OG REMARK 470 VAL A 382 CG1 CG2 REMARK 470 SER A 383 OG REMARK 470 PRO A 384 CG CD REMARK 470 LEU A 387 CG CD1 CD2 REMARK 470 ASN A 388 CG OD1 ND2 REMARK 470 ARG A 408 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 428 CG OD1 OD2 REMARK 470 SER A 443 OG REMARK 470 LYS A 444 CG CD CE NZ REMARK 470 VAL A 445 CG1 CG2 REMARK 470 LYS A 458 CG CD CE NZ REMARK 470 GLU A 471 CG CD OE1 OE2 REMARK 470 PRO A 521 CG CD REMARK 470 SER C 8 OG REMARK 470 ASP C 32 CG OD1 OD2 REMARK 470 LYS C 44 CG CD CE NZ REMARK 470 TYR C 55 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER C 72 OG REMARK 470 ASP C 74 CG OD1 OD2 REMARK 470 LYS C 77 CG CD CE NZ REMARK 470 ASN C 78 CG OD1 ND2 REMARK 470 SER C 86 OG REMARK 470 LYS C 102 CG CD CE NZ REMARK 470 ASP C 103 CG OD1 OD2 REMARK 470 GLN C 124 CG CD OE1 NE2 REMARK 470 GLN D 4 CG CD OE1 NE2 REMARK 470 PHE D 12 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU D 19 CG CD1 CD2 REMARK 470 ARG D 20 CG CD NE CZ NH1 NH2 REMARK 470 LEU D 24 CG CD1 CD2 REMARK 470 SER D 26 OG REMARK 470 TYR D 55 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN D 63 CG CD OE1 NE2 REMARK 470 VAL D 65 CG1 CG2 REMARK 470 THR D 70 OG1 CG2 REMARK 470 VAL D 71 CG1 CG2 REMARK 470 ASP D 74 CG OD1 OD2 REMARK 470 LYS D 77 CG CD CE NZ REMARK 470 TYR D 81 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU D 83 CG CD OE1 OE2 REMARK 470 LYS D 85 CG CD CE NZ REMARK 470 GLU D 88 CG CD OE1 OE2 REMARK 470 PRO D 89 CG CD REMARK 470 GLU D 90 CG CD OE1 OE2 REMARK 470 ASP D 91 CG OD1 OD2 REMARK 470 LYS D 102 CG CD CE NZ REMARK 470 PHE D 113 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR D 126 OG1 CG2 REMARK 470 VAL D 128 CG1 CG2 REMARK 470 VAL D 130 CG1 CG2 REMARK 470 LEU E 335 CG CD1 CD2 REMARK 470 ASP E 364 CG OD1 OD2 REMARK 470 SER E 366 OG REMARK 470 VAL E 367 CG1 CG2 REMARK 470 TYR E 369 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS E 378 CG CD CE NZ REMARK 470 SER E 383 OG REMARK 470 THR E 385 OG1 CG2 REMARK 470 LYS E 386 CG CD CE NZ REMARK 470 LEU E 387 CG CD1 CD2 REMARK 470 ASP E 389 CG OD1 OD2 REMARK 470 LEU E 390 CG CD1 CD2 REMARK 470 LYS E 444 CG CD CE NZ REMARK 470 VAL E 445 CG1 CG2 REMARK 470 LYS E 458 CG CD CE NZ REMARK 470 GLU E 471 CG CD OE1 OE2 REMARK 470 SER E 477 OG REMARK 470 ASN E 481 CG OD1 ND2 REMARK 470 SER E 494 OG REMARK 470 GLN E 498 CG CD OE1 NE2 REMARK 470 GLU E 516 CG CD OE1 OE2 REMARK 470 LEU E 517 CG CD1 CD2 REMARK 470 LEU E 518 CG CD1 CD2 REMARK 470 HIS E 519 CG ND1 CD2 CE1 NE2 REMARK 470 THR E 523 OG1 CG2 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 728 O HOH A 732 1.91 REMARK 500 O HOH A 723 O HOH A 730 1.95 REMARK 500 O HOH A 703 O HOH A 718 2.03 REMARK 500 O HOH A 715 O HOH A 716 2.17 REMARK 500 O LEU E 452 O HOH E 701 2.17 REMARK 500 O VAL A 524 O HOH A 701 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU D 5 CA - CB - CG ANGL. DEV. = 15.6 DEGREES REMARK 500 CYS D 97 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 352 48.22 -108.93 REMARK 500 ASN A 360 70.03 53.23 REMARK 500 LEU A 368 -60.07 -92.68 REMARK 500 TYR A 369 23.14 -70.90 REMARK 500 SER A 373 8.03 56.63 REMARK 500 PHE A 377 47.06 -143.08 REMARK 500 VAL A 382 -29.08 -33.43 REMARK 500 SER A 383 -89.05 -52.26 REMARK 500 LEU A 387 -134.00 79.55 REMARK 500 ASN A 388 -159.57 157.09 