HEADER IMMUNE SYSTEM 31-DEC-24 9MPX TITLE CRYSTAL STRUCTURE OF RM014, A MACAQUE-DERIVED HIV V2-APEX-TARGETING TITLE 2 ANTIBODY FROM APEXGT6 IMMUNIZATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA; SOURCE 3 ORGANISM_COMMON: MACAQUE; SOURCE 4 ORGANISM_TAXID: 9539; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA; SOURCE 10 ORGANISM_COMMON: MACAQUE; SOURCE 11 ORGANISM_TAXID: 9539; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, GERMLINE-TARGETING VACCINATION, APEXGT6, V2-APEX ANTIBODY, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.AGRAWAL,I.A.WILSON REVDAT 1 24-DEC-25 9MPX 0 JRNL AUTH K.M.MA,H.J.SUTTON,P.P.PRATAP,J.M.STEICHEN,D.CARNATHAN, JRNL AUTH 2 J.QUINN,O.KALYUZHNIY,A.LIGUORI,S.AGRAWAL,S.BABOO,P.MADDEN, JRNL AUTH 3 C.A.COTTRELL,J.R.WILLIS,J.H.LEE,E.LANDAIS,X.HU, JRNL AUTH 4 P.RAMEZANI-RAD,G.OZOROWSKI,V.R.LEWIS,J.K.DIEDRICH,X.ZHOU, JRNL AUTH 5 T.K.ALTHEIDE,N.PHELPS,E.GEORGESON,N.B.ALAVI,D.LU, JRNL AUTH 6 S.ESKANDARZADEH,M.KUBITZ,Y.ADACHI,T.M.MULLEN,M.SILVA, JRNL AUTH 7 M.B.MELO,S.HIMANSU,D.J.IRVINE,D.R.BURTON,J.R.YATES 3RD, JRNL AUTH 8 J.C.PAULSON,D.SOK,I.A.WILSON,G.SILVESTRI,A.B.WARD,S.CROTTY, JRNL AUTH 9 W.R.SCHIEF JRNL TITL HIV BROADLY NEUTRALIZING ANTIBODY PRECURSORS TO THE APEX JRNL TITL 2 EPITOPE INDUCED IN NONHUMAN PRIMATES. JRNL REF SCI IMMUNOL V. 10 T6660 2025 JRNL REFN ESSN 2470-9468 JRNL PMID 40845127 JRNL DOI 10.1126/SCIIMMUNOL.ADT6660 REMARK 2 REMARK 2 RESOLUTION. 1.88 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???) 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) : 1.88 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7 REMARK 3 NUMBER OF REFLECTIONS : 35317 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.191 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.690 REMARK 3 FREE R VALUE TEST SET COUNT : 2011 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 28.9000 - 4.5200 0.98 2484 148 0.1782 0.2041 REMARK 3 2 4.5100 - 3.5900 1.00 2465 152 0.1646 0.2270 REMARK 3 3 3.5900 - 3.1300 1.00 2487 141 0.1859 0.2415 REMARK 3 4 3.1300 - 2.8500 0.97 2367 148 0.1966 0.2510 REMARK 3 5 2.8500 - 2.6400 0.98 2410 147 0.1977 0.2394 REMARK 3 6 2.6400 - 2.4900 0.99 2441 147 0.1910 0.2455 REMARK 3 7 2.4900 - 2.3600 1.00 2445 147 0.1937 0.2392 REMARK 3 8 2.3600 - 2.2600 0.99 2433 141 0.1913 0.2816 REMARK 3 9 2.2600 - 2.1700 1.00 2426 145 0.2080 0.2502 REMARK 3 10 2.1700 - 2.1000 0.96 2353 146 0.2013 0.2736 REMARK 3 11 2.1000 - 2.0300 0.98 2389 148 0.2107 0.2511 REMARK 3 12 2.0300 - 1.9700 0.98 2388 146 0.2154 0.2753 REMARK 3 13 1.9700 - 1.9200 0.97 2343 133 0.2430 0.2748 REMARK 3 14 1.9200 - 1.8800 0.76 1875 122 0.2739 0.2919 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) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.220 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 : 0.008 NULL REMARK 3 ANGLE : 0.861 NULL REMARK 3 CHIRALITY : 0.052 515 REMARK 3 PLANARITY : 0.008 566 REMARK 3 DIHEDRAL : 17.045 1168 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 9MPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291231. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-AUG-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 : 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) : 0.98 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 : 35396 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 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 (%): 46.97 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE 0.1 M TRIS PH REMARK 280 7.0 20% PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.40450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.13500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.40450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.13500 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: 3330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 GLN H 1 REMARK 465 PRO H 95A REMARK 465 ASP H 95B REMARK 465 VAL H 95C REMARK 465 VAL H 95D REMARK 465 ALA H 95E REMARK 465 ASP H 95F REMARK 465 TYR H 95G REMARK 465 GLY H 95H REMARK 465 ASP H 95I REMARK 465 ASP H 95J REMARK 465 TYR H 95K REMARK 465 GLY H 95L REMARK 465 TYR H 95M REMARK 465 HIS H 95N REMARK 465 TYR H 95O REMARK 465 ARG H 95P REMARK 465 PRO H 95Q REMARK 465 GLU H 95R REMARK 465 ASP H 95S REMARK 465 ASN H 95T REMARK 465 CYS H 216 REMARK 465 ASP L 1 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 HE21 GLN H 61 OE1 GLN H 64 1.51 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 PRO H 52A 0.37 -66.14 REMARK 500 ILE H 102 107.10 62.28 REMARK 500 THR H 160 -30.08 -130.45 REMARK 500 ASN L 30 -119.19 51.75 REMARK 500 ALA L 51 -18.71 71.44 REMARK 500 PHE L 52 -4.68 -145.34 REMARK 500 ALA L 84 176.24 176.