HEADER IMMUNE SYSTEM 08-DEC-23 8RDF TITLE CRYSTAL STRUCTURE OF HAEMOPHILUS INFLUENZAE TYPE B (HIB) DP3 TITLE 2 OLIGOSACCHARIDE BOUND TO FAB CA4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB CA4 H CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB CA4 L CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIGEN, ANTIBODY, CARBOHYDRATE, HAEMOPHILUS INFLUENZAE TYPE B, HIB, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR F.NONNE,L.DELLO IACONO JRNL AUTH F.NONNE,L.D.IACONO,S.BERTUZZI,L.UNIONE,D.PROIETTI,N.NORAIS, JRNL AUTH 2 I.MARGARIT,R.ADAMO,J.JIMENEZ-BARBERO,F.CARBONI,M.R.ROMANO JRNL TITL A MULTIDISCIPLINARY STRUCTURAL APPROACH TO THE JRNL TITL 2 IDENTIFICATION OF THE HAEMOPHILUS INFLUENZAE TYPE B CAPSULAR JRNL TITL 3 POLYSACCHARIDE PROTECTIVE EPITOPE JRNL REF ACS CENT.SCI. 2024 JRNL REFN ESSN 2374-7951 JRNL DOI 10.1021/ACSCENTSCI.3C01515 REMARK 2 REMARK 2 RESOLUTION. 2.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.15.2_3472 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) : 2.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 14988 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 757 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 65.6400 - 4.6800 0.92 2885 130 0.1971 0.2227 REMARK 3 2 4.6800 - 3.7200 0.96 2862 148 0.1875 0.2527 REMARK 3 3 3.7200 - 3.2500 0.95 2816 143 0.2386 0.2802 REMARK 3 4 3.2500 - 2.9500 0.97 2833 174 0.2797 0.3491 REMARK 3 5 2.9500 - 2.7400 0.98 2835 162 0.3272 0.3597 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) : 0.357 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.608 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 44.02 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.62 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 : 0.003 3425 REMARK 3 ANGLE : 0.690 4675 REMARK 3 CHIRALITY : 0.048 548 REMARK 3 PLANARITY : 0.005 585 REMARK 3 DIHEDRAL : 20.600 1248 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 8RDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292135224. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-OCT-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : MASSIF-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.965 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15060 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740 REMARK 200 RESOLUTION RANGE LOW (A) : 65.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.18000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.94000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 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 (%): 60.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M NICKEL(II) CHLORIDE HEXAHYDRATE, REMARK 280 0.1M TRIS PH 8.5, 20% W/V PEG 2000 MME, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 72.48200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.48200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.46400 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.64400 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.46400 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.64400 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.48200 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.46400 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.64400 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.48200 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.46400 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.64400 REMARK 290 SMTRY3 8 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 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 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 H 424 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 LYS H 139 REMARK 465 SER H 140 REMARK 465 SER L 95 REMARK 465 PRO L 96 REMARK 465 CYS L 216 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 GLN H 115 CG CD OE1 NE2 REMARK 470 LYS H 224 CG CD CE NZ REMARK 470 PHE L 84 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS L 171 CG CD CE NZ REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 215 CG CD OE1 OE2 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 O TYR L 188 OH TYR L 194 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O LYS H 76 OG SER H 197 4555 2.17 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 SER H 55 17.75 58.87 REMARK 500 PRO H 100 2.46 -66.98 REMARK 500 THR H 108 -114.53 -143.74 REMARK 500 SER H 122 144.03 -171.57 REMARK 500 SER H 137 -143.57 -76.24 REMARK 500 ASP H 154 92.52 60.16 REMARK 500 SER H 166 64.95 36.06 REMARK 500 THR H 170 -34.54 -132.85 REMARK 500 SER L 31 19.27 59.44 REMARK 500 THR L 52 -45.51 67.23 REMARK 500 ALA L 69 -91.92 62.47 REMARK 500 TYR L 92 44.86 -145.96 REMARK 500 ASN L 140 86.58 47.78 REMARK 500 LYS L 192 -52.53 -128.93 REMARK 500 REMARK 500 REMARK: NULL REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 H09 H 301 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8RDA