HEADER VIRAL PROTEIN 04-DEC-24 9KUR TITLE CRYSTAL STRUCTURE OF MAB NCOV400FAB WITH SARS-COV-2 N-CTD COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: COV N CTD; COMPND 5 SYNONYM: N,NUCLEOCAPSID PROTEIN,NC,PROTEIN N; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 400FAB HEAVY CHAIN; COMPND 9 CHAIN: H, G; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 400FAB LIGHT CHAIN; COMPND 13 CHAIN: L, D; COMPND 14 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CORONAVIRUS, SARS-COV-2, NUCLEOCAPSID PROTEIN, C-TERMINAL KEYWDS 2 DIMERIZATION DOMAIN, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.J.XUE,S.D.CHEN REVDAT 1 15-OCT-25 9KUR 0 JRNL AUTH S.XUE,S.HE,Z.HUANG,M.YANG,G.HU,X.CHEN,Q.CHEN,W.ZHOU,S.LIN, JRNL AUTH 2 S.CHEN JRNL TITL STRUCTURAL BASIS OF A HUMAN ANTIBODY TARGETING SARS-COV-2 JRNL TITL 2 NUCLEOCAPSID PROTEIN DIMERIZATION DOMAIN AND INTERFERING JRNL TITL 3 WITH RNA-BINDING. JRNL REF COMMUN BIOL V. 8 1248 2025 JRNL REFN ESSN 2399-3642 JRNL PMID 40830575 JRNL DOI 10.1038/S42003-025-08648-X REMARK 2 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.98 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 74158 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.202 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730 REMARK 3 FREE R VALUE TEST SET COUNT : 3507 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 24.9800 - 6.0000 0.99 2896 116 0.1646 0.1936 REMARK 3 2 6.0000 - 4.7700 0.99 2892 132 0.1611 0.1909 REMARK 3 3 4.7700 - 4.1700 0.99 2880 130 0.1362 0.1720 REMARK 3 4 4.1700 - 3.7900 0.99 2866 153 0.1593 0.1981 REMARK 3 5 3.7900 - 3.5200 0.99 2818 170 0.1800 0.2480 REMARK 3 6 3.5200 - 3.3100 0.98 2860 149 0.1901 0.2451 REMARK 3 7 3.3100 - 3.1500 0.99 2851 128 0.2022 0.2483 REMARK 3 8 3.1500 - 3.0100 0.99 2877 122 0.2005 0.2714 REMARK 3 9 3.0100 - 2.8900 0.98 2870 123 0.2135 0.2878 REMARK 3 10 2.8900 - 2.8000 0.98 2828 151 0.2238 0.2883 REMARK 3 11 2.8000 - 2.7100 0.98 2807 155 0.2204 0.2858 REMARK 3 12 2.7100 - 2.6300 0.97 2838 136 0.2310 0.2706 REMARK 3 13 2.6300 - 2.5600 0.98 2795 140 0.2286 0.3028 REMARK 3 14 2.5600 - 2.5000 0.98 2872 149 0.2327 0.2794 REMARK 3 15 2.5000 - 2.4400 0.98 2809 147 0.2334 0.2729 REMARK 3 16 2.4400 - 2.3900 0.98 2836 133 0.2276 0.2878 REMARK 3 17 2.3900 - 2.3400 0.98 2851 126 0.2247 0.3034 REMARK 3 18 2.3400 - 2.3000 0.98 2770 140 0.2232 0.2800 REMARK 3 19 2.3000 - 2.2600 0.97 2850 140 0.2417 0.2700 REMARK 3 20 2.2600 - 2.2200 0.93 2693 133 0.2899 0.3269 REMARK 3 21 2.2200 - 2.1800 0.97 2773 157 0.2452 0.3077 REMARK 3 22 2.1800 - 2.1500 0.97 2822 143 0.2429 0.2822 REMARK 3 23 2.1500 - 2.1200 0.97 2787 148 0.2575 0.2955 REMARK 3 24 2.1200 - 2.0900 0.97 2829 147 0.2787 0.3106 REMARK 3 25 2.0900 - 2.0600 0.94 2681 139 0.3429 0.3545 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.750 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 : 0.002 8547 REMARK 3 ANGLE : 0.600 11644 REMARK 3 CHIRALITY : 0.043 1294 REMARK 3 PLANARITY : 0.005 1495 REMARK 3 DIHEDRAL : 5.350 1186 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -20.0896 19.0769 -35.4333 REMARK 3 T TENSOR REMARK 3 T11: 0.1630 T22: 0.1851 REMARK 3 T33: 0.1699 T12: 0.0199 REMARK 3 T13: -0.0021 T23: 0.0044 REMARK 3 L TENSOR REMARK 3 L11: 0.4879 L22: 0.3164 REMARK 3 L33: 0.1838 L12: 0.1356 REMARK 3 L13: 0.0120 L23: 0.0272 REMARK 3 S TENSOR REMARK 3 S11: -0.0189 S12: 0.1110 S13: -0.0000 REMARK 3 S21: -0.0301 S22: 0.0323 S23: 0.0198 REMARK 3 S31: -0.0046 S32: 0.0209 S33: -0.0167 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 9KUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 05-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1300054269. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JAN-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74510 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060 REMARK 200 RESOLUTION RANGE LOW (A) : 88.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.10100 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) : 2.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 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: 7DE1,6TCN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.74 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FORMATE, 16% PEG3350, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 47640 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, D, G 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 PRO A 365 REMARK 465 PRO B 365 REMARK 465 ALA H 106 REMARK 465 GLY H 107 REMARK 465 SER H 108 REMARK 465 LYS H 146 REMARK 465 SER H 147 REMARK 465 THR H 148 REMARK 465 SER H 149 REMARK 465 LYS H 231 REMARK 465 SER H 232 REMARK 465 CYS H 233 REMARK 465 ASP H 234 REMARK 465 LYS H 235 REMARK 465 THR L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 SER L 215 REMARK 465 CYS D 214 REMARK 465 SER D 215 REMARK 465 ALA G 104A REMARK 465 ALA G 104B REMARK 465 GLY G 104C REMARK 465 SER G 104D REMARK 465 GLN G 104E REMARK 465 SER G 142 REMARK 465 LYS G 143 REMARK 465 SER G 144 REMARK 465 THR G 145 REMARK 465 SER G 146 REMARK 465 GLY G 147 REMARK 465 SER G 229 REMARK 465 CYS G 230 REMARK 465 ASP G 231 REMARK 465 LYS G 232 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 GLU A 280 CG CD OE1 OE2 REMARK 470 GLN A 281 CG CD OE1 NE2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 LYS L 152 CG CD CE NZ REMARK 470 GLN L 197 CG CD OE1 NE2 REMARK 470 GLU D 213 CG CD OE1 OE2 REMARK 470 GLU G 1 CG CD OE1 OE2 REMARK 470 LYS G 228 CG CD CE NZ 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 TYR A 268 84.64 -171.77 REMARK 500 TYR B 268 80.16 -158.18 REMARK 500 ASP H 99 -158.07 -103.58 REMARK 500 ASP H 161 66.86 62.39 REMARK 500 ASP L 50 -45.80 72.42 REMARK 500 SER L 66 86.07 -150.36 REMARK 500 SER L 89 -166.19 -160.37 REMARK 500 HIS L 97 -156.82 -110.22 REMARK 500 LEU L 109 68.68 61.12 REMARK 500 LYS L 159 64.12 -112.24 REMARK 500 ASP D 50 -44.00 70.28 REMARK 500 SER D 51 10.05 -145.16 REMARK 500 SER D 89 -166.51 -160.32 REMARK 500 HIS D 97 -153.98 -111.43 REMARK 500 ASP D 154 -101.51 56.89 REMARK 500 ASP G 99 -158.44 -106.49 REMARK 500 ASP G 158 65.51 61.85 REMARK 500 REMARK 500 REMARK: NULL DBREF 9KUR A 250 365 UNP P0DTC9 NCAP_SARS2 250 365 DBREF 9KUR B 250 365 UNP P0DTC9 NCAP_SARS2 250 365 DBREF 9KUR H 1 235 PDB 9KUR 9KUR 1 235 DBREF 9KUR L 1 215 PDB 9KUR 9KUR 1 215 DBREF 9KUR D 1 215 PDB 9KUR 9KUR 1 215 DBREF 9KUR G 1 232 PDB 9KUR 9KUR 1 232 SEQADV 9KUR SER A 249 UNP P0DTC9 EXPRESSION TAG SEQADV 9KUR SER B 249 