HEADER DE NOVO PROTEIN 29-APR-20 6YWD TITLE DE NOVO DESIGNED PROTEIN 4H_01 IN COMPLEX WITH MOTA ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY MOTA, HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY MOTA, LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DE NOVO DESIGNED PROTEIN 4H_01; COMPND 11 CHAIN: C; COMPND 12 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 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 17 ORGANISM_TAXID: 32630; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DE NOVO DESIGNED PROTEIN, DE NOVO PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR C.YANG,F.SESTERHENN,F.POJER,B.E.CORREIA REVDAT 1 07-OCT-20 6YWD 0 JRNL AUTH C.YANG,F.SESTERHENN,B.E.CORREIA JRNL TITL BOTTOM-UP DE NOVO DESIGN OF FUNCTIONAL PROTEINS WITH COMPLEX JRNL TITL 2 STRUCTURAL FEATURES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.13_2998 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 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.04 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 34158 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.870 REMARK 3 FREE R VALUE TEST SET COUNT : 3372 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 47.0400 - 9.2100 1.00 1289 151 0.1762 0.1998 REMARK 3 2 9.2100 - 7.3200 1.00 1291 135 0.1610 0.1729 REMARK 3 3 7.3200 - 6.3900 1.00 1294 137 0.1988 0.2921 REMARK 3 4 6.3900 - 5.8100 1.00 1301 145 0.1990 0.2470 REMARK 3 5 5.8100 - 5.3900 1.00 1269 144 0.1856 0.2497 REMARK 3 6 5.3900 - 5.0800 1.00 1311 130 0.1716 0.2154 REMARK 3 7 5.0800 - 4.8200 1.00 1283 144 0.1562 0.1966 REMARK 3 8 4.8200 - 4.6100 1.00 1286 135 0.1669 0.1764 REMARK 3 9 4.6100 - 4.4400 1.00 1292 142 0.1657 0.2326 REMARK 3 10 4.4400 - 4.2800 1.00 1293 143 0.1679 0.1939 REMARK 3 11 4.2800 - 4.1500 1.00 1301 139 0.1679 0.2105 REMARK 3 12 4.1500 - 4.0300 1.00 1286 150 0.2163 0.2548 REMARK 3 13 4.0300 - 3.9200 1.00 1279 140 0.2283 0.2456 REMARK 3 14 3.9200 - 3.8300 1.00 1286 130 0.2199 0.2510 REMARK 3 15 3.8300 - 3.7400 1.00 1322 150 0.2241 0.3045 REMARK 3 16 3.7400 - 3.6600 0.99 1241 141 0.2509 0.2621 REMARK 3 17 3.6600 - 3.5900 0.98 1253 138 0.2525 0.2759 REMARK 3 18 3.5900 - 3.5200 0.99 1289 142 0.2584 0.3552 REMARK 3 19 3.5200 - 3.4600 0.99 1249 141 0.2694 0.3331 REMARK 3 20 3.4600 - 3.4000 0.99 1288 147 0.2841 0.3163 REMARK 3 21 3.4000 - 3.3500 1.00 1265 131 0.3075 0.3921 REMARK 3 22 3.3500 - 3.2900 0.99 1335 155 0.3321 0.3308 REMARK 3 23 3.2900 - 3.2500 1.00 1260 133 0.3413 0.3977 REMARK 3 24 3.2500 - 3.2000 0.97 1223 129 0.3751 0.4467 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.455 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.983 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 76.37 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.88 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 : 0.004 4000 REMARK 3 ANGLE : 0.797 5444 REMARK 3 CHIRALITY : 0.049 624 REMARK 3 PLANARITY : 0.004 687 REMARK 3 DIHEDRAL : 4.656 2394 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 6YWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-APR-20. REMARK 100 THE DEPOSITION ID IS D_1292108162. