HEADER IMMUNE SYSTEM 26-SEP-24 9DSC TITLE CRYSTAL STRUCTURE OF APO-241_2F04-A95A MUTANT FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 241_2F04-A95A, HEAVY CHAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 241_2F04-A95A, LIGHT CHAIN; COMPND 7 CHAIN: F, C; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.H.LIN,I.A.WILSON REVDAT 1 19-MAR-25 9DSC 0 JRNL AUTH T.H.LIN,C.D.LEE,M.L.FERNANDEZ-QUINTERO,J.A.FERGUSON,J.HAN, JRNL AUTH 2 X.ZHU,W.YU,J.J.GUTHMILLER,F.KRAMMER,P.C.WILSON,A.B.WARD, JRNL AUTH 3 I.A.WILSON JRNL TITL STRUCTURALLY CONVERGENT ANTIBODIES DERIVED FROM DIFFERENT JRNL TITL 2 VACCINE STRATEGIES TARGET THE INFLUENZA VIRUS HA ANCHOR JRNL TITL 3 EPITOPE WITH A SUBSET OF V H 3 AND V K 3 GENES. JRNL REF NAT COMMUN V. 16 1268 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39894881 JRNL DOI 10.1038/S41467-025-56496-4 REMARK 2 REMARK 2 RESOLUTION. 2.01 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) : 2.01 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.41 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 NUMBER OF REFLECTIONS : 76548 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) : 0.200 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 3958 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 46.4100 - 6.0800 0.98 2876 137 0.1713 0.1706 REMARK 3 2 6.0800 - 4.8300 1.00 2777 149 0.1453 0.1823 REMARK 3 3 4.8300 - 4.2200 1.00 2736 158 0.1350 0.1770 REMARK 3 4 4.2200 - 3.8400 1.00 2719 167 0.1658 0.1983 REMARK 3 5 3.8300 - 3.5600 1.00 2728 134 0.1884 0.2458 REMARK 3 6 3.5600 - 3.3500 1.00 2696 159 0.1872 0.2243 REMARK 3 7 3.3500 - 3.1800 0.99 2706 132 0.2040 0.2277 REMARK 3 8 3.1800 - 3.0400 0.99 2689 131 0.2131 0.2589 REMARK 3 9 3.0400 - 2.9300 0.99 2685 130 0.2168 0.2886 REMARK 3 10 2.9300 - 2.8300 0.98 2670 138 0.2170 0.2729 REMARK 3 11 2.8300 - 2.7400 0.98 2631 164 0.2100 0.2617 REMARK 3 12 2.7400 - 2.6600 0.98 2616 146 0.2151 0.2614 REMARK 3 13 2.6600 - 2.5900 0.98 2616 152 0.2187 0.3034 REMARK 3 14 2.5900 - 2.5300 0.97 2613 145 0.2316 0.2583 REMARK 3 15 2.5300 - 2.4700 0.97 2593 144 0.2318 0.2737 REMARK 3 16 2.4700 - 2.4200 0.97 2585 139 0.2379 0.2851 REMARK 3 17 2.4200 - 2.3700 0.96 2569 145 0.2431 0.3032 REMARK 3 18 2.3700 - 2.3200 0.95 2564 146 0.2540 0.2556 REMARK 3 19 2.3200 - 2.2800 0.95 2530 134 0.2541 0.2884 REMARK 3 20 2.2800 - 2.2400 0.95 2545 135 0.2504 0.2887 REMARK 3 21 2.2400 - 2.2100 0.93 2475 152 0.2524 0.2766 REMARK 3 22 2.2100 - 2.1700 0.94 2495 125 0.2646 0.2632 REMARK 3 23 2.1700 - 2.1400 0.94 2465 154 0.2629 0.2822 REMARK 3 24 2.1400 - 2.1100 0.93 2556 127 0.2678 0.2916 REMARK 3 25 2.1100 - 2.0800 0.92 2423 143 0.2866 0.3287 REMARK 3 26 2.0800 - 2.0600 0.91 2417 135 0.3062 0.3129 REMARK 3 27 2.0600 - 2.0300 0.92 2438 135 0.3328 0.3585 REMARK 3 28 2.0300 - 2.0100 0.81 2177 102 0.3428 0.3698 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) : 23.240 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 6824 REMARK 3 ANGLE : 0.590 9278 REMARK 3 CHIRALITY : 0.043 1046 REMARK 3 PLANARITY : 0.004 1186 REMARK 3 DIHEDRAL : 5.633 944 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 9DSC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288702. