HEADER IMMUNE SYSTEM 09-MAY-20 6WX1 TITLE ANTIGEN BINDING FRAGMENT OF OKT9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: OKT9 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: OKT9 FAB HEAVY CHAIN; COMPND 6 CHAIN: H SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 ATCC: CRL-8021; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 ATCC: CRL-8021 KEYWDS ANTI-HUTFR1, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.A.RODRIGUEZ,G.HELGUERA,M.SAWAYA,D.CASCIO,M.COLLAZO,M.FLORES,S.ZINK, AUTHOR 2 S.FERRERO,C.PAYES,D.FUENTES,C.SHORT REVDAT 1 26-MAY-21 6WX1 0 JRNL AUTH J.A.RODRIGUEZ,G.HELGUERA,M.SAWAYA,D.CASCIO,M.COLLAZO, JRNL AUTH 2 M.FLORES,S.ZINK,S.FERRERO,C.PAYES,D.FUENTES,C.SHORT JRNL TITL STRUCTURAL BASIS FOR ANTIBODY-BASED INHIBITION OF NEW WORLD JRNL TITL 2 HEMORRHAGIC FEVER MAMMARENAVIRUS INFECTION ACHIEVED BY JRNL TITL 3 STERIC OCCLUSION OF THE HUMAN TRANSFERRIN RECEPTOR 1 APICAL JRNL TITL 4 DOMAIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 30471 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3048 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 48.8200 - 5.6000 0.99 1382 154 0.1921 0.2148 REMARK 3 2 5.6000 - 4.4500 1.00 1296 144 0.1625 0.1972 REMARK 3 3 4.4500 - 3.8900 1.00 1287 143 0.1682 0.2428 REMARK 3 4 3.8900 - 3.5300 1.00 1271 142 0.1919 0.2042 REMARK 3 5 3.5300 - 3.2800 1.00 1259 139 0.2124 0.2321 REMARK 3 6 3.2800 - 3.0800 0.99 1238 138 0.2227 0.2563 REMARK 3 7 3.0800 - 2.9300 1.00 1242 138 0.2433 0.2534 REMARK 3 8 2.9300 - 2.8000 1.00 1265 141 0.2415 0.2716 REMARK 3 9 2.8000 - 2.6900 0.99 1236 137 0.2590 0.2889 REMARK 3 10 2.6900 - 2.6000 1.00 1235 137 0.2623 0.3348 REMARK 3 11 2.6000 - 2.5200 1.00 1246 139 0.2604 0.2822 REMARK 3 12 2.5200 - 2.4500 1.00 1233 137 0.2533 0.3319 REMARK 3 13 2.4500 - 2.3800 1.00 1238 137 0.2755 0.2918 REMARK 3 14 2.3800 - 2.3300 0.99 1246 139 0.2625 0.3167 REMARK 3 15 2.3300 - 2.2700 0.99 1198 133 0.2600 0.3010 REMARK 3 16 2.2700 - 2.2200 0.99 1259 140 0.2472 0.2625 REMARK 3 17 2.2200 - 2.1800 0.98 1202 134 0.2485 0.3040 REMARK 3 18 2.1800 - 2.1400 0.99 1205 134 0.2652 0.3353 REMARK 3 19 2.1400 - 2.1000 1.00 1237 137 0.2589 0.3030 REMARK 3 20 2.1000 - 2.0600 0.99 1205 134 0.2794 0.3596 REMARK 3 21 2.0600 - 2.0300 0.99 1222 136 0.2922 0.3561 REMARK 3 22 2.0300 - 2.0000 0.98 1221 135 0.2860 0.3114 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.020 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 40.63 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.29 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 6WX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1000249132. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-19 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 : APS REMARK 200 BEAMLINE : 21-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30479 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 48.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 5.058 REMARK 200 R MERGE (I) : 0.05700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.6600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.09 REMARK 200 R MERGE FOR SHELL (I) : 0.60000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.120 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: OKT9_FAB_P22121_REFINE_13.PDB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS, 190MM MAGNESIUM CHLORIDE, REMARK 280 26% (W/V) PEG 8,000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 47.33000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.98000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.33000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.98000 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: 4240 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 348 LIES ON A SPECIAL POSITION. 