HEADER IMMUNE SYSTEM 26-MAR-24 8YTO TITLE SINGLE-CHAIN FV ANTIBODY OF E11 COMPLEX WITH NP-GLYCINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SINGLE-CHAIN FV ANTIBODY OF E11; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIGEN BINDING, AFFINITY MATURATION, SOMATIC HYPERMUTATION, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.YOSHIDA,Y.HANAZONO,N.NUMOTO,N.ITO,M.ODA JRNL AUTH M.YOSHIDA,Y.HANAZONO,N.NUMOTO,S.NAGAO,S.YABUNO,Y.KITAGAWA, JRNL AUTH 2 H.SEKIGUCHI,N.ITO,T.AZUMA,M.ODA JRNL TITL AFFINITY-MATURED ANTIBODY WITH A DISULFIDE BOND IN H-CDR3 JRNL TITL 2 LOOP. JRNL REF ARCH.BIOCHEM.BIOPHYS. 10068 2024 JRNL REFN ESSN 1096-0384 JRNL PMID 38909835 JRNL DOI 10.1016/J.ABB.2024.110068 REMARK 2 REMARK 2 RESOLUTION. 1.04 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) : 1.04 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 108777 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.108 REMARK 3 R VALUE (WORKING SET) : 0.107 REMARK 3 FREE R VALUE : 0.124 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 5431 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 40.4300 - 3.2300 1.00 3795 199 0.1391 0.1350 REMARK 3 2 3.2300 - 2.5600 1.00 3591 189 0.1314 0.1448 REMARK 3 3 2.5600 - 2.2400 1.00 3566 188 0.1208 0.1329 REMARK 3 4 2.2400 - 2.0400 1.00 3568 188 0.1101 0.1179 REMARK 3 5 2.0400 - 1.8900 1.00 3500 184 0.0979 0.1248 REMARK 3 6 1.8900 - 1.7800 1.00 3506 184 0.0977 0.1128 REMARK 3 7 1.7800 - 1.6900 1.00 3497 185 0.0941 0.1168 REMARK 3 8 1.6900 - 1.6200 1.00 3489 183 0.0895 0.1221 REMARK 3 9 1.6200 - 1.5500 1.00 3510 183 0.0889 0.1030 REMARK 3 10 1.5500 - 1.5000 1.00 3480 184 0.0864 0.1199 REMARK 3 11 1.5000 - 1.4500 1.00 3449 181 0.0846 0.1071 REMARK 3 12 1.4500 - 1.4100 1.00 3462 183 0.0844 0.0960 REMARK 3 13 1.4100 - 1.3700 1.00 3496 184 0.0817 0.0977 REMARK 3 14 1.3700 - 1.3400 1.00 3401 179 0.0848 0.1133 REMARK 3 15 1.3400 - 1.3100 1.00 3508 185 0.0889 0.1076 REMARK 3 16 1.3100 - 1.2800 1.00 3457 180 0.0894 0.1325 REMARK 3 17 1.2800 - 1.2600 1.00 3445 180 0.0913 0.1137 REMARK 3 18 1.2600 - 1.2300 1.00 3432 182 0.0911 0.1186 REMARK 3 19 1.2300 - 1.2100 1.00 3455 180 0.0882 0.1018 REMARK 3 20 1.2100 - 1.1900 1.00 3424 179 0.0874 0.1092 REMARK 3 21 1.1900 - 1.1700 1.00 3478 184 0.0910 0.1052 REMARK 3 22 1.1700 - 1.1500 0.99 3384 178 0.0909 0.1200 REMARK 3 23 1.1500 - 1.1400 1.00 3433 180 0.0966 0.1088 REMARK 3 24 1.1400 - 1.1200 1.00 3413 179 0.0953 0.1189 REMARK 3 25 1.1200 - 1.1100 0.97 3402 179 0.0938 0.1165 REMARK 3 26 1.1100 - 1.0900 0.99 3350 175 0.0984 0.1217 REMARK 3 27 1.0900 - 1.0800 0.97 3379 177 0.1043 0.1228 REMARK 3 28 1.0800 - 1.0600 0.96 3293 174 0.1165 0.1609 REMARK 3 29 1.0600 - 1.0500 0.93 3193 167 0.1509 0.1723 REMARK 3 30 1.0500 - 1.0400 0.87 2990 158 0.1775 0.2070 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) : 0.060 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 9.820 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 : 0.011 2349 REMARK 3 ANGLE : 1.285 3255 REMARK 3 CHIRALITY : 0.093 345 REMARK 3 PLANARITY : 0.012 426 REMARK 3 DIHEDRAL : 15.542 886 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 8YTO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ. REMARK 100 THE DEPOSITION ID IS D_1300046353. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAY-23 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 : SPRING-8 REMARK 200 BEAMLINE : BL45XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109128 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.040 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 (%) : 99.1 REMARK 200 DATA REDUNDANCY : 70.40 REMARK 200 R MERGE (I) : 0.21600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.04 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2 REMARK 200 DATA REDUNDANCY IN SHELL : 54.60 REMARK 200 R MERGE FOR SHELL (I) : 1.44400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 8.800 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: 6K4Z REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 10% V/V 2 REMARK 280 -PROPANOL, 20% W/V POLYETHYLENE GLYCOL 4000, VAPOR DIFFUSION, REMARK 280 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 16.79500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.86000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.78500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.86000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.79500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.78500 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 GLY A 116 REMARK 465 GLY A 117 REMARK 465 GLY A 118 REMARK 465 SER A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 GLY A 122 REMARK 465 GLY A 123 REMARK 465 SER A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 GLY A 127 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 ASP A 46 22.16 106.31 REMARK 500 HIS A 47 51.80 38.82 REMARK 500 ASN A 56 -44.91 73.25 REMARK 500 SER A 98 -51.35 71.50 REMARK 500 SER A 98 -46.22 66.69 REMARK 500 ASN A 99 11.01 -149.55 REMARK 500 ARG A 172 -163.43 -117.30 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 A 835 DISTANCE = 6.79 ANGSTROMS REMARK 525 HOH A 836 DISTANCE = 8.10 ANGSTROMS REMARK 525 HOH A 837 DISTANCE = 8.16 ANGSTROMS DBREF 8YTO A 1 248 PDB 8YTO 8YTO 1 248 SEQRES 1 A 248 GLY SER ALA GLN ALA VAL VAL THR GLN GLU SER ALA LEU SEQRES 2 A 248 THR THR SER PRO GLY GLU THR VAL THR LEU THR CYS ARG SEQRES 3 A 248 SER SER THR GLY ALA VAL ILE SER SER ASN PHE VAL SER SEQRES 4 A 248 TRP VAL GLN GLU LYS PRO ASP HIS LEU PHE THR GLY LEU SEQRES 5 A 248 ILE GLY GLY ASN LYS ASN ARG ALA PRO GLY VAL PRO ALA SEQRES 6 A 248 ARG PHE SER GLY SER LEU ILE GLY ASP LYS ALA VAL LEU SEQRES 7 A 248 THR ILE THR GLY ALA GLN THR GLU ASP GLU ALA ILE TYR SEQRES 8 A 248 PHE CYS ALA LEU