HEADER IMMUNE SYSTEM/VIRAL PROTEIN 22-JAN-25 9MZ7 TITLE CRYSTAL STRUCTURE OF 19B FAB BOUND TO THE THIRD VARIABLE (V3) LOOP TITLE 2 PEPTIDE FROM THE HIV-1 92BR020 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: 92BR020 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 9MZ7 0 JRNL AUTH S.FETICS,P.ACHARYA JRNL TITL CRYSTAL STRUCTURE OF 19B FAB BOUND TO HIV-1 ENV 92BR020 JRNL TITL 2 PEPTIDE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.94 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) : 1.94 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.78 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 37735 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 2000 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 51.7800 - 4.6800 0.99 2767 155 0.1749 0.2061 REMARK 3 2 4.6800 - 3.7200 0.99 2658 149 0.1592 0.1862 REMARK 3 3 3.7200 - 3.2500 0.99 2604 146 0.1863 0.2415 REMARK 3 4 3.2500 - 2.9500 0.99 2593 145 0.2190 0.2876 REMARK 3 5 2.9500 - 2.7400 0.99 2552 143 0.2464 0.3154 REMARK 3 6 2.7400 - 2.5800 0.98 2554 142 0.2495 0.2907 REMARK 3 7 2.5800 - 2.4500 0.99 2539 142 0.2591 0.3661 REMARK 3 8 2.4500 - 2.3400 0.99 2534 142 0.2647 0.3103 REMARK 3 9 2.3400 - 2.2500 0.97 2524 141 0.2828 0.3686 REMARK 3 10 2.2500 - 2.1700 0.97 2485 139 0.3009 0.3537 REMARK 3 11 2.1700 - 2.1100 0.99 2542 143 0.2586 0.2624 REMARK 3 12 2.1100 - 2.0500 0.98 2475 138 0.2853 0.3144 REMARK 3 13 2.0500 - 1.9900 0.97 2475 139 0.2618 0.3545 REMARK 3 14 1.9900 - 1.9400 0.96 2433 136 0.2970 0.3472 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) : 0.270 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.176 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.99 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.31 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 3404 REMARK 3 ANGLE : 0.535 4662 REMARK 3 CHIRALITY : 0.042 536 REMARK 3 PLANARITY : 0.004 601 REMARK 3 DIHEDRAL : 15.274 1180 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 9MZ7 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_1000291278. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-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 : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL 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 : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37735 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940 REMARK 200 RESOLUTION RANGE LOW (A) : 51.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 5.800 REMARK 200 R MERGE (I) : 0.10700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99 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 (%): 50.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M AMMONIUM SULFATE, 0.09 M SODIUM REMARK 280 ACETATE TRIHYDRATE PH 4.6, 27% W/V POLYETHYLENE GLYCOL REMARK 280 MONOMETHYL ETHER 2,000 , 10% V/V GLYCEROL, VAPOR DIFFUSION, REMARK 280 SITTING DROP, 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 23.28600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.08000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.72700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.08000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.28600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.72700 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: 5090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 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 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 ASN D 302 REMARK 465 ASN D 303 REMARK 465 ASN D 304 REMARK 465 THR D 305 REMARK 465 GLY D 321 REMARK 465 ASP 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 ASP A 0 CG OD1 OD2 REMARK 470 LYS A 145 CG CD CE NZ REMARK 470 ASN A 158 CG OD1 ND2 REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 GLU A 213 CG CD OE1 OE2 REMARK 470 GLU B 1 CG CD OE1 OE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 GLN B 105 CG CD OE1 NE2 REMARK 470 SER B 127 OG REMARK 470 SER B 161 OG REMARK 470 LYS B 206 CG CD CE NZ REMARK 470 LYS B 214 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 417 O HOH A 576 2.07 REMARK 500 O HOH A 494 O HOH A 566 2.11 REMARK 500 O HOH B 550 O HOH B 569 2.12 REMARK 500 NE2 GLN A 27 O HOH A 401 2.12 REMARK 500 O HOH B 530 O HOH B 575 2.13 REMARK 500 O HOH B 549 O HOH B 579 2.15 REMARK 500 O HOH B 502 O HOH B 503 2.15 REMARK 500 O HOH B 582 O HOH B 624 2.17 REMARK 500 O HOH B 486 O HOH B 556 2.18 REMARK 500 OE1 GLU B 148 O HOH B 401 2.18 REMARK 500 O PRO B 41 O HOH B 402 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 -123.85 53.93 REMARK 500 LYS B 43 14.94 -150.63 REMARK 500 PHE B 97 40.13 77.70 REMARK 500 ASP B 144 61.04 61.45 REMARK 500 PRO D 313 107.83 -46.