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 H 102 REMARK 465 ALA H 136 REMARK 465 GLN H 137 REMARK 465 THR H 138 REMARK 465 ASN H 139 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 SER L 209 OG REMARK 470 GLN H 3 CG CD OE1 NE2 REMARK 470 MET H 18 SD CE REMARK 470 LYS H 67 CG CD CE NZ REMARK 470 SER H 101 OG REMARK 470 TYR H 103 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR H 103 OH REMARK 470 ALA H 135 CB REMARK 470 SER H 140 CB OG REMARK 470 GLN H 177 CG CD OE1 NE2 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 LEU L 53 -62.06 -98.43 REMARK 500 ALA L 57 -31.24 69.94 REMARK 500 ASN L 144 75.60 58.90 REMARK 500 GLN L 162 -70.07 -98.18 REMARK 500 LYS L 175 -33.89 -132.84 REMARK 500 ASN L 196 -43.38 -135.73 REMARK 500 ILE H 77 48.33 35.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 303 DBREF 6WX1 L 1 219 PDB 6WX1 6WX1 1 219 DBREF 6WX1 H 1 219 PDB 6WX1 6WX1 1 219 SEQRES 1 L 219 ASP ILE VAL MET THR GLN SER PRO SER SER LEU THR VAL SEQRES 2 L 219 THR ALA GLY GLU ARG VAL THR MET SER CYS LYS SER SER SEQRES 3 L 219 GLN SER LEU PHE ASN SER ALA ASN GLN GLU ASN TYR LEU SEQRES 4 L 219 THR TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 219 LEU ILE TYR TRP ALA SER THR ARG ASP SER GLY VAL PRO SEQRES 6 L 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 219 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 L 219 TYR TYR CYS GLN ASN ASP TYR SER TYR PRO LEU THR PHE SEQRES 9 L 219 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 L 219 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 L 219 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 L 219 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 L 219 GLU GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 L 219 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 L 219 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 L 219 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 L 219 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU SEQRES 1 H 219 GLN ILE GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 219 PRO GLY THR SER MET ASN ILE SER CYS LYS ALA SER GLY SEQRES 3 H 219 TYR THR PHE THR ASN TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 219 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR SEQRES 5 H 219 PRO GLY ASP GLY ASN THR HIS TYR ASN GLU LYS PHE LYS SEQRES 6 H 219 GLY LYS THR THR LEU THR ALA ASP THR SER SER ILE THR SEQRES 7 H 219 ALA TYR MET LEU LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 219 ALA VAL TYR PHE CYS ALA ARG ASP ASN SER GLY TYR VAL SEQRES 9 H 219 GLY PHE PRO TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 H 219 SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU SEQRES 11 H 219 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR SEQRES 12 H 219 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 H 219 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 H 219 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 H 219 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SEQRES 16 H 219 SER ASP THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 H 219 SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG HET GOL H 301 6 HET GOL H 302 6 HET GOL H 303 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 3(C3 H8 O3) FORMUL 6 HOH *146(H2 O) HELIX 1 AA1 GLN L 85 LEU L 89 5 5 HELIX 2 AA2 SER L 127 THR L 132 1 6 HELIX 3 AA3 LYS L 189 ARG L 194 