HEADER VIRAL PROTEIN 17-JUN-24 8ZYF TITLE CRYSTAL STRUCTURE OF ZW2G10 FAB IN COMPLEX WITH OMICRON RBD COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RBD DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ZW2G10 FAB LIGHT CHAIN; COMPND 8 CHAIN: D, C; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: ZW2G10 FAB HEAVY CHAIN; COMPND 12 CHAIN: H, E; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: 2019-NCOV, SARS-COV-2; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS OMICRON;NEUTRALIZATION ANTIBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR H.Y.YUAN,J.M.LI REVDAT 1 26-MAR-25 8ZYF 0 JRNL AUTH G.ZHANG,P.HUANG,H.YUAN,E.LI,X.CHI,H.SUN,J.HAN,T.FANG,Y.DONG, JRNL AUTH 2 J.LI,Y.WANG,J.LI,S.CHIU,C.YU JRNL TITL NASAL DELIVERY OF SECRETORY IGA CONFERS ENHANCED JRNL TITL 2 NEUTRALIZING ACTIVITY AGAINST OMICRON VARIANTS COMPARED TO JRNL TITL 3 ITS IGG COUNTERPART. JRNL REF MOL.THER. 2025 JRNL REFN ESSN 1525-0024 JRNL PMID 40025736 JRNL DOI 10.1016/J.YMTHE.2025.02.041 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.17_3644: ???) 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.53 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 43011 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 2181 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 39.5300 - 6.5500 0.99 2809 157 0.2747 0.2822 REMARK 3 2 6.5500 - 5.2000 1.00 2712 128 0.2507 0.2913 REMARK 3 3 5.2000 - 4.5500 1.00 2619 156 0.1975 0.2794 REMARK 3 4 4.5400 - 4.1300 1.00 2617 148 0.1894 0.2126 REMARK 3 5 4.1300 - 3.8300 1.00 2619 126 0.2066 0.2223 REMARK 3 6 3.8300 - 3.6100 0.99 2585 145 0.2150 0.2994 REMARK 3 7 3.6100 - 3.4300 0.99 2509 136 0.2252 0.2812 REMARK 3 8 3.4300 - 3.2800 0.98 2584 152 0.2305 0.2615 REMARK 3 9 3.2800 - 3.1500 0.98 2506 142 0.2334 0.3110 REMARK 3 10 3.1500 - 3.0400 0.98 2511 139 0.2484 0.3160 REMARK 3 11 3.0400 - 2.9500 0.97 2521 120 0.2499 0.3174 REMARK 3 12 2.9500 - 2.8600 0.97 2481 143 0.2635 0.3383 REMARK 3 13 2.8600 - 2.7900 0.96 2412 132 0.2522 0.3239 REMARK 3 14 2.7900 - 2.7200 0.97 2550 116 0.2570 0.3129 REMARK 3 15 2.7200 - 2.6600 0.96 2435 134 0.2603 0.3647 REMARK 3 16 2.6600 - 2.6000 0.92 2360 107 0.2602 0.3204 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) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.050 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 : 0.011 9353 REMARK 3 ANGLE : 1.070 12744 REMARK 3 CHIRALITY : 0.067 1397 REMARK 3 PLANARITY : 0.006 1644 REMARK 3 DIHEDRAL : 14.478 1295 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 8ZYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 21-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1300048749. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-AUG-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 : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43011 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 39.