HEADER IMMUNE SYSTEM/VIRAL PROTEIN 22-JAN-25 9MZ6 TITLE CRYSTAL STRUCTURE OF 19B FAB BOUND TO THE THIRD VARIABLE (V3) LOOP TITLE 2 PEPTIDE FROM THE HIV-1 5768-P27 ENVELOPE (ENV) GLYCOPROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: 19B FAB LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 19B FAB HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 5768-P27 ENVELOPE GLYCOPROTEIN; COMPND 11 CHAIN: D; COMPND 12 FRAGMENT: THIRD VARIABLE LOOP PEPTIDE; COMPND 13 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; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 14 ORGANISM_TAXID: 11676 KEYWDS 19B, FAB, FRAGMENT ANTIGEN-BINDING, HIV-1 ENVELOPE, IMMUNE SYSTEM, KEYWDS 2 IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.FETICS,P.ACHARYA REVDAT 1 21-JAN-26 9MZ6 0 JRNL AUTH S.FETICS,P.ACHARYA JRNL TITL CRYSTAL STRUCTURE OF 19B FAB BOUND TO HIV-1 ENV 5768-P27 JRNL TITL 2 PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.1_5286 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.81 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 18997 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.195 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1900 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 22.8100 - 5.9800 0.99 1330 148 0.2203 0.2411 REMARK 3 2 5.9800 - 4.7600 1.00 1257 140 0.1716 0.2032 REMARK 3 3 4.7600 - 4.1700 1.00 1235 138 0.1433 0.1635 REMARK 3 4 4.1700 - 3.7900 1.00 1225 135 0.1563 0.2328 REMARK 3 5 3.7900 - 3.5200 1.00 1212 135 0.1729 0.2116 REMARK 3 6 3.5200 - 3.3100 1.00 1237 137 0.1781 0.2294 REMARK 3 7 3.3100 - 3.1400 1.00 1213 134 0.1903 0.2328 REMARK 3 8 3.1400 - 3.0100 1.00 1200 135 0.2020 0.3102 REMARK 3 9 3.0100 - 2.8900 1.00 1203 133 0.2155 0.2835 REMARK 3 10 2.8900 - 2.7900 1.00 1215 135 0.2149 0.2836 REMARK 3 11 2.7900 - 2.7100 1.00 1193 132 0.2105 0.2546 REMARK 3 12 2.7100 - 2.6300 1.00 1206 135 0.2208 0.3138 REMARK 3 13 2.6300 - 2.5600 1.00 1185 132 0.2297 0.2969 REMARK 3 14 2.5600 - 2.5000 0.98 1186 131 0.2472 0.2807 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) : 0.284 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.684 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.58 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.59 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 3398 REMARK 3 ANGLE : 0.557 4646 REMARK 3 CHIRALITY : 0.043 535 REMARK 3 PLANARITY : 0.004 599 REMARK 3 DIHEDRAL : 12.593 1182 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 9MZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291272. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-SEP-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : SEALED TUBE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : BRUKER D8 VENTURE REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : BRUKER PHOTON III REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT REMARK 200 DATA SCALING SOFTWARE : SADABS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18997 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 22.810 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 8.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM SULFATE, 0.085 M REMARK 280 SODIUM CACODYLATE TRIHYDRATE PH 6.5, 25.5% W/V POLYETHYLENE REMARK 280 GLYCOL 8,000, 15% V/V GLYCEROL, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 295K 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 22.97550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.83850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.58800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.83850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.97550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.58800 