HEADER IMMUNE SYSTEM 13-OCT-23 8UKI TITLE CRYSTAL STRUCTURE OF 04_A06 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 04_A06 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 04_A06 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL: HEK293 KEYWDS FAB, BROADLY NEUTRALIZING ANTIBODY, HIV-1, CD4 BINDING SITE, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.T.DELAITSCH,H.B.GRISTICK,P.J.BJORKMAN REVDAT 1 16-APR-25 8UKI 0 JRNL AUTH A.T.DELAITSCH,H.B.GRISTICK,P.J.BJORKMAN JRNL TITL CRYSTAL STRUCTURE OF 04_A06 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX V1.20.1-4487 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 NUMBER OF REFLECTIONS : 43827 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL 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 : 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 8UKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1000277862. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-NOV-22 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) : 1 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 : IMOSFLM V7.4 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52273 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 38.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 0.71000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: PDB ENTRY 3NGB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8% V/V TACSIMATE, PH 7.0, 20% W/V REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 66.64000 REMARK 290 SMTRY3 2 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: 3260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 SER H 1 REMARK 465 SER H 127 REMARK 465 SER H 128 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 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 TYR L 1 REMARK 465 GLY L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 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 ARG H 3 CG CD NE CZ NH1 NH2 REMARK 470 ARG H 32 CG CD NE CZ NH1 NH2 REMARK 470 ARG H 34 CG CD NE CZ NH1 NH2 REMARK 470 PHE H 35D CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG H 54 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 58 CG CD CE NZ REMARK 470 ARG H 62 CG CD NE CZ NH1 NH2 REMARK 470 GLN H 64 CG CD OE1 NE2 REMARK 470 ASP H 99 CG OD1 OD2 REMARK 470 ASP H 100 CG OD1 OD2 REMARK 470 LYS H 201 CG CD CE NZ REMARK 470 GLU H 212 CG CD OE1 OE2 REMARK 470 GLN L 3 CG CD OE1 NE2 REMARK 470 GLU L 24 CG CD OE1 OE2 REMARK 470 LYS L 127 CG CD CE NZ REMARK 470 ARG L 143 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 146 CG CD CE NZ REMARK 470 GLN L 148 CG CD OE1 NE2 REMARK 470 LYS L 170 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 LYS L 191 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 L 311 O HOH L 406 2.08 REMARK 500 O HOH H 400 O HOH H 500 2.09 REMARK 500 O HOH L 379 O HOH L 383 2.11 REMARK 500 O HOH H 461 O HOH H 474 2.12 REMARK 500 O HOH L 472 O HOH L 499 2.12 REMARK 500 O HOH H 310 O HOH H 474 2.16 REMARK 500 O HOH H 544 O HOH L 500 2.17 REMARK 500 O HOH H 464 O HOH H 519 2.17 REMARK 500 O HOH H 404 O HOH H 496 2.17 REMARK 500 O HOH H 364 O HOH H 471 2.17 REMARK 500 O HOH L 379 O HOH L 493 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 ALA L 32 49.29 -82.87 REMARK 500 ALA L 51 -42.55 76.46 REMARK 500 HIS L 52 -1.33 -143.38 REMARK 500 PHE L 91 -123.62 51.23 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 H 551 DISTANCE = 5.85 ANGSTROMS REMARK 525 HOH H 552 DISTANCE = 5.86 ANGSTROMS REMARK 525 HOH H 553 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH H 554 DISTANCE = 6.38 ANGSTROMS REMARK 525 HOH H 555 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH H 556 DISTANCE = 7.16 ANGSTROMS REMARK 525 HOH L 500 DISTANCE = 6.88 ANGSTROMS DBREF 8UKI H 1 225 PDB 8UKI 8UKI 1 225 DBREF 8UKI L 1 215 PDB 8UKI 8UKI 1 215 SEQRES 1 H 245 SER VAL ARG LEU ASP GLN SER GLY THR ALA VAL LYS LYS SEQRES 2 H 245 PRO GLY ALA SER VAL ARG VAL SER CYS ARG ALA PRO ASP SEQRES 3 H 245 SER PHE THR VAL TYR ARG PRO ARG LEU SER ALA TYR PHE SEQRES 4 H 245 ILE GLY GLU PHE ASN ILE HIS TRP LEU ARG GLN ALA PRO SEQRES 5 H 245 GLY GLN GLY LEU GLU TRP LEU GLY PHE VAL ASN ILE PHE SEQRES 6 H 245 ARG GLY ALA VAL LYS TYR SER SER ARG PHE GLN GLY ARG SEQRES 7 H 245 ILE THR ILE THR ARG ASP THR SER SER GLU THR SER TYR SEQRES 8 H 245 LEU ASP LEU GLY ALA LEU LYS ALA ASP ASP THR ALA THR SEQRES 9 H 245 TYR TYR CYS ALA TRP ASP LYS ASN VAL ASP ASP ASN PRO SEQRES 10 H 245 TRP ARG LEU ASP SER TRP GLY GLN GLY THR LEU VAL ILE SEQRES 11 H 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 