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.4 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 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 : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.17 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M MES PH REMARK 280 6.5, 15% W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 289K 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 22.33200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 149.67600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.76450 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 149.67600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.33200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.76450 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6120 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26350 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6350 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLY D 204 REMARK 465 SER D 205 REMARK 465 THR D 206 REMARK 465 VAL D 207 REMARK 465 GLU D 208 REMARK 465 LYS D 209 REMARK 465 THR D 210 REMARK 465 VAL D 211 REMARK 465 ALA D 212 REMARK 465 PRO D 213 REMARK 465 THR D 214 REMARK 465 SER H 142 REMARK 465 SER H 143 REMARK 465 LYS H 144 REMARK 465 SER H 145 REMARK 465 THR H 146 REMARK 465 SER H 147 REMARK 465 GLY H 148 REMARK 465 GLY H 149 REMARK 465 THR H 150 REMARK 465 ALA H 151 REMARK 465 ALA H 152 REMARK 465 LEU H 153 REMARK 465 GLY H 154 REMARK 465 CYS H 155 REMARK 465 TRP H 169 REMARK 465 ASN H 170 REMARK 465 SER H 171 REMARK 465 GLY H 172 REMARK 465 ALA H 173 REMARK 465 LEU H 174 REMARK 465 THR H 175 REMARK 465 SER H 176 REMARK 465 GLY H 177 REMARK 465 VAL H 178 REMARK 465 SER H 203 REMARK 465 LEU H 204 REMARK 465 GLY H 205 REMARK 465 THR H 206 REMARK 465 GLN H 207 REMARK 465 THR H 208 REMARK 465 TYR H 209 REMARK 465 ILE H 210 REMARK 465 CYS H 211 REMARK 465 ASN H 212 REMARK 465 VAL H 213 REMARK 465 ASN H 214 REMARK 465 HIS H 215 REMARK 465 LYS H 216 REMARK 465 PRO H 217 REMARK 465 SER H 218 REMARK 465 ASN H 219 REMARK 465 THR H 220 REMARK 465 LYS H 221 REMARK 465 VAL H 222 REMARK 465 ASP H 223 REMARK 465 LYS H 224 REMARK 465 LYS H 225 REMARK 465 VAL H 226 REMARK 465 GLU H 227 REMARK 465 PRO H 228 REMARK 465 LYS H 229 REMARK 465 GLU C 128 REMARK 465 GLU C 129 REMARK 465 LEU C 130 REMARK 465 GLN C 131 REMARK 465 SER E 142 REMARK 465 SER E 143 REMARK 465 LYS E 144 REMARK 465 SER E 145 REMARK 465 THR E 146 REMARK 465 SER E 147 REMARK 465 GLY E 148 REMARK 465 GLY E 149 REMARK 465 TRP E 169 REMARK 465 ASN E 170 REMARK 465 SER E 171 REMARK 465 GLY E 172 REMARK 465 ALA E 173 REMARK 465 LEU E 174 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 HD21 ASN A 343 C1 NAG A 601 1.09 REMARK 500 NZ LYS B 478 HD2 PHE B 486 1.10 REMARK 500 HH TYR B 380 O HOH B 701 1.24 REMARK 500 HZ1 LYS B 356 O HOH B 708 1.38 REMARK 500 OD1 ASN E 212 OD2 ASP E 223 1.41 REMARK 500 H VAL C 35 OD1 ASN C 53 1.45 REMARK 500 HH TYR C 145 O HOH C 307 1.46 REMARK 500 O THR E 208 O HOH E 301 1.53 REMARK 500 OD1 ASN A 448 HH12 ARG A 498 1.54 REMARK 500 HH TYR D 182 O HOH D 304 1.60 REMARK 500 O HOH E 305 O HOH E 306 1.81 REMARK 500 O SER C 205 O HOH C 301 1.82 REMARK 500 O HOH A 731 O HOH A 767 1.82 REMARK 500 O LEU H 4 O HOH H 301 1.83 REMARK 500 O HOH E 311 O HOH E 336 1.85 REMARK 500 O HOH A 761 O HOH H 318 1.86 REMARK 500 O HOH A 766 O HOH A 768 1.89 REMARK 500 N THR E 150 O HOH E 302 1.89 REMARK 500 O TYR A 369 O HOH A 701 1.92 REMARK 500 NZ LYS B 478 CD2 PHE B 486 1.92 REMARK 500 ND2 ASN B 343 C1 NAG B 601 1.95 REMARK 500 OG1 THR A 500 O HOH A 702 1.96 REMARK 500 O GLY E 15 O HOH E 303 1.96 REMARK 500 O HOH H 341 