HEADER IMMUNE SYSTEM 17-FEB-25 9NCY TITLE FAB1392 IN COMPLEX WITH THE C-TERMINAL ALPHA-TSR DOMAIN OF THE P. TITLE 2 FALCIPARUM CIRCUMSPOROZOITE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB1392 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB1392 LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: CS,PFCSP; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 13 ORGANISM_TAXID: 36329; SOURCE 14 GENE: CSP, PF3D7_0304600; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.MOSKOVITZ,I.A.WILSON REVDAT 1 11-MAR-26 9NCY 0 JRNL AUTH R.MOSKOVITZ,I.A.WILSON JRNL TITL FAB1392 IN COMPLEX WITH THE C-TERMINAL ALPHA-TSR DOMAIN OF JRNL TITL 2 THE P. FALCIPARUM CIRCUMSPOROZOITE PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.63 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) : 1.63 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.15 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 114853 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.175 REMARK 3 R VALUE (WORKING SET) : 0.174 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890 REMARK 3 FREE R VALUE TEST SET COUNT : 5617 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 42.1500 - 5.0600 0.99 4039 187 0.2024 0.2120 REMARK 3 2 5.0600 - 4.0200 1.00 3952 205 0.1391 0.1645 REMARK 3 3 4.0200 - 3.5100 1.00 3924 186 0.1565 0.1661 REMARK 3 4 3.5100 - 3.1900 0.99 3838 196 0.1652 0.1806 REMARK 3 5 3.1900 - 2.9600 0.99 3855 185 0.1766 0.2036 REMARK 3 6 2.9600 - 2.7900 1.00 3830 219 0.1743 0.1861 REMARK 3 7 2.7900 - 2.6500 0.99 3889 169 0.1694 0.2002 REMARK 3 8 2.6500 - 2.5300 1.00 3842 201 0.1641 0.1841 REMARK 3 9 2.5300 - 2.4400 1.00 3822 215 0.1639 0.1690 REMARK 3 10 2.4400 - 2.3500 1.00 3823 192 0.1666 0.1972 REMARK 3 11 2.3500 - 2.2800 1.00 3844 186 0.1692 0.1867 REMARK 3 12 2.2800 - 2.2100 0.98 3807 174 0.1639 0.1994 REMARK 3 13 2.2100 - 2.1500 1.00 3854 163 0.1622 0.1829 REMARK 3 14 2.1500 - 2.1000 0.99 3837 198 0.1564 0.2012 REMARK 3 15 2.1000 - 2.0500 0.99 3778 214 0.1667 0.1811 REMARK 3 16 2.0500 - 2.0100 0.99 3800 191 0.1655 0.1922 REMARK 3 17 2.0100 - 1.9700 0.99 3787 218 0.1728 0.1790 REMARK 3 18 1.9700 - 1.9300 1.00 3771 228 0.1884 0.2272 REMARK 3 19 1.9300 - 1.9000 0.99 3790 190 0.2018 0.2418 REMARK 3 20 1.9000 - 1.8700 0.99 3805 226 0.2081 0.2266 REMARK 3 21 1.8700 - 1.8400 0.99 3760 211 0.2063 0.2344 REMARK 3 22 1.8400 - 1.8100 0.99 3776 187 0.2049 0.2264 REMARK 3 23 1.8100 - 1.7800 0.98 3772 172 0.2150 0.2596 REMARK 3 24 1.7800 - 1.7600 0.95 3665 192 0.2176 0.2402 REMARK 3 25 1.7600 - 1.7300 0.91 3436 184 0.2387 0.2526 REMARK 3 26 1.7300 - 1.7100 0.86 3249 198 0.2605 0.2882 REMARK 3 27 1.7100 - 1.6900 0.80 3089 168 0.2940 0.2766 REMARK 3 28 1.6900 - 1.6700 0.76 2874 140 0.3569 0.3757 REMARK 3 29 1.6700 - 1.6500 0.68 2577 124 0.4337 0.5399 REMARK 3 30 1.6500 - 1.6300 0.56 2151 98 0.5186 0.5071 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) : 20.540 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.81 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 : 0.017 4144 REMARK 3 ANGLE : 1.481 5616 REMARK 3 CHIRALITY : 0.086 616 REMARK 3 PLANARITY : 0.014 718 REMARK 3 DIHEDRAL : 15.494 1521 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 9NCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000293062. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-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 : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03317 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 : 114968 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630 REMARK 200 RESOLUTION RANGE LOW (A) : 42.140 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 200 DATA REDUNDANCY : 12.30 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 65.7 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 1.27000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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 (%): 71.31 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG-600, 10% (V/V) GLYCEROL, 0.5 M REMARK 280 NH4-SULFATE, 0.1 M TRIS PH 7.0, FINAL PH 5.6., VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 68.19650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.19650 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 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 47.67750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.07300 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.67750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.07300 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.19650 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.67750 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.07300 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.19650 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.67750 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.07300 REMARK 290 SMTRY3 8 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 APPLY THE FOLLOWING TO CHAINS: H, L, A 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 215 REMARK 465 CYS H 216 REMARK 465 CYS L 219 REMARK 465 SER A 375 REMARK 465 SER A 376 REMARK 465 HIS A 377 REMARK 465 HIS A 378 REMARK 465 HIS A 379 REMARK 465 HIS A 380 REMARK 465 HIS A 381 REMARK 465 HIS A 382 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 L 145 CG CD CE NZ REMARK 470 GLU A 372 CD OE1 OE2 REMARK 470 