HEADER IMMUNE SYSTEM 04-JUL-22 7YDS TITLE THE STRUCTURE OF THE BISPECIFIC ANTIBODY TARGETED PD-L1 AND 4-1BB COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROGRAMMED CELL DEATH 1 LIGAND 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PD-L1,PDCD1 LIGAND 1,PROGRAMMED DEATH LIGAND 1,HPD-L1,B7 COMPND 5 HOMOLOG 1,B7-H1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: ANTI-PDL1-VH-CH1; COMPND 10 CHAIN: B; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: ANTI-PDL1-VL-CL; COMPND 14 CHAIN: C; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CD274, B7H1, PDCD1L1, PDCD1LG1, PDL1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; 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_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F KEYWDS COMPLEX, CHECKPOINT INHIBITORS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.GAO,M.ZHU,W.T.LIU,L.S.CHENG,Z.L.ZHU,L.W.NIU REVDAT 1 19-JUL-23 7YDS 0 JRNL AUTH M.ZHU,Y.GAO JRNL TITL A BISPECIFIC ANTIBODY TARGETED PD-L1 AND 4-1BB INDUCES A JRNL TITL 2 POTENT ANTITUMOR IMMUNE ACTIVITY IN COLORECTAL CANCER JRNL TITL 3 WITHOUT SYSTEMIC TOXICITY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.14 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 29320 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820 REMARK 3 FREE R VALUE TEST SET COUNT : 1412 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 13.1400 - 4.8800 1.00 2951 137 0.1649 0.2038 REMARK 3 2 4.8800 - 3.9100 1.00 2814 165 0.1421 0.1907 REMARK 3 3 3.9100 - 3.4200 1.00 2796 143 0.1637 0.2221 REMARK 3 4 3.4200 - 3.1100 1.00 2774 138 0.1840 0.2108 REMARK 3 5 3.1100 - 2.8900 1.00 2789 145 0.2056 0.2940 REMARK 3 6 2.8900 - 2.7200 1.00 2782 116 0.2272 0.3112 REMARK 3 7 2.7200 - 2.5900 1.00 2783 131 0.2383 0.2719 REMARK 3 8 2.5900 - 2.4800 1.00 2757 143 0.2559 0.3195 REMARK 3 9 2.4800 - 2.3800 1.00 2713 158 0.2731 0.3297 REMARK 3 10 2.3800 - 2.3000 1.00 2749 136 0.2891 0.3366 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.710 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.81 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 7YDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-22. REMARK 100 THE DEPOSITION ID IS D_1300030636. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-APR-22 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 : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : CU FINE FOCUS REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54056 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 200K REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29320 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 13.140 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.10910 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.2300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.58170 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.290 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MLPHARE REMARK 200 STARTING MODEL: 6WKM, 3BIS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.87 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG4000, 0.1M BIS-TRIS PH 6.2, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K 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 35.53800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.03450 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.44000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.03450 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.53800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.44000 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: 5380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 MET A 1 REMARK 465 ARG A 2 REMARK 465 ILE A 3 REMARK 465 PHE A 4 REMARK 465 ALA A 5 REMARK 465 VAL A 6 REMARK 465 PHE A 7 REMARK 465 ILE A 8 REMARK 465 PHE A 9 REMARK 465 MET A 10 REMARK 465 THR A 11 REMARK 465 TYR A 12 REMARK 465 TRP A 13 REMARK 465 HIS A 14 REMARK 465 LEU A 15 REMARK 465 LEU A 16 REMARK 465 ASN A 17 REMARK 465 ASN A 135 REMARK 465 LYS A 136 REMARK 465 LEU A 137 REMARK 465 GLU A 138 REMARK 465 GLY A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 HIS A 142 REMARK 465 HIS A 143 REMARK 465 HIS A 144 REMARK 465 HIS A 145 REMARK 465 HIS A 146 REMARK 465 HIS A 147 REMARK 465 CYS B 221 REMARK 465 GLY C 215 REMARK 465 GLU C 216 REMARK 465 CYS C 217 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 A 61 -4.00 67.50 REMARK 500 ASP B 98 -169.05 64.81 REMARK 500 PRO B 152 -157.75 -89.88 REMARK 500 GLU B 153 71.11 -119.43 REMARK 500 SER C 31 19.61 55.17 REMARK 500 THR C 53 -21.16 73.89 REMARK 500 SER C 54 1.46 -151.42 REMARK 500 ALA C 86 -169.84 -168.