H 245 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 13 H 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 H 245 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 15 H 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 H 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 H 245 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 18 H 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 19 H 245 SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 211 TYR ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 211 SER ILE GLY ASP THR ILE THR VAL ALA CYS GLU VAL SER SEQRES 3 L 211 GLN ASP VAL GLY TRP ALA VAL ASN TRP TYR HIS GLN ARG SEQRES 4 L 211 PRO GLY ARG PRO PRO TYR ASN LEU ILE TYR THR ALA HIS SEQRES 5 L 211 ASN LEU ALA PRO GLY VAL ALA SER ARG PHE ARG GLY SER SEQRES 6 L 211 ARG VAL GLY THR TYR PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 L 211 LEU PRO GLU ASP VAL GLY THR TYR TYR CYS GLN VAL PHE SEQRES 8 L 211 ASP SER PHE ALA PRO GLY GLY THR ARG VAL ASP LEU ARG SEQRES 9 L 211 GLY THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 L 211 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 L 211 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 L 211 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 L 211 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 L 211 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 L 211 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS SEQRES 16 L 211 GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG SEQRES 17 L 211 GLY GLU CYS FORMUL 3 HOH *456(H2 O) HELIX 1 AA1 SER H 61 GLN H 64 5 4 HELIX 2 AA2 LYS H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 LEU L 79 VAL L 83 5 5 HELIX 7 AA7 SER L 122 LYS L 127 1 6 HELIX 8 AA8 LYS L 184 GLU L 188 1 5 SHEET 1 AA1 4 ASP H 5 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 ARG H 23 -1 O ARG H 23 N ASP H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O LEU H 80 N VAL H 20 SHEET 4 AA1 4 ILE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 ALA H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 ASN H 35I GLN H 39 -1 N HIS H 35K O ALA H 93 SHEET 5 AA2 6 LEU H 45 ASN H 52 -1 O GLY H 49 N TRP H 36 SHEET 6 AA2 6 VAL H 57 TYR H 59 -1 O LYS H 58 N PHE H 50 SHEET 1 AA3 4 ALA H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O ILE H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 SER H 102 TRP H 103 -1 O SER H 102 N TRP H 94 SHEET 1 AA4 2 THR H 29 ARG H 32 0 SHEET 2 AA4 2 ALA H 35B ILE H 35E-1 O PHE H 35D N VAL H 30 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 LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA6 4 SER H 120 LEU H 124 0 SHEET 2 AA6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA6 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA7 3 THR H 151 TRP H 154 0 SHEET 2 AA7 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA7 3 THR H 205 ARG H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA8 4 VAL L 4 SER L 7 0 SHEET 2 AA8 4 ILE L 19 VAL L 25 -1 O GLU L 24 N THR L 5 SHEET 3 AA8 4 TYR L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA8 4 PHE L 62 VAL L 67 -1 N ARG L 63 O THR L 74 SHEET 1 AA9 6 SER L 10 ALA L 13 0 SHEET 2 AA9 6 THR L 103 LEU L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AA9 6 GLY L 84 VAL L 90 -1 N GLY L 84 O VAL L 105 SHEET 4 AA9 6 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA9 6 TYR L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA9 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AB1 4 SER L 10 ALA L 13 0 SHEET 2 AB1 4 THR L 103 LEU L 107 1 O ARG L 104 N LEU L 11 SHEET 3 AB1 4 GLY L 84 VAL L 90 -1 N GLY L 84 O VAL L 105 SHEET 4 AB1 4 SER L 97 PHE L 98 -1 O SER L 97 N VAL L 90 SHEET 1 AB2 4 SER L 115 PHE L 119 0 SHEET 2 AB2 4 THR L 130 PHE L 140 -1 O ASN L 138 N SER L 115 SHEET 3 AB2 4 TYR L 174 SER L 183 -1 O LEU L 180 N VAL L 133 SHEET 4 AB2 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB3 4 ALA L 154 LEU L 155 0 SHEET 2 AB3 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB3 4 VAL L 192 THR L 198 -1 O GLU L 196 N GLN L 148 SHEET 4 AB3 4 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.05 CISPEP 1 PHE H 146 PRO H 147 0 -8.87 CISPEP 2 GLU H 148 PRO H 149 0 -0.31 CISPEP 3 SER L 7 PRO L 8 0 -5.04 CISPEP 4 TYR L 141 PRO L 142 0 3.97 CRYST1 42.680 133.280 43.360 90.00 111.26 90.00 P 1 21 1 2 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 0.023430 0.000000 0.009116 0.00000 SCALE2 0.000000 0.007503 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024747 0.00000