HEADER IMMUNE SYSTEM 10-MAY-24 9BR5 TITLE IL1RAP-SPECIFIC FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: IL1RAP-SPECIFIC FAB LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: FAB LIGHT CHAIN; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IL1RAP-SPECIFIC FAB HEAVY CHAIN; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: FAB HEAVY CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS FAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.C.MALLETT,J.C.WILLIAMS,M.PARK REVDAT 1 27-AUG-25 9BR5 0 JRNL AUTH Y.ZHANG,M.PARK,L.Y.GHODA,D.ZHAO,M.VALERIO,E.NAFIE, JRNL AUTH 2 A.GONZALEZ,K.LY,B.PARCUTELA,H.CHOI,X.GONG,F.CHEN,K.HARADA, JRNL AUTH 3 Z.CHEN,L.X.T.NGUYEN,F.PICHIORRI,J.CHEN,J.SONG,S.J.FORMAN, JRNL AUTH 4 I.AMANAM,B.ZHANG,J.JIN,J.C.WILLIAMS,G.MARCUCCI JRNL TITL IL1RAP-SPECIFIC T CELL ENGAGER DEPLETES ACUTE MYELOID JRNL TITL 2 LEUKEMIA STEM CELLS. JRNL REF J HEMATOL ONCOL V. 17 67 2024 JRNL REFN ISSN 1756-8722 JRNL PMID 39143574 JRNL DOI 10.1186/S13045-024-01586-X REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019 REMARK 1 REF 2 BIOL. CRYSTALLOGR. REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.K.SCHNEIDER,A.S.SOARES,E.O.LAZO,D.F.KREITLER,K.QIAN, REMARK 1 AUTH 2 M.R.FUCHS,D.K.BHOGADI,S.ANTONELLI,S.S.MYERS,B.S.MARTINS, REMARK 1 AUTH 3 J.M.SKINNER,J.AISHIMA,H.J.BERNSTEIN,T.LANGDON,J.LARA, REMARK 1 AUTH 4 R.PETKUS,M.COWAN,L.FLAKS,T.SMITH,G.SHEA-MCCARTHY,M.IDIR, REMARK 1 AUTH 5 L.HUANG,O.CHUBAR,R.M.SWEET,L.E.BERMAN,S.MCSWEENEY,J.JAKONCIC REMARK 1 TITL AMX - THE HIGHLY AUTOMATED MACROMOLECULAR CRYSTALLOGRAPHY REMARK 1 TITL 2 (17-ID-1) BEAMLINE AT THE NSLS-II. REMARK 1 REF J SYNCHROTRON RADIAT V. 29 1480 2022 REMARK 1 REFN ESSN 1600-5775 REMARK 1 PMID 36345756 REMARK 1 DOI 10.1107/S1600577522009377 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 10418 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.230 REMARK 3 FREE R VALUE TEST SET COUNT : 441 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 32.7200 - 4.1800 1.00 3342 134 0.1713 0.2132 REMARK 3 2 4.1800 - 3.3200 1.00 3315 147 0.2428 0.3028 REMARK 3 3 3.3200 - 2.9000 1.00 3320 160 0.3159 0.3444 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) : 0.047 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.504 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 66.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.08 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 : 0.008 3376 REMARK 3 ANGLE : 0.808 4605 REMARK 3 CHIRALITY : 0.053 523 REMARK 3 PLANARITY : 0.007 580 REMARK 3 DIHEDRAL : 20.217 1203 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 6.7059 -12.3628 -8.1619 REMARK 3 T TENSOR REMARK 3 T11: 0.7582 T22: 0.3063 REMARK 3 T33: 0.4468 T12: 0.0512 REMARK 3 T13: -0.0697 T23: -0.0091 REMARK 3 L TENSOR REMARK 3 L11: 0.9974 L22: 3.0363 REMARK 3 L33: 1.1762 L12: 0.6730 REMARK 3 L13: -0.0178 L23: -0.2152 REMARK 3 S TENSOR REMARK 3 S11: 0.5928 S12: -0.0135 S13: -0.1180 REMARK 3 S21: 0.4039 S22: -0.4522 S23: 0.0793 REMARK 3 S31: 0.5166 S32: 0.1252 S33: 0.0758 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 9BR5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283957. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9201 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103107 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 32.720 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5 REMARK 200 DATA REDUNDANCY IN SHELL : 7.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.900 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 (%): 52.