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU B 153 PRO B 154 116.74 REMARK 500 REMARK 500 REMARK: NULL DBREF 7YDS A 1 136 UNP Q9NZQ7 PD1L1_HUMAN 1 136 DBREF 7YDS B 1 221 PDB 7YDS 7YDS 1 221 DBREF 7YDS C 1 217 PDB 7YDS 7YDS 1 217 SEQADV 7YDS GLN A 35 UNP Q9NZQ7 ASN 35 ENGINEERED MUTATION SEQADV 7YDS LEU A 137 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS GLU A 138 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS GLY A 139 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS GLY A 140 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS GLY A 141 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 142 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 143 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 144 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 145 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 146 UNP Q9NZQ7 EXPRESSION TAG SEQADV 7YDS HIS A 147 UNP Q9NZQ7 EXPRESSION TAG SEQRES 1 A 147 MET ARG ILE PHE ALA VAL PHE ILE PHE MET THR TYR TRP SEQRES 2 A 147 HIS LEU LEU ASN ALA PHE THR VAL THR VAL PRO LYS ASP SEQRES 3 A 147 LEU TYR VAL VAL GLU TYR GLY SER GLN MET THR ILE GLU SEQRES 4 A 147 CYS LYS PHE PRO VAL GLU LYS GLN LEU ASP LEU ALA ALA SEQRES 5 A 147 LEU ILE VAL TYR TRP GLU MET GLU ASP LYS ASN ILE ILE SEQRES 6 A 147 GLN PHE VAL HIS GLY GLU GLU ASP LEU LYS VAL GLN HIS SEQRES 7 A 147 SER SER TYR ARG GLN ARG ALA ARG LEU LEU LYS ASP GLN SEQRES 8 A 147 LEU SER LEU GLY ASN ALA ALA LEU GLN ILE THR ASP VAL SEQRES 9 A 147 LYS LEU GLN ASP ALA GLY VAL TYR ARG CYS MET ILE SER SEQRES 10 A 147 TYR GLY GLY ALA ASP TYR LYS ARG ILE THR VAL LYS VAL SEQRES 11 A 147 ASN ALA PRO TYR ASN LYS LEU GLU GLY GLY GLY HIS HIS SEQRES 12 A 147 HIS HIS HIS HIS SEQRES 1 B 221 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 221 PRO GLY GLY SER LEU ARG LEU SER CYS THR VAL SER GLY SEQRES 3 B 221 ILE ASP LEU SER SER TYR ASP MET THR TRP VAL ARG GLN SEQRES 4 B 221 ALA PRO GLY LYS GLY LEU GLU TYR ILE GLY TYR ILE SER SEQRES 5 B 221 TYR VAL SER ARG THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 B 221 ARG PHE THR ILE SER LYS ASP THR SER LYS ASN THR VAL SEQRES 7 B 221 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 B 221 VAL TYR TYR CYS ALA ARG ASP ARG PRO ASP GLY ALA ALA SEQRES 9 B 221 THR ASN LEU TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 B 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 B 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 B 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 B 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 B 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 B 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 B 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 B 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 C 217 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 C 217 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN SER SER SEQRES 3 C 217 GLN ASN VAL TYR SER ASN ASN ARG LEU SER TRP TYR GLN SEQRES 4 C 217 GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TRP SEQRES 5 C 217 THR SER PHE LEU ALA SER GLY VAL PRO SER ARG PHE SER SEQRES 6 C 217 GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SER SEQRES 7 C 217 SER LEU GLN PRO ASP ASP PHE ALA THR TYR TYR CYS ALA SEQRES 8 C 217 GLY GLY TYR SER GLY ASN LEU TYR THR PHE GLY GLN GLY SEQRES 9 C 217 THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 C 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 C 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 C 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 C 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 