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-FEB-20 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 : SLS REMARK 200 BEAMLINE : X06DA 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 2M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 757244 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 47.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 14.70 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.96 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : 14.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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: 4JLR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 72.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH 9.3, 22% V/V PEG SMEAR REMARK 280 BROAD, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.07433 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.14867 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 60.14867 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.07433 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: 5180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 GLY A 2 REMARK 465 CYS A 3 REMARK 465 VAL A 4 REMARK 465 ALA A 5 REMARK 465 GLU A 6 REMARK 465 THR A 7 REMARK 465 GLY A 8 REMARK 465 ASP A 232 REMARK 465 LYS A 233 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 CYS B 3 REMARK 465 VAL B 4 REMARK 465 ALA B 5 REMARK 465 GLU B 6 REMARK 465 THR B 7 REMARK 465 GLY B 8 REMARK 465 MET C 1 REMARK 465 GLU C 2 REMARK 465 GLY C 45 REMARK 465 HIS C 46 REMARK 465 VAL C 80 REMARK 465 LYS C 81 REMARK 465 TYR C 82 REMARK 465 GLN C 83 REMARK 465 GLY C 84 REMARK 465 SER C 85 REMARK 465 HIS C 86 REMARK 465 HIS C 87 REMARK 465 HIS C 88 REMARK 465 HIS C 89 REMARK 465 HIS C 90 REMARK 465 HIS C 91 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 LYS C 28 OG SER C 32 2.18 REMARK 500 OG SER A 218 OG1 THR A 220 2.19 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 O GLY B 71 NZ LYS B 195 2544 2.15 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 LEU A 73 57.03 -98.71 REMARK 500 ASP A 75 -15.90 77.00 REMARK 500 PRO A 141 92.09 -57.61 REMARK 500 ASP A 159 64.02 60.95 REMARK 500 ASP B 57 -114.45 52.88 REMARK 500 ASN B 145 77.22 49.28 REMARK 500 LYS B 197 -76.02 -111.83 REMARK 500 SER C 64 -106.99 52.28 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6YWC RELATED DB: PDB DBREF 6YWD A 1 233 PDB 6YWD 6YWD 1 233 DBREF 6YWD B 1 221 PDB 6YWD 6YWD 1 221 DBREF 6YWD C 1 91 PDB 6YWD 6YWD 1 91 SEQRES 1 A 233 MET GLY CYS VAL ALA GLU THR GLY GLN VAL THR LEU ARG SEQRES 2 A 233 GLU SER GLY PRO ALA LEU VAL LYS PRO THR GLN THR LEU SEQRES 3 A 233 THR LEU THR CYS THR PHE SER GLY PHE SER LEU SER THR SEQRES 4 A 233 ALA GLY MET SER VAL GLY TRP ILE ARG GLN PRO PRO GLY SEQRES 5 A 233 LYS ALA LEU GLU TRP LEU ALA ASP ILE TRP TRP ASP ASP SEQRES 6 A 233 LYS LYS HIS TYR ASN PRO SER LEU LYS ASP ARG LEU THR SEQRES 7 A 