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M SODIUM ACETATE, 0.085 M TRIS-CL REMARK 280 PH 8.5, 25.5% (W/V) PEG 4000, 15% (V/V) GLYCEROL, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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 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 32.79100 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 65.58200 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: 3800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 GLY B 42 REMARK 465 LYS B 43 REMARK 465 CYS B 220 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 LYS A 168 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 OG SER B 7 H SER B 21 1.58 REMARK 500 H SER A 14 OE2 GLU A 17 1.60 REMARK 500 OG SER A 14 OE2 GLU A 17 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 193 CA - CB - SG ANGL. DEV. = 7.0 DEGREES 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 PRO A 15 140.48 -39.51 REMARK 500 TRP A 46 -53.53 -130.17 REMARK 500 THR A 50 40.48 34.65 REMARK 500 SER A 51 -44.46 179.02 REMARK 500 ASN A 137 71.40 57.06 REMARK 500 LYS A 189 -70.57 -106.86 REMARK 500 GLN B 3 123.68 -175.22 REMARK 500 PRO B 14 154.75 -48.97 REMARK 500 VAL B 16 -159.07 -66.65 REMARK 500 ALA B 92 -179.39 -177.33 REMARK 500 ALA B 109 0.96 -68.47 REMARK 500 SER B 136 118.63 -165.22 REMARK 500 ASP B 148 65.91 66.32 REMARK 500 SER B 160 34.54 38.60 REMARK 500 THR B 164 -29.81 -141.15 REMARK 500 REMARK 500 REMARK: NULL DBREF 9BR5 A 1 213 PDB 9BR5 9BR5 1 213 DBREF 9BR5 B 1 220 PDB 9BR5 9BR5 1 220 SEQRES 1 A 213 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 A 213 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER SEQRES 3 A 213 SER THR ILE ILE TYR ILE HIS TRP TYR GLN GLN LYS PRO SEQRES 4 A 213 GLY THR SER PRO LYS GLY TRP ILE TYR ASP THR SER LYS SEQRES 5 A 213 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 A 213 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 A 213 ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN ARG THR SEQRES 8 A 213 SER TYR PRO TRP THR PHE GLY GLY GLY THR LYS LEU GLU SEQRES 9 A 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 A 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 A 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 A 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 A 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 A 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 A 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 A 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 A 213 ASN ARG GLY GLU CYS SEQRES 1 B 220 GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL ARG SEQRES 2 B 220 PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY SER GLY SEQRES 3 B 220 TYR THR PHE THR ASP TYR ALA MET HIS TRP VAL LYS GLN SEQRES 4 B 220 SER HIS GLY LYS GLY LEU GLU TRP ILE GLY ILE ILE SER SEQRES 5 B 220 THR TYR SER GLY ASN THR LYS PHE HIS GLN LYS PHE LYS SEQRES 6 B 220 GLY LYS ALA THR MET THR VAL ASP LYS SER SER SER THR SEQRES 7 B 220 ALA TYR MET GLU LEU ALA ARG LEU THR SER GLU ASP SER SEQRES 8 B 220 ALA ILE TYR TYR CYS ALA ARG GLN GLY THR TRP TYR PHE SEQRES 9 B 220 ASP VAL TRP GLY ALA GLY THR THR VAL THR VAL SER SER SEQRES 10 B 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 B 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 B 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 B 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 B 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 B 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 B 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 