HEADER BIOSYNTHETIC PROTEIN 22-NOV-20 7DJY TITLE CLEC4F NANOBODY 322 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CLEC4F NANOBODY 322; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMIUM MACULATUM; SOURCE 3 ORGANISM_TAXID: 53163; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS NANOBODY, CLEC4F, IGV DOMAIN, BIOSYNTHETIC PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.WEN,F.ZHENG REVDAT 1 24-NOV-21 7DJY 0 JRNL AUTH Y.WEN,F.ZHENG JRNL TITL CLEC4F NANOBODY 322 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.80 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 3 NUMBER OF REFLECTIONS : 16709 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1862 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) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1227 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.01 REMARK 3 BIN R VALUE (WORKING SET) : 0.4000 REMARK 3 BIN FREE R VALUE SET COUNT : 138 REMARK 3 BIN FREE R VALUE : 0.4110 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3667 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 62 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.72 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.23 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.10000 REMARK 3 B22 (A**2) : 0.10000 REMARK 3 B33 (A**2) : -0.21000 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): 0.926 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.354 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.335 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.051 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3743 ; 0.005 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3394 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5084 ; 1.064 ; 1.862 REMARK 3 BOND ANGLES OTHERS (DEGREES): 7825 ; 1.052 ; 2.929 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 487 ; 5.142 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;28.388 ;22.848 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 562 ;12.923 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.684 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 563 ; 0.095 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4273 ; 0.002 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 831 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL 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): 1960 ; 2.347 ; 5.912 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1959 ; 2.348 ; 5.911 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2443 ; 3.970 ; 8.858 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2444 ; 3.970 ; 8.859 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1783 ; 2.327 ; 6.045 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1783 ; 2.325 ; 6.045 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2642 ; 3.824 ; 8.979 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3704 ; 6.573 ;63.442 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3701 ; 6.547 ;63.461 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 REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.00 REMARK 3 ION PROBE RADIUS : 0.90 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 7DJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-20. REMARK 100 THE DEPOSITION ID IS D_1300019552. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-NOV-17 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 : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18555 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 44.800 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.25840 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.7400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL 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: MOLREP REMARK 200 STARTING MODEL: 5IMM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CITRIC ACID, 0.04M BIS-TRIS REMARK 280 PROPANE PH 5.0, 16% POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z+1/2 REMARK 290 4555 Y,-X,Z+1/2 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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.86650 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 53.86650 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 201 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 223 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 201 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 211 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 201 LIES ON A SPECIAL POSITION. 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 HIS A 124 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 HIS A 128 REMARK 465 HIS A 129 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 GLN D 1 REMARK 465 HIS D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 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 VAL A 48 -57.67 -121.13 REMARK 500 ALA A 92 175.83 175.15 REMARK 500 TRP A 101 -40.39 81.15 REMARK 500 VAL B 48 -57.75 -120.76 REMARK 500 ALA B 92 175.49 175.28 REMARK 500 TRP B 101 -40.09 81.55 REMARK 500 VAL C 48 -57.58 -120.93 REMARK 500 ALA C 92 174.65 175.84 REMARK 500 TRP C 101 -37.71 79.46 REMARK 500 VAL D 48 -57.80 -120.86 REMARK 500 ALA D 92 174.72 174.65 REMARK 500 REMARK 500 REMARK: NULL DBREF 7DJY A 1 129 PDB 7DJY 7DJY 1 129 DBREF 7DJY B 1 129 PDB 7DJY 7DJY 1 129 DBREF 7DJY C 1 129 PDB 7DJY 7DJY 1 129 DBREF 7DJY D 1 129 PDB 7DJY 7DJY 1 129 SEQRES 1 A 129 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 129 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 129 ALA THR PHE ILE THR TYR GLY MET THR TRP PHE ARG GLN SEQRES 4 A 129 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL THR SEQRES 5 A 129 GLY ASN GLY ALA GLY THR THR TYR LEU PRO SER VAL LYS SEQRES 6 A 129 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 A 129 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 A 129 ALA VAL TYR TYR CYS GLY GLY ARG ARG TRP VAL PRO ALA SEQRES 9 A 129 THR ALA VAL ASP GLN VAL ALA TYR TRP GLY GLN GLY THR SEQRES 10 A 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 129 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 129 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 129 ALA THR PHE ILE THR TYR GLY MET THR TRP PHE ARG GLN SEQRES 4 B 129 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL THR SEQRES 5 B 129 GLY ASN GLY ALA GLY THR THR TYR LEU PRO SER VAL LYS SEQRES 6 B 129 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 B 129 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 B 129 ALA VAL TYR TYR CYS GLY GLY ARG ARG TRP VAL PRO ALA SEQRES 9 B 129 THR ALA VAL ASP GLN VAL ALA TYR TRP GLY GLN GLY THR SEQRES 10 B 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 129 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 129 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 129 ALA THR PHE ILE THR TYR GLY MET THR TRP PHE ARG GLN SEQRES 4 C 129 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL THR SEQRES 5 C 129 GLY ASN GLY ALA GLY THR THR TYR LEU PRO SER VAL LYS SEQRES 6 C 129 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 129 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 C 129 ALA VAL TYR TYR CYS GLY GLY ARG ARG TRP VAL PRO ALA SEQRES 9 C 129 THR ALA VAL ASP GLN VAL ALA TYR TRP GLY GLN GLY THR SEQRES 10 C 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 D 129 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 129 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 129 ALA THR PHE ILE THR TYR GLY MET THR TRP PHE ARG GLN SEQRES 4 D 129 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL THR SEQRES 5 D 129 GLY ASN GLY ALA GLY THR THR TYR LEU PRO SER VAL LYS SEQRES 6 D 129 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 129 VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP THR SEQRES 8 D 129 ALA