HEADER VIRAL PROTEIN 01-JUL-20 6ZLR TITLE SOAKING COMPETENT CRYSTAL FORM OF THE SARS-COV-2 RECEPTOR BINDING TITLE 2 DOMAIN (RBD):CR3022 COMPLEX. COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: EEE, AAA, DDD; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CR3022 FAB HEAVY CHAIN; COMPND 8 CHAIN: HHH, BBB, FFF; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: CR3022 FAB LIGHT CHAIN; COMPND 12 CHAIN: LLL, CCC, GGG; 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; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 8 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, VIRAL PROTEIN COMPLEX, ANTIBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.F.DE NICOLA,C.E.NICHOLS JRNL AUTH C.NICHOLS,J.NG,A.KESHU,F.FRATERNALI,G.F.DE NICOLA JRNL TITL A NEW CRYSTAL FORM OF THE SARS-COV-2 RECEPTOR BINDING JRNL TITL 2 DOMAIN: CR3022 COMPLEX-AN IDEAL TARGET FOR IN-CRYSTAL JRNL TITL 3 FRAGMENT SCREENING OF THE ACE2 BINDING SITE SURFACE. JRNL REF FRONT PHARMACOL V. 11 15211 2020 JRNL REFN ESSN 1663-9812 JRNL PMID 33381049 JRNL DOI 10.3389/FPHAR.2020.615211 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0253 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 3 NUMBER OF REFLECTIONS : 71615 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.123 REMARK 3 FREE R VALUE TEST SET COUNT : 3669 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5035 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.05 REMARK 3 BIN R VALUE (WORKING SET) : 0.3500 REMARK 3 BIN FREE R VALUE SET COUNT : 291 REMARK 3 BIN FREE R VALUE : 0.3570 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 14694 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 42 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.64 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.06300 REMARK 3 B22 (A**2) : 0.06300 REMARK 3 B33 (A**2) : -0.12500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.908 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.375 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.303 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.006 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15134 ; 0.008 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 13355 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20619 ; 1.548 ; 1.650 REMARK 3 BOND ANGLES OTHERS (DEGREES): 31205 ; 1.227 ; 1.573 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1902 ; 7.622 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 672 ;35.099 ;23.393 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2364 ;16.873 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;16.110 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1986 ; 0.057 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16981 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 3130 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2181 ; 0.183 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 50 ; 0.192 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7262 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 217 ; 0.185 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7635 ; 4.992 ; 5.871 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7634 ; 4.992 ; 5.870 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9528 ; 8.047 ; 8.792 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9529 ; 8.047 ; 8.793 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7499 ; 5.153 ; 6.224 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7497 ; 5.149 ; 6.223 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11091 ; 8.243 ; 9.157 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11091 ; 8.243 ; 9.157 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 9 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains E A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains E D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : Chains H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : Chains H F REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : Chains L C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : Chains L G REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : Chains A D REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : Chains B F REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : Chains C G REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6ZLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292109738. