HEADER IMMUNE SYSTEM 13-AUG-25 9Q0P TITLE HUMAN ANTI-EBV GH/GL FAB (AMMO1) WITH G111T LIGHT CHAIN MUTATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG LAMBDA LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS EBV, ANTIBODY, FAB, LAMBDA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.YOUNG REVDAT 1 03-DEC-25 9Q0P 0 JRNL AUTH Y.JEWEL,T.YOUNG,M.PARK,K.LY,A.GONZALEZ,T.C.MALLETT, JRNL AUTH 2 J.C.WILLIAMS JRNL TITL SINGLE-RESIDUE ENGINEERING OF LAMBDA ( LAMBDA ) ANTIBODY JRNL TITL 2 LIGHT CHAINS REDUCES CONFORMATIONAL FLEXIBILITY AND ENHANCES JRNL TITL 3 THERMAL STABILITY. JRNL REF COMPUT STRUCT BIOTECHNOL J V. 27 4730 2025 JRNL REFN ESSN 2001-0370 JRNL PMID 41245890 JRNL DOI 10.1016/J.CSBJ.2025.10.045 REMARK 2 REMARK 2 RESOLUTION. 2.08 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1 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) : 2.08 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.34 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 26824 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.193 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.460 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.3400 - 5.0200 0.99 1927 155 0.1633 0.1931 REMARK 3 2 5.0200 - 3.9800 0.98 1805 146 0.1352 0.1827 REMARK 3 3 3.9800 - 3.4800 0.99 1800 145 0.1681 0.2139 REMARK 3 4 3.4800 - 3.1600 0.97 1740 139 0.1921 0.2434 REMARK 3 5 3.1600 - 2.9400 0.99 1796 146 0.2094 0.2547 REMARK 3 6 2.9400 - 2.7600 1.00 1791 144 0.2057 0.2704 REMARK 3 7 2.7600 - 2.6200 0.99 1764 142 0.2115 0.2975 REMARK 3 8 2.6200 - 2.5100 1.00 1771 143 0.2110 0.2596 REMARK 3 9 2.5100 - 2.4100 1.00 1775 143 0.2162 0.2810 REMARK 3 10 2.4100 - 2.3300 1.00 1759 141 0.2216 0.2761 REMARK 3 11 2.3300 - 2.2600 1.00 1780 144 0.2193 0.2986 REMARK 3 12 2.2600 - 2.1900 1.00 1748 141 0.2390 0.3035 REMARK 3 13 2.1900 - 2.1400 1.00 1778 143 0.2391 0.2955 REMARK 3 14 2.1300 - 2.0800 0.90 1590 128 0.2513 0.3096 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) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.720 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 : 0.006 3420 REMARK 3 ANGLE : 0.850 4681 REMARK 3 CHIRALITY : 0.054 527 REMARK 3 PLANARITY : 0.006 604 REMARK 3 DIHEDRAL : 15.674 1222 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 9Q0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298837. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26825 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080 REMARK 200 RESOLUTION RANGE LOW (A) : 39.340 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.2200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 170 MM AMMONIUM ACETATE, 85 MM SODIUM REMARK 280 CITRATE-HCL, PH 5.6, 25.5% (W/V) PEG 4000, AND 15% (V/V) REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING 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 25.36100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.32950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.88700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.32950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.36100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.88700 REMARK 290 SMTRY3 4 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 SER A 225 REMARK 465 CYS A 226 REMARK 465 ASP A 227 REMARK 465 GLU B 214 REMARK 465 CYS B 215 REMARK 465 SER B 216 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 SER A 142 171.91 -56.97 REMARK 500 ASP B 50 -48.16 70.61 REMARK 500 SER B 51 12.64 -148.69 REMARK 500 GLN B 130 -7.35 -58.56 REMARK 500 ASP B 155 -104.86 55.