REMARK 500 ALA A 411 144.61 -174.15 REMARK 500 PRO A 412 125.09 -24.77 REMARK 500 ASN A 422 -61.96 -128.26 REMARK 500 ASP A 428 36.42 -85.98 REMARK 500 VAL C 49 -65.10 -105.95 REMARK 500 ALA C 93 -179.28 -174.56 REMARK 500 SER D 8 157.32 179.16 REMARK 500 ASP D 32 4.33 -64.59 REMARK 500 SER D 62 -141.02 -87.24 REMARK 500 GLN D 63 46.35 -99.01 REMARK 500 ALA D 93 -175.34 -172.63 REMARK 500 ARG D 101 -70.60 -77.40 REMARK 500 ALA E 352 48.15 -98.98 REMARK 500 LEU E 368 -80.67 -67.76 REMARK 500 PHE E 377 59.05 -155.10 REMARK 500 ASN E 422 -57.15 -128.67 REMARK 500 ASP E 428 42.48 -82.77 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG D 73 0.18 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 601 REMARK 610 NAG E 601 DBREF 8ZRD A 319 529 UNP P0DTC2 SPIKE_SARS2 319 529 DBREF 8ZRD C 1 144 PDB 8ZRD 8ZRD 1 144 DBREF 8ZRD D 1 144 PDB 8ZRD 8ZRD 1 144 DBREF 8ZRD E 319 529 UNP P0DTC2 SPIKE_SARS2 319 529 SEQADV 8ZRD ALA A 316 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD ASP A 317 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD PRO A 318 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 530 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 531 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 532 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 533 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 534 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD ALA E 316 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD ASP E 317 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD PRO E 318 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 530 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 531 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 532 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 533 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 534 UNP P0DTC2 EXPRESSION TAG SEQADV 8ZRD HIS E 535 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 220 ALA ASP PRO ARG VAL GLN PRO THR GLU SER ILE VAL ARG SEQRES 2 A 220 PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL SEQRES 3 A 220 PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN SEQRES 4 A 220 ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL SEQRES 5 A 220 LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR SEQRES 6 A 220 GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR SEQRES 7 A 220 ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU SEQRES 8 A 220 VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA SEQRES 9 A 220 ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS SEQRES 10 A 220 VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL SEQRES 11 A 220 GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SEQRES 12 A 220 SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU SEQRES 13 A 220 ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU SEQRES 14 A 220 GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE SEQRES 15 A 220 GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL SEQRES 16 A 220 VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR SEQRES 17 A 220 VAL CYS GLY PRO LYS LYS HIS HIS HIS HIS HIS HIS SEQRES 1 C 144 MET ALA VAL GLN LEU VAL GLU SER GLY GLY GLY PHE VAL SEQRES 2 C 144 GLN PRO GLY GLY SER LEU ARG LEU SER CYS LEU ALA SER