O HOH H 351 1.96 REMARK 500 OE1 GLN C 81 O HOH C 302 1.98 REMARK 500 O HOH H 352 O HOH H 359 1.99 REMARK 500 O PRO C 124 O HOH C 303 2.00 REMARK 500 O ASP H 116 O HOH H 302 2.02 REMARK 500 O HOH H 322 O HOH H 353 2.02 REMARK 500 OD1 ASN H 84 O HOH H 303 2.03 REMARK 500 OE2 GLU C 85 O HOH C 304 2.03 REMARK 500 OD2 ASP A 467 O HOH A 703 2.04 REMARK 500 O HOH H 366 O HOH H 367 2.05 REMARK 500 O HOH B 734 O HOH B 753 2.05 REMARK 500 N LEU H 156 O HOH H 304 2.06 REMARK 500 OH TYR B 380 O HOH B 701 2.07 REMARK 500 OE2 GLU C 203 O HOH C 305 2.08 REMARK 500 OE1 GLU C 83 O HOH C 302 2.08 REMARK 500 O HOH C 329 O HOH E 319 2.08 REMARK 500 O HOH B 757 O HOH B 761 2.09 REMARK 500 O TYR A 449 O HOH A 704 2.09 REMARK 500 OG1 THR B 376 O HOH B 702 2.10 REMARK 500 O TYR B 451 O HOH B 703 2.10 REMARK 500 N LEU B 335 O HOH B 704 2.11 REMARK 500 OD1 ASP B 405 O HOH B 705 2.11 REMARK 500 O CYS A 480 O HOH A 705 2.11 REMARK 500 O GLY H 189 O HOH H 305 2.12 REMARK 500 OG1 THR B 393 O HOH B 706 2.12 REMARK 500 O HOH B 737 O HOH B 755 2.14 REMARK 500 O PRO B 373 O HOH B 707 2.17 REMARK 500 REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS 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 B 762 O HOH B 764 1455 1.88 REMARK 500 O HOH D 310 O HOH D 339 4455 2.06 REMARK 500 O HOH B 740 O HOH B 764 1455 2.07 REMARK 500 O HOH D 321 O HOH D 338 4555 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO D 169 N PRO D 169 CA 0.213 REMARK 500 PRO C 124 N PRO C 124 CA 0.203 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 ASN A 477 CB - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 LYS D 134 N - CA - CB ANGL. DEV. = -11.6 DEGREES REMARK 500 PRO D 169 C - N - CA ANGL. DEV. = 16.3 DEGREES REMARK 500 PRO D 169 CA - N - CD ANGL. DEV. = -12.0 DEGREES REMARK 500 PRO C 124 C - N - CA ANGL. DEV. = 16.6 DEGREES REMARK 500 PRO C 124 CA - N - CD ANGL. DEV. = -9.3 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 PHE A 374 64.67 -102.05 REMARK 500 ASN A 422 -54.50 -123.79 REMARK 500 ASN D 53 -23.37 73.70 REMARK 500 ASN D 54 7.01 -151.40 REMARK 500 LEU D 80 128.72 -39.73 REMARK 500 ASP D 143 35.07 71.12 REMARK 500 GLN D 172 -156.94 -97.75 REMARK 500 LYS D 194 -61.23 -102.07 REMARK 500 LYS H 43 -169.36 -124.86 REMARK 500 ASN H 54 30.61 -95.86 REMARK 500 PRO H 138 130.15 -37.80 REMARK 500 ALA H 140 -63.83 -92.74 REMARK 500 PRO B 337 47.86 -82.69 REMARK 500 PHE B 374 50.88 -118.56 REMARK 500 ASN B 422 -51.45 -122.03 REMARK 500 ASP B 428 30.50 -97.06 REMARK 500 ARG B 457 143.08 -172.26 REMARK 500 ASN C 53 -20.75 75.04 REMARK 500 ASN C 54 3.37 -151.63 REMARK 500 SER C 92 -165.07 -160.53 REMARK 500 ASN C 133 57.23 36.24 REMARK 500 ASP C 156 -24.05 92.47 REMARK 500 LYS C 161 -100.54 47.57 REMARK 500 ALA C 162 79.25 46.68 REMARK 500 LYS C 209 -17.67 -142.49 REMARK 500 THR C 210 79.26 59.69 REMARK 500 THR E 28 98.20 -68.42 REMARK 500 ALA E 151 -64.32 -98.54 REMARK 500 ALA E 152 69.90 60.30 REMARK 500 VAL E 199 164.91 178.77 REMARK 500 SER E 201 88.71 -64.78 REMARK 500 ASN E 212 120.32 -29.39 REMARK 500 ASN E 219 51.79 36.