LYS A 373 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 330 CD GLU A 330 OE1 0.098 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 ASP L 28 CB - CG - OD1 ANGL. DEV. = 6.3 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 SER H 15 -4.00 74.24 REMARK 500 ASN L 30 -132.38 57.34 REMARK 500 ALA L 51 -34.78 69.79 REMARK 500 LEU L 93 -28.02 65.81 REMARK 500 ASN L 152 -2.66 68.78 REMARK 500 REMARK 500 REMARK: NULL DBREF 9NCY H 1 216 PDB 9NCY 9NCY 1 216 DBREF 9NCY L 1 219 PDB 9NCY 9NCY 1 219 DBREF 9NCY A 310 376 UNP Q7K740 CSP_PLAF7 310 376 SEQADV 9NCY HIS A 377 UNP Q7K740 EXPRESSION TAG SEQADV 9NCY HIS A 378 UNP Q7K740 EXPRESSION TAG SEQADV 9NCY HIS A 379 UNP Q7K740 EXPRESSION TAG SEQADV 9NCY HIS A 380 UNP Q7K740 EXPRESSION TAG SEQADV 9NCY HIS A 381 UNP Q7K740 EXPRESSION TAG SEQADV 9NCY HIS A 382 UNP Q7K740 EXPRESSION TAG SEQRES 1 H 230 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 H 230 SER SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 230 ASP SER MET ARG ARG TYR PHE ARG ASN TRP ILE ARG GLN SEQRES 4 H 230 SER PRO GLY ARG GLY LEU GLU TRP ILE GLY ALA ILE PHE SEQRES 5 H 230 ASP ASN GLY SER THR ARG TYR ASN PRO SER LEU LYS SER SEQRES 6 H 230 ARG VAL THR MET SER VAL ASP VAL SER LYS ASN GLN PHE SEQRES 7 H 230 SER LEU ARG LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 230 VAL TYR TYR CYS ALA ARG ALA ARG ASP TYR TYR ASP PHE SEQRES 9 H 230 LEU THR ARG THR TYR ARG ASN PHE TYR PHE ASP TYR TRP SEQRES 10 H 230 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 H 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 213 SER VAL GLY GLU ARG VAL ILE ILE THR CYS GLN ALA SER SEQRES 3 L 213 GLN ASP ILE ASN HIS TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 213 LYS LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR ASP PHE THR PHE THR ILE ALA SER LEU SEQRES 7 L 213 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN HIS TYR SEQRES 8 L 213 ASP LEU TYR PRO LEU PHE GLY GLY GLY THR LYS VAL ASP SEQRES 9 L 213 VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 A 73 GLU PRO SER ASP LYS HIS ILE LYS GLU TYR LEU ASN LYS SEQRES 2 A 73 ILE GLN ASN SER LEU SER THR GLU TRP SER PRO CYS SER SEQRES 3 A 73 VAL THR CYS GLY ASN GLY ILE GLN VAL ARG ILE LYS PRO SEQRES 4 A 73 GLY SER ALA ASN LYS PRO LYS ASP GLU LEU ASP TYR ALA SEQRES 5 A 73 ASN ASP ILE GLU LYS LYS ILE CYS LYS MET GLU LYS CYS SEQRES 6 A 73 SER SER HIS HIS HIS HIS HIS HIS HET PEG H 301 17 HET GOL H 302 14 HET GOL H 303 14 HET PEG H 304 17 HET GOL H 305 14 HET GOL H 306 14 HET SO4 L1501 5 HET PEG L1502 17 HET GOL L1503 14 HET PEG L1504 17 HET GOL L1505 14 HET GOL L1506 14 HET SO4 A 401 5 HET PEG A 402 17 HET GOL A 403 14 HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM GOL GLYCEROL HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 PEG 5(C4 H10 O3) FORMUL 5 GOL 8(C3 H8 O3) FORMUL 10 SO4 2(O4 S 2-) FORMUL 19 HOH *331(H2 O) HELIX 1 AA1 LEU H 63 SER H 65 5 3 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 SER H 127 LYS H 129 5 3 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 THR H 191 5 5 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 LYS L 126 1 6 HELIX 9 AA9 LYS L 183 HIS L 189 1 7 HELIX 10 AB1 SER A 312 GLN A 324 1 13 HELIX 11 AB2 ASN A 325 LEU A 327 5 3 HELIX 12 AB3 PRO A 354 ALA A 361 1 8 SHEET 1 AA1 4 VAL H 2 SER H 7 0 SHEET 2 AA1 4 LEU H 18 GLY H 26 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ASP H 100 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 PHE H 33 SER H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLY H 44 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ARG H 58 N ALA H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ASP H 100 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 THR H 100E TRP H 103 -1 O THR H 100E N ASP H 100 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 LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 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 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 VAL H 207 N VAL H 198 SHEET 1 AA7 4 THR L 5 GLN L 6 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O GLN L 24 N GLN L 6 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA8 6 ALA L 84 TYR L 91 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 ASN L 34 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 LYS L 53 LEU L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 AA9 4 ALA L 84 TYR L 91 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 PRO L 96 PHE L 98 -1 O LEU L 97 N HIS L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 181 N ALA L 130 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 2 ASN A 340 ILE A 346 0 SHEET 2 AB3 2 ILE A 364 LYS A 370 -1 O CYS A 369 N GLY A 341 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.39 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.08 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.32 SSBOND 4 CYS L 134 CYS L 194 1555 1555 1.95 SSBOND 5 CYS A 334 CYS A 369 1555 1555 2.02 SSBOND 6 CYS A 338 CYS A 374 1555 1555 2.06 CISPEP 1 PHE H 146 PRO H 147 0 -9.46 CISPEP 2 GLU H 148 PRO H 149 0 -2.79 CISPEP 3 TYR L 140 PRO L 141 0 0.92 CRYST1 95.355 150.146 136.393 90.00 90.00 90.00 C 2 2 21 8 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 0.010487 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006660 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007332 0.00000