233 ILE SER LYS ASP THR SER LYS ASN GLN VAL VAL LEU LYS SEQRES 8 A 233 VAL THR ASN MET ASP PRO ALA ASP THR ALA THR TYR TYR SEQRES 9 A 233 CYS ALA ARG ASP MET ILE PHE ASN PHE TYR PHE ASP VAL SEQRES 10 A 233 TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SER SEQRES 11 A 233 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER SEQRES 12 A 233 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 A 233 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 A 233 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 A 233 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 A 233 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 A 233 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 A 233 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS SEQRES 1 B 221 MET GLY CYS VAL ALA GLU THR GLY ASP ILE GLN MET THR SEQRES 2 B 221 GLN SER PRO SER THR LEU SER ALA SER VAL GLY ASP ARG SEQRES 3 B 221 VAL THR ILE THR CYS SER ALA SER SER ARG VAL GLY TYR SEQRES 4 B 221 MET HIS TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS SEQRES 5 B 221 LEU LEU ILE TYR ASP THR SER LYS LEU ALA SER GLY VAL SEQRES 6 B 221 PRO SER ARG PHE SER GLY SER GLY SER GLY THR GLU PHE SEQRES 7 B 221 THR LEU THR ILE SER SER LEU GLN PRO ASP ASP PHE ALA SEQRES 8 B 221 THR TYR TYR CYS PHE GLN GLY SER GLY TYR PRO PHE THR SEQRES 9 B 221 PHE GLY GLY GLY THR LYS VAL GLU ILE LYS ARG THR VAL SEQRES 10 B 221 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 11 B 221 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 12 B 221 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 13 B 221 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 14 B 221 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 15 B 221 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 16 B 221 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 17 B 221 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 91 MET GLU VAL GLU ARG GLU LEU ARG ASN TRP LEU SER GLU SEQRES 2 C 91 VAL LEU SER LYS ILE ASN ASP ALA PRO VAL THR ASN ASP SEQRES 3 C 91 ILE LYS LYS ALA ILE SER ASN GLN VAL LEU LYS VAL ALA SEQRES 4 C 91 GLU GLN VAL TRP ASN GLY HIS SER LYS GLU GLU LEU GLN SEQRES 5 C 91 GLU ARG VAL ARG LYS GLU VAL CYS SER VAL CYS SER ASN SEQRES 6 C 91 VAL PRO ALA CYS TRP ALA ILE CYS GLY GLY LEU LEU GLU SEQRES 7 C 91 VAL VAL LYS TYR GLN GLY SER HIS HIS HIS HIS HIS HIS HELIX 1 AA1 PRO A 71 LYS A 74 5 4 HELIX 2 AA2 ASP A 96 THR A 100 5 5 HELIX 3 AA3 SER A 171 ALA A 173 5 3 HELIX 4 AA4 SER A 202 LEU A 204 5 3 HELIX 5 AA5 GLN B 86 PHE B 90 5 5 HELIX 6 AA6 SER B 128 LYS B 133 1 6 HELIX 7 AA7 LYS B 190 LYS B 195 1 6 HELIX 8 AA8 GLU C 4 ASP C 20 1 17 HELIX 9 AA9 THR C 24 GLN C 41 1 18 HELIX 10 AB1 GLU C 50 CYS C 60 1 11 HELIX 11 AB2 SER C 61 SER C 64 5 4 HELIX 12 AB3 VAL C 66 VAL C 79 1 14 SHEET 1 AA1 4 THR A 11 SER A 15 0 SHEET 2 AA1 4 LEU A 26 SER A 33 -1 O THR A 29 N SER A 15 SHEET 3 AA1 4 GLN A 87 VAL A 92 -1 O LEU A 90 N LEU A 28 SHEET 4 AA1 4 LEU A 77 ASP A 82 -1 N ASP A 82 O GLN A 87 SHEET 1 AA2 6 LEU A 19 VAL A 20 