HEADER IMMUNE SYSTEM 20-SEP-22 8EKF TITLE X-RAY CRYSTAL STRUCTURE OF 311R FAB IN COMPLEX WITH THE PFCSP PEPTIDE TITLE 2 NPNA-3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 311R HEAVY CHAIN; COMPND 3 CHAIN: HHH; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 311R LIGHT CHAIN; COMPND 7 CHAIN: LLL; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PFCSP PEPTIDE NPNA-3; COMPND 11 CHAIN: CCC; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 14 ORGANISM_TAXID: 36329 KEYWDS ANTIBODY, ANTIGEN, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.MOSKOVITZ,I.A.WILSON JRNL AUTH R.MOSKOVITZ,I.A.WILSON JRNL TITL X-RAY CRYSTAL STRUCTURE OF 311R FAB IN COMPLEX WITH THE JRNL TITL 2 PFCSP PEPTIDE NPNA-3 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0267 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.27 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 44095 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.222 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.971 REMARK 3 FREE R VALUE TEST SET COUNT : 2192 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2979 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.81 REMARK 3 BIN R VALUE (WORKING SET) : 0.2930 REMARK 3 BIN FREE R VALUE SET COUNT : 144 REMARK 3 BIN FREE R VALUE : 0.3060 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3323 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 174 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.15000 REMARK 3 B22 (A**2) : -0.47200 REMARK 3 B33 (A**2) : -0.67800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.126 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.092 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3412 ; 0.012 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 3104 ; 0.001 ; 0.015 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4660 ; 1.718 ; 1.643 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7191 ; 1.408 ; 1.574 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 444 ; 7.586 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 134 ;35.624 ;23.060 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 506 ;14.817 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;22.382 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 449 ; 0.078 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3904 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 754 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 526 ; 0.193 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 39 ; 0.173 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1633 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 156 ; 0.154 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1785 ; 3.584 ; 3.793 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1784 ; 3.569 ; 3.791 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2226 ; 4.818 ; 5.661 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2227 ; 4.821 ; 5.662 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1627 ; 4.276 ; 4.081 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1628 ; 4.275 ; 4.082 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2434 ; 6.213 ; 5.933 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2435 ; 6.212 ; 5.935 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 8EKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000268641. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-MAY-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 : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 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 : AIMLESS, POINTLESS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44216 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 44.270 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: 6AXK REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04 M KH2PO4, 20% GLYCEROL, AND 16% REMARK 280 PEG3000, VAPOR DIFFUSION, TEMPERATURE 293K 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 22.70600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.12300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.38250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.12300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.70600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.38250 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: 4530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, LLL, CCC 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 CYS H 217 REMARK 465 GLN L 1 REMARK 465 GLU L 209 REMARK 465 CYS L 210 REMARK 465 SER L 211 REMARK 465 ASN C 44 REMARK 465 PRO C 55 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 TYRHH 99 -104.19 -104.67 REMARK 500 SERHH 131 1.56 81.00 REMARK 500 SERHH 133 52.52 103.82 REMARK 500 ASPHH 145 60.82 63.06 REMARK 500 ASNLL 26B -101.56 -127.46 REMARK 500 ASNLL 50 -45.90 77.18 REMARK 500 SERLL 89 -151.64 -147.39 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6AXK RELATED DB: PDB REMARK 900 WILD-TYPE ANTIBODY SEQUENCE DBREF 8EKFHH 1 217 PDB 8EKF 8EKF 1 217 DBREF 8EKFLL 1 211 PDB 8EKF 8EKF 1 211 DBREF 8EKFCC 44 55 PDB 8EKF 8EKF 44 55 SEQRES 1HH 224 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL PRO SEQRES 2HH 224 PRO GLY ARG SER LEU ARG LEU SER CYS ALA THR SER GLY SEQRES 3HH 224 PHE THR PHE SER SER TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4HH 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5HH 224 TYR ASP GLY SER ASN LYS PHE TYR ALA ALA