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-MAY-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72060 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.090 REMARK 200 RESOLUTION RANGE LOW (A) : 68.028 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 6W41 REMARK 200 REMARK 200 REMARK: THIN ROD REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 76.02 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM MALONATE, 0.1 M TRIS PH REMARK 280 7.7, 22% W/V POLYETHYLENE GLYCOL 1,000, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.93300 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 103.56500 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 103.56500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.96650 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 103.56500 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 103.56500 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 149.89950 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 103.56500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 103.56500 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.96650 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 103.56500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 103.56500 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 149.89950 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 99.93300 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: 5840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28560 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: EEE, HHH, LLL 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: 5860 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, CCC 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: 3 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: 5800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28640 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: DDD, FFF, GGG 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 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 LYS E 529 REMARK 465 SER E 530 REMARK 465 THR E 531 REMARK 465 ASN E 532 REMARK 465 LEU E 533 REMARK 465 VAL E 534 REMARK 465 LYS E 535 REMARK 465 ASN E 536 REMARK 465 LYS E 537 REMARK 465 CYS E 538 REMARK 465 VAL E 539 REMARK 465 ASN E 540 REMARK 465 PHE E 541 REMARK 465 SER E 542 REMARK 465 GLY E 543 REMARK 465 HIS E 544 REMARK 465 HIS E 545 REMARK 465 HIS E 546 REMARK 465 HIS E 547 REMARK 465 HIS E 548 REMARK 465 HIS E 549 REMARK 465 CYS L 220 REMARK 465 SER L 221 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 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LEU A 533 REMARK 465 VAL A 534 REMARK 465 LYS A 535 REMARK 465 ASN A 536 REMARK 465 LYS A 537 REMARK 465 CYS A 538 REMARK 465 VAL A 539 REMARK 465 ASN A 540 REMARK 465 PHE A 541 REMARK 465 SER A 542 REMARK 465 GLY A 543 REMARK 465 HIS A 544 REMARK 465 HIS A 545 REMARK 465 HIS A 546 REMARK 465 HIS A 547 REMARK 465 HIS A 548 REMARK 465 HIS A 549 REMARK 465 CYS C 220 REMARK 465 SER C 221 REMARK 465 ARG D 319 REMARK 465 VAL D 320 REMARK 465 GLN D 321 REMARK 465 PRO D 322 REMARK 465 THR D 323 REMARK 465 GLU D 324 REMARK 465 SER D 325 REMARK 465 ILE D 326 REMARK 465 VAL D 327 REMARK 465 ARG D 328 REMARK 465 PHE D 329 REMARK 465 PRO D 330 REMARK 465 ASN D 331 REMARK 465 ILE D 332 REMARK 465 LYS D 529 REMARK 465 SER D 530 REMARK 465 THR D 531 REMARK 465 ASN D 532 REMARK 465 LEU D 533 REMARK 465 VAL D 534 REMARK 465 LYS D 535 REMARK 465 ASN D 536 REMARK 465 LYS D 537 REMARK 465 CYS D 538 REMARK 465 VAL D 539 REMARK 465 ASN D 540 REMARK 465 PHE D 541 REMARK 465 SER D 542 REMARK 465 GLY D 543 REMARK 465 HIS D 544 REMARK 465 HIS D 545 REMARK 465 HIS D 546 REMARK 465 HIS D 547 REMARK 465 HIS D 548 REMARK 465 HIS D 549 REMARK 465 CYS G 220 REMARK 465 SER G 221 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 LYS E 528 CG CD CE NZ REMARK 470 LYS A 528 CG CD CE NZ REMARK 470 LYS D 528 CG CD CE NZ 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 ND2 ASNAA 343 C1 NAGAA 601 1.93 REMARK 500 ND2 ASNDD 343 O5 NAGDD 601 2.11 REMARK 500 ND2 ASNAA 343 O5 NAGAA 601 2.17 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 ARGGG 148 NE - CZ - NH1 ANGL. DEV. = 3.4 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 ASNEE 334 47.46 -103.57 REMARK 500 ALAEE 352 48.52 -103.74 REMARK 500 PHEEE 377 59.65 -159.52 REMARK 500 ASNEE 422 -57.45 -134.90 REMARK 500 ASPEE 428 31.82 -99.38 REMARK 500 ASNEE 481 60.19 -103.83 REMARK 500 SERHH 103 52.47 74.91 REMARK 500 ASPHH 150 67.95 68.19 REMARK 500 ASNLL 35 79.82 -69.81 REMARK 500 ALALL 57 -24.87 64.76 REMARK 500 SERLL 58 0.35 -155.62 REMARK 500 SERLL 83 74.84 54.90 REMARK 500 ASNLL 144 76.24 50.72 REMARK 500 ASNAA 334 49.80 -106.28 REMARK 500 ALAAA 352 49.03 -104.68 REMARK 500 PHEAA 377 62.22 -159.64 REMARK 500 ASNAA 422 -57.76 -134.97 REMARK 500 ASNAA 481 54.67 -103.33 REMARK 500 SERBB 103 52.57 73.44 REMARK 500 ASPBB 150 66.29 69.27 REMARK 500 ALACC 57 -24.07 63.35 REMARK 500 SERCC 58 0.66 -155.62 REMARK 500 SERCC 83 74.62 53.96 REMARK 500 VALCC 89 107.29 -58.90 REMARK 500 ASNCC 144 76.56 49.54 REMARK 500 ASNDD 334 49.58 -101.13 REMARK 500 ALADD 352 49.68 -103.64 REMARK 500 PHEDD 377 61.24 -159.29 REMARK 500 ASNDD 422 -57.01 -134.64 REMARK 500 ASPDD 428 30.54 -99.01 REMARK 500 ASNDD 481 56.35 -103.14 REMARK 500 CYSFF 22 104.53 -161.25 REMARK 500 ALAFF 92 -169.12 -162.74 REMARK 500 SERFF 103 53.54 72.98 REMARK 500 ASPFF 150 68.67 69.09 REMARK 500 ASNGG 35 80.98 -69.14 REMARK 500 ALAGG 57 -24.81 64.26 REMARK 500 SERGG 58 -0.36 -154.98 REMARK 500 SERGG 83 73.65 54.76 REMARK 500 VALGG 89 109.19 -56.19 REMARK 500 ASNGG 144 76.52 49.51 REMARK 500 LYSGG 196 -59.19 -120.73 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 DBREF 6ZLREE 319 541 UNP P0DTC2 SPIKE_SARS2 319 541 DBREF 6ZLRHH 1 222 PDB 6ZLR 6ZLR 1 222 DBREF 6ZLRLL 1 221 PDB 6ZLR 6ZLR 1 221 DBREF 6ZLRAA 319 541 UNP P0DTC2 SPIKE_SARS2 319 541 DBREF 6ZLRBB 1 222 PDB 6ZLR 6ZLR 1 222 DBREF 6ZLRCC 1 221 PDB 6ZLR 6ZLR 1 221 DBREF 6ZLRDD 319 541 UNP P0DTC2 SPIKE_SARS2 319 541 DBREF 6ZLRFF 1 222 PDB 6ZLR 6ZLR 1 222 DBREF 6ZLRGG 1 221 PDB 6ZLR 6ZLR 1 221 SEQADV 6ZLR SEREE 542 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR GLYEE 543 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 544 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 545 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 546 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 547 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 548 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISEE 549 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR SERAA 542 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR GLYAA 543 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 544 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 545 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 546 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 547 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 548 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISAA 549 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR SERDD 542 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR GLYDD 543 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 544 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 545 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 546 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 547 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 548 UNP P0DTC2 EXPRESSION TAG SEQADV 6ZLR HISDD 549 UNP P0DTC2 EXPRESSION TAG SEQRES 1EE 231 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2EE 231 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3EE 231 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4EE 231 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5EE 231 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6EE 231 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7EE 231 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8EE 231 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9EE 231 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10EE 231 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11EE 231 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12EE 231 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13EE 231 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14EE 231 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15EE 231 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16EE 231 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17EE 231 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL SEQRES 18EE 231 ASN PHE SER GLY HIS HIS HIS HIS HIS HIS SEQRES 1HH 222 GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS LYS SEQRES 2HH 222 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3HH 