HEADER IMMUNE SYSTEM 30-DEC-24 9MPB TITLE CRYSTAL STRUCTURE OF THE HIV V2-APEX-TARGETING ANTIBODY RM038, DERIVED TITLE 2 FROM MACAQUE 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 30-JUL-25 9MPB 0 JRNL AUTH S.AGRAWAL,I.A.WILSON JRNL TITL INDUCTION OF HIV BROADLY NEUTRALIZING ANTIBODY PRECURSORS TO JRNL TITL 2 THE APEX EPITOPE IN NON-HUMAN PRIMATES JRNL REF SCI IMMUNOL 2025 JRNL REFN ESSN 2470-9468 REMARK 2 REMARK 2 RESOLUTION. 1.98 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) : 1.98 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.58 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 40421 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 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 41.5800 - 4.7800 0.93 2807 150 0.1750 0.1948 REMARK 3 2 4.7800 - 3.7900 0.90 2673 144 0.1568 0.1960 REMARK 3 3 3.7900 - 3.3100 0.86 2506 130 0.1933 0.2072 REMARK 3 4 3.3100 - 3.0100 0.94 2756 144 0.1969 0.2150 REMARK 3 5 3.0100 - 2.7900 0.97 2833 145 0.2070 0.2523 REMARK 3 6 2.7900 - 2.6300 0.97 2831 146 0.2031 0.2394 REMARK 3 7 2.6300 - 2.5000 0.93 2705 141 0.1908 0.2385 REMARK 3 8 2.5000 - 2.3900 0.92 2692 133 0.2021 0.2704 REMARK 3 9 2.3900 - 2.3000 0.96 2773 144 0.2004 0.2540 REMARK 3 10 2.3000 - 2.2200 0.96 2791 146 0.1995 0.2624 REMARK 3 11 2.2200 - 2.1500 0.97 2815 153 0.1889 0.2506 REMARK 3 12 2.1500 - 2.0900 0.96 2816 134 0.1768 0.2175 REMARK 3 13 2.0900 - 2.0300 0.96 2752 161 0.1755 0.2314 REMARK 3 14 2.0300 - 1.9800 0.91 2674 126 0.1683 0.1942 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.200 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.33 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 : 0.022 NULL REMARK 3 ANGLE : 1.653 NULL REMARK 3 CHIRALITY : 0.108 521 REMARK 3 PLANARITY : 0.014 608 REMARK 3 DIHEDRAL : 19.865 1243 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 9MPB 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_1000291241. 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 : 40445 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1 REMARK 200 DATA REDUNDANCY : 5.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 28.7200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01 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 (%): 61.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE PH 8.0 1.0 M SODIUM REMARK 280 CITRATE, 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 90.62550 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.25600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.62550 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.25600 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: 3460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 CYS H 0 REMARK 465 VAL H 1 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 GLU L 28A REMARK 465 ALA L 28B 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 HZ3 LYS H 201 O HOH H 301 1.02 REMARK 500 HZ1 LYS H 206 O HOH H 302 1.43 REMARK 500 NZ LYS H 201 O HOH H 301 1.48 REMARK 500 HZ1 LYS H 201 O HOH H 301 1.54 REMARK 500 H LYS H 214 O HOH H 304 1.60 REMARK 500 NZ LYS H 206 O HOH H 302 1.89 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 OE2 GLU H 2 O3 TYS H 100D 2555 1.84 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 ASP H 100B -5.95 86.14 REMARK 500 ASP H 144 67.85 64.81 REMARK 500 VAL L 51 -41.50 80.78 REMARK 500 SER L 52 -0.46 -143.95 REMARK 500 ASP L 68 -83.60 68.