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18990 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D 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 B 127 REMARK 465 SER B 128 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 THR B 131 REMARK 465 SER B 132 REMARK 465 GLY B 133 REMARK 465 LYS B 214 REMARK 465 SER B 215 REMARK 465 GLU D 295 REMARK 465 ILE D 296 REMARK 465 ASN D 297 REMARK 465 CYS D 298 REMARK 465 THR D 299 REMARK 465 ARG D 300 REMARK 465 PRO D 301 REMARK 465 GLY D 321 REMARK 465 GLU D 322 REMARK 465 ILE D 323 REMARK 465 ILE D 324 REMARK 465 GLY D 325 REMARK 465 ASP D 326 REMARK 465 ILE D 327 REMARK 465 ARG D 328 REMARK 465 GLN D 329 REMARK 465 ALA D 330 REMARK 465 HIS D 331 REMARK 465 CYS D 332 REMARK 465 ASN D 333 REMARK 465 ILE D 334 REMARK 465 SER D 335 REMARK 465 ARG D 336 REMARK 465 ALA D 337 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 LYS A 145 CG CD CE NZ REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 GLU B 1 CG CD OE1 OE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 SER B 186 OG REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 LYS D 307 CG CD CE NZ 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 HOH A 598 O HOH A 599 2.07 REMARK 500 O GLU B 1 O HOH B 301 2.09 REMARK 500 O HOH A 533 O HOH B 414 2.17 REMARK 500 NE ARG B 19 O HOH B 302 2.18 REMARK 500 O HOH A 497 O HOH A 583 2.19 REMARK 500 O HOH B 390 O HOH B 419 2.19 REMARK 500 O HOH A 530 O HOH A 538 2.19 REMARK 500 O HOH B 402 O HOH B 414 2.19 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 A 30 -121.28 53.34 REMARK 500 ALA A 84 -177.46 172.15 REMARK 500 LYS A 190 -52.67 -124.56 REMARK 500 THR B 28 99.51 -67.73 REMARK 500 LYS B 43 -15.52 -176.79 REMARK 500 VAL B 96 47.11 -83.64 REMARK 500 ASP B 144 52.21 73.16 REMARK 500 THR B 160 -33.40 -132.58 REMARK 500 HIS B 200 76.92 -116.25 REMARK 500 ASN D 303 134.13 -174.23 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MZ6 A 1 213 PDB 9MZ6 9MZ6 1 213 DBREF 9MZ6 B 1 215 PDB 9MZ6 9MZ6 1 215 DBREF 9MZ6 D 295 337 UNP D2CJY3 D2CJY3_HV1 27 69 SEQADV 9MZ6 VAL D 316 UNP D2CJY3 ALA 48 CONFLICT SEQRES 1 A 213 ASP ILE VAL LEU THR GLN SER PRO PRO SER LEU SER ALA SEQRES 2 A 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 A 213 GLN ASP ILE SER ASP HIS LEU SER TRP PHE GLN GLN LYS SEQRES 4 A 213 PRO GLY LYS ALA PRO LYS LEU LEU VAL TYR GLY VAL SER SEQRES 5 A 213 SER LEU GLU ALA GLY VAL PRO SER ARG PHE SER VAL SER SEQRES 6 A 213 GLY SER GLY THR HIS PHE THR PHE THR VAL ASN GLY LEU SEQRES 7 A 213 GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN GLN TYR SEQRES 8 A 213 ASP ASP LEU PRO TRP THR PHE GLY PRO GLY THR VAL VAL SEQRES 9 A 213 GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 213 PHE ASN ARG GLY GLU SEQRES 1 B 216 GLU VAL GLN LEU VAL GLN SER GLY GLY ALA LEU ILE GLN SEQRES 2 B 216 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 216 PHE THR PHE VAL ASP TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 B 216 ALA PRO GLY LYS GLY LEU GLN TRP VAL SER THR ILE ILE SEQRES 5 B 216 GLY SER GLY ALA ASP THR TYR TYR THR ASP SER VAL LYS SEQRES 6 B 216 GLY ARG PHE THR ILE SER ARG ASP ASN SER ASN ASN THR SEQRES 7 B 216 VAL HIS LEU GLN MET ASN SER LEU ARG ALA ASP ASP THR SEQRES 8 B 216 ALA LEU TYR TYR CYS VAL ARG GLY VAL PHE ASP LEU TRP SEQRES 9 B 216 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 10 B 216 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 11 B 216 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 12 B 216 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 13 B 216 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 14 B 216 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 