UNP P0DTC9 EXPRESSION TAG SEQRES 1 A 117 SER SER ALA ALA GLU ALA SER LYS LYS PRO ARG GLN LYS SEQRES 2 A 117 ARG THR ALA THR LYS ALA TYR ASN VAL THR GLN ALA PHE SEQRES 3 A 117 GLY ARG ARG GLY PRO GLU GLN THR GLN GLY ASN PHE GLY SEQRES 4 A 117 ASP GLN GLU LEU ILE ARG GLN GLY THR ASP TYR LYS HIS SEQRES 5 A 117 TRP PRO GLN ILE ALA GLN PHE ALA PRO SER ALA SER ALA SEQRES 6 A 117 PHE PHE GLY MET SER ARG ILE GLY MET GLU VAL THR PRO SEQRES 7 A 117 SER GLY THR TRP LEU THR TYR THR GLY ALA ILE LYS LEU SEQRES 8 A 117 ASP ASP LYS ASP PRO ASN PHE LYS ASP GLN VAL ILE LEU SEQRES 9 A 117 LEU ASN LYS HIS ILE ASP ALA TYR LYS THR PHE PRO PRO SEQRES 1 B 117 SER SER ALA ALA GLU ALA SER LYS LYS PRO ARG GLN LYS SEQRES 2 B 117 ARG THR ALA THR LYS ALA TYR ASN VAL THR GLN ALA PHE SEQRES 3 B 117 GLY ARG ARG GLY PRO GLU GLN THR GLN GLY ASN PHE GLY SEQRES 4 B 117 ASP GLN GLU LEU ILE ARG GLN GLY THR ASP TYR LYS HIS SEQRES 5 B 117 TRP PRO GLN ILE ALA GLN PHE ALA PRO SER ALA SER ALA SEQRES 6 B 117 PHE PHE GLY MET SER ARG ILE GLY MET GLU VAL THR PRO SEQRES 7 B 117 SER GLY THR TRP LEU THR TYR THR GLY ALA ILE LYS LEU SEQRES 8 B 117 ASP ASP LYS ASP PRO ASN PHE LYS ASP GLN VAL ILE LEU SEQRES 9 B 117 LEU ASN LYS HIS ILE ASP ALA TYR LYS THR PHE PRO PRO SEQRES 1 H 235 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 235 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 235 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 H 235 SER GLY GLY SER SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 235 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA LYS ASP HIS LEU GLU LEU SER SEQRES 9 H 235 ALA ALA GLY SER GLN ILE ASN TYR TYR TYR TYR GLY MET SEQRES 10 H 235 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 11 H 235 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 H 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 H 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 H 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 H 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 H 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 H 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 H 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 H 235 LYS SEQRES 1 L 215 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 L 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 L 215 LEU PRO LYS GLN TYR ALA TYR TRP TYR GLN GLN LYS PRO SEQRES 4 L 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS ASP SER GLU SEQRES 5 L 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 L 215 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 L 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER ALA ASP SEQRES 8 L 215 SER SER GLY THR SER HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 L 215 LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 L 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 L 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 L 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 L 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 L 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 L 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 L 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 L 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 