HEADER VIRAL PROTEIN/IMMUNE SYSTEM 03-SEP-24 9JEB TITLE CRYSTAL STRUCTURE OF SARS-COV-2 RBD IN COMPLEX WITH A NEUTRALIZING TITLE 2 ANTIBODY SCFV N1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: N1 SCFV; COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SPIKE PROTEIN S1; COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7110; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 8 2; SOURCE 9 ORGANISM_COMMON: 2019-NCOV,SARS-COV-2; SOURCE 10 ORGANISM_TAXID: 2697049; SOURCE 11 GENE: S, 2; SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7110 KEYWDS SARS-COV-2, RBD, ANTIBODY, SCFV, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR K.GUO,N.ZHANG,Y.GUO REVDAT 1 03-SEP-25 9JEB 0 JRNL AUTH N.ZHANG,K.GUO,Y.GUO JRNL TITL MINING ANTIBODY FUNCTIONALITY VIA AI-GUIDED STRUCTURAL JRNL TITL 2 LANDSCAPE PROFILING JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.18.2_3874: ???) 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.98 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 3 NUMBER OF REFLECTIONS : 50406 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.178 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.020 REMARK 3 FREE R VALUE TEST SET COUNT : 2024 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 32.9800 - 5.5400 0.79 3136 132 0.2070 0.2394 REMARK 3 2 5.5300 - 4.4000 0.74 2864 127 0.1545 0.1669 REMARK 3 3 4.4000 - 3.8400 0.77 2968 118 0.1564 0.1513 REMARK 3 4 3.8400 - 3.4900 0.80 3066 133 0.1735 0.2058 REMARK 3 5 3.4900 - 3.2400 0.85 3229 138 0.1716 0.1912 REMARK 3 6 3.2400 - 3.0500 0.91 3455 144 0.1825 0.2237 REMARK 3 7 3.0500 - 2.9000 0.94 3566 153 0.1869 0.2319 REMARK 3 8 2.9000 - 2.7700 0.96 3653 150 0.1755 0.2165 REMARK 3 9 2.7700 - 2.6700 0.97 3702 152 0.1832 0.2071 REMARK 3 10 2.6700 - 2.5700 0.98 3697 153 0.1851 0.2275 REMARK 3 11 2.5700 - 2.4900 0.99 3736 158 0.1911 0.2412 REMARK 3 12 2.4900 - 2.4200 0.99 3762 155 0.1857 0.2378 REMARK 3 13 2.4200 - 2.3600 1.00 3784 156 0.1881 0.2330 REMARK 3 14 2.3600 - 2.3000 1.00 3764 155 0.1945 0.2320 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) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.260 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 : 0.009 6891 REMARK 3 ANGLE : 1.274 9360 REMARK 3 CHIRALITY : 0.114 999 REMARK 3 PLANARITY : 0.009 1207 REMARK 3 DIHEDRAL : 19.800 2443 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 9JEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300051141. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-MAY-21 REMARK 200 TEMPERATURE (KELVIN) : 80 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 : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50406 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 32.980 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 200 DATA REDUNDANCY : 9.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 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: SAD 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 (%): 62.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM SULFATE HEPTAHYDRATE, REMARK 280 20% W/V POLYETHYLENE GLYCOL 3350, PH 6.0, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z REMARK 290 5555 Y,-X+Y,Z+2/3 REMARK 290 6555 X-Y,X,Z+1/3 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 40.09200 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 20.04600 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 0.00000 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 40.09200 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 20.04600 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 506 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 