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH H 366 DISTANCE = 6.05 ANGSTROMS REMARK 525 HOH H 367 DISTANCE = 7.21 ANGSTROMS REMARK 525 HOH H 368 DISTANCE = 8.12 ANGSTROMS 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 B 601 DBREF 8ZYF A 335 529 UNP P0DTC2 SPIKE_SARS2 335 529 DBREF 8ZYF D 1 214 PDB 8ZYF 8ZYF 1 214 DBREF 8ZYF H 1 229 PDB 8ZYF 8ZYF 1 229 DBREF 8ZYF B 335 529 UNP P0DTC2 SPIKE_SARS2 335 529 DBREF 8ZYF C 1 214 PDB 8ZYF 8ZYF 1 214 DBREF 8ZYF E 1 229 PDB 8ZYF 8ZYF 1 229 SEQADV 8ZYF ASP A 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 8ZYF LEU A 371 UNP P0DTC2 SER 371 VARIANT SEQADV 8ZYF PRO A 373 UNP P0DTC2 SER 373 VARIANT SEQADV 8ZYF PHE A 375 UNP P0DTC2 SER 375 VARIANT SEQADV 8ZYF ASN A 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 8ZYF LYS A 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 8ZYF SER A 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 8ZYF ASN A 477 UNP P0DTC2 SER 477 VARIANT SEQADV 8ZYF LYS A 478 UNP P0DTC2 THR 478 VARIANT SEQADV 8ZYF ALA A 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 8ZYF ARG A 493 UNP P0DTC2 GLN 493 VARIANT SEQADV 8ZYF SER A 496 UNP P0DTC2 GLY 496 VARIANT SEQADV 8ZYF ARG A 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 8ZYF TYR A 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 8ZYF HIS A 505 UNP P0DTC2 TYR 505 VARIANT SEQADV 8ZYF ASP B 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 8ZYF LEU B 371 UNP P0DTC2 SER 371 VARIANT SEQADV 8ZYF PRO B 373 UNP P0DTC2 SER 373 VARIANT SEQADV 8ZYF PHE B 375 UNP P0DTC2 SER 375 VARIANT SEQADV 8ZYF ASN B 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 8ZYF LYS B 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 8ZYF SER B 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 8ZYF ASN B 477 UNP P0DTC2 SER 477 VARIANT SEQADV 8ZYF LYS B 478 UNP P0DTC2 THR 478 VARIANT SEQADV 8ZYF ALA B 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 8ZYF ARG B 493 UNP P0DTC2 GLN 493 VARIANT SEQADV 8ZYF SER B 496 UNP P0DTC2 GLY 496 VARIANT SEQADV 8ZYF ARG B 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 8ZYF TYR B 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 8ZYF HIS B 505 UNP P0DTC2 TYR 505 VARIANT SEQRES 1 A 195 LEU CYS PRO PHE ASP GLU VAL PHE ASN ALA THR ARG PHE SEQRES 2 A 195 ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SER ASN SEQRES 3 A 195 CYS VAL ALA ASP TYR SER VAL LEU TYR ASN LEU ALA PRO SEQRES 4 A 195 PHE PHE THR PHE LYS CYS TYR GLY VAL SER PRO THR LYS SEQRES 5 A 195 LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SER SEQRES 6 A 195 PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA PRO SEQRES 7 A 195 GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR LYS LEU SEQRES 8 A 195 PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SER SEQRES 9 A 195 ASN LYS LEU ASP SER LYS VAL SER GLY ASN TYR ASN TYR SEQRES 10 A 195 LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO PHE SEQRES 11 A 195 GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY ASN SEQRES 12 A 195 LYS PRO CYS ASN GLY VAL ALA GLY PHE ASN CYS TYR PHE SEQRES 13 A 195 PRO LEU ARG SER TYR SER PHE ARG PRO THR TYR GLY VAL SEQRES 14 A 195 GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE GLU SEQRES 15 A 195 LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO LYS LYS SEQRES 1 D 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 D 214 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 D 214 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 D 214 