SEQRES 3 C 144 GLY PHE ALA PHE GLY ASP HIS TYR MET THR TRP VAL ARG SEQRES 4 C 144 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SEQRES 5 C 144 ASN ASN TYR GLY ASP ASN THR PHE TYR SER GLN SER VAL SEQRES 6 C 144 LYS GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS ASN SEQRES 7 C 144 THR LEU TYR LEU GLU MET LYS SER LEU GLU PRO GLU ASP SEQRES 8 C 144 THR ALA LEU TYR TYR CYS ALA ARG PRO ARG LYS ASP VAL SEQRES 9 C 144 GLY GLY SER TYR LEU TYR THR HIS PHE PRO GLY LEU THR SEQRES 10 C 144 GLU TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 11 C 144 SER SER GLY GLY GLY SER LEU GLU HIS HIS HIS HIS HIS SEQRES 12 C 144 HIS SEQRES 1 D 144 MET ALA VAL GLN LEU VAL GLU SER GLY GLY GLY PHE VAL SEQRES 2 D 144 GLN PRO GLY GLY SER LEU ARG LEU SER CYS LEU ALA SER SEQRES 3 D 144 GLY PHE ALA PHE GLY ASP HIS TYR MET THR TRP VAL ARG SEQRES 4 D 144 GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SEQRES 5 D 144 ASN ASN TYR GLY ASP ASN THR PHE TYR SER GLN SER VAL SEQRES 6 D 144 LYS GLY ARG PHE THR VAL SER ARG ASP ASN ALA LYS ASN SEQRES 7 D 144 THR LEU TYR LEU GLU MET LYS SER LEU GLU PRO GLU ASP SEQRES 8 D 144 THR ALA LEU TYR TYR CYS ALA ARG PRO ARG LYS ASP VAL SEQRES 9 D 144 GLY GLY SER TYR LEU TYR THR HIS PHE PRO GLY LEU THR SEQRES 10 D 144 GLU TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 11 D 144 SER SER GLY GLY GLY SER LEU GLU HIS HIS HIS HIS HIS SEQRES 12 D 144 HIS SEQRES 1 E 220 ALA ASP PRO ARG VAL GLN PRO THR GLU SER ILE VAL ARG SEQRES 2 E 220 PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU VAL SEQRES 3 E 220 PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN SEQRES 4 E 220 ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL SEQRES 5 E 220 LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS TYR SEQRES 6 E 220 GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR SEQRES 7 E 220 ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU SEQRES 8 E 220 VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE ALA SEQRES 9 E 220 ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS SEQRES 10 E 220 VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS VAL SEQRES 11 E 220 GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SEQRES 12 E 220 SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU SEQRES 13 E 220 ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL GLU SEQRES 14 E 220 GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY PHE SEQRES 15 E 220 GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL SEQRES 16 E 220 VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR SEQRES 17 E 220 VAL CYS GLY PRO LYS LYS HIS HIS HIS HIS HIS HIS HET NAG A 601 14 HET NAG E 601 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 5 NAG 2(C8 H15 N O6) FORMUL 7 HOH *43(H2 O) HELIX 1 AA1 PHE A 338 ASN A 343 1 6 HELIX 2 AA2 SER A 349 TRP A 353 5 5 HELIX 3 AA3 ASP A 364 LEU A 368 5 5 HELIX 4 AA4 GLY A 404 ILE A 410 5 7 HELIX 5 AA5 GLY A 416 ASN A 422 1 7 HELIX 6 AA6 SER A 438 SER A 443 1 6 HELIX 7 AA7 GLY A 502 GLN A 506 5 5 HELIX 8 AA8 ALA C 29 HIS C 33 5 5 HELIX 9 AA9 GLU C 88 THR C 92 5 5 HELIX 10 AB1 ALA D 29 HIS D 33 5 5 HELIX 11 AB2 GLU D 88 THR D 92 5 5 HELIX 12 AB3 PHE E 338 ASN E 343 1 6 HELIX 13 AB4 ASP E 364 TYR E 369 1 6 HELIX 14 AB5 PRO E 384 ASP E 389 5 6 HELIX 15 AB6 ASP E 