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 657 DISTANCE = 6.84 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 303 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 165 OE2 REMARK 620 2 HOH A 415 O 86.6 REMARK 620 3 HOH A 511 O 82.6 130.8 REMARK 620 4 HOH A 584 O 132.2 50.0 109.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 304 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 173 OH REMARK 620 2 HOH A 569 O 93.7 REMARK 620 3 HOH A 594 O 82.4 63.7 REMARK 620 4 HOH A 607 O 72.2 124.3 153.5 REMARK 620 5 HOH A 638 O 109.6 156.0 123.4 61.2 REMARK 620 N 1 2 3 4 DBREF 9MZ7 A 0 213 PDB 9MZ7 9MZ7 0 213 DBREF 9MZ7 B 1 215 PDB 9MZ7 9MZ7 1 215 DBREF 9MZ7 D 295 337 UNP A8DM03 A8DM03_HV1 48 90 SEQRES 1 A 214 ASP ASP ILE VAL LEU THR GLN SER PRO PRO SER LEU SER SEQRES 2 A 214 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SEQRES 3 A 214 SER GLN ASP ILE SER ASP HIS LEU SER TRP PHE GLN GLN SEQRES 4 A 214 LYS PRO GLY LYS ALA PRO LYS LEU LEU VAL TYR GLY VAL SEQRES 5 A 214 SER SER LEU GLU ALA GLY VAL PRO SER ARG PHE SER VAL SEQRES 6 A 214 SER GLY SER GLY THR HIS PHE THR PHE THR VAL ASN GLY SEQRES 7 A 214 LEU GLN PRO GLU ASP LEU ALA THR TYR PHE CYS GLN GLN SEQRES 8 A 214 TYR ASP ASP LEU PRO TRP THR PHE GLY PRO GLY THR VAL SEQRES 9 A 214 VAL GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 A 214 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 A 214 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 A 214 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 A 214 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 A 214 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 A 214 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 A 214 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 A 214 SER 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 ILE GLY PRO GLY ARG ALA PHE TYR ALA THR SEQRES 3 D 43 GLY ASP 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 HET NA A 303 1 HET NA A 304 1 HET SO4 B 301 5 HETNAM SO4 SULFATE ION HETNAM NA SODIUM ION FORMUL 4 SO4 3(O4 S 2-) FORMUL 6 NA 2(NA 1+) FORMUL 9 HOH *511(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 PRO B 41 LYS B 43 5 3 HELIX 6 AA6 ASP B 61 LYS B 64 5 4 HELIX 7 AA7 ARG B 83 THR B 87 5 5 HELIX 8 AA8 SER B 156 ALA B 158 5 3 HELIX 9 AA9 SER B 187 LEU B 189 5 3 HELIX 10 AB1 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 PHE A 71 N CYS A 23 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 179 N VAL A 132 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 LEU B 80 N LEU B 20 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 ALA B 88 O VAL B 109 SHEET 4 AA7 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 91 SHEET 5 AA7 6 LEU B 45 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 LEU B 141 N PHE B 122 SHEET 3 AA8 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 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 LEU B 141 N PHE B 122 SHEET 3 AA9 4 TYR B 176 PRO B 185 -1 O VAL B 184 N ALA B 136 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 ARG D 315 ALA D 319 -1 O ALA 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 2.03 LINK OE2 GLU A 165 NA NA A 303 1555 1555 2.75 LINK OH TYR A 173 NA NA A 304 1555 1555 2.97 LINK NA NA A 303 O HOH A 415 1555 1555 2.83 LINK NA NA A 303 O HOH A 511 1555 1555 2.33 LINK NA NA A 303 O HOH A 584 1555 1555 3.20 LINK NA NA A 304 O HOH A 569 1555 1555 2.94 LINK NA NA A 304 O HOH A 594 1555 1555 2.09 LINK NA NA A 304 O HOH A 607 1555 1555 2.72 LINK NA NA A 304 O HOH A 638 1555 1555 2.15 CISPEP 1 SER A 7 PRO A 8 0 -3.44 CISPEP 2 LEU A 94 PRO A 95 0 -1.67 CISPEP 3 TYR A 140 PRO A 141 0 3.71 CISPEP 4 PHE B 146 PRO B 147 0 -1.26 CISPEP 5 GLU B 148 PRO B 149 0 0.76 CRYST1 46.572 81.454 134.160 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 0.021472 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012277 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007454 0.00000