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ASP SEQRES 5 D 214 ASN ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 214 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 D 214 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 D 214 SER PHE ASP SER SER LEU SER GLY VAL VAL PHE GLY GLY SEQRES 9 D 214 GLY THR ARG LEU THR VAL LEU ARG GLN PRO LYS ALA ALA SEQRES 10 D 214 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 D 214 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 D 214 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 D 214 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 D 214 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 D 214 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER SEQRES 16 D 214 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 D 214 LYS THR VAL ALA PRO THR SEQRES 1 H 229 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 229 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 229 PHE THR PHE ASP ASP TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 H 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE THR SEQRES 5 H 229 TRP ASN SER GLY THR ILE GLY TYR ALA ASP SER VAL LYS SEQRES 6 H 229 GLY ARG PHE ILE ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 229 LEU HIS LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 H 229 ALA LEU TYR TYR CYS ALA LYS ASP ASN SER ASP TYR SER SEQRES 9 H 229 GLY TYR TYR TRP GLU LEU GLU ASN TYR GLY MET ASP VAL SEQRES 10 H 229 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 11 H 229 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 H 229 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 H 229 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 H 229 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 H 229 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 229 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 H 229 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 H 229 VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 B 195 LEU CYS PRO PHE ASP GLU VAL PHE ASN ALA THR ARG PHE SEQRES 2 B 195 ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SER ASN SEQRES 3 B 195 CYS VAL ALA ASP TYR SER VAL LEU TYR ASN LEU ALA PRO SEQRES 4 B 195 PHE PHE THR PHE LYS CYS TYR GLY VAL SER PRO THR LYS SEQRES 5 B 195 LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA ASP SER SEQRES 6 B 195 PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE ALA PRO SEQRES 7 B 195 GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR LYS LEU SEQRES 8 B 195 PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP ASN SER SEQRES 9 B 195 ASN LYS LEU ASP SER LYS VAL SER GLY ASN TYR ASN TYR SEQRES 10 B 195 LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS PRO PHE SEQRES 11 B 195 GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA GLY ASN SEQRES 12 B 195 LYS PRO CYS ASN GLY VAL ALA GLY PHE ASN CYS TYR PHE SEQRES 13 B 195 PRO LEU ARG SER TYR SER PHE ARG PRO THR TYR GLY VAL SEQRES 14 B 195 GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE GLU SEQRES 15 B 195 LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO LYS LYS SEQRES 1 C 214 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 C 214 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3 C 214 