D 215 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 D 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA SEQRES 3 D 215 LEU PRO LYS GLN TYR ALA TYR TRP TYR GLN GLN LYS PRO SEQRES 4 D 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS ASP SER GLU SEQRES 5 D 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER SER SEQRES 6 D 215 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 D 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER ALA ASP SEQRES 8 D 215 SER SER GLY THR SER HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 D 215 LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER SEQRES 10 D 215 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA SEQRES 11 D 215 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR SEQRES 12 D 215 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER SEQRES 13 D 215 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS SEQRES 14 D 215 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER SEQRES 15 D 215 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER SEQRES 16 D 215 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR SEQRES 17 D 215 VAL ALA PRO THR GLU CYS SER SEQRES 1 G 235 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 G 235 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 235 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 G 235 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER VAL ILE TYR SEQRES 5 G 235 SER GLY GLY SER SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 G 235 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 G 235 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 G 235 ALA VAL TYR TYR CYS ALA LYS ASP HIS LEU GLU LEU SER SEQRES 9 G 235 ALA ALA GLY SER GLN ILE ASN TYR TYR TYR TYR GLY MET SEQRES 10 G 235 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 11 G 235 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 G 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 G 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 G 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 G 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 G 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 G 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 G 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 G 235 LYS FORMUL 7 HOH *780(H2 O) HELIX 1 AA1 SER A 249 SER A 255 1 7 HELIX 2 AA2 PRO A 258 ARG A 262 5 5 HELIX 3 AA3 ASN A 269 GLY A 275 1 7 HELIX 4 AA4 ASP A 288 GLY A 295 1 8 HELIX 5 AA5 THR A 296 TYR A 298 5 3 HELIX 6 AA6 HIS A 300 GLN A 306 1 7 HELIX 7 AA7 SER A 310 SER A 318 1 9 HELIX 8 AA8 ASN A 345 ILE A 357 1 13 HELIX 9 AA9 ASP A 358 THR A 362 5 5 HELIX 10 AB1 SER B 250 SER B 255 1 6 HELIX 11 AB2 PRO B 258 ARG B 262 5 5 HELIX 12 AB3 ASN B 269 GLY B 275 1 7 HELIX 13 AB4 ASP B 288 GLY B 295 1 8 HELIX 14 AB5 THR B 296 TYR B 298 5 3 HELIX 15 AB6 HIS B 300 GLN B 306 1 7 HELIX 16 AB7 SER B 310 SER B 318 1 9 HELIX 17 AB8 ASN B 345 ILE B 357 1 13 HELIX 18 AB9 ASP B 358 PHE B 363 5 6 HELIX 19 AC1 THR H 28 SER H 30 5 3 HELIX 20 AC2 ARG H 87 THR H 91 5 5 HELIX 21 AC3 SER H 173 ALA H 175 5 3 HELIX 22 AC4 SER H 204 LEU H 206 5 3 HELIX 23 AC5 LYS H 218 ASN H 221 5 4 HELIX 24 AC6 GLN L 78 GLU L 82 5 5 HELIX 25 AC7 SER L 124 GLN