222 TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4HH 222 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5HH 222 PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE GLN SEQRES 6HH 222 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN THR SEQRES 7HH 222 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8HH 222 ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER THR SEQRES 9HH 222 PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10HH 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11HH 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12HH 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13HH 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14HH 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15HH 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16HH 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17HH 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18HH 222 CYS SEQRES 1LL 221 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2LL 221 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3LL 221 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4LL 221 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5LL 221 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6LL 221 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7LL 221 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8LL 221 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9LL 221 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10LL 221 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11LL 221 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12LL 221 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13LL 221 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14LL 221 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15LL 221 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16LL 221 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17LL 221 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SER SEQRES 1AA 231 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2AA 231 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3AA 231 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4AA 231 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5AA 231 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6AA 231 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7AA 231 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8AA 231 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9AA 231 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10AA 231 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11AA 231 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12AA 231 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13AA 231 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14AA 231 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15AA 231 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16AA 231 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17AA 231 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL SEQRES 18AA 231 ASN PHE SER GLY HIS HIS HIS HIS HIS HIS SEQRES 1BB 222 GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS LYS SEQRES 2BB 222 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3BB 222 TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4BB 222 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5BB 222 PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE GLN SEQRES 6BB 222 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN THR SEQRES 7BB 222 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8BB 222 ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER THR SEQRES 9BB 222 PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10BB 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11BB 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12BB 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13BB 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14BB 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15BB 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16BB 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17BB 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18BB 222 CYS SEQRES 1CC 221 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2CC 221 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3CC 221 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4CC 