515 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 544 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 459 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 484 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 501 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 GLY A 127 REMARK 465 GLY A 128 REMARK 465 SER A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 GLY A 138 REMARK 465 SER A 139 REMARK 465 LYS B 529 REMARK 465 GLY C 125 REMARK 465 GLY C 126 REMARK 465 GLY C 127 REMARK 465 GLY C 128 REMARK 465 SER C 129 REMARK 465 GLY C 130 REMARK 465 GLY C 131 REMARK 465 GLY C 132 REMARK 465 GLY C 133 REMARK 465 SER C 134 REMARK 465 GLY C 135 REMARK 465 GLY C 136 REMARK 465 GLY C 137 REMARK 465 GLY C 138 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 315 O HOH A 513 1.92 REMARK 500 O HOH C 380 O HOH C 427 1.99 REMARK 500 O HOH A 469 O HOH A 493 2.02 REMARK 500 O HOH A 457 O HOH A 490 2.02 REMARK 500 OG1 THR D 393 O HOH D 701 2.02 REMARK 500 O HOH B 609 O HOH B 637 2.04 REMARK 500 O HOH D 815 O HOH D 823 2.05 REMARK 500 O HOH C 349 O HOH C 407 2.05 REMARK 500 O HOH B 604 O HOH B 645 2.06 REMARK 500 O HOH B 605 O HOH B 732 2.06 REMARK 500 O HOH C 455 O HOH C 480 2.06 REMARK 500 O HOH B 724 O HOH B 754 2.08 REMARK 500 O HOH D 812 O HOH D 820 2.09 REMARK 500 O HOH C 422 O HOH C 488 2.10 REMARK 500 O HOH A 538 O HOH B 620 2.10 REMARK 500 O HOH B 688 O HOH B 751 2.11 REMARK 500 OG SER A 71 O HOH A 301 2.12 REMARK 500 O HOH D 722 O HOH D 869 2.12 REMARK 500 O HOH A 489 O HOH A 492 2.13 REMARK 500 ND2 ASN D 370 O HOH D 702 2.13 REMARK 500 O HOH D 841 O HOH D 865 2.14 REMARK 500 O HOH C 386 O HOH C 475 2.15 REMARK 500 O HOH A 499 O HOH A 531 2.15 REMARK 500 OE2 GLU A 220 O HOH A 302 2.15 REMARK 500 O HOH C 347 O HOH C 450 2.16 REMARK 500 O HOH A 523 O HOH A 536 2.16 REMARK 500 O HOH C 474 O HOH C 487 2.17 REMARK 500 O HOH B 665 O HOH B 742 2.19 REMARK 500 NH2 ARG D 408 O HOH D 703 2.19 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 746 O HOH D 880 4456 1.81 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 GLU A 99 CD GLU A 99 OE1 -0.069 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 ARG A 16 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES REMARK 500 ARG A 16 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES REMARK 500 PHE B 347 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 PHE B 377 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG C 87 CG - CD - NE ANGL. DEV. = 12.6 DEGREES REMARK 500 LEU C 172 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES REMARK 500 LEU C 217 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES REMARK 500 PHE D 347 CB - CG - CD2 ANGL. DEV. = -5.2 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 92 163.29 177.85 REMARK 500 SER A 169 -120.20 53.81 REMARK 500 ALA A 190 -39.60 74.65 REMARK 500 ALA B 352 44.73 -109.66 REMARK 500 ASN B 422 -53.35 -124.81 REMARK 500 LEU B 517 62.83 -111.62 REMARK 500 ALA C 92 168.58 179.48 REMARK 500 SER C 169 -120.71 49.24 REMARK 500 ALA C 190 -35.55 72.32 REMARK 500 ASN D 422 -54.99 -125.17 REMARK 500 PHE D 464 18.93 59.14 REMARK 500 LEU D 517 69.00 -107.72 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 A 16 0.10 SIDE CHAIN REMARK 500 PHE B 377 0.07 SIDE CHAIN REMARK 500 PHE D 347 0.06 SIDE CHAIN 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 C 510 DISTANCE = 6.73 ANGSTROMS DBREF 9JEB A 1 247 PDB 9JEB 9JEB 1 247 DBREF 9JEB B 333 529 UNP P0DTC2 SPIKE_SARS2 333 529 DBREF 9JEB C 1 247 PDB 9JEB 9JEB 1 247 DBREF 9JEB D 333 529 UNP P0DTC2 SPIKE_SARS2 333 529 SEQRES 1 A 247 GLU VAL HIS LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 A 247 PRO GLY ARG SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 A 247 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 A 247 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 A 247 HIS ASP GLY SER SER LYS PHE TYR ALA ASP SER VAL LYS SEQRES 6 A 247 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 247 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 247 ALA VAL TYR TYR CYS ALA LYS GLU PHE TYR ASP SER GLY SEQRES 9 A 247 ASN TYR ARG PRO GLU LEU PHE ASP TYR TRP GLY GLN GLY SEQRES 10 A 247 THR THR ILE THR VAL SER SER GLY GLY GLY GLY SER GLY SEQRES 11 A 247 GLY GLY GLY SER GLY GLY GLY GLY SER GLU ILE VAL LEU SEQRES 12 A 247 THR GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP SEQRES 13 A 247 ARG VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SEQRES 14 A 247 SER TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA SEQRES 15 A 247 PRO LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER SEQRES 16 A 247 GLY VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR SEQRES 17 A 247 ASP PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP SEQRES 18 A 247 PHE ALA THR TYR TYR CYS GLN GLN SER TYR SER THR PRO SEQRES 19 A 247 PRO TRP THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 B 197 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 B 197 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 B 197 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 B 197 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 B 197 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 B 197 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 7 B 197 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 8 B 197 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 B 197 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 B 197 ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 B 197 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 B 197 GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 13 B 197 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 14 B 197 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 B 197 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 B 197 LYS LYS SEQRES 1 C 247 GLU VAL HIS LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 247 PRO GLY ARG SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 C 247 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 247 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5 C 247 HIS ASP GLY SER SER LYS PHE TYR ALA ASP SER VAL LYS SEQRES 6 C 247 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 C 247 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 C 247 ALA VAL TYR TYR CYS ALA LYS GLU PHE TYR ASP SER GLY SEQRES 9 C 247 ASN TYR ARG PRO GLU LEU PHE ASP TYR TRP GLY GLN GLY SEQRES 10 C 247 THR THR ILE THR VAL SER SER GLY GLY GLY GLY SER GLY SEQRES 11 C 247 GLY GLY GLY SER GLY GLY GLY GLY SER GLU ILE VAL LEU SEQRES 12 C 247 THR GLN SER PRO SER SER LEU SER ALA SER VAL GLY ASP SEQRES 13 C 247 ARG VAL THR ILE THR CYS ARG ALA SER GLN SER ILE SER SEQRES 14 C 247 SER TYR LEU ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA SEQRES 15 C 247 PRO LYS LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER SEQRES 16 C 247 GLY VAL PRO SER ARG PHE SER GLY SER GLY SER GLY THR SEQRES 17 C 247 ASP PHE THR LEU THR ILE SER SER LEU GLN PRO GLU ASP SEQRES 18 C 247 PHE ALA THR TYR TYR CYS GLN GLN SER TYR SER THR PRO SEQRES 19 C 247 PRO TRP THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 D 197 THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR SEQRES 2 D 197 