L 129 1 6 HELIX 26 AC8 THR L 184 HIS L 191 1 8 HELIX 27 AC9 GLN D 78 GLU D 82 5 5 HELIX 28 AD1 SER D 124 GLN D 129 1 6 HELIX 29 AD2 THR D 184 HIS D 191 1 8 HELIX 30 AD3 THR G 28 SER G 30 5 3 HELIX 31 AD4 ARG G 87 THR G 91 5 5 HELIX 32 AD5 SER G 201 LEU G 203 5 3 HELIX 33 AD6 LYS G 215 ASN G 218 5 4 SHEET 1 AA1 4 ARG A 319 THR A 325 0 SHEET 2 AA1 4 GLY A 328 LYS A 338 -1 O THR A 334 N ARG A 319 SHEET 3 AA1 4 GLY B 328 LEU B 339 -1 O ILE B 337 N LEU A 331 SHEET 4 AA1 4 ARG B 319 THR B 325 -1 N GLU B 323 O TRP B 330 SHEET 1 AA2 4 GLN H 3 SER H 7 0 SHEET 2 AA2 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA2 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA2 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AA3 6 LEU H 11 VAL H 12 0 SHEET 2 AA3 6 THR H 124 VAL H 128 1 O THR H 127 N VAL H 12 SHEET 3 AA3 6 ALA H 92 LEU H 103 -1 N TYR H 94 O THR H 124 SHEET 4 AA3 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA3 6 THR H 58 TYR H 60 -1 O TYR H 59 N VAL H 50 SHEET 1 AA4 4 LEU H 11 VAL H 12 0 SHEET 2 AA4 4 THR H 124 VAL H 128 1 O THR H 127 N VAL H 12 SHEET 3 AA4 4 ALA H 92 LEU H 103 -1 N TYR H 94 O THR H 124 SHEET 4 AA4 4 ASN H 111 TYR H 113 -1 O TYR H 113 N LEU H 101 SHEET 1 AA5 4 SER H 137 LEU H 141 0 SHEET 2 AA5 4 THR H 152 TYR H 162 -1 O GLY H 156 N LEU H 141 SHEET 3 AA5 4 TYR H 193 PRO H 202 -1 O VAL H 199 N LEU H 155 SHEET 4 AA5 4 VAL H 180 THR H 182 -1 N HIS H 181 O VAL H 198 SHEET 1 AA6 4 SER H 137 LEU H 141 0 SHEET 2 AA6 4 THR H 152 TYR H 162 -1 O GLY H 156 N LEU H 141 SHEET 3 AA6 4 TYR H 193 PRO H 202 -1 O VAL H 199 N LEU H 155 SHEET 4 AA6 4 VAL H 186 LEU H 187 -1 N VAL H 186 O SER H 194 SHEET 1 AA7 3 THR H 168 TRP H 171 0 SHEET 2 AA7 3 ILE H 212 HIS H 217 -1 O ASN H 214 N SER H 170 SHEET 3 AA7 3 THR H 222 ARG H 227 -1 O VAL H 224 N VAL H 215 SHEET 1 AA8 5 SER L 9 SER L 11 0 SHEET 2 AA8 5 THR L 104 THR L 107 1 O THR L 107 N VAL L 10 SHEET 3 AA8 5 ALA L 83 ALA L 90 -1 N ALA L 83 O LEU L 106 SHEET 4 AA8 5 TYR L 33 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AA8 5 VAL L 44 ILE L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AA9 4 SER L 9 SER L 11 0 SHEET 2 AA9 4 THR L 104 THR L 107 1 O THR L 107 N VAL L 10 SHEET 3 AA9 4 ALA L 83 ALA L 90 -1 N ALA L 83 O LEU L 106 SHEET 4 AA9 4 TRP L 98 PHE L 100 -1 O VAL L 99 N SER L 89 SHEET 1 AB1 3 ALA L 18 SER L 23 0 SHEET 2 AB1 3 THR L 69 ILE L 74 -1 O LEU L 72 N ILE L 20 SHEET 3 AB1 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AB2 4 SER L 117 PHE L 121 0 SHEET 2 AB2 4 ALA L 133 PHE L 142 -1 O SER L 140 N SER L 117 SHEET 3 AB2 4 TYR L 175 LEU L 183 -1 O ALA L 177 N ILE L 139 SHEET 4 AB2 4 VAL L 162 THR L 164 -1 N GLU L 163 O TYR L 180 SHEET 1 AB3 4 SER L 117 PHE L 121 0 SHEET 2 AB3 4 ALA L 133 PHE L 142 -1 O SER L 140 N SER L 117 SHEET 3 AB3 4 TYR L 175 LEU L 183 -1 O ALA L 177 N ILE L 139 SHEET 4 AB3 4 SER L 168 LYS L 169 -1 N SER L 168 O ALA L 176 SHEET 1 AB4 3 THR L 148 LYS L 152 0 SHEET 2 AB4 3 TYR L 194 HIS L 200 -1 O GLN L 197 N ALA L 150 SHEET 3 AB4 3 SER L 203 VAL L 209 -1 O VAL L 205 N VAL L 198 SHEET 1 AB5 5 SER D 9 VAL D 12 0 SHEET 2 AB5 5 THR D 104 VAL D 108 1 O THR D 107 N VAL D 10 SHEET 3 AB5 5 ALA D 83 ALA D 90 -1 N ALA D 83 O LEU D 106 SHEET 4 AB5 5 TYR D 33 GLN D 37 -1 N