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG H 97 0.24 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MPC RELATED DB: PDB REMARK 900 RELATED ID: 9MPX RELATED DB: PDB DBREF 9MPB H -1 216 PDB 9MPB 9MPB -1 216 DBREF 9MPB L 1 214 PDB 9MPB 9MPB 1 214 SEQRES 1 H 237 GLN CYS VAL GLU GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 H 237 VAL GLN PRO GLY ALA SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 237 SER GLU PHE THR PHE SER ASP SER ASP MET HIS TRP VAL SEQRES 4 H 237 ARG GLN VAL PRO GLY GLN GLY LEU GLU TRP VAL SER ALA SEQRES 5 H 237 ILE SER LEU GLY GLY ASP THR HIS TYR PRO ASP SER VAL SEQRES 6 H 237 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 H 237 SER LEU TYR LEU GLN MET ASN SER LEU ARG PRO GLU ASP SEQRES 8 H 237 THR ALA VAL TYR TYR CYS ALA ARG GLY GLY ARG GLY GLY SEQRES 9 H 237 TYR GLU ASP ASP TYS GLY TYR PHE TYR PHE ILE GLY GLY SEQRES 10 H 237 ARG ARG SER LEU ASP VAL TRP GLY ARG GLY ALA LEU VAL SEQRES 11 H 237 THR VAL 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 220 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 220 THR PRO GLY GLU PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 220 GLN SER LEU LEU ASP SER GLU ALA GLY ASN THR TYR LEU SEQRES 4 L 220 ASP TRP TYR LEU GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 L 220 LEU ILE TYR GLU VAL SER ASN ARG ALA SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE SER GLY SER GLY SER ASP THR ASP PHE THR SEQRES 7 L 220 LEU LYS VAL SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 L 220 TYR TYR CYS MET GLN GLY ILE GLN LEU PRO TYR SER PHE SEQRES 9 L 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET TYS H 100D 16 HETNAM TYS O-SULFO-L-TYROSINE FORMUL 1 TYS C9 H11 N O6 S FORMUL 3 HOH *165(H2 O) HELIX 1 AA1 THR H 28 SER H 30 5 3 HELIX 2 AA2 ASN H 73 LYS H 75 5 3 HELIX 3 AA3 ARG H 83 THR H 87 5 5 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLU L 79 VAL L 83 5 5 HELIX 8 AA8 SER L 121 GLY L 128 1 8 HELIX 9 AA9 LYS L 183 HIS L 189 1 7 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 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA2 4 GLY H 10 VAL H 12 0 SHEET 2 AA2 4 ALA H 107 VAL H 111 1 O THR H 110 N GLY H 10 SHEET 3 AA2 4 ALA H 88 TYR H 100 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 4 TYR H 100F TYR H 100H-1 O PHE H 100G N GLY H 99 SHEET 1 AA3 5 THR H 57 HIS H 58 0 SHEET 2 AA3 5 GLU H 46 ILE H 51 -1 N ALA H 50 O HIS H 58 SHEET 3 AA3 5 SER H 32 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AA3 5 ALA H 88 TYR H 100 -1 O TYR H 91 N VAL H 37 SHEET 5 AA3 5 VAL H 102 TRP H 103 -1 O VAL 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 LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 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 THR H 205 N HIS H 200 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 ALA L 19 SER L 25 -1 O SER L 22 N THR L 7 SHEET 3 AA7 4 ASP L 70 VAL L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AA8 6 SER L 10 VAL L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 GLY L 84 GLN L 90 -1 N GLY L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 GLN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 VAL L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 GLY L 84 GLN L 90 -1 N GLY L 84 O VAL L 104 SHEET 4 AA9 4 SER L 97 PHE L 98 -1 O SER L 97 N GLN L 90 SHEET 1 AB1 2 LEU L 27C ASP L 27D 0 SHEET 2 AB1 2 ASN L 30 THR L 31 -1 O ASN L 30 N ASP L 27D SHEET 1 AB2 4 SER L 114 PHE L 118 0 SHEET 2 AB2 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB2 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB2 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB3 4 ALA L 153 LEU L 154 0 SHEET 2 AB3 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB3 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB3 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 2.35 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.08 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 LINK C ASP H 100C N TYS H 100D 1555 1555 1.34 LINK C TYS H 100D N GLY H 100E 1555 1555 1.33 CISPEP 1 PHE H 146 PRO H 147 0 -14.02 CISPEP 2 GLU H 148 PRO H 149 0 0.54 CISPEP 3 THR L 7 PRO L 8 0 -4.80 CISPEP 4 LEU L 94 PRO L 95 0 1.22 CISPEP 5 TYR L 140 PRO L 141 0 2.22 CRYST1 181.251 66.512 53.405 90.00 103.18 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 0.005517 0.000000 0.001292 0.00000 SCALE2 0.000000 0.015035 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019231 0.00000