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE SEQRES 3 D 197 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER SEQRES 4 D 197 ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO SEQRES 5 D 197 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 6 D 197 ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE SEQRES 7 D 197 ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR SEQRES 8 D 197 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 9 D 197 ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR SEQRES 10 D 197 ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS SEQRES 11 D 197 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 12 D 197 GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS SEQRES 13 D 197 TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN SEQRES 14 D 197 GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER SEQRES 15 D 197 PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO SEQRES 16 D 197 LYS LYS HET NAG D 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 C8 H15 N O6 FORMUL 6 HOH *819(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASP A 62 LYS A 65 5 4 HELIX 3 AA3 ASN A 74 LYS A 76 5 3 HELIX 4 AA4 ARG A 87 THR A 91 5 5 HELIX 5 AA5 GLN A 218 PHE A 222 5 5 HELIX 6 AA6 PRO B 337 ASN B 343 1 7 HELIX 7 AA7 SER B 349 TRP B 353 5 5 HELIX 8 AA8 TYR B 365 SER B 371 1 7 HELIX 9 AA9 LYS B 386 ASP B 389 5 4 HELIX 10 AB1 ASP B 405 ILE B 410 5 6 HELIX 11 AB2 GLY B 416 ASN B 422 1 7 HELIX 12 AB3 SER B 438 SER B 443 1 6 HELIX 13 AB4 GLY B 502 TYR B 505 5 4 HELIX 14 AB5 THR C 28 TYR C 32 5 5 HELIX 15 AB6 ASP C 62 LYS C 65 5 4 HELIX 16 AB7 ARG C 87 THR C 91 5 5 HELIX 17 AB8 GLN C 218 PHE C 222 5 5 HELIX 18 AB9 PRO D 337 ASN D 343 1 7 HELIX 19 AC1 SER D 349 TRP D 353 5 5 HELIX 20 AC2 TYR D 365 ASN D 370 1 6 HELIX 21 AC3 LYS D 386 ASP D 389 5 4 HELIX 22 AC4 ASP D 405 ILE D 410 5 6 HELIX 23 AC5 GLY D 416 ASN D 422 1 7 HELIX 24 AC6 SER D 438 SER D 443 1 6 HELIX 25 AC7 GLY D 502 TYR D 505 5 4 SHEET 1 AA1 4 HIS A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N HIS A 3 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 118 VAL A 122 1 O THR A 121 N VAL A 12 SHEET 3 AA2 6 ALA A 92 GLU A 99 -1 N TYR A 94 O THR A 118 SHEET 4 AA2 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 LYS A 58 TYR A 60 -1 O PHE A 59 N VAL A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 118 VAL A 122 1 O THR A 121 N VAL A 12 SHEET 3 AA3 4 ALA A 92 GLU A 99 -1 N TYR A 94 O THR A 118 SHEET 4 AA3 4 PHE A 111 TRP A 114 -1 O TYR A 113 N LYS A 98 SHEET 1 AA4 4 LEU A 143 SER A 146 0 SHEET 2 AA4 4 VAL A 158 ALA A 164 -1 O THR A 161 N SER A 146 SHEET 3 AA4 4 ASP A 209 ILE A 214 -1 O LEU A 212 N ILE A 160 SHEET 4 AA4 4 PHE A 201 SER A 206 -1 N SER A 202 O THR A 213 SHEET 1 AA5 6 SER A 149 ALA A 152 0 SHEET 2 AA5 6 THR A 242 ILE A 246 1 O GLU A 245 N LEU A 150 SHEET 3 AA5 6 ALA A 223 GLN A 229 -1 N ALA A 223 O VAL A 244 SHEET 4 AA5 6 LEU A 172 GLN A 177 -1 N ASN A 173 O GLN A 228 SHEET 5 AA5 6 LYS A 184 TYR A 188 -1 O LYS A 184 N GLN A 176 SHEET 6 AA5 6 SER A 192 LEU A 193 -1 O SER A 192 N TYR A 188 SHEET 1 AA6 4 SER A 149 ALA A 152 0 SHEET 2 AA6 4 THR A 242 ILE A 246 1 O GLU A 245 N LEU A 150 SHEET 3 AA6 4 ALA A 223 GLN A 229 -1 N ALA A 223 O VAL A 244 SHEET 4 AA6 4 THR A 237 PHE A 238 -1 O THR A 237 N GLN A 229 SHEET 1 AA7 6 SER A 232 THR A 233 0 SHEET 2 AA7 6 THR B 376 TYR B 380 -1 O CYS B 379 N THR A 233 SHEET 3 AA7 6 GLY B 431 ASN B 437 -1 O GLY B 431 N TYR B 380 SHEET 4 AA7 6 PRO B 507 PHE B 515 -1 O LEU B 513 N CYS B 432 SHEET 5 AA7 6 VAL B 395 ARG B 403 -1 N ILE B 402 O TYR B 508 SHEET 6 AA7 6 ASN B 354 ILE B 358 -1 N ILE B 358 O VAL B 395 