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 472 DISTANCE = 6.66 ANGSTROMS REMARK 525 HOH B 473 DISTANCE = 6.82 ANGSTROMS REMARK 525 HOH B 474 DISTANCE = 7.63 ANGSTROMS DBREF 9Q0P A 1 227 PDB 9Q0P 9Q0P 1 227 DBREF 9Q0P B 1 216 PDB 9Q0P 9Q0P 1 216 SEQRES 1 A 227 GLU VAL GLN LEU VAL GLN SER GLY ALA ASP VAL LYS LYS SEQRES 2 A 227 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 A 227 TYR THR PHE ILE HIS PHE GLY ILE SER TRP VAL ARG GLN SEQRES 4 A 227 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASP SEQRES 5 A 227 THR ASN ASN GLY ASN THR ASN TYR ALA GLN SER LEU GLN SEQRES 6 A 227 GLY ARG VAL THR MET THR THR ASP THR SER THR GLY THR SEQRES 7 A 227 ALA TYR MET GLU LEU ARG SER LEU SER THR ASP ASP THR SEQRES 8 A 227 ALA VAL TYR PHE CYS ALA ARG ALA LEU GLU MET GLY HIS SEQRES 9 A 227 ARG SER GLY PHE PRO PHE ASP TYR TRP GLY GLN GLY VAL SEQRES 10 A 227 LEU VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 A 227 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 A 227 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 A 227 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 A 227 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 A 227 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 A 227 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 A 227 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 A 227 GLU PRO LYS SER CYS ASP SEQRES 1 B 216 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 B 216 PRO GLY GLN ARG ALA THR ILE THR CYS GLY GLY HIS ASN SEQRES 3 B 216 ILE GLY ALA LYS ASN VAL HIS TRP TYR GLN GLN LYS PRO SEQRES 4 B 216 GLY GLN ALA PRO VAL LEU VAL ILE GLN TYR ASP SER ASP SEQRES 5 B 216 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 B 216 SER GLY SER THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 B 216 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 B 216 SER GLY ARG GLY HIS PRO LEU TYR VAL PHE GLY GLY GLY SEQRES 9 B 216 THR LYS VAL THR VAL LEU THR GLN PRO LYS ALA ASN PRO SEQRES 10 B 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 B 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 B 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 B 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 B 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 B 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 B 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 B 216 THR VAL ALA PRO THR GLU CYS SER HET GOL A 301 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL C3 H8 O3 FORMUL 4 HOH *358(H2 O) HELIX 1 AA1 THR A 28 PHE A 32 5 5 HELIX 2 AA2 GLN A 62 GLN A 65 5 4 HELIX 3 AA3 SER A 87 THR A 91 5 5 HELIX 4 AA4 SER A 166 ALA A 168 5 3 HELIX 5 AA5 SER A 197 LEU A 199 5 3 HELIX 6 AA6 LYS A 211 ASN A 214 5 4 HELIX 7 AA7 ASN B 26 LYS B 30 5 5 HELIX 8 AA8 GLU B 78 GLU B 82 5 5 HELIX 9 AA9 SER B 92 HIS B 96 5 5 HELIX 10 AB1 SER B 