HEADER IMMUNE SYSTEM 08-AUG-25 9PZ6 TITLE ANTI-NANP FAB WITH G112T LIGHT CHAIN MUTATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: 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 NANP, ANTIBODY, FAB, LAMBDA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.YOUNG REVDAT 1 03-DEC-25 9PZ6 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. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.1_4122 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.30 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 3 NUMBER OF REFLECTIONS : 50372 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 2542 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 39.3000 - 4.4500 1.00 2973 147 0.1420 0.1643 REMARK 3 2 4.4500 - 3.5400 1.00 2802 154 0.1340 0.1646 REMARK 3 3 3.5400 - 3.0900 1.00 2795 146 0.1644 0.1788 REMARK 3 4 3.0900 - 2.8100 1.00 2761 148 0.1801 0.1914 REMARK 3 5 2.8100 - 2.6100 1.00 2746 140 0.1951 0.2717 REMARK 3 6 2.6100 - 2.4500 1.00 2732 138 0.1951 0.2291 REMARK 3 7 2.4500 - 2.3300 1.00 2746 149 0.2001 0.2313 REMARK 3 8 2.3300 - 2.2300 1.00 2730 143 0.2031 0.2737 REMARK 3 9 2.2300 - 2.1400 1.00 2712 140 0.2126 0.2598 REMARK 3 10 2.1400 - 2.0700 1.00 2720 167 0.2202 0.2582 REMARK 3 11 2.0700 - 2.0000 1.00 2715 131 0.2401 0.3015 REMARK 3 12 2.0000 - 1.9500 1.00 2689 142 0.2513 0.2773 REMARK 3 13 1.9500 - 1.8900 1.00 2722 135 0.2690 0.3273 REMARK 3 14 1.8900 - 1.8500 0.99 2686 146 0.2809 0.3359 REMARK 3 15 1.8500 - 1.8100 0.98 2616 150 0.3100 0.3351 REMARK 3 16 1.8100 - 1.7700 0.92 2512 138 0.3457 0.3543 REMARK 3 17 1.7700 - 1.7300 0.81 2171 106 0.3606 0.3955 REMARK 3 18 1.7300 - 1.7000 0.74 2002 122 0.3779 0.4369 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.261 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.708 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.47 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 : 0.007 3571 REMARK 3 ANGLE : 0.975 4883 REMARK 3 CHIRALITY : 0.065 543 REMARK 3 PLANARITY : 0.008 634 REMARK 3 DIHEDRAL : 17.061 1277 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 9PZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298827. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUN-21 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 : 51978 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 39.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 13.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.6600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76 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 (%): 49.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM AMMONIUM ACETATE, 100 MM BIS REMARK 280 -TRIS-HCL, PH 5.5, 25% (W/V) PEG 3350, VAPOR DIFFUSION, SITTING REMARK 280 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 23.48700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.68200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.88050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.68200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.48700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.88050 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: 4440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 