1 6 HELIX 4 AA4 THR H 28 TYR H 32 5 5 HELIX 5 AA5 ASN H 61 GLY H 66 1 6 HELIX 6 AA6 THR H 87 SER H 91 5 5 HELIX 7 AA7 SER H 162 SER H 164 5 3 SHEET 1 AA1 4 MET L 4 SER L 7 0 SHEET 2 AA1 4 VAL L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AA1 4 ASP L 76 ILE L 81 -1 O PHE L 77 N CYS L 23 SHEET 4 AA1 4 PHE L 68 SER L 73 -1 N THR L 69 O THR L 80 SHEET 1 AA2 6 SER L 10 THR L 14 0 SHEET 2 AA2 6 THR L 108 LYS L 113 1 O LYS L 109 N LEU L 11 SHEET 3 AA2 6 ALA L 90 ASN L 96 -1 N ALA L 90 O LEU L 110 SHEET 4 AA2 6 LEU L 39 GLN L 44 -1 N TYR L 42 O TYR L 93 SHEET 5 AA2 6 LYS L 51 TYR L 55 -1 O ILE L 54 N TRP L 41 SHEET 6 AA2 6 THR L 59 ARG L 60 -1 O THR L 59 N TYR L 55 SHEET 1 AA3 4 SER L 10 THR L 14 0 SHEET 2 AA3 4 THR L 108 LYS L 113 1 O LYS L 109 N LEU L 11 SHEET 3 AA3 4 ALA L 90 ASN L 96 -1 N ALA L 90 O LEU L 110 SHEET 4 AA3 4 THR L 103 PHE L 104 -1 O THR L 103 N ASN L 96 SHEET 1 AA4 2 PHE L 30 ASN L 31 0 SHEET 2 AA4 2 GLU L 36 ASN L 37 -1 O GLU L 36 N ASN L 31 SHEET 1 AA5 4 THR L 120 PHE L 124 0 SHEET 2 AA5 4 GLY L 135 PHE L 145 -1 O PHE L 141 N SER L 122 SHEET 3 AA5 4 TYR L 179 THR L 188 -1 O LEU L 185 N VAL L 138 SHEET 4 AA5 4 VAL L 165 TRP L 169 -1 N LEU L 166 O THR L 184 SHEET 1 AA6 4 SER L 159 ARG L 161 0 SHEET 2 AA6 4 ASN L 151 ILE L 156 -1 N ILE L 156 O SER L 159 SHEET 3 AA6 4 SER L 197 THR L 203 -1 O GLU L 201 N LYS L 153 SHEET 4 AA6 4 ILE L 211 ASN L 216 -1 O ILE L 211 N ALA L 202 SHEET 1 AA7 4 GLN H 3 GLN H 6 0 SHEET 2 AA7 4 MET H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA7 4 THR H 78 LEU H 83 -1 O LEU H 83 N MET H 18 SHEET 4 AA7 4 THR H 68 ASP H 73 -1 N THR H 69 O LEU H 82 SHEET 1 AA8 6 GLU H 10 VAL H 12 0 SHEET 2 AA8 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA8 6 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115 SHEET 4 AA8 6 MET H 34 GLN H 39 -1 N HIS H 35 O ALA H 97 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA8 6 THR H 58 TYR H 60 -1 O HIS H 59 N TRP H 50 SHEET 1 AA9 4 GLU H 10 VAL H 12 0 SHEET 2 AA9 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA9 4 ALA H 92 ARG H 98 -1 N ALA H 92 O VAL H 115 SHEET 4 AA9 4 TYR H 108 TRP H 109 -1 O TYR H 108 N ARG H 98 SHEET 1 AB1 4 SER H 126 LEU H 130 0 SHEET 2 AB1 4 MET H 141 TYR H 151 -1 O LEU H 147 N TYR H 128 SHEET 3 AB1 4 LEU H 180 PRO H 190 -1 O VAL H 187 N LEU H 144 SHEET 4 AB1 4 VAL H 169 THR H 171 -1 N HIS H 170 O SER H 186 SHEET 1 AB2 4 SER H 126 LEU H 130 0 SHEET 2 AB2 4 MET H 141 TYR H 151 -1 O LEU H 147 N TYR H 128 SHEET 3 AB2 4 LEU H 180 PRO H 190 -1 O VAL H 187 N LEU H 144 SHEET 4 AB2 4 VAL H 175 GLN H 177 -1 N GLN H 177 O LEU H 180 SHEET 1 AB3 3 THR H 157 TRP H 160 0 SHEET 2 AB3 3 THR H 200 HIS H 205 -1 O ASN H 202 N THR H 159 SHEET 3 AB3 3 THR H 210 LYS H 215 -1 O THR H 210 N HIS H 205 SSBOND 1 CYS L 23 CYS L 94 1555 1555 2.04 SSBOND 2 CYS L 140 CYS L 200 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 4 CYS H 146 CYS H 201 1555 1555 2.08 CISPEP 1 SER L 7 PRO L 8 0 -5.55 CISPEP 2 TYR L 100 PRO L 101 0 -2.43 CISPEP 3 TYR L 146 PRO L 147 0 3.43 CISPEP 4 PHE H 152 PRO H 153 0 -2.11 CISPEP 5 GLU H 154 PRO H 155 0 -2.28 CISPEP 6 TRP H 194 PRO H 195 0 2.14 SITE 1 AC1 6 GLU H 154 PRO H 155 VAL H 156 PRO H 173 SITE 2 AC1 6 ALA H 174 LEU H 183 SITE 1 AC2 6 ARG H 38 LYS H 63 PHE H 64 GLU H 89 SITE 2 AC2 6 ASP H 90 HOH H 441 SITE 1 AC3 2 ASN H 19 HOH H 404 CRYST1 94.660 113.960 40.840 90.00 90.00 90.00 P 21 21 2 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 0.010564 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008775 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024486 0.00000