125 GLN B 130 1 6 HELIX 11 AB2 THR B 185 HIS B 192 1 8 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O ALA A 79 N CYS A 22 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N THR A 69 O GLU A 82 SHEET 1 AA2 6 ASP A 10 LYS A 12 0 SHEET 2 AA2 6 VAL A 117 VAL A 121 1 O THR A 120 N LYS A 12 SHEET 3 AA2 6 ALA A 92 ALA A 99 -1 N TYR A 94 O VAL A 117 SHEET 4 AA2 6 GLY A 33 GLN A 39 -1 N VAL A 37 O PHE A 95 SHEET 5 AA2 6 GLU A 46 ILE A 51 -1 O MET A 48 N TRP A 36 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O ASN A 59 N TRP A 50 SHEET 1 AA3 4 ASP A 10 LYS A 12 0 SHEET 2 AA3 4 VAL A 117 VAL A 121 1 O THR A 120 N LYS A 12 SHEET 3 AA3 4 ALA A 92 ALA A 99 -1 N TYR A 94 O VAL A 117 SHEET 4 AA3 4 TYR A 112 TRP A 113 -1 O TYR A 112 N ARG A 98 SHEET 1 AA4 4 SER A 130 LEU A 134 0 SHEET 2 AA4 4 THR A 145 TYR A 155 -1 O LYS A 153 N SER A 130 SHEET 3 AA4 4 TYR A 186 PRO A 195 -1 O TYR A 186 N TYR A 155 SHEET 4 AA4 4 VAL A 173 THR A 175 -1 N HIS A 174 O VAL A 191 SHEET 1 AA5 4 SER A 130 LEU A 134 0 SHEET 2 AA5 4 THR A 145 TYR A 155 -1 O LYS A 153 N SER A 130 SHEET 3 AA5 4 TYR A 186 PRO A 195 -1 O TYR A 186 N TYR A 155 SHEET 4 AA5 4 VAL A 179 LEU A 180 -1 N VAL A 179 O SER A 187 SHEET 1 AA6 3 THR A 161 TRP A 164 0 SHEET 2 AA6 3 ILE A 205 HIS A 210 -1 O ASN A 209 N THR A 161 SHEET 3 AA6 3 THR A 215 ARG A 220 -1 O VAL A 217 N VAL A 208 SHEET 1 AA7 5 SER B 9 VAL B 12 0 SHEET 2 AA7 5 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AA7 5 ALA B 83 ASP B 91 -1 N ALA B 83 O VAL B 107 SHEET 4 AA7 5 HIS B 33 GLN B 37 -1 N TYR B 35 O TYR B 86 SHEET 5 AA7 5 VAL B 44 ILE B 47 -1 O ILE B 47 N TRP B 34 SHEET 1 AA8 4 SER B 9 VAL B 12 0 SHEET 2 AA8 4 THR B 105 VAL B 109 1 O THR B 108 N VAL B 10 SHEET 3 AA8 4 ALA B 83 ASP B 91 -1 N ALA B 83 O VAL B 107 SHEET 4 AA8 4 LEU B 98 PHE B 101 -1 O LEU B 98 N ASP B 91 SHEET 1 AA9 3 ALA B 18 GLY B 23 0 SHEET 2 AA9 3 THR B 69 ILE B 74 -1 O ALA B 70 N CYS B 22 SHEET 3 AA9 3 PHE B 61 SER B 66 -1 N SER B 62 O THR B 73 SHEET 1 AB1 4 THR B 118 PHE B 122 0 SHEET 2 AB1 4 ALA B 134 PHE B 143 -1 O LEU B 139 N THR B 120 SHEET 3 AB1 4 TYR B 176 LEU B 184 -1 O SER B 180 N CYS B 138 SHEET 4 AB1 4 VAL B 163 THR B 165 -1 N GLU B 164 O TYR B 181 SHEET 1 AB2 4 THR B 118 PHE B 122 0 SHEET 2 AB2 4 ALA B 134 PHE B 143 -1 O LEU B 139 N THR B 120 SHEET 3 AB2 4 TYR B 176 LEU B 184 -1 O SER B 180 N CYS B 138 SHEET 4 AB2 4 SER B 169 LYS B 170 -1 N SER B 169 O ALA B 177 SHEET 1 AB3 4 SER B 157 VAL B 159 0 SHEET 2 AB3 4 THR B 149 ALA B 154 -1 N ALA B 154 O SER B 157 SHEET 3 AB3 4 TYR B 195 HIS B 201 -1 O GLN B 198 N ALA B 151 SHEET 4 AB3 4 SER B 204 VAL B 210 -1 O SER B 204 N HIS B 201 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.06 SSBOND 2 CYS A 150 CYS A 206 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 87 1555 1555 2.07 SSBOND 4 CYS B 138 CYS B 197 1555 1555 2.03 CISPEP 1 PHE A 156 PRO A 157 0 -5.90 CISPEP 2 GLU A 158 PRO A 159 0 1.33 CISPEP 3 TYR B 144 PRO B 145 0 1.84 CRYST1 50.722 69.774 124.659 90.00 90.00 90.00 P 21 21 21 4 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 0.019715 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014332 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008022 0.00000