C 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 C 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 C 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 C 217 THR LYS SER PHE ASN ARG GLY GLU CYS FORMUL 4 HOH *398(H2 O) HELIX 1 AA1 ASP A 49 ALA A 52 5 4 HELIX 2 AA2 HIS A 78 ARG A 82 5 5 HELIX 3 AA3 LEU A 88 SER A 93 1 6 HELIX 4 AA4 LYS A 105 ALA A 109 5 5 HELIX 5 AA5 ASP B 61 LYS B 64 5 4 HELIX 6 AA6 THR B 73 LYS B 75 5 3 HELIX 7 AA7 ARG B 86 THR B 90 5 5 HELIX 8 AA8 SER B 161 ALA B 163 5 3 HELIX 9 AA9 PRO B 190 LEU B 194 5 5 HELIX 10 AB1 LYS B 206 ASN B 209 5 4 HELIX 11 AB2 VAL C 29 ASN C 33 5 5 HELIX 12 AB3 GLN C 81 PHE C 85 5 5 HELIX 13 AB4 SER C 124 GLY C 131 1 8 HELIX 14 AB5 LYS C 186 LYS C 191 1 6 SHEET 1 AA1 6 LEU A 27 VAL A 30 0 SHEET 2 AA1 6 ALA A 121 VAL A 130 1 O LYS A 129 N TYR A 28 SHEET 3 AA1 6 GLY A 110 SER A 117 -1 N TYR A 112 O ILE A 126 SHEET 4 AA1 6 ILE A 54 MET A 59 -1 N ILE A 54 O SER A 117 SHEET 5 AA1 6 LYS A 62 VAL A 68 -1 O PHE A 67 N VAL A 55 SHEET 6 AA1 6 GLU A 71 ASP A 73 -1 O ASP A 73 N GLN A 66 SHEET 1 AA2 3 MET A 36 LYS A 41 0 SHEET 2 AA2 3 ASN A 96 ILE A 101 -1 O LEU A 99 N ILE A 38 SHEET 3 AA2 3 ALA A 85 LEU A 87 -1 N ARG A 86 O GLN A 100 SHEET 1 AA3 4 GLN B 3 SER B 7 0 SHEET 2 AA3 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA3 4 THR B 77 MET B 82 -1 O MET B 82 N LEU B 18 SHEET 4 AA3 4 PHE B 67 ASP B 72 -1 N THR B 68 O GLN B 81 SHEET 1 AA4 6 LEU B 11 VAL B 12 0 SHEET 2 AA4 6 THR B 112 VAL B 116 1 O THR B 115 N VAL B 12 SHEET 3 AA4 6 ALA B 91 ARG B 97 -1 N TYR B 93 O THR B 112 SHEET 4 AA4 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 94 SHEET 5 AA4 6 LEU B 45 ILE B 51 -1 O GLY B 49 N TRP B 36 SHEET 6 AA4 6 THR B 57 TYR B 59 -1 O TYR B 58 N TYR B 50 SHEET 1 AA5 4 SER B 125 LEU B 129 0 SHEET 2 AA5 4 ALA B 141 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AA5 4 TYR B 181 VAL B 189 -1 O TYR B 181 N TYR B 150 SHEET 4 AA5 4 VAL B 168 THR B 170 -1 N HIS B 169 O VAL B 186 SHEET 1 AA6 4 SER B 125 LEU B 129 0 SHEET 2 AA6 4 ALA B 141 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AA6 4 TYR B 181 VAL B 189 -1 O TYR B 181 N TYR B 150 SHEET 4 AA6 4 VAL B 174 LEU B 175 -1 N VAL B 174 O SER B 182 SHEET 1 AA7 3 THR B 156 TRP B 159 0 SHEET 2 AA7 3 TYR B 199 HIS B 205 -1 O ASN B 202 N SER B 158 SHEET 3 AA7 3 THR B 210 VAL B 216 -1 O VAL B 216 N TYR B 199 SHEET 1 AA8 4 MET C 4 SER C 7 0 SHEET 2 AA8 4 VAL C 19 SER C 25 -1 O THR C 22 N SER C 7 SHEET 3 AA8 4 GLU C 72 ILE C 77 -1 O PHE C 73 N CYS C 23 SHEET 4 AA8 4 PHE C 64 SER C 69 -1 N SER C 65 O THR C 76 SHEET 1 AA9 6 THR C 10 ALA C 13 0 SHEET 2 AA9 6 THR C 105 ILE C 109 1 O LYS C 106 N LEU C 11 SHEET 3 AA9 6 THR C 87 TYR C 94 -1 N TYR C 88 O THR C 105 SHEET 4 AA9 6 LEU C 35 GLN C 40 -1 N SER C 36 O ALA C 91 SHEET 5 AA9 6 LYS C 47 TYR C 51 -1 O LYS C 47 N GLN C 39 SHEET 6 AA9 6 PHE C 55 LEU C 56 -1 O PHE C 55 N TYR C 51 SHEET 1 AB1 4 THR C 10 ALA C 13 0 SHEET 2 AB1 4 THR C 105 ILE C 109 1 O LYS C 106 N LEU C 11 SHEET 3 AB1 4 THR C 87 TYR C 94 -1 N TYR C 88 O THR C 105 SHEET 4 AB1 4 LEU C 98 PHE C 101 -1 O LEU C 98 N TYR C 94 SHEET 1 AB2 4 SER C 117 PHE C 121 0 SHEET 2 AB2 4 THR C 132 PHE C 142 -1 O LEU C 138 N PHE C 119 SHEET 3 AB2 4 TYR C 176 SER C 185 -1 O LEU C 178 N LEU C 139 SHEET 4 AB2 4 SER C 162 VAL C 166 -1 N GLN C 163 O THR C 181 SHEET 1 AB3 4 ALA C 156 LEU C 157 0 SHEET 2 AB3 4 LYS C 148 VAL C 153 -1 N VAL C 153 O ALA C 156 SHEET 3 AB3 4 TYR C 195 THR C 200 -1 O ALA C 196 N LYS C 152 SHEET 4 AB3 4 VAL C 208 PHE C 212 -1 O LYS C 210 N CYS C 197 SSBOND 1 CYS A 40 CYS A 114 1555 1555 2.03 SSBOND 2 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 3 CYS B 145 CYS B 201 1555 1555 2.03 SSBOND 4 CYS C 23 CYS C 90 1555 1555 2.04 SSBOND 5 CYS C 137 CYS C 197 1555 1555 2.03 CISPEP 1 PHE B 151 PRO B 152 0 -4.68 CISPEP 2 SER C 7 PRO C 8 0 -2.69 CISPEP 3 TYR C 143 PRO C 144 0 2.48 CRYST1 71.076 94.880 96.069 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 0.014069 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010540 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010409 0.00000