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-FEB-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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9183 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76548 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.90 REMARK 200 R MERGE (I) : 0.14000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.20000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM ACETATE, PH 6.3, 18% REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.12700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.40600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.82950 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.40600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.12700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.82950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F 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: 3450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C 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 CYS F 215 REMARK 465 CYS C 215 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 C 498 O HOH C 500 1.87 REMARK 500 O HOH A 343 O HOH A 427 1.87 REMARK 500 O PRO B 137 O HOH B 301 1.92 REMARK 500 OG SER B 141 O HOH B 302 1.93 REMARK 500 O HOH F 418 O HOH F 425 1.94 REMARK 500 O HOH B 449 O HOH B 453 1.96 REMARK 500 O HOH C 429 O HOH C 461 1.97 REMARK 500 O HOH A 380 O HOH F 369 2.00 REMARK 500 O HOH F 412 O HOH F 420 2.02 REMARK 500 O THR A 194 O HOH A 301 2.04 REMARK 500 OE2 GLU A 89 O HOH A 302 2.05 REMARK 500 O VAL F 3 O HOH F 301 2.05 REMARK 500 NZ LYS B 154 O HOH B 303 2.06 REMARK 500 O HOH B 419 O HOH B 437 2.07 REMARK 500 O HOH B 323 O HOH B 433 2.08 REMARK 500 N GLU F 1 O HOH F 302 2.09 REMARK 500 OG1 THR A 58 O HOH A 303 2.11 REMARK 500 O HOH B 314 O HOH B 414 2.11 REMARK 500 O HOH B 354 O HOH B 435 2.12 REMARK 500 O HOH A 380 O HOH F 424 2.12 REMARK 500 O HOH A 414 O HOH A 420 2.13 REMARK 500 O SER B 138 O HOH B 304 2.14 REMARK 500 O VAL A 222 O HOH A 304 2.14 REMARK 500 OG SER B 17 O HOH B 305 2.17 REMARK 500 O HOH B 405 O HOH B 414 2.18 REMARK 500 O HOH B 390 O HOH B 436 2.18 REMARK 500 O HOH C 356 O HOH C 427 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 427 O HOH C 421 4444 2.13 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 GLN A 104 -159.29 -126.88 REMARK 500 LYS A 140 99.21 -69.02 REMARK 500 THR A 142 -10.63 72.42 REMARK 500 SER A 143 1.31 58.56 REMARK 500 ASP A 155 64.32 62.58 REMARK 500 SER F 30 -131.39 57.73 REMARK 500 ALA F 51 -11.14 72.65 REMARK 500 SER F 52 -3.79 -142.65 REMARK 500 ASN F 93 53.22 -93.94 REMARK 500 ILE B 105 -71.30 24.57 REMARK 500 ASP B 155 67.26 61.68 REMARK 500 LYS B 225 -78.31 -66.66 REMARK 500 SER B 226 160.47 174.98 REMARK 500 SER C 30 -124.04 55.04 REMARK 500 ALA C 51 -10.99 72.14 REMARK 500 SER C 52 -3.44 -143.55 REMARK 500 ASN C 93 30.30 -89.78 REMARK 500 ASN C 153 -5.70 73.17 REMARK 500 REMARK 500 REMARK: NULL DBREF 9DSC A 1 227 PDB 9DSC 9DSC 1 227 DBREF 9DSC F 1 215 PDB 9DSC 9DSC 1 215 DBREF 9DSC B 1 227 PDB 9DSC 9DSC 1 227 DBREF 9DSC C 1 215 PDB 9DSC 9DSC 1 215 SEQRES 1 A 227 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 227 