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 H 43 CE NZ REMARK 470 LYS H 78 NZ REMARK 470 GLN H 119 CD OE1 NE2 REMARK 470 GLU L 1 CD OE1 OE2 REMARK 470 LYS L 134 CE NZ REMARK 470 LYS L 161 CD CE NZ REMARK 470 LYS L 191 CD CE NZ REMARK 470 ARG L 194 CZ NH1 NH2 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 ARG H 16 -166.78 -100.85 REMARK 500 ARG H 16 -167.50 -100.85 REMARK 500 ASP H 158 66.07 62.08 REMARK 500 ASN L 28 -98.26 -137.71 REMARK 500 ASN L 53 -42.24 76.32 REMARK 500 ASN L 175 -2.52 74.10 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 H 675 DISTANCE = 7.82 ANGSTROMS DBREF 9PZ6 H 1 230 PDB 9PZ6 9PZ6 1 230 DBREF 9PZ6 L 1 217 PDB 9PZ6 9PZ6 1 217 SEQRES 1 H 230 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 230 PRO GLY ARG SER LEU ARG LEU PRO CYS THR ALA SER GLY SEQRES 3 H 230 PHE SER PHE GLY ASP HIS ALA MET SER TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY PHE ILE ARG SEQRES 5 H 230 LYS THR THR TYR GLY ALA THR THR HIS TYR ALA ALA ALA SEQRES 6 H 230 VAL ARG GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 230 SER ILE VAL TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 H 230 ASP THR ALA VAL TYR PHE CYS THR ARG VAL GLN LEU ASP SEQRES 9 H 230 TYR GLY PRO GLY TYR GLN TYR TYR GLY MET ASP VAL TRP SEQRES 10 H 230 GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER THR SEQRES 11 H 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 217 GLU SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 217 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY MET ASN SEQRES 3 L 217 SER ASN ILE GLY ALA GLY TYR ASP VAL TYR TRP TYR GLN SEQRES 4 L 217 GLN LEU PRO GLY ARG ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5 L 217 ASN SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 217 GLY SER ARG SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7 L 217 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8 L 217 SER TYR ASP THR SER LEU ASN GLY TRP ALA PHE GLY GLY SEQRES 9 L 217 GLY THR LYS LEU THR VAL LEU THR GLN PRO LYS ALA ALA SEQRES 10 L 217 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11 L 217 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU VAL SER ASP SEQRES 12 L 217 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13 L 217 GLY SER PRO VAL LYS VAL GLY VAL GLU THR THR LYS PRO SEQRES 14 L 217 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15 L 217 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16 L 217 TYR SER CYS ARG VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17 L 217 LYS THR VAL ALA PRO ALA GLU CYS SER HET PGE H 301 24 HET NA H 302 1 HET PEG L 301 17 HET PGE L 302 24 HETNAM PGE TRIETHYLENE GLYCOL HETNAM NA SODIUM ION HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 3 PGE 2(C6 H14 O4) FORMUL 4 NA NA 1+ FORMUL 5 PEG C4 H10 O3 FORMUL 7 HOH *492(H2 O) HELIX 1 AA1 SER H 28 HIS H 32 5 5 HELIX 2 AA2 LYS H 53 GLY H 57 5 5 HELIX 3 AA3 ALA H 64 ARG H 67 5 4 HELIX 4 AA4 LYS H 89 THR H 93 5 5 HELIX 5 AA5 SER H 141 LYS H 143 5 3 HELIX 6 AA6 SER H 170 ALA H 172 5 3 HELIX 7 AA7 SER H 201 THR H 205 5 5 HELIX 8 AA8 LYS H 215 ASN H 218 5 4 HELIX 9 AA9 ASN L 28 GLY L 32 5 5 HELIX 10 AB1 GLN L 81 GLU L 85 5 5 HELIX 11 AB2 SER L 126 ALA L 132 1 7 