405 ILE E 410 5 6 HELIX 16 AB7 GLY E 416 ASN E 422 1 7 HELIX 17 AB8 SER E 438 SER E 443 1 6 HELIX 18 AB9 GLY E 502 TYR E 505 5 4 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ILE A 402 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 TYR A 508 GLU A 516 -1 O GLU A 516 N ASN A 394 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 LYS A 378 -1 N LYS A 378 O VAL A 433 SHEET 1 AA2 2 LEU A 452 ARG A 454 0 SHEET 2 AA2 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA3 2 TYR A 473 GLN A 474 0 SHEET 2 AA3 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA4 4 GLN C 4 SER C 8 0 SHEET 2 AA4 4 LEU C 19 SER C 26 -1 O LEU C 24 N VAL C 6 SHEET 3 AA4 4 THR C 79 MET C 84 -1 O LEU C 82 N LEU C 21 SHEET 4 AA4 4 PHE C 69 ASP C 74 -1 N SER C 72 O TYR C 81 SHEET 1 AA5 6 GLY C 11 VAL C 13 0 SHEET 2 AA5 6 THR C 126 VAL C 130 1 O THR C 129 N GLY C 11 SHEET 3 AA5 6 ALA C 93 PRO C 100 -1 N ALA C 93 O VAL C 128 SHEET 4 AA5 6 MET C 35 GLN C 40 -1 N VAL C 38 O TYR C 96 SHEET 5 AA5 6 GLU C 47 ILE C 52 -1 O GLU C 47 N ARG C 39 SHEET 6 AA5 6 THR C 59 TYR C 61 -1 O PHE C 60 N ASP C 51 SHEET 1 AA6 4 GLY C 11 VAL C 13 0 SHEET 2 AA6 4 THR C 126 VAL C 130 1 O THR C 129 N GLY C 11 SHEET 3 AA6 4 ALA C 93 PRO C 100 -1 N ALA C 93 O VAL C 128 SHEET 4 AA6 4 TYR C 119 TRP C 122 -1 O TYR C 121 N ARG C 99 SHEET 1 AA7 4 GLN D 4 SER D 8 0 SHEET 2 AA7 4 SER D 18 SER D 26 -1 O SER D 22 N SER D 8 SHEET 3 AA7 4 THR D 79 LYS D 85 -1 O MET D 84 N LEU D 19 SHEET 4 AA7 4 THR D 70 ASP D 74 -1 N SER D 72 O TYR D 81 SHEET 1 AA8 5 THR D 59 TYR D 61 0 SHEET 2 AA8 5 GLU D 47 ILE D 52 -1 N ASP D 51 O PHE D 60 SHEET 3 AA8 5 MET D 35 GLN D 40 -1 N ARG D 39 O GLU D 47 SHEET 4 AA8 5 ALA D 93 PRO D 100 -1 O TYR D 96 N VAL D 38 SHEET 5 AA8 5 TYR D 119 TRP D 122 -1 O TYR D 121 N ARG D 99 SHEET 1 AA9 5 THR D 59 TYR D 61 0 SHEET 2 AA9 5 GLU D 47 ILE D 52 -1 N ASP D 51 O PHE D 60 SHEET 3 AA9 5 MET D 35 GLN D 40 -1 N ARG D 39 O GLU D 47 SHEET 4 AA9 5 ALA D 93 PRO D 100 -1 O TYR D 96 N VAL D 38 SHEET 5 AA9 5 THR D 126 VAL D 128 -1 O VAL D 128 N ALA D 93 SHEET 1 AB1 5 ASN E 354 ILE E 358 0 SHEET 2 AB1 5 ASN E 394 ARG E 403 -1 O VAL E 395 N ILE E 358 SHEET 3 AB1 5 PRO E 507 GLU E 516 -1 O TYR E 508 N ILE E 402 SHEET 4 AB1 5 GLY E 431 ASN E 437 -1 N ILE E 434 O VAL E 511 SHEET 5 AB1 5 THR E 376 TYR E 380 -1 N LYS E 378 O VAL E 433 SHEET 1 AB2 2 CYS E 391 PHE E 392 0 SHEET 2 AB2 2 VAL E 524 CYS E 525 -1 O VAL E 524 N PHE E 392 SHEET 1 AB3 2 LEU E 452 ARG E 454 0 SHEET 2 AB3 2 LEU E 492 SER E 494 -1 O GLN E 493 N TYR E 453 SHEET 1 AB4 2 TYR E 473 GLN E 474 0 SHEET 2 AB4 2 CYS E 488 TYR E 489 -1 O TYR E 489 N TYR E 473 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.07 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.05 SSBOND 3 CYS A 480 CYS A 488 1555 1555 2.06 SSBOND 4 CYS C 23 CYS C 97 1555 1555 2.05 SSBOND 5 CYS D 23 CYS D 97 1555 1555 2.03 SSBOND 6 CYS E 336 CYS E 361 1555 1555 2.05 SSBOND 7 CYS E 379 CYS E 432 1555 1555 2.08 SSBOND 8 CYS E 391 CYS E 525 1555 1555 2.05 SSBOND 9 CYS E 480 CYS E 488 1555 1555 2.05 CRYST1 116.187 116.187 248.496 90.00 90.00 120.00 P 61 2 2 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 0.008607 0.004969 0.000000 0.00000 SCALE2 0.000000 0.009938 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004024 0.00000