15 B 216 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 16 B 216 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 17 B 216 ASP LYS ARG VAL GLU PRO LYS SER SEQRES 1 D 43 GLU ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SEQRES 2 D 43 SER ILE HIS MET GLY PRO GLY LYS VAL PHE TYR THR THR SEQRES 3 D 43 GLY GLU ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN SEQRES 4 D 43 ILE SER ARG ALA HET SO4 A 301 5 HET SO4 A 302 5 HETNAM SO4 SULFATE ION FORMUL 4 SO4 2(O4 S 2-) FORMUL 6 HOH *350(H2 O) HELIX 1 AA1 GLN A 79 LEU A 83 5 5 HELIX 2 AA2 SER A 121 SER A 127 1 7 HELIX 3 AA3 LYS A 183 LYS A 188 1 6 HELIX 4 AA4 THR B 28 TYR B 32 5 5 HELIX 5 AA5 ASP B 61 LYS B 64 5 4 HELIX 6 AA6 ARG B 83 THR B 87 5 5 HELIX 7 AA7 SER B 156 ALA B 158 5 3 HELIX 8 AA8 LYS B 201 ASN B 204 5 4 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 ARG A 18 ALA A 25 -1 O GLN A 24 N THR A 5 SHEET 3 AA1 4 HIS A 70 ASN A 76 -1 O VAL A 75 N VAL A 19 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AA2 5 SER A 10 ALA A 13 0 SHEET 2 AA2 5 THR A 102 VAL A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA2 5 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 AA2 5 LEU A 33 GLN A 38 -1 N PHE A 36 O PHE A 87 SHEET 5 AA2 5 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 1 AA3 4 SER A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 102 VAL A 106 1 O GLU A 105 N LEU A 11 SHEET 3 AA3 4 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 AA3 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 AA4 4 SER A 114 PHE A 118 0 SHEET 2 AA4 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 AA4 4 TYR A 173 SER A 182 -1 O LEU A 181 N ALA A 130 SHEET 4 AA4 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA5 4 ALA A 153 LEU A 154 0 SHEET 2 AA5 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA5 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA5 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA6 4 GLN B 3 GLN B 6 0 SHEET 2 AA6 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA6 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA6 4 PHE B 67 ASP B 72 -1 N SER B 70 O HIS B 79 SHEET 1 AA7 6 ALA B 10 ILE B 12 0 SHEET 2 AA7 6 THR B 107 VAL B 111 1 O THR B 110 N ILE B 12 SHEET 3 AA7 6 ALA B 88 ARG B 94 -1 N TYR B 90 O THR B 107 SHEET 4 AA7 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 91 SHEET 5 AA7 6 GLN B 46 ILE B 51 -1 O VAL B 48 N TRP B 36 SHEET 6 AA7 6 THR B 57 TYR B 59 -1 O TYR B 58 N THR B 50 SHEET 1 AA8 4 SER B 120 LEU B 124 0 SHEET 2 AA8 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120 SHEET 3 AA8 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AA8 4 VAL B 163 THR B 165 -1 N HIS B 164 O VAL B 181 SHEET 1 AA9 4 SER B 120 LEU B 124 0 SHEET 2 AA9 4 THR B 135 TYR B 145 -1 O LYS B 143 N SER B 120 SHEET 3 AA9 4 TYR B 176 PRO B 185 -1 O LEU B 178 N VAL B 142 SHEET 4 AA9 4 VAL B 169 LEU B 170 -1 N VAL B 169 O SER B 177 SHEET 1 AB1 3 THR B 151 TRP B 154 0 SHEET 2 AB1 3 ILE B 195 HIS B 200 -1 O ASN B 197 N SER B 153 SHEET 3 AB1 3 THR B 205 ARG B 210 -1 O THR B 205 N HIS B 200 SHEET 1 AB2 2 LYS D 307 GLY D 312 0 SHEET 2 AB2 2 LYS D 315 THR D 319 -1 O THR D 319 N LYS D 307 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 92 1555 1555 2.04 SSBOND 4 CYS B 140 CYS B 196 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 -5.22 CISPEP 2 LEU A 94 PRO A 95 0 -1.21 CISPEP 3 TYR A 140 PRO A 141 0 1.79 CISPEP 4 PHE B 146 PRO B 147 0 -3.06 CISPEP 5 GLU B 148 PRO B 149 0 -5.12 CRYST1 45.951 87.176 131.677 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 0.021762 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011471 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007594 0.00000