SER VAL LYS SEQRES 6HH 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7HH 224 LEU TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR SEQRES 8HH 224 ALA VAL TYR TYR CYS ALA ARG ALA ALA TYR TYR ASP THR SEQRES 9HH 224 SER GLY TYR GLY ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10HH 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11HH 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12HH 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13HH 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14HH 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15HH 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16HH 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17HH 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18HH 224 LYS SER CYS SEQRES 1LL 218 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2LL 218 PRO GLY GLN THR VAL THR ILE SER CYS THR GLY GLY SER SEQRES 3LL 218 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4LL 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5LL 218 ASN ILE ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6LL 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7LL 218 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8LL 218 SER TYR ASP SER SER LEU SER GLY SER TRP VAL PHE GLY SEQRES 9LL 218 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10LL 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11LL 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU VAL SER SEQRES 12LL 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13LL 218 ASP GLY SER PRO VAL LYS VAL GLY VAL GLU THR THR LYS SEQRES 14LL 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15LL 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16LL 218 SER TYR SER CYS ARG VAL THR HIS GLU GLY SER THR VAL SEQRES 17LL 218 GLU LYS THR VAL ALA PRO ALA GLU CYS SER SEQRES 1CC 12 ASN ALA ASN PRO ASN ALA ASN PRO ASN ALA ASN PRO FORMUL 4 HOH *174(H2 O) HELIX 1 AA1 THRHH 28 TYRHH 32 5 5 HELIX 2 AA2 ALAHH 62 LYSHH 65 5 4 HELIX 3 AA3 ASNHH 74 LYSHH 76 5 3 HELIX 4 AA4 ARGHH 84 THRHH 88 5 5 HELIX 5 AA5 SERHH 157 ALAHH 159 5 3 HELIX 6 AA6 SERHH 188 THRHH 192 5 5 HELIX 7 AA7 LYSHH 202 ASNHH 205 5 4 HELIX 8 AA8 GLNLL 78 GLULL 82 5 5 HELIX 9 AA9 SERLL 120 ALALL 126 1 7 HELIX 10 AB1 THRLL 180 SERLL 186 1 7 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O ALAHH 23 N VALHH 5 SHEET 3 AA1 4 THRHH 78 METHH 83 -1 O LEUHH 81 N LEUHH 20 SHEET 4 AA1 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA2 6 GLYHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 108 VALHH 112 1 O THRHH 111 N GLYHH 10 SHEET 3 AA2 6 ALAHH 89 TYRHH 98 -1 N ALAHH 89 O VALHH 110 SHEET 4 AA2 6 METHH 34 GLNHH 39 -1 N VALHH 37 O TYRHH 92 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O VALHH 48 N TRPHH 36 SHEET 6 AA2 6 LYSHH 58 TYRHH 60 -1 O PHEHH 59 N ILEHH 50 SHEET 1 AA3 4 GLYHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 108 VALHH 112 1 O THRHH 111 N GLYHH 10 SHEET 3 AA3 4 ALAHH 89 TYRHH 98 -1 N ALAHH 89 O VALHH 110 SHEET 4 AA3 4 GLYHH 101B TRPHH 104 -1 O TYRHH 103 N ARGHH 95 SHEET 1 AA4 4 SERHH 121 LEUHH 125 0 SHEET 2 AA4 4 THRHH 136 TYRHH 146 -1 O LYSHH 144 N SERHH 121 SHEET 3 AA4 4 TYRHH 177 PROHH 186 -1 O LEUHH 179 N VALHH 143 SHEET 4 AA4 4 VALHH 164 THRHH 166 -1 N HISHH 165 O VALHH 182 SHEET 1 AA5 4 SERHH 121 LEUHH 125 0 SHEET 2 AA5 4 THRHH 136 TYRHH 146 -1 O LYSHH 144 N SERHH 121 SHEET 3 AA5 4 TYRHH 177 PROHH 186 -1 O LEUHH 179 N VALHH 143 SHEET 4 AA5 4 VALHH 170 LEUHH 171 -1 N VALHH 170 O SERHH 178 SHEET 1 AA6 3 THRHH 152 TRPHH 155 0 SHEET 2 AA6 3 ILEHH 196 HISHH 201 -1 O ASNHH 198 N SERHH 154 SHEET 3 AA6 3 THRHH 206 LYSHH 211 -1 O VALHH 208 N VALHH 199 SHEET 1 AA7 5 SERLL 9 GLYLL 12 0 SHEET 2 AA7 5 THRLL 101 VALLL 105 1 O THRLL 104 N VALLL 10 SHEET 3 AA7 5 ALALL 83 SERLL 89 -1 N ALALL 83 O LEULL 103 SHEET 4 AA7 5 HISLL 33 GLNLL 37 -1 N GLNLL 37 O ASPLL 84 SHEET 5 AA7 5 LYSLL 44 ILELL 47 -1 O LEULL 46 N TRPLL 34 SHEET 1 AA8 4 SERLL 9 GLYLL 12 0 SHEET 2 AA8 4 THRLL 101 VALLL 105 1 O THRLL 104 N VALLL 10 SHEET 3 AA8 4 ALALL 83 SERLL 89 -1 N ALALL 83 O LEULL 103 SHEET 4 AA8 4 VALLL 96 PHELL 97 -1 O VALLL 96 N SERLL 89 SHEET 1 AA9 3 VALLL 18 THRLL 23 0 SHEET 2 AA9 3 SERLL 69 ILELL 74 -1 O LEULL 72 N ILELL 20 SHEET 3 AA9 3 PHELL 61 SERLL 66 -1 N SERLL 66 O SERLL 69 SHEET 1 AB1 4 SERLL 113 PHELL 117 0 SHEET 2 AB1 4 ALALL 129 PHELL 138 -1 O SERLL 136 N SERLL 113 SHEET 3 AB1 4 TYRLL 171 LEULL 179 -1 O LEULL 177 N LEULL 131 SHEET 4 AB1 4 VALLL 158 THRLL 160 -1 N GLULL 159 O TYRLL 176 SHEET 1 AB2 4 SERLL 113 PHELL 117 0 SHEET 2 AB2 4 ALALL 129 PHELL 138 -1 O SERLL 136 N SERLL 113 SHEET 3 AB2 4 TYRLL 171 LEULL 179 -1 O LEULL 177 N LEULL 131 SHEET 4 AB2 4 SERLL 164 LYSLL 165 -1 N SERLL 164 O ALALL 172 SHEET 1 AB3 4 SERLL 152 VALLL 154 0 SHEET 2 AB3 4 THRLL 144 ALALL 149 -1 N ALALL 149 O SERLL 152 SHEET 3 AB3 4 TYRLL 190 HISLL 196 -1 O ARGLL 193 N ALALL 146 SHEET 4 AB3 4 SERLL 199 VALLL 205 -1 O VALLL 201 N VALLL 194 SSBOND 1 CYSHH 22 CYSHH 93 1555 1555 2.17 SSBOND 2 CYSHH 141 CYSHH 197 1555 1555 2.10 SSBOND 3 CYSLL 22 CYSLL 87 1555 1555 2.18 SSBOND 4 CYSLL 133 CYSLL 192 1555 1555 2.07 CISPEP 1 PHEHH 147 PROHH 148 0 -9.78 CISPEP 2 GLUHH 149 PROHH 150 0 -5.36 CISPEP 3 TYRLL 139 PROLL 140 0 -1.57 CRYST1 45.412 70.765 170.246 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 0.022021 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014131 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005874 0.00000