221 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5CC 221 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6CC 221 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7CC 221 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8CC 221 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9CC 221 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10CC 221 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11CC 221 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12CC 221 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13CC 221 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14CC 221 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15CC 221 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16CC 221 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17CC 221 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SER SEQRES 1DD 231 ARG VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN SEQRES 2DD 231 ILE THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA SEQRES 3DD 231 THR ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG SEQRES 4DD 231 ILE SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SEQRES 5DD 231 SER ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER SEQRES 6DD 231 PRO THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR SEQRES 7DD 231 ALA ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN SEQRES 8DD 231 ILE ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN SEQRES 9DD 231 TYR LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA SEQRES 10DD 231 TRP ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN SEQRES 11DD 231 TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU SEQRES 12DD 231 LYS PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN SEQRES 13DD 231 ALA GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN SEQRES 14DD 231 CYS TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR SEQRES 15DD 231 ASN GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SEQRES 16DD 231 SER PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY SEQRES 17DD 231 PRO LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL SEQRES 18DD 231 ASN PHE SER GLY HIS HIS HIS HIS HIS HIS SEQRES 1FF 222 GLN MET GLN LEU VAL GLN SER GLY THR GLU VAL LYS LYS SEQRES 2FF 222 PRO GLY GLU SER LEU LYS ILE SER CYS LYS GLY SER GLY SEQRES 3FF 222 TYR GLY PHE ILE THR TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4FF 222 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5FF 222 PRO GLY ASP SER GLU THR ARG TYR SER PRO SER PHE GLN SEQRES 6FF 222 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE ASN THR SEQRES 7FF 222 ALA TYR LEU GLN TRP SER SER LEU LYS ALA SER ASP THR SEQRES 8FF 222 ALA ILE TYR TYR CYS ALA GLY GLY SER GLY ILE SER THR SEQRES 9FF 222 PRO MET ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10FF 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11FF 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12FF 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13FF 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14FF 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15FF 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16FF 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17FF 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18FF 222 CYS SEQRES 1GG 221 ASP ILE GLN LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2GG 221 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3GG 221 GLN SER VAL LEU TYR SER SER ILE ASN LYS ASN TYR LEU SEQRES 4GG 221 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5GG 221 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6GG 221 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7GG 221 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8GG 221 TYR TYR CYS GLN GLN TYR TYR SER THR PRO TYR THR PHE SEQRES 9GG 221 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10GG 221 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11GG 221 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12GG 221 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13GG 221 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14GG 221 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15GG 221 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16GG 221 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17GG 221 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SER HET