RELATED DB: PDB DBREF 8RDF H 1 224 PDB 8RDF 8RDF 1 224 DBREF 8RDF L 1 216 PDB 8RDF 8RDF 1 216 SEQRES 1 H 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL THR SEQRES 2 H 224 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 224 PHE THR PHE ASN THR TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 H 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 H 224 ARG SER SER ASP TYR ILE TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 224 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 224 VAL TYR LEU GLN MET THR SER LEU ARG ASP GLU ASP THR SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA ARG ASP PRO GLY GLY MET PRO SEQRES 9 H 224 THR THR VAL THR THR TRP LEU TYR TRP GLY GLN GLY THR SEQRES 10 H 224 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 224 GLU PRO LYS SEQRES 1 L 216 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 216 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 216 GLN SER VAL THR SER ASN TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 216 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP THR SEQRES 5 L 216 SER ARG ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 216 SER GLY SER ALA THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 216 LEU GLU PRO ASP ASP PHE ALA ILE TYR TYR CYS GLN GLN SEQRES 8 L 216 TYR GLY SER SER PRO PRO VAL THR PHE GLY HIS GLY THR SEQRES 9 L 216 LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 216 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 L 216 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 216 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 216 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 216 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 216 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 216 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 216 LYS SER PHE ASN ARG GLY GLU CYS HET H09 H 301 67 HET ZN L 301 1 HETNAM ZN ZINC ION FORMUL 3 H09 FORMUL 4 ZN ZN 2+ FORMUL 5 HOH *54(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 SER H 197 GLN H 202 1 6 HELIX 4 AA4 LYS H 211 ASN H 214 5 4 HELIX 5 AA5 VAL L 29 ASN L 32 5 4 HELIX 6 AA6 GLU L 80 PHE L 84 5 5 HELIX 7 AA7 ASP L 124 GLY L 130 1 7 HELIX 8 AA8 LYS L 185 LYS L 190 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 SER H 78 MET H 83 -1 O MET H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA2 6 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 117 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O SER H 49 N TRP H 36 SHEET 6 AA2 6 ILE H 58 TYR H 60 -1 O TYR H 59 N SER H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12 SHEET 3 AA3 4 ALA H 92 ARG H 98 -1 N TYR H 94 O THR H 117 SHEET 4 AA3 4 TYR H 112 TRP H 113 -1 O TYR H 112 N ARG H 98 SHEET 1 AA4 4 SER H 130 LEU H 134 0 SHEET 2 AA4 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA4 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AA4 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AA5 4 SER H 130 LEU H 134 0 SHEET 2 AA5 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA5 4 TYR H 186 PRO H 195 -1 O VAL H 194 N ALA H 146 SHEET 4 AA5 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AA6 3 THR H 161 TRP H 164 0 SHEET 2 AA6 3 TYR H 204 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AA6 3 THR H 215 VAL H 221 -1 O VAL H 217 N VAL H 208 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O LEU L 74 N LEU L 21 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA8 6 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 106 SHEET 4 AA8 6 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA8 6 ARG L 46 TYR L 50 -1 O ARG L 46 N GLN L 38 SHEET 6 AA8 6 ARG L 54 ARG L 55 -1 O ARG L 54 N TYR L 50 SHEET 1 AA9 4 THR L 10 LEU L 13 0 SHEET 2 AA9 4 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA9 4 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 106 SHEET 4 AA9 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 91 SHEET 1 AB1 4 SER L 116 PHE L 120 0 SHEET 2 AB1 4 THR L 131 PHE L 141 -1 O LEU L 137 N PHE L 118 SHEET 3 AB1 4 TYR L 175 SER L 184 -1 O LEU L 181 N VAL L 134 SHEET 4 AB1 4 SER L 161 VAL L 165 -1 N SER L 164 O SER L 178 SHEET 1 AB2 4 ALA L 155 LEU L 156 0 SHEET 2 AB2 4 ALA L 146 VAL L 152 -1 N VAL L 152 O ALA L 155 SHEET 3 AB2 4 VAL L 193 HIS L 200 -1 O GLU L 197 N GLN L 149 SHEET 4 AB2 4 VAL L 207 ASN L 212 -1 O VAL L 207 N VAL L 198 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 150 CYS H 206 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.04 SSBOND 4 CYS L 136 CYS L 196 1555 1555 2.03 CISPEP 1 PHE H 156 PRO H 157 0 -4.69 CISPEP 2 GLU H 158 PRO H 159 0 -3.70 CISPEP 3 SER L 7 PRO L 8 0 -3.18 CISPEP 4 TYR L 142 PRO L 143 0 5.03 CRYST1 60.928 131.288 144.964 90.00 90.00 90.00 C 2 2 21 8 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 0.016413 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007617 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006898 0.00000