B 220 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS ALA CYS HELIX 1 AA1 GLU A 78 ALA A 82 5 5 HELIX 2 AA2 SER A 120 SER A 126 1 7 HELIX 3 AA3 LYS A 182 GLU A 186 1 5 HELIX 4 AA4 THR B 28 TYR B 32 5 5 HELIX 5 AA5 GLN B 62 LYS B 65 5 4 HELIX 6 AA6 THR B 87 SER B 91 5 5 HELIX 7 AA7 SER B 131 THR B 135 5 5 HELIX 8 AA8 SER B 160 ALA B 162 5 3 HELIX 9 AA9 SER B 191 LEU B 193 5 3 HELIX 10 AB1 LYS B 205 ASN B 208 5 4 SHEET 1 AA1 4 LEU A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 AA1 4 SER A 69 ILE A 74 -1 O TYR A 70 N CYS A 23 SHEET 4 AA1 4 PHE A 61 SER A 66 -1 N SER A 62 O THR A 73 SHEET 1 AA2 6 ILE A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 101 ILE A 105 1 O GLU A 104 N MET A 11 SHEET 3 AA2 6 THR A 84 GLN A 89 -1 N TYR A 85 O THR A 101 SHEET 4 AA2 6 ILE A 32 GLN A 37 -1 N TYR A 35 O TYR A 86 SHEET 5 AA2 6 LYS A 44 TYR A 48 -1 O ILE A 47 N TRP A 34 SHEET 6 AA2 6 LYS A 52 LEU A 53 -1 O LYS A 52 N TYR A 48 SHEET 1 AA3 4 ILE A 10 ALA A 13 0 SHEET 2 AA3 4 THR A 101 ILE A 105 1 O GLU A 104 N MET A 11 SHEET 3 AA3 4 THR A 84 GLN A 89 -1 N TYR A 85 O THR A 101 SHEET 4 AA3 4 THR A 96 PHE A 97 -1 O THR A 96 N GLN A 89 SHEET 1 AA4 4 SER A 113 PHE A 117 0 SHEET 2 AA4 4 THR A 128 PHE A 138 -1 O VAL A 132 N PHE A 117 SHEET 3 AA4 4 TYR A 172 SER A 181 -1 O LEU A 174 N LEU A 135 SHEET 4 AA4 4 SER A 158 VAL A 162 -1 N GLN A 159 O THR A 177 SHEET 1 AA5 4 ALA A 152 LEU A 153 0 SHEET 2 AA5 4 LYS A 144 VAL A 149 -1 N VAL A 149 O ALA A 152 SHEET 3 AA5 4 VAL A 190 THR A 196 -1 O GLU A 194 N GLN A 146 SHEET 4 AA5 4 VAL A 204 ASN A 209 -1 O VAL A 204 N VAL A 195 SHEET 1 AA6 4 GLN B 3 GLN B 6 0 SHEET 2 AA6 4 VAL B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA6 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AA6 4 THR B 69 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 AA7 6 GLU B 10 VAL B 12 0 SHEET 2 AA7 6 THR B 111 VAL B 115 1 O THR B 112 N GLU B 10 SHEET 3 AA7 6 ALA B 92 GLN B 99 -1 N ALA B 92 O VAL B 113 SHEET 4 AA7 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA7 6 TRP B 47 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AA7 6 THR B 58 PHE B 60 -1 O LYS B 59 N ILE B 50 SHEET 1 AA8 4 GLU B 10 VAL B 12 0 SHEET 2 AA8 4 THR B 111 VAL B 115 1 O THR B 112 N GLU B 10 SHEET 3 AA8 4 ALA B 92 GLN B 99 -1 N ALA B 92 O VAL B 113 SHEET 4 AA8 4 PHE B 104 TRP B 107 -1 O VAL B 106 N ARG B 98 SHEET 1 AA9 4 SER B 124 LEU B 128 0 SHEET 2 AA9 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 AA9 4 TYR B 180 PRO B 189 -1 O VAL B 186 N LEU B 142 SHEET 4 AA9 4 VAL B 167 THR B 169 -1 N HIS B 168 O VAL B 185 SHEET 1 AB1 4 SER B 124 LEU B 128 0 SHEET 2 AB1 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 AB1 4 TYR B 180 PRO B 189 -1 O VAL B 186 N LEU B 142 SHEET 4 AB1 4 VAL B 173 LEU B 174 -1 N VAL B 173 O SER B 181 SHEET 1 AB2 3 THR B 155 TRP B 158 0 SHEET 2 AB2 3 ILE B 199 HIS B 204 -1 O ASN B 201 N SER B 157 SHEET 3 AB2 3 THR B 209 ARG B 214 -1 O VAL B 211 N VAL B 202 SSBOND 1 CYS A 23 CYS A 87 1555 1555 2.05 SSBOND 2 CYS A 133 CYS A 193 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 4 CYS B 144 CYS B 200 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 -1.70 CISPEP 2 TYR A 93 PRO A 94 0 -0.58 CISPEP 3 TYR A 139 PRO A 140 0 4.10 CISPEP 4 PHE B 150 PRO B 151 0 -2.16 CISPEP 5 GLU B 152 PRO B 153 0 2.84 CRYST1 65.440 65.440 98.373 90.00 90.00 120.00 P 31 3 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 0.015281 0.008823 0.000000 0.00000 SCALE2 0.000000 0.017645 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010165 0.00000