HELIX 12 AB3 THR L 186 HIS L 193 1 8 SHEET 1 AA1 4 GLN H 3 GLU H 6 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N VAL H 5 SHEET 3 AA1 4 ILE H 80 MET H 85 -1 O MET H 85 N LEU H 18 SHEET 4 AA1 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 121 VAL H 125 1 O THR H 124 N VAL H 12 SHEET 3 AA2 6 ALA H 94 VAL H 101 -1 N TYR H 96 O THR H 121 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O PHE H 97 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA2 6 THR H 60 TYR H 62 -1 O HIS H 61 N PHE H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 121 VAL H 125 1 O THR H 124 N VAL H 12 SHEET 3 AA3 4 ALA H 94 VAL H 101 -1 N TYR H 96 O THR H 121 SHEET 4 AA3 4 MET H 114 TRP H 117 -1 O VAL H 116 N ARG H 100 SHEET 1 AA4 4 SER H 134 LEU H 138 0 SHEET 2 AA4 4 THR H 149 TYR H 159 -1 O LYS H 157 N SER H 134 SHEET 3 AA4 4 TYR H 190 PRO H 199 -1 O VAL H 198 N ALA H 150 SHEET 4 AA4 4 HIS H 178 THR H 179 -1 N HIS H 178 O VAL H 195 SHEET 1 AA5 4 THR H 145 SER H 146 0 SHEET 2 AA5 4 THR H 149 TYR H 159 -1 O THR H 149 N SER H 146 SHEET 3 AA5 4 TYR H 190 PRO H 199 -1 O VAL H 198 N ALA H 150 SHEET 4 AA5 4 VAL H 183 LEU H 184 -1 N VAL H 183 O SER H 191 SHEET 1 AA6 3 THR H 165 TRP H 168 0 SHEET 2 AA6 3 ILE H 209 HIS H 214 -1 O ASN H 211 N SER H 167 SHEET 3 AA6 3 THR H 219 LYS H 224 -1 O VAL H 221 N VAL H 212 SHEET 1 AA7 5 SER L 9 GLY L 12 0 SHEET 2 AA7 5 THR L 106 VAL L 110 1 O THR L 109 N VAL L 10 SHEET 3 AA7 5 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AA7 5 TYR L 36 GLN L 40 -1 N GLN L 40 O ASP L 87 SHEET 5 AA7 5 LYS L 47 ILE L 50 -1 O LEU L 49 N TRP L 37 SHEET 1 AA8 4 SER L 9 GLY L 12 0 SHEET 2 AA8 4 THR L 106 VAL L 110 1 O THR L 109 N VAL L 10 SHEET 3 AA8 4 ALA L 86 ASP L 94 -1 N ALA L 86 O LEU L 108 SHEET 4 AA8 4 GLY L 99 PHE L 102 -1 O ALA L 101 N SER L 92 SHEET 1 AA9 3 ARG L 17 THR L 23 0 SHEET 2 AA9 3 SER L 72 THR L 78 -1 O ALA L 73 N CYS L 22 SHEET 3 AA9 3 PHE L 64 SER L 69 -1 N SER L 65 O ALA L 76 SHEET 1 AB1 4 SER L 119 PHE L 123 0 SHEET 2 AB1 4 ALA L 135 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AB1 4 TYR L 177 LEU L 185 -1 O ALA L 179 N VAL L 141 SHEET 4 AB1 4 VAL L 164 THR L 166 -1 N GLU L 165 O TYR L 182 SHEET 1 AB2 4 SER L 119 PHE L 123 0 SHEET 2 AB2 4 ALA L 135 PHE L 144 -1 O VAL L 138 N PHE L 123 SHEET 3 AB2 4 TYR L 177 LEU L 185 -1 O ALA L 179 N VAL L 141 SHEET 4 AB2 4 SER L 170 LYS L 171 -1 N SER L 170 O ALA L 178 SHEET 1 AB3 4 SER L 158 VAL L 160 0 SHEET 2 AB3 4 THR L 150 ALA L 155 -1 N ALA L 155 O SER L 158 SHEET 3 AB3 4 TYR L 196 HIS L 202 -1 O ARG L 199 N ALA L 152 SHEET 4 AB3 4 SER L 205 VAL L 211 -1 O SER L 205 N HIS L 202 SSBOND 1 CYS H 22 CYS H 98 1555 1555 2.03 SSBOND 2 CYS H 154 CYS H 210 1555 1555 2.04 SSBOND 3 CYS H 230 CYS L 216 1555 1555 2.04 SSBOND 4 CYS L 22 CYS L 90 1555 1555 2.04 SSBOND 5 CYS L 139 CYS L 198 1555 1555 2.03 LINK NA NA H 302 O HOH H 618 1555 1555 2.84 CISPEP 1 PHE H 160 PRO H 161 0 -6.61 CISPEP 2 GLU H 162 PRO H 163 0 0.55 CISPEP 3 TYR L 145 PRO L 146 0 2.18 CRYST1 46.974 71.761 137.364 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 0.021288 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013935 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007280 0.00000