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 A 227 PHE THR PHE SER LYS TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 A 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 A 227 GLY SER GLY ILE SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 227 GLY ARG PHE THR ILE SER ARG ASP THR SER LYS ASN MET SEQRES 7 A 227 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 227 ALA ILE TYR TYR CYS ALA LYS ASP ALA ILE SER GLY GLN SEQRES 9 A 227 ILE TRP LEU GLN GLY THR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 A 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 A 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 A 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 A 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 A 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 A 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 A 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 A 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 A 227 VAL GLU PRO LYS SER CYS SEQRES 1 F 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 F 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 215 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 F 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 F 215 THR ARG ALA THR GLY ILE PRO PRO ARG PHE SER GLY SER SEQRES 6 F 215 GLY SER GLY THR GLU PHE SER LEU THR ILE SER SER LEU SEQRES 7 F 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 F 215 ASN ASN TRP PRO ALA ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 F 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 227 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 227 PRO GLY GLY SER LEU ARG LEU SER CYS ALA VAL SER GLY SEQRES 3 B 227 PHE THR PHE SER LYS TYR ALA MET ASN TRP VAL ARG GLN SEQRES 4 B 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER HIS ILE SER SEQRES 5 B 227 GLY SER GLY ILE SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 227 GLY ARG PHE THR ILE SER ARG ASP THR SER LYS ASN MET SEQRES 7 B 227 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 227 ALA ILE TYR TYR CYS ALA LYS ASP ALA ILE SER GLY GLN SEQRES 9 B 227 ILE TRP LEU GLN GLY THR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 B 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 B 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 B 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 B 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 B 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 B 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 B 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 B 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 B 227 VAL GLU PRO LYS SER CYS SEQRES 1 C 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 C 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 C 215 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 C 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 C 215 THR ARG ALA THR GLY ILE PRO PRO ARG PHE SER GLY SER SEQRES 6 C 215 GLY SER GLY THR GLU PHE SER LEU THR ILE SER SER LEU SEQRES 7 C 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 C 215 ASN ASN TRP PRO ALA ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 