VAL TYR TYR CYS GLY GLY ARG ARG TRP VAL PRO ALA SEQRES 9 D 129 THR ALA VAL ASP GLN VAL ALA TYR TRP GLY GLN GLY THR SEQRES 10 D 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS FORMUL 5 HOH *62(H2 O) HELIX 1 AA1 THR A 28 ILE A 30 5 3 HELIX 2 AA2 PRO A 62 LYS A 65 5 4 HELIX 3 AA3 LYS A 87 THR A 91 5 5 HELIX 4 AA4 ALA A 106 VAL A 110 5 5 HELIX 5 AA5 THR B 28 ILE B 30 5 3 HELIX 6 AA6 PRO B 62 LYS B 65 5 4 HELIX 7 AA7 LYS B 87 THR B 91 5 5 HELIX 8 AA8 ALA B 106 VAL B 110 5 5 HELIX 9 AA9 THR C 28 ILE C 30 5 3 HELIX 10 AB1 PRO C 62 LYS C 65 5 4 HELIX 11 AB2 LYS C 87 THR C 91 5 5 HELIX 12 AB3 ALA C 106 VAL C 110 5 5 HELIX 13 AB4 THR D 28 ILE D 30 5 3 HELIX 14 AB5 PRO D 62 LYS D 65 5 4 HELIX 15 AB6 LYS D 87 THR D 91 5 5 HELIX 16 AB7 ALA D 106 VAL D 110 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N THR A 69 O GLN A 82 SHEET 1 AA2 6 GLY A 10 GLN A 13 0 SHEET 2 AA2 6 THR A 117 SER A 122 1 O THR A 120 N GLY A 10 SHEET 3 AA2 6 ALA A 92 ARG A 100 -1 N TYR A 94 O THR A 117 SHEET 4 AA2 6 TYR A 32 GLN A 39 -1 N GLY A 33 O ARG A 99 SHEET 5 AA2 6 GLU A 46 VAL A 51 -1 O ALA A 49 N TRP A 36 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O THR A 59 N ALA A 50 SHEET 1 AA3 4 GLY A 10 GLN A 13 0 SHEET 2 AA3 4 THR A 117 SER A 122 1 O THR A 120 N GLY A 10 SHEET 3 AA3 4 ALA A 92 ARG A 100 -1 N TYR A 94 O THR A 117 SHEET 4 AA3 4 TYR A 112 TRP A 113 -1 O TYR A 112 N GLY A 98 SHEET 1 AA4 4 GLN B 3 SER B 7 0 SHEET 2 AA4 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA4 4 THR B 78 MET B 83 -1 O LEU B 81 N LEU B 20 SHEET 4 AA4 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA5 6 GLY B 10 GLN B 13 0 SHEET 2 AA5 6 THR B 117 SER B 122 1 O THR B 120 N GLY B 10 SHEET 3 AA5 6 ALA B 92 ARG B 100 -1 N TYR B 94 O THR B 117 SHEET 4 AA5 6 TYR B 32 GLN B 39 -1 N GLY B 33 O ARG B 99 SHEET 5 AA5 6 GLU B 46 VAL B 51 -1 O ALA B 49 N TRP B 36 SHEET 6 AA5 6 THR B 58 TYR B 60 -1 O THR B 59 N ALA B 50 SHEET 1 AA6 4 GLY B 10 GLN B 13 0 SHEET 2 AA6 4 THR B 117 SER B 122 1 O THR B 120 N GLY B 10 SHEET 3 AA6 4 ALA B 92 ARG B 100 -1 N TYR B 94 O THR B 117 SHEET 4 AA6 4 TYR B 112 TRP B 113 -1 O TYR B 112 N GLY B 98 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AA7 4 THR C 78 MET C 83 -1 O LEU C 81 N LEU C 20 SHEET 4 AA7 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA8 6 GLY C 10 GLN C 13 0 SHEET 2 AA8 6 THR C 117 SER C 122 1 O THR C 120 N GLY C 10 SHEET 3 AA8 6 ALA C 92 ARG C 100 -1 N TYR C 94 O THR C 117 SHEET 4 AA8 6 TYR C 32 GLN C 39 -1 N GLY C 33 O ARG C 99 SHEET 5 AA8 6 GLU C 46 VAL C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AA8 6 THR C 58 TYR C 60 -1 O THR C 59 N ALA C 50 SHEET 1 AA9 4 GLY C 10 GLN C 13 0 SHEET 2 AA9 4 THR C 117 SER C 122 1 O THR C 120 N GLY C 10 SHEET 3 AA9 4 ALA C 92 ARG C 100 -1 N TYR C 94 O THR C 117 SHEET 4 AA9 4 TYR C 112 TRP C 113 -1 O TYR C 112 N GLY C 98 SHEET 1 AB1 4 GLN D 3 SER D 7 0 SHEET 2 AB1 4 LEU D 18 SER D 25 -1 O SER D 25 N GLN D 3 SHEET 3 AB1 4 THR D 78 MET D 83 -1 O LEU D 81 N LEU D 20 SHEET 4 AB1 4 THR D 69 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AB2 6 GLY D 10 GLN D 13 0 SHEET 2 AB2 6 THR D 117 SER D 122 1 O THR D 120 N GLY D 10 SHEET 3 AB2 6 ALA D 92 ARG D 100 -1 N TYR D 94 O THR D 117 SHEET 4 AB2 6 TYR D 32 GLN D 39 -1 N GLY D 33 O ARG D 99 SHEET 5 AB2 6 GLU D 46 VAL D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AB2 6 THR D 58 TYR D 60 -1 O THR D 59 N ALA D 50 SHEET 1 AB3 4 GLY D 10 GLN D 13 0 SHEET 2 AB3 4 THR D 117 SER D 122 1 O THR D 120 N GLY D 10 SHEET 3 AB3 4 ALA D 92 ARG D 100 -1 N TYR D 94 O THR D 117 SHEET 4 AB3 4 TYR D 112 TRP D 113 -1 O TYR D 112 N GLY D 98 CISPEP 1 ARG D 100 TRP D 101 0 -16.82 CRYST1 80.469 80.469 107.733 90.00 90.00 90.00 P 42 16 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 0.012427 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012427 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009282 0.00000