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4 C 214 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ASP SEQRES 5 C 214 ASN ASN ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 C 214 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 C 214 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 C 214 SER PHE ASP SER SER LEU SER GLY VAL VAL PHE GLY GLY SEQRES 9 C 214 GLY THR ARG LEU THR VAL LEU ARG GLN PRO LYS ALA ALA SEQRES 10 C 214 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 C 214 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12 C 214 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 C 214 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14 C 214 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 C 214 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER SEQRES 16 C 214 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 C 214 LYS THR VAL ALA PRO THR SEQRES 1 E 229 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 229 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 229 PHE THR PHE ASP ASP TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 E 229 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE THR SEQRES 5 E 229 TRP ASN SER GLY THR ILE GLY TYR ALA ASP SER VAL LYS SEQRES 6 E 229 GLY ARG PHE ILE ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 E 229 LEU HIS LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8 E 229 ALA LEU TYR TYR CYS ALA LYS ASP ASN SER ASP TYR SER SEQRES 9 E 229 GLY TYR TYR TRP GLU LEU GLU ASN TYR GLY MET ASP VAL SEQRES 10 E 229 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 11 E 229 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 E 229 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 E 229 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 E 229 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 E 229 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 E 229 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 E 229 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 E 229 VAL ASP LYS LYS VAL GLU PRO LYS HET NAG A 601 14 HET NAG B 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 7 NAG 2(C8 H15 N O6) FORMUL 9 HOH *323(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 ASP A 364 LEU A 368 5 5 HELIX 3 AA3 LYS A 386 ASP A 389 5 4 HELIX 4 AA4 ASP A 405 ILE A 410 5 6 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 LYS A 444 ASN A 448 5 5 HELIX 8 AA8 GLY A 502 HIS A 505 5 4 HELIX 9 AA9 GLN D 81 GLU D 85 5 5 HELIX 10 AB1 SER D 126 GLN D 131 1 6 HELIX 11 AB2 THR D 186 HIS D 193 1 8 HELIX 12 AB3 THR H 28 TYR H 32 5 5 HELIX 13 AB4 ARG H 87 THR H 91 5 5 HELIX 14 AB5 PRO B 337 ALA B 344 1 8 HELIX 15 AB6 ASP B 364 LEU B 368 5 5 HELIX 16 AB7 SER B 383 ASP B 389 5 7 HELIX 17 AB8 ASP B 405 ILE B 410 5 6 HELIX 18 AB9 GLY B 416 ASN B 422 1 7 HELIX 19 AC1 LYS B 444 ASN B 448 5 5 HELIX 20 AC2 GLY B 502 HIS B 505 5 4 HELIX 21 AC3 GLN C 81 GLU C 85 5 5 HELIX 22 AC4 THR C 186 SER C 192 1 7 HELIX 23 AC5 THR E 28 TYR E 32 5 5 HELIX 24 AC6 ARG E 87 THR E 91 5 5 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O VAL A 512 N ASP A 398 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 TYR A 380 -1 N LYS A 378 O VAL A 433 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 LEU