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MPB RELATED DB: PDB REMARK 900 RELATED ID: 9MPC RELATED DB: PDB DBREF 9MPX H 1 216 PDB 9MPX 9MPX 1 216 DBREF 9MPX L 1 214 PDB 9MPX 9MPX 1 214 SEQRES 1 H 237 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 237 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 237 TYR THR PHE THR VAL HIS ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 237 ALA PRO GLY GLN GLY LEU ASP TRP MET GLY GLY ILE ILE SEQRES 5 H 237 PRO LEU VAL GLY MET THR ASN TYR ALA GLN ARG PHE GLN SEQRES 6 H 237 GLY ARG VAL THR ILE THR ALA ASP THR SER THR THR THR SEQRES 7 H 237 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 237 ALA VAL TYR TYR CYS ALA ARG GLY PRO ASP VAL VAL ALA SEQRES 9 H 237 ASP TYR GLY ASP ASP TYR GLY TYR HIS TYR ARG PRO GLU SEQRES 10 H 237 ASP ASN TYR LEU ASP ILE TRP GLY PRO GLY THR PRO ILE SEQRES 11 H 237 THR ILE SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 12 H 237 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 13 H 237 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 14 H 237 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 15 H 237 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 16 H 237 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 17 H 237 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 18 H 237 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 19 H 237 LYS SER CYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLU ASN VAL ASN ASN CYS LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA PHE SEQRES 5 L 214 THR LEU GLN ASN GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE THR SER LEU SEQRES 7 L 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS SER SEQRES 8 L 214 TYR GLY SER PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *142(H2 O) HELIX 1 AA1 THR H 28 HIS H 32 5 5 HELIX 2 AA2 GLN H 61 GLN H 64 5 4 HELIX 3 AA3 THR H 73 THR H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 127 LYS H 129 5 3 HELIX 6 AA6 SER H 156 ALA H 158 5 3 HELIX 7 AA7 SER H 187 LEU H 189 5 3 HELIX 8 AA8 LYS H 201 ASN H 204 5 4 HELIX 9 AA9 GLN L 79 VAL L 83 5 5 HELIX 10 AB1 SER L 121 SER L 127 1 7 HELIX 11 AB2 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 ILE H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 ARG H 94 -1 N ALA H 88 O ILE H 109 SHEET 4 AA2 6 ILE H 34 ALA H 40 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLY H 44 ILE H 52 -1 O ASP H 46 N ARG H 38 SHEET 6 AA2 6 MET H 56 TYR H 59 -1 O MET H 56 N ILE H 52 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 ILE H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 ARG H 94 -1 N ALA H 88 O ILE H 109 SHEET 4 AA3 4 ASP H 101 TRP H 103 -1 O ILE H 102 N ARG 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 GLY H 139 N LEU H 124 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 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 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 ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 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 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N HIS L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 THR L 53 LEU L 54 -1 O THR 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 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N HIS L 90 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 LEU L 179 N VAL L 132 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 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.08 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.09 CISPEP 1 PHE H 146 PRO H 147 0 -7.64 CISPEP 2 GLU H 148 PRO H 149 0 -3.25 CISPEP 3 SER L 7 PRO L 8 0 -6.62 CISPEP 4 SER L 94 PRO L 95 0 -3.98 CISPEP 5 TYR L 140 PRO L 141 0 1.69 CRYST1 98.809 60.270 81.995 90.00 112.89 90.00 C 1 2 1 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 0.010121 0.000000 0.004272 0.00000 SCALE2 0.000000 0.016592 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013238 0.00000