NAG EE 601 14 HET NAG AA 601 14 HET NAG DD 601 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE FORMUL 10 NAG 3(C8 H15 N O6) HELIX 1 AA1 PHEEE 338 ASNEE 343 1 6 HELIX 2 AA2 TYREE 365 ASNEE 370 1 6 HELIX 3 AA3 SEREE 383 LEUEE 387 5 5 HELIX 4 AA4 ASPEE 405 ILEEE 410 5 6 HELIX 5 AA5 GLYEE 416 ASNEE 422 1 7 HELIX 6 AA6 PROHH 62 GLNHH 65 5 4 HELIX 7 AA7 LYSHH 87 THRHH 91 5 5 HELIX 8 AA8 SERHH 162 ALAHH 164 5 3 HELIX 9 AA9 SERHH 193 GLYHH 196 5 4 HELIX 10 AB1 LYSHH 207 ASNHH 210 5 4 HELIX 11 AB2 GLNLL 85 VALLL 89 5 5 HELIX 12 AB3 SERLL 127 GLYLL 134 1 8 HELIX 13 AB4 LYSLL 189 GLULL 193 1 5 HELIX 14 AB5 PHEAA 338 ASNAA 343 1 6 HELIX 15 AB6 TYRAA 365 ASNAA 370 1 6 HELIX 16 AB7 SERAA 383 LEUAA 387 5 5 HELIX 17 AB8 ASPAA 405 ILEAA 410 5 6 HELIX 18 AB9 GLYAA 416 ASNAA 422 1 7 HELIX 19 AC1 LYSBB 87 THRBB 91 5 5 HELIX 20 AC2 SERBB 162 ALABB 164 5 3 HELIX 21 AC3 SERBB 193 GLYBB 196 5 4 HELIX 22 AC4 LYSBB 207 ASNBB 210 5 4 HELIX 23 AC5 GLNCC 85 VALCC 89 5 5 HELIX 24 AC6 SERCC 127 GLYCC 134 1 8 HELIX 25 AC7 LYSCC 189 GLUCC 193 1 5 HELIX 26 AC8 PHEDD 338 ASNDD 343 1 6 HELIX 27 AC9 TYRDD 365 ASNDD 370 1 6 HELIX 28 AD1 SERDD 383 LEUDD 387 5 5 HELIX 29 AD2 ASPDD 405 ILEDD 410 5 6 HELIX 30 AD3 GLYDD 416 ASNDD 422 1 7 HELIX 31 AD4 PROFF 62 GLNFF 65 5 4 HELIX 32 AD5 LYSFF 87 THRFF 91 5 5 HELIX 33 AD6 SERFF 162 ALAFF 164 5 3 HELIX 34 AD7 SERFF 193 GLYFF 196 5 4 HELIX 35 AD8 LYSFF 207 ASNFF 210 5 4 HELIX 36 AD9 GLNGG 85 VALGG 89 5 5 HELIX 37 AE1 SERGG 127 GLYGG 134 1 8 HELIX 38 AE2 LYSGG 189 LYSGG 194 1 6 SHEET 1 AA1 5 ASNEE 354 ILEEE 358 0 SHEET 2 AA1 5 ASNEE 394 ARGEE 403 -1 O VALEE 395 N ILEEE 358 SHEET 3 AA1 5 PROEE 507 GLUEE 516 -1 O TYREE 508 N ILEEE 402 SHEET 4 AA1 5 GLYEE 431 ASNEE 437 -1 N ILEEE 434 O VALEE 511 SHEET 5 AA1 5 THREE 376 TYREE 380 -1 N TYREE 380 O GLYEE 431 SHEET 1 AA2 3 CYSEE 361 VALEE 362 0 SHEET 2 AA2 3 VALEE 524 CYSEE 525 1 O CYSEE 525 N CYSEE 361 SHEET 3 AA2 3 CYSEE 391 PHEEE 392 -1 N PHEEE 392 O VALEE 524 SHEET 1 AA3 2 LEUEE 452 ARGEE 454 0 SHEET 2 AA3 2 LEUEE 492 SEREE 494 -1 O GLNEE 493 N TYREE 453 SHEET 1 AA4 2 TYREE 473 GLNEE 474 0 SHEET 2 AA4 2 CYSEE 488 TYREE 489 -1 O TYREE 489 N TYREE 473 SHEET 1 AA5 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA5 4 LEUHH 18 SERHH 25 -1 O LYSHH 23 N VALHH 5 SHEET 3 AA5 4 THRHH 78 TRPHH 83 -1 O ALAHH 79 N CYSHH 22 SHEET 4 AA5 4 THRHH 69 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA6 6 GLUHH 10 LYSHH 12 0 SHEET 2 AA6 6 THRHH 113 VALHH 117 1 O THRHH 114 N GLUHH 10 SHEET 3 AA6 6 ALAHH 92 GLYHH 99 -1 N ALAHH 92 O VALHH 115 SHEET 4 AA6 6 TRPHH 33 GLNHH 39 -1 N TRPHH 33 O GLYHH 99 SHEET 5 AA6 6 LEUHH 45 TYRHH 52 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA6 6 GLUHH 57 TYRHH 60 -1 O ARGHH 59 N ILEHH 50 SHEET 1 AA7 4 GLUHH 10 LYSHH 12 0 SHEET 2 AA7 4 THRHH 113 VALHH 117 1 O THRHH 114 N GLUHH 10 SHEET 3 AA7 4 ALAHH 92 GLYHH 99 -1 N ALAHH 92 O VALHH 115 SHEET 4 AA7 4 VALHH 108 TRPHH 109 -1 O VALHH 108 N GLYHH 98 SHEET 1 AA8 4 SERHH 126 LEUHH 130 0 SHEET 2 AA8 4 THRHH 141 TYRHH 151 -1 O GLYHH 145 N LEUHH 130 SHEET 3 AA8 4 TYRHH 182 PROHH 191 -1 O TYRHH 182 N TYRHH 151 SHEET 4 AA8 4 VALHH 169 THRHH 171 -1 N HISHH 170 O VALHH 187 SHEET 1 AA9 4 SERHH 126 LEUHH 130 0 SHEET 2 AA9 4 THRHH 141 TYRHH 151 -1 O GLYHH 145 N LEUHH 130 SHEET 3 AA9 4 TYRHH 182 PROHH 191 -1 O TYRHH 182 N TYRHH 151 SHEET 4 AA9 4 VALHH 175 LEUHH 176 -1 N VALHH 175 O SERHH 183 SHEET 1 AB1 3 THRHH 157 TRPHH 160 0 SHEET 2 AB1 3 TYRHH 200 HISHH 206 -1 O ASNHH 203 N SERHH 159 SHEET 3 AB1 3 THRHH 211 VALHH 217 -1 O VALHH 213 N VALHH 204 SHEET 1 AB2 4 LEULL 4 SERLL 7 0 SHEET 2 AB2 4 ALALL 19 SERLL 25 -1 O ASNLL 22 N SERLL 7 SHEET 3 AB2 4 ASPLL 76 ILELL 81 -1 O ILELL 81 N ALALL 19 SHEET 4 AB2 4 PHELL 68 SERLL 73 -1 N SERLL 69 O THRLL 80 SHEET 1 AB3 6 SERLL 10 VALLL 13 0 SHEET 2 AB3 6 THRLL 108 ILELL 112 1 O GLULL 111 N LEULL 11 SHEET 3 AB3 6 ALALL 90 GLNLL 96 -1 N ALALL 90 O VALLL 110 SHEET 4 AB3 6 LEULL 39 GLNLL 44 -1 N ALALL 40 O GLNLL 95 SHEET 5 AB3 6 LYSLL 51 TYRLL 55 -1 O LYSLL 51 N GLNLL 43 SHEET 6 AB3 6 THRLL 59 ARGLL 60 -1 O THRLL 59 N TYRLL 55 SHEET 1 AB4 4 SERLL 10 VALLL 13 0 SHEET 2 AB4 4 THRLL 108 ILELL 112 1 O GLULL 111 N LEULL 11 SHEET 3 AB4 4 ALALL 90 GLNLL 96 -1 N ALALL 90 O VALLL 110 SHEET 4 AB4 4 THRLL 103 PHELL 104 -1 O THRLL 103 N GLNLL 96 SHEET 1 AB5 2 LEULL 30 TYRLL 31 0 SHEET 2 AB5 2 LYSLL 36 ASNLL 37 -1 O LYSLL 36 N TYRLL 31 SHEET 1 AB6 4 SERLL 120 PHELL 124 0 SHEET 