HEADER IMMUNE SYSTEM 10-OCT-23 8UIG TITLE ANTI-PHOSPHOHISTIDINE FAB HSC44.CK.20 WITH 3PHIS PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HSC44.CK.20 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: FAB HEAVY CHAIN; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HSC44.CK.20 FAB LIGHT CHAIN; COMPND 8 CHAIN: L; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: FAB LIGHT CHAIN; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 3PHIS PEPTIDE; COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 8 ORGANISM_TAXID: 9986; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 14 ORGANISM_TAXID: 32630 KEYWDS ANTI-PHOSPHOHISTIDINE ANTIBODY POST-TRANSLATIONAL MODIFICATION KEYWDS 2 ANTIBODY HUMANIZATION, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.KALAGIRI,R.L.STANFIELD,T.HUNTER,I.A.WILSON REVDAT 1 19-MAR-25 8UIG 0 JRNL AUTH G.D.MARTYN,R.KALAGIRI,G.VEGGIANI,R.L.STANFIELD,I.CHOUDHURI, JRNL AUTH 2 M.SALA,J.MEISENHELDER,C.CHEN,A.BISWAS,R.M.LEVY,D.LYUMKIS, JRNL AUTH 3 I.A.WILSON,T.HUNTER,S.S.SIDHU JRNL TITL USING PHAGE DISPLAY FOR RATIONAL ENGINEERING OF A HIGHER JRNL TITL 2 AFFINITY HUMANIZED 3' PHOSPHOHISTIDINE-SPECIFIC ANTIBODY. JRNL REF BIORXIV 2024 JRNL REFN ISSN 2692-8205 JRNL PMID 39574610 JRNL DOI 10.1101/2024.11.04.621849 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9 REMARK 3 NUMBER OF REFLECTIONS : 33283 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.213 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 1721 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 34.8200 - 4.3500 0.98 2758 142 0.1402 0.1853 REMARK 3 2 4.3500 - 3.4500 0.96 2644 153 0.1432 0.1633 REMARK 3 3 3.4500 - 3.0200 0.98 2726 131 0.1821 0.2294 REMARK 3 4 3.0200 - 2.7400 0.99 2711 130 0.1806 0.2448 REMARK 3 5 2.7400 - 2.5400 0.99 2702 170 0.1875 0.2189 REMARK 3 6 2.5400 - 2.3900 0.95 2603 151 0.1842 0.2248 REMARK 3 7 2.3900 - 2.2700 0.99 2660 154 0.1809 0.2108 REMARK 3 8 2.2700 - 2.1800 0.98 2649 183 0.1839 0.2528 REMARK 3 9 2.1800 - 2.0900 0.98 2689 135 0.1834 0.2236 REMARK 3 10 2.0900 - 2.0200 0.98 2693 129 0.2020 0.2301 REMARK 3 11 2.0200 - 1.9600 0.95 2611 131 0.2195 0.2665 REMARK 3 12 1.9600 - 1.9000 0.78 2116 112 0.2389 0.2791 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) : 0.204 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.960 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.88 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.57 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 : 0.005 3409 REMARK 3 ANGLE : 0.769 4637 REMARK 3 CHIRALITY : 0.049 522 REMARK 3 PLANARITY : 0.005 592 REMARK 3 DIHEDRAL : 14.288 1204 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 8UIG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000277407. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-JUN-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 : BL12-1 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33299 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 34.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.16200 REMARK 200 R SYM (I) : 0.16200 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) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 1.20000 REMARK 200 R SYM FOR SHELL (I) : 1.20000 REMARK 200 FOR SHELL : 1.800 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M TRI-POTASSIUM CITRATE, 20% PEG REMARK 280 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.30250 REMARK 290 SMTRY3 2 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 THR H 221 REMARK 465 ALA C 1 REMARK 465 GLY C 2 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 L 29 16.76 57.66 REMARK 500 ILE L 51 -52.37 72.59 REMARK 500 ALA L 84 173.07 173.84 REMARK 500 ASN L 138 72.19 56.80 REMARK 500 REMARK 500 REMARK: NULL DBREF 8UIG H 1 221 PDB 8UIG 8UIG 1 221 DBREF 8UIG L 1 212 PDB 8UIG 8UIG 1 212 DBREF 8UIG C 1 9 PDB 8UIG 8UIG 1 9 SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS THR ALA SER GLY SEQRES 3 H 