C 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 C 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS FORMUL 5 HOH *669(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 ARG A 87 THR A 91 5 5 HELIX 4 AA4 GLN A 104 GLN A 108 5 5 HELIX 5 AA5 SER A 198 LEU A 200 5 3 HELIX 6 AA6 LYS A 212 ASN A 215 5 4 HELIX 7 AA7 GLN F 79 PHE F 83 5 5 HELIX 8 AA8 SER F 122 SER F 128 1 7 HELIX 9 AA9 LYS F 184 GLU F 188 1 5 HELIX 10 AB1 THR B 28 TYR B 32 5 5 HELIX 11 AB2 ASP B 62 LYS B 65 5 4 HELIX 12 AB3 ARG B 87 THR B 91 5 5 HELIX 13 AB4 GLN B 104 GLN B 108 5 5 HELIX 14 AB5 SER B 167 ALA B 169 5 3 HELIX 15 AB6 LYS B 212 ASN B 215 5 4 HELIX 16 AB7 GLN C 79 PHE C 83 5 5 HELIX 17 AB8 SER C 122 LYS C 127 1 6 HELIX 18 AB9 LYS C 184 GLU C 188 1 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA1 4 MET A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 6 LEU A 11 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 ASP 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 THR A 58 TYR A 60 -1 O TYR A 59 N HIS A 50 SHEET 1 AA3 4 LEU A 11 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 ASP 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 SER A 131 LEU A 135 0 SHEET 2 AA4 4 THR A 146 TYR A 156 -1 O GLY A 150 N LEU A 135 SHEET 3 AA4 4 TYR A 187 PRO A 196 -1 O TYR A 187 N TYR A 156 SHEET 4 AA4 4 VAL A 174 THR A 176 -1 N HIS A 175 O VAL A 192 SHEET 1 AA5 4 SER A 131 LEU A 135 0 SHEET 2 AA5 4 THR A 146 TYR A 156 -1 O GLY A 150 N LEU A 135 SHEET 3 AA5 4 TYR A 187 PRO A 196 -1 O TYR A 187 N TYR A 156 SHEET 4 AA5 4 VAL A 180 LEU A 181 -1 N VAL A 180 O SER A 188 SHEET 1 AA6 3 THR A 162 TRP A 165 0 SHEET 2 AA6 3 TYR A 205 HIS A 211 -1 O ASN A 208 N SER A 164 SHEET 3 AA6 3 THR A 216 VAL A 222 -1 O VAL A 218 N VAL A 209 SHEET 1 AA7 4 MET F 4 THR F 5 0 SHEET 2 AA7 4 ALA F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AA7 4 GLU F 70 ILE F 75 -1 O LEU F 73 N LEU F 21 SHEET 4 AA7 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AA8 6 THR F 10 VAL F 13 0 SHEET 2 AA8 6 THR F 103 ILE F 107 1 O GLU F 106 N LEU F 11 SHEET 3 AA8 6 ALA F 84 GLN F 90 -1 N TYR F 86 O THR F 103 SHEET 4 AA8 6 LEU F 33 GLN F 38 -1 N TYR F 36 O TYR F 87 SHEET 5 AA8 6 ARG F 45 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AA8 6 THR F 53 ARG F 54 -1 O THR F 53 N TYR F 49 SHEET 1 AA9 4 THR F 10 VAL F 13 0 SHEET 2 AA9 4 THR F 103 ILE F 107 1 O GLU F 106 N LEU F 11 SHEET 3 AA9 4 ALA F 84 GLN F 90 -1 N TYR F 86 O THR F 103 SHEET 4 AA9 4 THR F 98 PHE F 99 -1 O THR F 98 N GLN F 90 SHEET 1 AB1 4 SER F 115 PHE F 119 0 SHEET 2 AB1 4 THR F 130 PHE F 140 -1 O LEU F 136 N PHE F 117 SHEET 3 AB1 4 TYR F 174 SER F 183 -1 O LEU F 180 N VAL F 133 SHEET 4 AB1 4 SER F 160 VAL F 164 -1 N GLN F 161 O THR F 179 SHEET 1 AB2 3 LYS F 146 VAL F 151 0 SHEET 2 AB2 3 VAL F 192 THR F 198 -1 O GLU F 196 N GLN F 148 SHEET 3 AB2 3 VAL F 206 ASN F 211 -1 O LYS F 208 N CYS F 195 SHEET 1 AB3 4 GLN B 3 SER B 7 0 SHEET 2 AB3 4 LEU B 18 SER B 25 -1 O ALA B 23 N LEU B 5 SHEET 3 AB3 4 MET B 78 MET B 83 -1 O LEU B 81 N LEU B 20 SHEET 4 AB3 4 PHE B 68 ASP B 73 -1 N SER B 71 O TYR B 80 SHEET 1 AB4 6 LEU B 11 VAL B 12 0 SHEET 2 AB4 6 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AB4 