SHEET 1 AA8 3 CYS B 361 VAL B 362 0 SHEET 2 AA8 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361 SHEET 3 AA8 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524 SHEET 1 AA9 2 LEU B 452 ARG B 454 0 SHEET 2 AA9 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453 SHEET 1 AB1 2 TYR B 473 GLN B 474 0 SHEET 2 AB1 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473 SHEET 1 AB2 4 HIS C 3 SER C 7 0 SHEET 2 AB2 4 LEU C 18 SER C 25 -1 O SER C 25 N HIS C 3 SHEET 3 AB2 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AB2 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AB3 6 GLY C 10 VAL C 12 0 SHEET 2 AB3 6 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AB3 6 ALA C 92 GLU C 99 -1 N TYR C 94 O THR C 118 SHEET 4 AB3 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AB3 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB3 6 LYS C 58 TYR C 60 -1 O PHE C 59 N VAL C 50 SHEET 1 AB4 4 GLY C 10 VAL C 12 0 SHEET 2 AB4 4 THR C 118 VAL C 122 1 O THR C 121 N VAL C 12 SHEET 3 AB4 4 ALA C 92 GLU C 99 -1 N TYR C 94 O THR C 118 SHEET 4 AB4 4 PHE C 111 TRP C 114 -1 O TYR C 113 N LYS C 98 SHEET 1 AB5 4 LEU C 143 SER C 146 0 SHEET 2 AB5 4 VAL C 158 ALA C 164 -1 O THR C 161 N SER C 146 SHEET 3 AB5 4 ASP C 209 ILE C 214 -1 O LEU C 212 N ILE C 160 SHEET 4 AB5 4 PHE C 201 SER C 206 -1 N SER C 202 O THR C 213 SHEET 1 AB6 6 SER C 149 ALA C 152 0 SHEET 2 AB6 6 THR C 242 ILE C 246 1 O GLU C 245 N LEU C 150 SHEET 3 AB6 6 ALA C 223 GLN C 229 -1 N ALA C 223 O VAL C 244 SHEET 4 AB6 6 LEU C 172 GLN C 177 -1 N ASN C 173 O GLN C 228 SHEET 5 AB6 6 LYS C 184 TYR C 188 -1 O LEU C 186 N TRP C 174 SHEET 6 AB6 6 SER C 192 LEU C 193 -1 O SER C 192 N TYR C 188 SHEET 1 AB7 4 SER C 149 ALA C 152 0 SHEET 2 AB7 4 THR C 242 ILE C 246 1 O GLU C 245 N LEU C 150 SHEET 3 AB7 4 ALA C 223 GLN C 229 -1 N ALA C 223 O VAL C 244 SHEET 4 AB7 4 THR C 237 PHE C 238 -1 O THR C 237 N GLN C 229 SHEET 1 AB8 6 SER C 232 THR C 233 0 SHEET 2 AB8 6 THR D 376 TYR D 380 -1 O CYS D 379 N THR C 233 SHEET 3 AB8 6 GLY D 431 ASN D 437 -1 O VAL D 433 N LYS D 378 SHEET 4 AB8 6 PRO D 507 SER D 514 -1 O LEU D 513 N CYS D 432 SHEET 5 AB8 6 VAL D 395 ARG D 403 -1 N ASP D 398 O VAL D 512 SHEET 6 AB8 6 ASN D 354 ILE D 358 -1 N ILE D 358 O VAL D 395 SHEET 1 AB9 3 CYS D 361 VAL D 362 0 SHEET 2 AB9 3 VAL D 524 CYS D 525 1 O CYS D 525 N CYS D 361 SHEET 3 AB9 3 CYS D 391 PHE D 392 -1 N PHE D 392 O VAL D 524 SHEET 1 AC1 2 LEU D 452 ARG D 454 0 SHEET 2 AC1 2 LEU D 492 SER D 494 -1 O GLN D 493 N TYR D 453 SHEET 1 AC2 2 TYR D 473 GLN D 474 0 SHEET 2 AC2 2 CYS D 488 TYR D 489 -1 O TYR D 489 N TYR D 473 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 162 CYS A 227 1555 1555 2.11 SSBOND 3 CYS B 336 CYS B 361 1555 1555 2.06 SSBOND 4 CYS B 379 CYS B 432 1555 1555 2.04 SSBOND 5 CYS B 391 CYS B 525 1555 1555 2.08 SSBOND 6 CYS B 480 CYS B 488 1555 1555 2.08 SSBOND 7 CYS C 22 CYS C 96 1555 1555 2.06 SSBOND 8 CYS C 162 CYS C 227 1555 1555 2.12 SSBOND 9 CYS D 336 CYS D 361 1555 1555 2.04 SSBOND 10 CYS D 379 CYS D 432 1555 1555 2.04 SSBOND 11 CYS D 391 CYS D 525 1555 1555 2.07 SSBOND 12 CYS D 480 CYS D 488 1555 1555 2.05 LINK ND2 ASN D 343 C1 NAG D 601 1555 1555 1.46 CISPEP 1 SER A 146 PRO A 147 0 -9.10 CISPEP 2 THR A 233 PRO A 234 0 -8.46 CISPEP 3 PRO A 234 PRO A 235 0 -4.66 CISPEP 4 SER C 146 PRO C 147 0 -4.82 CISPEP 5 THR C 233 PRO C 234 0 -10.44 CISPEP 6 PRO C 234 PRO C 235 0 -2.53 CRYST1 190.399 190.399 60.138 90.00 90.00 120.00 P 62 12 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 0.005252 0.003032 0.000000 0.00000 SCALE2 0.000000 0.006065 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016628 0.00000