225 PHE SER ILE ASP SER TYR GLY PHE SER TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU HIS ILE GLY TYR LEU THR SEQRES 5 H 225 ALA GLY GLY ARG ALA PHE TYR ALA SER TRP ALA LYS SER SEQRES 6 H 225 ARG SER THR ILE THR ARG ASN THR ASN GLU ASN THR VAL SEQRES 7 H 225 THR LEU LYS MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 225 VAL TYR TYR CYS ALA LYS LEU GLY THR GLY SER ARG PHE SEQRES 9 H 225 ALA ILE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 H 225 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 H 225 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 H 225 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 H 225 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 H 225 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 H 225 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 H 225 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 H 225 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 18 H 225 LYS THR HIS THR SEQRES 1 L 218 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 218 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 218 GLN SER VAL TRP ARG ASN LYS ASN VAL ALA TRP TYR GLN SEQRES 4 L 218 GLN LYS PRO GLY LYS ALA PRO LYS ARG LEU ILE TYR ALA SEQRES 5 L 218 ILE ALA SER LEU TYR SER GLY VAL PRO SER ARG PHE SER SEQRES 6 L 218 GLY SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SEQRES 7 L 218 SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS VAL SEQRES 8 L 218 GLY HIS TYR GLY SER GLU ASN ASP ALA TYR TYR ALA PHE SEQRES 9 L 218 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 L 218 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 218 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 218 ASN PHE TYR PRO ARG GLU ALA LYS VAL SER TRP TYR VAL SEQRES 13 L 218 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 218 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 218 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 218 LYS VAL TYR ALA CYS GLU VAL THR GLN GLY THR THR SER SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 9 ALA GLY ALA GLY NEP ALA GLY ALA GLY HET NEP C 5 19 HETNAM NEP N1-PHOSPHONOHISTIDINE FORMUL 3 NEP C6 H10 N3 O5 P FORMUL 4 HOH *187(H2 O) HELIX 1 AA1 SER H 28 TYR H 32 5 5 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 GLY H 190 5 4 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 VAL L 27B LYS L 31 5 5 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 LYS L 126 1 6 HELIX 9 AA9 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 SER H 67 ASN H 72 -1 N THR H 70 O THR H 79 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 LYS H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 PHE H 34 GLN H 39 -1 N SER H 35 O ALA H 93 SHEET 5 AA2 6 LEU H 45 LEU H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 ALA H 57 TYR H 59 -1 O PHE H 58 N TYR H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 LYS H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 ILE H 102 TRP H 103 -1 O ILE H 102 N LYS H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA8 6 ALA L 84 SER L 94 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 VAL L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA9 4 ALA L 84 SER L 94 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 ASP L 95B PHE L 98 -1 O TYR L 95D N TYR L 92 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 GLN L 198 -1 O ALA L 193 N TYR L 149 SHEET 4 AB2 4 THR L 201 ASN L 208 -1 O VAL L 203 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 LINK C GLY C 4 N NEP C 5 1555 1555 1.33 LINK C NEP C 5 N ALA C 6 1555 1555 1.33 CISPEP 1 PHE H 146 PRO H 147 0 -6.37 CISPEP 2 GLU H 148 PRO H 149 0 -1.53 CISPEP 3 SER L 7 PRO L 8 0 -3.24 CISPEP 4 TYR L 140 PRO L 141 0 0.42 CRYST1 44.111 72.605 70.325 90.00 98.21 90.00 P 1 21 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 0.022670 0.000000 0.003270 0.00000 SCALE2 0.000000 0.013773 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014367 0.00000