A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O ARG A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 5 SER D 9 GLY D 12 0 SHEET 2 AA5 5 THR D 106 VAL D 110 1 O ARG D 107 N VAL D 10 SHEET 3 AA5 5 ALA D 86 ASP D 94 -1 N ALA D 86 O LEU D 108 SHEET 4 AA5 5 HIS D 36 GLN D 40 -1 N HIS D 36 O GLN D 91 SHEET 5 AA5 5 LYS D 47 ILE D 50 -1 O LEU D 49 N TRP D 37 SHEET 1 AA6 4 SER D 9 GLY D 12 0 SHEET 2 AA6 4 THR D 106 VAL D 110 1 O ARG D 107 N VAL D 10 SHEET 3 AA6 4 ALA D 86 ASP D 94 -1 N ALA D 86 O LEU D 108 SHEET 4 AA6 4 GLY D 99 PHE D 102 -1 O GLY D 99 N ASP D 94 SHEET 1 AA7 3 VAL D 18 THR D 23 0 SHEET 2 AA7 3 SER D 72 ILE D 77 -1 O ILE D 77 N VAL D 18 SHEET 3 AA7 3 PHE D 64 SER D 69 -1 N SER D 69 O SER D 72 SHEET 1 AA8 4 SER D 119 PHE D 123 0 SHEET 2 AA8 4 ALA D 135 PHE D 144 -1 O SER D 142 N SER D 119 SHEET 3 AA8 4 TYR D 177 LEU D 185 -1 O LEU D 185 N ALA D 135 SHEET 4 AA8 4 VAL D 164 THR D 166 -1 N GLU D 165 O TYR D 182 SHEET 1 AA9 4 SER D 119 PHE D 123 0 SHEET 2 AA9 4 ALA D 135 PHE D 144 -1 O SER D 142 N SER D 119 SHEET 3 AA9 4 TYR D 177 LEU D 185 -1 O LEU D 185 N ALA D 135 SHEET 4 AA9 4 SER D 170 LYS D 171 -1 N SER D 170 O ALA D 178 SHEET 1 AB1 3 SER D 158 VAL D 160 0 SHEET 2 AB1 3 VAL D 149 ALA D 155 -1 N ALA D 155 O SER D 158 SHEET 3 AB1 3 TYR D 196 HIS D 202 -1 O GLN D 199 N ALA D 152 SHEET 1 AB2 4 GLN H 3 SER H 7 0 SHEET 2 AB2 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AB2 4 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AB2 4 PHE H 68 ASP H 73 -1 N SER H 71 O HIS H 80 SHEET 1 AB3 6 GLY H 10 VAL H 12 0 SHEET 2 AB3 6 THR H 122 VAL H 126 1 O THR H 125 N VAL H 12 SHEET 3 AB3 6 ALA H 92 ASP H 99 -1 N TYR H 94 O THR H 122 SHEET 4 AB3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB3 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AB3 6 THR H 57 TYR H 60 -1 O ILE H 58 N GLY H 50 SHEET 1 AB4 4 GLY H 10 VAL H 12 0 SHEET 2 AB4 4 THR H 122 VAL H 126 1 O THR H 125 N VAL H 12 SHEET 3 AB4 4 ALA H 92 ASP H 99 -1 N TYR H 94 O THR H 122 SHEET 4 AB4 4 MET H 115 TRP H 118 -1 O VAL H 117 N LYS H 98 SHEET 1 AB5 4 SER H 135 VAL H 136 0 SHEET 2 AB5 4 VAL H 157 TYR H 160 -1 O LYS H 158 N SER H 135 SHEET 3 AB5 4 TYR H 191 LEU H 193 -1 O TYR H 191 N TYR H 160 SHEET 4 AB5 4 VAL H 184 LEU H 185 -1 N VAL H 184 O SER H 192 SHEET 1 AB6 5 ASN B 354 ILE B 358 0 SHEET 2 AB6 5 ASN B 394 ARG B 403 -1 O VAL B 395 N ILE B 358 SHEET 3 AB6 5 PRO B 507 GLU B 516 -1 O TYR B 508 N ILE B 402 SHEET 4 AB6 5 GLY B 431 ASN B 437 -1 N ILE B 434 O VAL B 511 SHEET 5 AB6 5 THR B 376 TYR B 380 -1 N LYS B 378 O VAL B 433 SHEET 1 AB7 3 CYS B 361 VAL B 362 0 SHEET 2 AB7 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361 SHEET 3 AB7 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524 SHEET 1 AB8 2 LEU B 452 ARG B 454 0 SHEET 2 AB8 2 LEU B 492 SER B 494 -1 O ARG B 493 N TYR B 453 SHEET 1 AB9 5 SER C 9 GLY C 12 0 SHEET 2 AB9 5 THR C 106 VAL C 110 1 O THR C 109 N VAL C 10 SHEET 3 AB9 5 ASP C 87 ASP C 94 -1 N TYR C 88 O THR C 106 SHEET 4 AB9 5 HIS C 36 GLN C 40 -1 N GLN C 40 O ASP C 87 SHEET 5 AB9 5 LYS C 47 ILE C 50 -1 O LYS C 47 N GLN C 39 SHEET 1 AC1 4 SER C 9 GLY C 12 0 SHEET 2 AC1 4 THR C 106 VAL C 110 1 O THR C 109 N VAL C 10 SHEET 3 AC1 4 ASP C 87 ASP C 94 -1 N TYR C 88 O THR C 106 SHEET 4 AC1 4 GLY C 99 PHE C 102 -1 O VAL