2 AB6 4 THRLL 135 PHELL 145 -1 O LEULL 141 N PHELL 122 SHEET 3 AB6 4 TYRLL 179 SERLL 188 -1 O SERLL 183 N CYSLL 140 SHEET 4 AB6 4 SERLL 165 GLNLL 166 -1 N GLNLL 166 O THRLL 184 SHEET 1 AB7 4 ALALL 159 GLNLL 161 0 SHEET 2 AB7 4 ALALL 150 VALLL 156 -1 N VALLL 156 O ALALL 159 SHEET 3 AB7 4 VALLL 197 HISLL 204 -1 O GLULL 201 N GLNLL 153 SHEET 4 AB7 4 VALLL 211 ASNLL 216 -1 O VALLL 211 N VALLL 202 SHEET 1 AB8 5 ASNAA 354 ILEAA 358 0 SHEET 2 AB8 5 ASNAA 394 ARGAA 403 -1 O VALAA 395 N ILEAA 358 SHEET 3 AB8 5 PROAA 507 GLUAA 516 -1 O TYRAA 508 N ILEAA 402 SHEET 4 AB8 5 GLYAA 431 ASNAA 437 -1 N ILEAA 434 O VALAA 511 SHEET 5 AB8 5 THRAA 376 TYRAA 380 -1 N TYRAA 380 O GLYAA 431 SHEET 1 AB9 3 CYSAA 361 VALAA 362 0 SHEET 2 AB9 3 VALAA 524 CYSAA 525 1 O CYSAA 525 N CYSAA 361 SHEET 3 AB9 3 CYSAA 391 PHEAA 392 -1 N PHEAA 392 O VALAA 524 SHEET 1 AC1 2 LEUAA 452 ARGAA 454 0 SHEET 2 AC1 2 LEUAA 492 SERAA 494 -1 O GLNAA 493 N TYRAA 453 SHEET 1 AC2 2 TYRAA 473 GLNAA 474 0 SHEET 2 AC2 2 CYSAA 488 TYRAA 489 -1 O TYRAA 489 N TYRAA 473 SHEET 1 AC3 4 GLNBB 3 GLNBB 6 0 SHEET 2 AC3 4 LEUBB 18 SERBB 25 -1 O LYSBB 23 N VALBB 5 SHEET 3 AC3 4 THRBB 78 TRPBB 83 -1 O ALABB 79 N CYSBB 22 SHEET 4 AC3 4 THRBB 69 ASPBB 73 -1 N SERBB 71 O TYRBB 80 SHEET 1 AC4 6 GLUBB 10 LYSBB 12 0 SHEET 2 AC4 6 THRBB 113 VALBB 117 1 O THRBB 114 N GLUBB 10 SHEET 3 AC4 6 ALABB 92 GLYBB 99 -1 N ALABB 92 O VALBB 115 SHEET 4 AC4 6 TRPBB 33 GLNBB 39 -1 N TRPBB 33 O GLYBB 99 SHEET 5 AC4 6 LEUBB 45 TYRBB 52 -1 O GLUBB 46 N ARGBB 38 SHEET 6 AC4 6 GLUBB 57 TYRBB 60 -1 O ARGBB 59 N ILEBB 50 SHEET 1 AC5 4 GLUBB 10 LYSBB 12 0 SHEET 2 AC5 4 THRBB 113 VALBB 117 1 O THRBB 114 N GLUBB 10 SHEET 3 AC5 4 ALABB 92 GLYBB 99 -1 N ALABB 92 O VALBB 115 SHEET 4 AC5 4 VALBB 108 TRPBB 109 -1 O VALBB 108 N GLYBB 98 SHEET 1 AC6 4 SERBB 126 LEUBB 130 0 SHEET 2 AC6 4 THRBB 141 TYRBB 151 -1 O GLYBB 145 N LEUBB 130 SHEET 3 AC6 4 TYRBB 182 PROBB 191 -1 O TYRBB 182 N TYRBB 151 SHEET 4 AC6 4 VALBB 169 THRBB 171 -1 N HISBB 170 O VALBB 187 SHEET 1 AC7 4 SERBB 126 LEUBB 130 0 SHEET 2 AC7 4 THRBB 141 TYRBB 151 -1 O GLYBB 145 N LEUBB 130 SHEET 3 AC7 4 TYRBB 182 PROBB 191 -1 O TYRBB 182 N TYRBB 151 SHEET 4 AC7 4 VALBB 175 LEUBB 176 -1 N VALBB 175 O SERBB 183 SHEET 1 AC8 3 THRBB 157 TRPBB 160 0 SHEET 2 AC8 3 TYRBB 200 HISBB 206 -1 O ASNBB 203 N SERBB 159 SHEET 3 AC8 3 THRBB 211 VALBB 217 -1 O VALBB 213 N VALBB 204 SHEET 1 AC9 4 LEUCC 4 SERCC 7 0 SHEET 2 AC9 4 ALACC 19 SERCC 25 -1 O ASNCC 22 N SERCC 7 SHEET 3 AC9 4 ASPCC 76 ILECC 81 -1 O ILECC 81 N ALACC 19 SHEET 4 AC9 4 PHECC 68 SERCC 73 -1 N SERCC 69 O THRCC 80 SHEET 1 AD1 6 SERCC 10 VALCC 13 0 SHEET 2 AD1 6 THRCC 108 ILECC 112 1 O GLUCC 111 N LEUCC 11 SHEET 3 AD1 6 ALACC 90 GLNCC 96 -1 N ALACC 90 O VALCC 110 SHEET 4 AD1 6 LEUCC 39 GLNCC 44 -1 N ALACC 40 O GLNCC 95 SHEET 5 AD1 6 LYSCC 51 TYRCC 55 -1 O LYSCC 51 N GLNCC 43 SHEET 6 AD1 6 THRCC 59 ARGCC 60 -1 O THRCC 59 N TYRCC 55 SHEET 1 AD2 4 SERCC 10 VALCC 13 0 SHEET 2 AD2 4 THRCC 108 ILECC 112 1 O GLUCC 111 N LEUCC 11 SHEET 3 AD2 4 ALACC 90 GLNCC 96 -1 N ALACC 90 O VALCC 110 SHEET 4 AD2 4 THRCC 103 PHECC 104 -1 O THRCC 103 N GLNCC 96 SHEET 1 AD3 2 LEUCC 30 TYRCC 31 0 SHEET 2 AD3 2 LYSCC 36 ASNCC 37 -1 O LYSCC 36 N TYRCC 31 SHEET 1 AD4 4 SERCC 120 PHECC 124 0 SHEET 2 AD4 4 THRCC 135 PHECC 145 -1 O LEUCC 141 N PHECC 122 SHEET 3 AD4 4 TYRCC 179 SERCC 188 -1 O SERCC 183 N CYSCC 140 SHEET 4 AD4 4 SERCC 165 VALCC 169 -1 N SERCC 168 O SERCC 182 SHEET 1 AD5 4 ALACC 159 GLNCC 161 0 SHEET 2 AD5 4 ALACC 150 VALCC 156 -1 N VALCC 156 O ALACC 159 SHEET 3 AD5 4 VALCC 197 HISCC 204 -1 O GLUCC 201 N GLNCC 153 SHEET 4 AD5 4 VALCC 211 ASNCC 216 -1 O VALCC 211 N VALCC 202 SHEET 1 AD6 5 ASNDD 354 ILEDD 358 0 SHEET 2 AD6 5 ASNDD 394 ARGDD 403 -1 O VALDD 395 N ILEDD 358 SHEET 3 AD6 5 PRODD 507 GLUDD 516 -1 O VALDD 512 N ASPDD 398 SHEET 4 AD6 5 GLYDD 431 ASNDD 437 -1 N ILEDD 434 O VALDD 511 SHEET 5 AD6 5 THRDD 376 TYRDD 380 -1 N TYRDD 380 O GLYDD 431 SHEET 1 AD7 3 CYSDD 361 VALDD 362 0 SHEET 2 AD7 3 VALDD 524 CYSDD 525 1 O CYSDD 525 N CYSDD 361 SHEET 3 AD7 3 CYSDD 391 PHEDD 392 -1 N PHEDD 392 O VALDD 524 SHEET 1 AD8 2 LEUDD 452 ARGDD 454 0 SHEET 2 AD8 2 LEUDD 492 SERDD 494 -1 O GLNDD 493 N TYRDD 453 SHEET 1 AD9 2 TYRDD 473 GLNDD 474 0 SHEET 2 AD9 2 CYSDD 488 TYRDD 489 -1 O TYRDD 489 N TYRDD 473 SHEET 1 AE1 4 GLNFF 3 GLNFF 6 0 SHEET 2 AE1 4 LEUFF 18 SERFF 25 -1 O LYSFF 23 N VALFF 5 SHEET 3 AE1 4 THRFF 78 TRPFF 83 -1 O ALAFF 79 N CYSFF 22 