0 SHEET 2 AA2 6 THR A 122 VAL A 126 1 O THR A 125 N VAL A 20 SHEET 3 AA2 6 ALA A 101 MET A 109 -1 N TYR A 103 O THR A 122 SHEET 4 AA2 6 MET A 42 GLN A 49 -1 N ILE A 47 O TYR A 104 SHEET 5 AA2 6 GLU A 56 TRP A 62 -1 O LEU A 58 N TRP A 46 SHEET 6 AA2 6 LYS A 67 TYR A 69 -1 O HIS A 68 N ASP A 60 SHEET 1 AA3 4 LEU A 19 VAL A 20 0 SHEET 2 AA3 4 THR A 122 VAL A 126 1 O THR A 125 N VAL A 20 SHEET 3 AA3 4 ALA A 101 MET A 109 -1 N TYR A 103 O THR A 122 SHEET 4 AA3 4 PHE A 115 TRP A 118 -1 O VAL A 117 N ARG A 107 SHEET 1 AA4 4 SER A 135 LEU A 139 0 SHEET 2 AA4 4 THR A 150 TYR A 160 -1 O LYS A 158 N SER A 135 SHEET 3 AA4 4 TYR A 191 PRO A 200 -1 O LEU A 193 N VAL A 157 SHEET 4 AA4 4 VAL A 178 THR A 180 -1 N HIS A 179 O VAL A 196 SHEET 1 AA5 4 SER A 135 LEU A 139 0 SHEET 2 AA5 4 THR A 150 TYR A 160 -1 O LYS A 158 N SER A 135 SHEET 3 AA5 4 TYR A 191 PRO A 200 -1 O LEU A 193 N VAL A 157 SHEET 4 AA5 4 VAL A 184 LEU A 185 -1 N VAL A 184 O SER A 192 SHEET 1 AA6 3 VAL A 165 TRP A 169 0 SHEET 2 AA6 3 ILE A 210 HIS A 215 -1 O ASN A 214 N THR A 166 SHEET 3 AA6 3 THR A 220 LYS A 225 -1 O THR A 220 N HIS A 215 SHEET 1 AA7 4 THR B 13 SER B 15 0 SHEET 2 AA7 4 VAL B 27 SER B 32 -1 O THR B 30 N SER B 15 SHEET 3 AA7 4 GLU B 77 ILE B 82 -1 O LEU B 80 N ILE B 29 SHEET 4 AA7 4 PHE B 69 SER B 74 -1 N SER B 70 O THR B 81 SHEET 1 AA8 6 THR B 18 SER B 22 0 SHEET 2 AA8 6 THR B 109 LYS B 114 1 O GLU B 112 N LEU B 19 SHEET 3 AA8 6 ALA B 91 GLN B 97 -1 N ALA B 91 O VAL B 111 SHEET 4 AA8 6 HIS B 41 GLN B 45 -1 N TYR B 43 O TYR B 94 SHEET 5 AA8 6 LYS B 52 TYR B 56 -1 O LEU B 54 N TRP B 42 SHEET 6 AA8 6 LYS B 60 LEU B 61 -1 O LYS B 60 N TYR B 56 SHEET 1 AA9 4 THR B 18 SER B 22 0 SHEET 2 AA9 4 THR B 109 LYS B 114 1 O GLU B 112 N LEU B 19 SHEET 3 AA9 4 ALA B 91 GLN B 97 -1 N ALA B 91 O VAL B 111 SHEET 4 AA9 4 THR B 104 PHE B 105 -1 O THR B 104 N GLN B 97 SHEET 1 AB1 4 SER B 121 PHE B 125 0 SHEET 2 AB1 4 THR B 136 PHE B 146 -1 O LEU B 142 N PHE B 123 SHEET 3 AB1 4 TYR B 180 SER B 189 -1 O LEU B 182 N LEU B 143 SHEET 4 AB1 4 SER B 166 VAL B 170 -1 N GLN B 167 O THR B 185 SHEET 1 AB2 4 ALA B 160 GLN B 162 0 SHEET 2 AB2 4 LYS B 152 VAL B 157 -1 N VAL B 157 O ALA B 160 SHEET 3 AB2 4 TYR B 199 THR B 204 -1 O GLU B 202 N GLN B 154 SHEET 4 AB2 4 VAL B 212 PHE B 216 -1 O LYS B 214 N CYS B 201 SSBOND 1 CYS A 30 CYS A 105 1555 1555 2.03 SSBOND 2 CYS A 155 CYS A 211 1555 1555 2.04 SSBOND 3 CYS A 231 CYS B 221 1555 1555 2.03 SSBOND 4 CYS B 31 CYS B 95 1555 1555 2.04 SSBOND 5 CYS B 141 CYS B 201 1555 1555 2.03 SSBOND 6 CYS C 60 CYS C 73 1555 1555 2.03 SSBOND 7 CYS C 63 CYS C 69 1555 1555 2.03 CISPEP 1 PHE A 161 PRO A 162 0 -1.63 CISPEP 2 GLU A 163 PRO A 164 0 3.61 CISPEP 3 SER B 15 PRO B 16 0 -0.06 CISPEP 4 TYR B 101 PRO B 102 0 0.41 CISPEP 5 TYR B 147 PRO B 148 0 1.03 CRYST1 143.710 143.710 90.223 90.00 90.00 120.00 P 31 2 1 6 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 0.006958 0.004017 0.000000 0.00000 SCALE2 0.000000 0.008035 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011084 0.00000