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AB4 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AB4 6 LEU B 45 ILE B 51 -1 O VAL B 48 N TRP B 36 SHEET 6 AB4 6 THR B 58 TYR B 60 -1 O TYR B 59 N HIS B 50 SHEET 1 AB5 4 LEU B 11 VAL B 12 0 SHEET 2 AB5 4 THR B 118 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AB5 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AB5 4 PHE B 111 TRP B 114 -1 O TYR B 113 N LYS B 98 SHEET 1 AB6 4 SER B 131 LEU B 135 0 SHEET 2 AB6 4 THR B 146 TYR B 156 -1 O LEU B 152 N PHE B 133 SHEET 3 AB6 4 TYR B 187 PRO B 196 -1 O TYR B 187 N TYR B 156 SHEET 4 AB6 4 VAL B 174 THR B 176 -1 N HIS B 175 O VAL B 192 SHEET 1 AB7 4 SER B 131 LEU B 135 0 SHEET 2 AB7 4 THR B 146 TYR B 156 -1 O LEU B 152 N PHE B 133 SHEET 3 AB7 4 TYR B 187 PRO B 196 -1 O TYR B 187 N TYR B 156 SHEET 4 AB7 4 VAL B 180 LEU B 181 -1 N VAL B 180 O SER B 188 SHEET 1 AB8 3 THR B 162 TRP B 165 0 SHEET 2 AB8 3 TYR B 205 HIS B 211 -1 O ASN B 208 N SER B 164 SHEET 3 AB8 3 THR B 216 VAL B 222 -1 O VAL B 218 N VAL B 209 SHEET 1 AB9 4 MET C 4 THR C 5 0 SHEET 2 AB9 4 ALA C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AB9 4 GLU C 70 ILE C 75 -1 O LEU C 73 N LEU C 21 SHEET 4 AB9 4 PHE C 62 SER C 67 -1 N SER C 63 O THR C 74 SHEET 1 AC1 6 THR C 10 VAL C 13 0 SHEET 2 AC1 6 THR C 103 ILE C 107 1 O GLU C 106 N LEU C 11 SHEET 3 AC1 6 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 103 SHEET 4 AC1 6 LEU C 33 GLN C 38 -1 N ALA C 34 O GLN C 89 SHEET 5 AC1 6 ARG C 45 TYR C 49 -1 O LEU C 47 N TRP C 35 SHEET 6 AC1 6 THR C 53 ARG C 54 -1 O THR C 53 N TYR C 49 SHEET 1 AC2 4 THR C 10 VAL C 13 0 SHEET 2 AC2 4 THR C 103 ILE C 107 1 O GLU C 106 N LEU C 11 SHEET 3 AC2 4 ALA C 84 GLN C 90 -1 N TYR C 86 O THR C 103 SHEET 4 AC2 4 THR C 98 PHE C 99 -1 O THR C 98 N GLN C 90 SHEET 1 AC3 4 SER C 115 PHE C 119 0 SHEET 2 AC3 4 THR C 130 PHE C 140 -1 O LEU C 136 N PHE C 117 SHEET 3 AC3 4 TYR C 174 SER C 183 -1 O LEU C 176 N LEU C 137 SHEET 4 AC3 4 SER C 160 VAL C 164 -1 N SER C 163 O SER C 177 SHEET 1 AC4 4 ALA C 154 GLN C 156 0 SHEET 2 AC4 4 LYS C 146 VAL C 151 -1 N TRP C 149 O GLN C 156 SHEET 3 AC4 4 VAL C 192 THR C 198 -1 O GLU C 196 N GLN C 148 SHEET 4 AC4 4 VAL C 206 ASN C 211 -1 O VAL C 206 N VAL C 197 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS A 151 CYS A 207 1555 1555 2.03 SSBOND 3 CYS F 23 CYS F 88 1555 1555 2.03 SSBOND 4 CYS F 135 CYS F 195 1555 1555 2.03 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 6 CYS B 151 CYS B 207 1555 1555 2.03 SSBOND 7 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 8 CYS C 135 CYS C 195 1555 1555 2.03 CISPEP 1 PHE A 157 PRO A 158 0 -3.31 CISPEP 2 GLU A 159 PRO A 160 0 -1.30 CISPEP 3 SER F 7 PRO F 8 0 -0.77 CISPEP 4 TRP F 94 PRO F 95 0 4.08 CISPEP 5 TYR F 141 PRO F 142 0 1.96 CISPEP 6 PHE B 157 PRO B 158 0 -4.34 CISPEP 7 GLU B 159 PRO B 160 0 -1.76 CISPEP 8 SER C 7 PRO C 8 0 0.38 CISPEP 9 TRP C 94 PRO C 95 0 7.85 CISPEP 10 TYR C 141 PRO C 142 0 0.04 CRYST1 64.254 113.659 160.812 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015563 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008798 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006218 0.00000