GLN D 37 O ASP D 84 SHEET 5 AB5 5 VAL D 44 ILE D 47 -1 O VAL D 44 N GLN D 36 SHEET 1 AB6 4 SER D 9 VAL D 12 0 SHEET 2 AB6 4 THR D 104 VAL D 108 1 O THR D 107 N VAL D 10 SHEET 3 AB6 4 ALA D 83 ALA D 90 -1 N ALA D 83 O LEU D 106 SHEET 4 AB6 4 TRP D 98 PHE D 100 -1 O VAL D 99 N SER D 89 SHEET 1 AB7 3 ALA D 18 SER D 23 0 SHEET 2 AB7 3 THR D 69 ILE D 74 -1 O LEU D 72 N ILE D 20 SHEET 3 AB7 3 PHE D 61 SER D 66 -1 N SER D 62 O THR D 73 SHEET 1 AB8 4 SER D 117 PHE D 121 0 SHEET 2 AB8 4 ALA D 133 PHE D 142 -1 O LEU D 138 N THR D 119 SHEET 3 AB8 4 TYR D 175 LEU D 183 -1 O SER D 179 N CYS D 137 SHEET 4 AB8 4 VAL D 162 THR D 164 -1 N GLU D 163 O TYR D 180 SHEET 1 AB9 4 SER D 117 PHE D 121 0 SHEET 2 AB9 4 ALA D 133 PHE D 142 -1 O LEU D 138 N THR D 119 SHEET 3 AB9 4 TYR D 175 LEU D 183 -1 O SER D 179 N CYS D 137 SHEET 4 AB9 4 SER D 168 LYS D 169 -1 N SER D 168 O ALA D 176 SHEET 1 AC1 4 SER D 156 VAL D 158 0 SHEET 2 AC1 4 THR D 148 ALA D 153 -1 N ALA D 153 O SER D 156 SHEET 3 AC1 4 TYR D 194 HIS D 200 -1 O GLN D 197 N ALA D 150 SHEET 4 AC1 4 SER D 203 VAL D 209 -1 O SER D 203 N HIS D 200 SHEET 1 AC2 4 GLN G 3 SER G 7 0 SHEET 2 AC2 4 LEU G 18 SER G 25 -1 O ALA G 23 N LEU G 5 SHEET 3 AC2 4 THR G 78 MET G 83 -1 O MET G 83 N LEU G 18 SHEET 4 AC2 4 PHE G 68 ASP G 73 -1 N SER G 71 O TYR G 80 SHEET 1 AC3 6 LEU G 11 VAL G 12 0 SHEET 2 AC3 6 THR G 121 VAL G 125 1 O THR G 124 N VAL G 12 SHEET 3 AC3 6 ALA G 92 LEU G 103 -1 N TYR G 94 O THR G 121 SHEET 4 AC3 6 TYR G 32 GLN G 39 -1 N VAL G 37 O TYR G 95 SHEET 5 AC3 6 LEU G 45 ILE G 51 -1 O VAL G 48 N TRP G 36 SHEET 6 AC3 6 THR G 58 TYR G 60 -1 O TYR G 59 N VAL G 50 SHEET 1 AC4 4 LEU G 11 VAL G 12 0 SHEET 2 AC4 4 THR G 121 VAL G 125 1 O THR G 124 N VAL G 12 SHEET 3 AC4 4 ALA G 92 LEU G 103 -1 N TYR G 94 O THR G 121 SHEET 4 AC4 4 ASN G 108 TYR G 110 -1 O TYR G 110 N LEU G 101 SHEET 1 AC5 4 SER G 134 LEU G 138 0 SHEET 2 AC5 4 THR G 149 TYR G 159 -1 O GLY G 153 N LEU G 138 SHEET 3 AC5 4 TYR G 190 PRO G 199 -1 O TYR G 190 N TYR G 159 SHEET 4 AC5 4 VAL G 177 THR G 179 -1 N HIS G 178 O VAL G 195 SHEET 1 AC6 4 SER G 134 LEU G 138 0 SHEET 2 AC6 4 THR G 149 TYR G 159 -1 O GLY G 153 N LEU G 138 SHEET 3 AC6 4 TYR G 190 PRO G 199 -1 O TYR G 190 N TYR G 159 SHEET 4 AC6 4 VAL G 183 LEU G 184 -1 N VAL G 183 O SER G 191 SHEET 1 AC7 3 THR G 165 TRP G 168 0 SHEET 2 AC7 3 ILE G 209 HIS G 214 -1 O ASN G 211 N SER G 167 SHEET 3 AC7 3 THR G 219 ARG G 224 -1 O THR G 219 N HIS G 214 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 157 CYS H 213 1555 1555 2.03 SSBOND 3 CYS L 22 CYS L 87 1555 1555 2.03 SSBOND 4 CYS L 137 CYS L 196 1555 1555 2.03 SSBOND 5 CYS D 22 CYS D 87 1555 1555 2.03 SSBOND 6 CYS D 137 CYS D 196 1555 1555 2.03 SSBOND 7 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 8 CYS G 154 CYS G 210 1555 1555 2.03 CISPEP 1 PHE H 163 PRO H 164 0 -5.18 CISPEP 2 GLU H 165 PRO H 166 0 -0.08 CISPEP 3 TYR L 143 PRO L 144 0 3.55 CISPEP 4 TYR D 143 PRO D 144 0 -0.06 CISPEP 5 PHE G 160 PRO G 161 0 -4.02 CISPEP 6 GLU G 162 PRO G 163 0 0.94 CRYST1 48.408 74.222 96.510 106.63 103.63 96.07 P 1 2 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 0.020658 0.002197 0.006038 0.00000 SCALE2 0.000000 0.013549 0.004607 0.00000 SCALE3 0.000000 0.000000 0.011261 0.00000