C 101 N SER C 92 SHEET 1 AC2 3 VAL C 18 THR C 23 0 SHEET 2 AC2 3 SER C 72 ILE C 77 -1 O ALA C 73 N CYS C 22 SHEET 3 AC2 3 PHE C 64 SER C 69 -1 N SER C 69 O SER C 72 SHEET 1 AC3 4 SER C 119 PHE C 123 0 SHEET 2 AC3 4 ALA C 135 PHE C 144 -1 O LEU C 140 N THR C 121 SHEET 3 AC3 4 TYR C 177 LEU C 185 -1 O ALA C 179 N ILE C 141 SHEET 4 AC3 4 VAL C 164 THR C 166 -1 N GLU C 165 O TYR C 182 SHEET 1 AC4 4 SER C 119 PHE C 123 0 SHEET 2 AC4 4 ALA C 135 PHE C 144 -1 O LEU C 140 N THR C 121 SHEET 3 AC4 4 TYR C 177 LEU C 185 -1 O ALA C 179 N ILE C 141 SHEET 4 AC4 4 SER C 170 LYS C 171 -1 N SER C 170 O ALA C 178 SHEET 1 AC5 3 THR C 150 LYS C 154 0 SHEET 2 AC5 3 SER C 197 HIS C 202 -1 O GLN C 199 N ALA C 152 SHEET 3 AC5 3 SER C 205 VAL C 207 -1 O SER C 205 N HIS C 202 SHEET 1 AC6 4 GLN E 3 SER E 7 0 SHEET 2 AC6 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AC6 4 SER E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AC6 4 PHE E 68 ASP E 73 -1 N SER E 71 O HIS E 80 SHEET 1 AC7 6 GLY E 10 VAL E 12 0 SHEET 2 AC7 6 THR E 122 VAL E 126 1 O THR E 125 N VAL E 12 SHEET 3 AC7 6 ALA E 92 ASP E 99 -1 N ALA E 92 O VAL E 124 SHEET 4 AC7 6 MET E 34 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AC7 6 LEU E 45 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AC7 6 THR E 57 TYR E 60 -1 O ILE E 58 N GLY E 50 SHEET 1 AC8 4 GLY E 10 VAL E 12 0 SHEET 2 AC8 4 THR E 122 VAL E 126 1 O THR E 125 N VAL E 12 SHEET 3 AC8 4 ALA E 92 ASP E 99 -1 N ALA E 92 O VAL E 124 SHEET 4 AC8 4 MET E 115 TRP E 118 -1 O VAL E 117 N LYS E 98 SHEET 1 AC9 4 SER E 135 LEU E 139 0 SHEET 2 AC9 4 LEU E 153 TYR E 160 -1 O LYS E 158 N SER E 135 SHEET 3 AC9 4 TYR E 191 VAL E 197 -1 O TYR E 191 N TYR E 160 SHEET 4 AC9 4 VAL E 178 THR E 180 -1 N HIS E 179 O VAL E 196 SHEET 1 AD1 4 SER E 135 LEU E 139 0 SHEET 2 AD1 4 LEU E 153 TYR E 160 -1 O LYS E 158 N SER E 135 SHEET 3 AD1 4 TYR E 191 VAL E 197 -1 O TYR E 191 N TYR E 160 SHEET 4 AD1 4 VAL E 184 LEU E 185 -1 N VAL E 184 O SER E 192 SHEET 1 AD2 3 THR E 166 VAL E 167 0 SHEET 2 AD2 3 VAL E 213 HIS E 215 -1 O ASN E 214 N THR E 166 SHEET 3 AD2 3 THR E 220 VAL E 222 -1 O THR E 220 N HIS E 215 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 391 CYS A 525 1555 1555 2.03 SSBOND 4 CYS A 480 CYS A 488 1555 1555 1.98 SSBOND 5 CYS D 22 CYS D 90 1555 1555 2.04 SSBOND 6 CYS D 139 CYS D 198 1555 1555 2.04 SSBOND 7 CYS H 22 CYS H 96 1555 1555 2.05 SSBOND 8 CYS B 336 CYS B 361 1555 1555 2.03 SSBOND 9 CYS B 379 CYS B 432 1555 1555 2.03 SSBOND 10 CYS B 391 CYS B 525 1555 1555 2.02 SSBOND 11 CYS B 480 CYS B 488 1555 1555 2.03 SSBOND 12 CYS C 22 CYS C 90 1555 1555 2.04 SSBOND 13 CYS C 139 CYS C 198 1555 1555 2.04 SSBOND 14 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 15 CYS E 155 CYS E 211 1555 1555 2.00 LINK ND2 ASN A 343 C1 NAG A 601 1555 1555 1.79 CISPEP 1 TYR D 145 PRO D 146 0 -0.48 CISPEP 2 PHE H 161 PRO H 162 0 -5.58 CISPEP 3 GLU H 163 PRO H 164 0 10.33 CISPEP 4 TYR C 145 PRO C 146 0 0.36 CISPEP 5 PHE E 161 PRO E 162 0 -2.08 CISPEP 6 GLU E 163 PRO E 164 0 4.77 CRYST1 44.664 103.529 299.352 90.00 90.00 90.00 P 21 21 21 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 0.022389 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009659 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003341 0.00000