TRP TYR SER ASN HIS TRP VAL PHE GLY SEQRES 9 A 248 GLY GLY THR LYS LEU THR VAL LEU GLY GLN GLY GLY GLY SEQRES 10 A 248 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLN SEQRES 11 A 248 VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU ALA LYS PRO SEQRES 12 A 248 GLY ALA SER VAL GLN LEU SER CYS LYS GLY SER GLY TYR SEQRES 13 A 248 THR PHE PRO ASN TYR TRP MET HIS TRP VAL THR GLN ARG SEQRES 14 A 248 PRO GLY ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP PRO SEQRES 15 A 248 ASN SER GLY PHE ILE ARG TYR ASP GLU ARG PHE LYS THR SEQRES 16 A 248 LYS ALA THR LEU THR VAL ASP LYS PRO SER SER THR ALA SEQRES 17 A 248 TYR MET GLN LEU SER SER LEU THR SER ASP ASP SER ALA SEQRES 18 A 248 VAL TYR PHE CYS ALA ARG GLY CYS TYR GLY CYS ILE HIS SEQRES 19 A 248 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 20 A 248 SER HET LZO A 401 27 HET GOL A 402 28 HET GOL A 403 14 HET GOL A 404 28 HET EPE A 405 36 HETNAM GOL GLYCEROL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EPE HEPES FORMUL 2 LZO FORMUL 3 GOL 3(C3 H8 O3) FORMUL 6 EPE C8 H18 N2 O4 S FORMUL 7 HOH *337(H2 O) HELIX 1 AA1 ILE A 33 PHE A 37 5 5 HELIX 2 AA2 GLN A 84 GLU A 88 5 5 HELIX 3 AA3 THR A 157 TYR A 161 5 5 HELIX 4 AA4 THR A 216 SER A 220 5 5 SHEET 1 AA1 4 VAL A 7 GLN A 9 0 SHEET 2 AA1 4 THR A 20 SER A 27 -1 O ARG A 26 N THR A 8 SHEET 3 AA1 4 LYS A 75 THR A 81 -1 O LEU A 78 N LEU A 23 SHEET 4 AA1 4 PHE A 67 ILE A 72 -1 N SER A 70 O VAL A 77 SHEET 1 AA2 6 ALA A 12 THR A 15 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N THR A 15 SHEET 3 AA2 6 ALA A 89 TRP A 96 -1 N ALA A 89 O LEU A 109 SHEET 4 AA2 6 SER A 39 LYS A 44 -1 N GLU A 43 O ILE A 90 SHEET 5 AA2 6 LEU A 48 GLY A 54 -1 O LEU A 52 N TRP A 40 SHEET 6 AA2 6 ASN A 58 ARG A 59 -1 O ASN A 58 N GLY A 54 SHEET 1 AA3 4 ALA A 12 THR A 15 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N THR A 15 SHEET 3 AA3 4 ALA A 89 TRP A 96 -1 N ALA A 89 O LEU A 109 SHEET 4 AA3 4 TRP A 101 PHE A 103 -1 O VAL A 102 N LEU A 95 SHEET 1 AA4 4 GLN A 132 GLN A 134 0 SHEET 2 AA4 4 VAL A 147 SER A 154 -1 O SER A 154 N GLN A 132 SHEET 3 AA4 4 THR A 207 LEU A 212 -1 O ALA A 208 N CYS A 151 SHEET 4 AA4 4 ALA A 197 ASP A 202 -1 N THR A 200 O TYR A 209 SHEET 1 AA5 6 ALA A 138 ALA A 141 0 SHEET 2 AA5 6 THR A 242 VAL A 246 1 O THR A 243 N GLU A 139 SHEET 3 AA5 6 ALA A 221 GLY A 228 -1 N ALA A 221 O LEU A 244 SHEET 4 AA5 6 TRP A 162 GLN A 168 -1 N HIS A 164 O ALA A 226 SHEET 5 AA5 6 LEU A 174 ILE A 180 -1 O ILE A 177 N TRP A 165 SHEET 6 AA5 6 ILE A 187 TYR A 189 -1 O ARG A 188 N ARG A 179 SSBOND 1 CYS A 25 CYS A 93 1555 1555 2.06 SSBOND 2 CYS A 151 CYS A 225 1555 1555 2.04 SSBOND 3 CYS A 229 CYS A 232 1555 1555 2.03 CRYST1 33.590 41.570 161.720 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 0.029771 0.000000 0.000000 0.00000 SCALE2 0.000000 0.024056 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006184 0.00000