SHEET 4 AE1 4 THRFF 69 ASPFF 73 -1 N SERFF 71 O TYRFF 80 SHEET 1 AE2 6 GLUFF 10 LYSFF 12 0 SHEET 2 AE2 6 THRFF 113 VALFF 117 1 O THRFF 114 N GLUFF 10 SHEET 3 AE2 6 ALAFF 92 GLYFF 99 -1 N ALAFF 92 O VALFF 115 SHEET 4 AE2 6 TRPFF 33 GLNFF 39 -1 N TRPFF 33 O GLYFF 99 SHEET 5 AE2 6 LEUFF 45 TYRFF 52 -1 O GLUFF 46 N ARGFF 38 SHEET 6 AE2 6 GLUFF 57 TYRFF 60 -1 O ARGFF 59 N ILEFF 50 SHEET 1 AE3 4 GLUFF 10 LYSFF 12 0 SHEET 2 AE3 4 THRFF 113 VALFF 117 1 O THRFF 114 N GLUFF 10 SHEET 3 AE3 4 ALAFF 92 GLYFF 99 -1 N ALAFF 92 O VALFF 115 SHEET 4 AE3 4 VALFF 108 TRPFF 109 -1 O VALFF 108 N GLYFF 98 SHEET 1 AE4 4 SERFF 126 LEUFF 130 0 SHEET 2 AE4 4 THRFF 141 TYRFF 151 -1 O GLYFF 145 N LEUFF 130 SHEET 3 AE4 4 TYRFF 182 PROFF 191 -1 O TYRFF 182 N TYRFF 151 SHEET 4 AE4 4 VALFF 169 THRFF 171 -1 N HISFF 170 O VALFF 187 SHEET 1 AE5 4 SERFF 126 LEUFF 130 0 SHEET 2 AE5 4 THRFF 141 TYRFF 151 -1 O GLYFF 145 N LEUFF 130 SHEET 3 AE5 4 TYRFF 182 PROFF 191 -1 O TYRFF 182 N TYRFF 151 SHEET 4 AE5 4 VALFF 175 LEUFF 176 -1 N VALFF 175 O SERFF 183 SHEET 1 AE6 3 THRFF 157 TRPFF 160 0 SHEET 2 AE6 3 TYRFF 200 HISFF 206 -1 O ASNFF 203 N SERFF 159 SHEET 3 AE6 3 THRFF 211 VALFF 217 -1 O VALFF 213 N VALFF 204 SHEET 1 AE7 4 LEUGG 4 SERGG 7 0 SHEET 2 AE7 4 ALAGG 19 SERGG 25 -1 O ASNGG 22 N SERGG 7 SHEET 3 AE7 4 ASPGG 76 ILEGG 81 -1 O ILEGG 81 N ALAGG 19 SHEET 4 AE7 4 PHEGG 68 SERGG 73 -1 N SERGG 69 O THRGG 80 SHEET 1 AE8 6 SERGG 10 VALGG 13 0 SHEET 2 AE8 6 THRGG 108 ILEGG 112 1 O GLUGG 111 N LEUGG 11 SHEET 3 AE8 6 ALAGG 90 GLNGG 96 -1 N ALAGG 90 O VALGG 110 SHEET 4 AE8 6 LEUGG 39 GLNGG 44 -1 N ALAGG 40 O GLNGG 95 SHEET 5 AE8 6 LYSGG 51 TYRGG 55 -1 O LYSGG 51 N GLNGG 43 SHEET 6 AE8 6 THRGG 59 ARGGG 60 -1 O THRGG 59 N TYRGG 55 SHEET 1 AE9 4 SERGG 10 VALGG 13 0 SHEET 2 AE9 4 THRGG 108 ILEGG 112 1 O GLUGG 111 N LEUGG 11 SHEET 3 AE9 4 ALAGG 90 GLNGG 96 -1 N ALAGG 90 O VALGG 110 SHEET 4 AE9 4 THRGG 103 PHEGG 104 -1 O THRGG 103 N GLNGG 96 SHEET 1 AF1 2 LEUGG 30 TYRGG 31 0 SHEET 2 AF1 2 LYSGG 36 ASNGG 37 -1 O LYSGG 36 N TYRGG 31 SHEET 1 AF2 4 SERGG 120 PHEGG 124 0 SHEET 2 AF2 4 THRGG 135 PHEGG 145 -1 O LEUGG 141 N PHEGG 122 SHEET 3 AF2 4 TYRGG 179 SERGG 188 -1 O LEUGG 185 N VALGG 138 SHEET 4 AF2 4 SERGG 165 GLNGG 166 -1 N GLNGG 166 O THRGG 184 SHEET 1 AF3 4 ALAGG 159 LEUGG 160 0 SHEET 2 AF3 4 LYSGG 151 VALGG 156 -1 N VALGG 156 O ALAGG 159 SHEET 3 AF3 4 VALGG 197 THRGG 203 -1 O GLUGG 201 N GLNGG 153 SHEET 4 AF3 4 VALGG 211 ASNGG 216 -1 O VALGG 211 N VALGG 202 SSBOND 1 CYSEE 336 CYSEE 361 1555 1555 2.02 SSBOND 2 CYSEE 379 CYSEE 432 1555 1555 2.10 SSBOND 3 CYSEE 391 CYSEE 525 1555 1555 2.05 SSBOND 4 CYSEE 480 CYSEE 488 1555 1555 2.03 SSBOND 5 CYSHH 22 CYSHH 96 1555 1555 2.08 SSBOND 6 CYSHH 146 CYSHH 202 1555 1555 2.02 SSBOND 7 CYSLL 23 CYSLL 94 1555 1555 2.11 SSBOND 8 CYSLL 140 CYSLL 200 1555 1555 2.01 SSBOND 9 CYSAA 336 CYSAA 361 1555 1555 2.04 SSBOND 10 CYSAA 379 CYSAA 432 1555 1555 2.08 SSBOND 11 CYSAA 391 CYSAA 525 1555 1555 2.06 SSBOND 12 CYSAA 480 CYSAA 488 1555 1555 2.07 SSBOND 13 CYSBB 22 CYSBB 96 1555 1555 2.05 SSBOND 14 CYSBB 146 CYSBB 202 1555 1555 2.02 SSBOND 15 CYSCC 23 CYSCC 94 1555 1555 2.11 SSBOND 16 CYSCC 140 CYSCC 200 1555 1555 1.98 SSBOND 17 CYSDD 336 CYSDD 361 1555 1555 2.04 SSBOND 18 CYSDD 379 CYSDD 432 1555 1555 2.07 SSBOND 19 CYSDD 391 CYSDD 525 1555 1555 2.06 SSBOND 20 CYSDD 480 CYSDD 488 1555 1555 2.07 SSBOND 21 CYSFF 22 CYSFF 96 1555 1555 2.04 SSBOND 22 CYSFF 146 CYSFF 202 1555 1555 2.06 SSBOND 23 CYSGG 23 CYSGG 94 1555 1555 2.11 SSBOND 24 CYSGG 140 CYSGG 200 1555 1555 2.01 LINK ND2 ASNEE 343 C1 NAGEE 601 1555 1555 1.40 LINK ND2 ASNDD 343 C1 NAGDD 601 1555 1555 1.43 CISPEP 1 PHEHH 152 PROHH 153 0 -8.31 CISPEP 2 GLUHH 154 PROHH 155 0 -5.90 CISPEP 3 SERLL 7 PROLL 8 0 -9.76 CISPEP 4 THRLL 100 PROLL 101 0 3.57 CISPEP 5 TYRLL 146 PROLL 147 0 -3.11 CISPEP 6 PHEBB 152 PROBB 153 0 -8.53 CISPEP 7 GLUBB 154 PROBB 155 0 -8.35 CISPEP 8 SERCC 7 PROCC 8 0 -7.04 CISPEP 9 THRCC 100 PROCC 101 0 2.91 CISPEP 10 TYRCC 146 PROCC 147 0 -3.47 CISPEP 11 PHEFF 152 PROFF 153 0 -7.84 CISPEP 12 GLUFF 154 PROFF 155 0 -5.86 CISPEP 13 SERGG 7 PROGG 8 0 -9.08 CISPEP 14 THRGG 100 PROGG 101 0 2.99 CISPEP 15 TYRGG 146 PROGG 147 0 -2.51 CRYST1 207.130 207.130 199.866 90.00 90.00 90.00 P 41 21 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 0.004828 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004828 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005003 0.00000