HEADER IMMUNE SYSTEM 25-NOV-21 7QCQ TITLE VHH Z70 IN INTERACTION WITH PHF6 TAU PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: VHH Z70; COMPND 3 CHAIN: AAA; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TAU 301-312; COMPND 7 CHAIN: BBB; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 8 ORGANISM_TAXID: 9844; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693 KEYWDS NANOBODY, VHH, TAU, PHF6, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.DANIS,E.DUPRE,O.ZEJNELI,R.CAILLIEREZ,A.ARRIAL,S.BEGARD,A.LOYENS, AUTHOR 2 J.MORTELECQUE,F.-X.CANTRELLE,X.HANOULLE,J.-C.RAIN,M.COLIN,L.BUEE, AUTHOR 3 I.LANDRIEU JRNL AUTH C.DANIS,E.DUPRE,O.ZEJNELI,R.CAILLIEREZ,A.ARRIAL,S.BEGARD, JRNL AUTH 2 A.LOYENS,J.MORTELECQUE,F.-X.CANTRELLE,X.HANOULLE,J.-C.RAIN, JRNL AUTH 3 M.COLIN,L.BUEE,I.LANDRIEU JRNL TITL INHIBITION OF TAU SEEDING BY TARGETING TAU NUCLEATION CORE JRNL TITL 2 WITHIN NEURONS WITH A SINGLE DOMAIN ANTIBODY FRAGMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.70 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) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.38 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 21711 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) : 0.195 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.002 REMARK 3 FREE R VALUE TEST SET COUNT : 1086 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) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1474 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3510 REMARK 3 BIN FREE R VALUE SET COUNT : 78 REMARK 3 BIN FREE R VALUE : 0.3450 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 912 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 109 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.89500 REMARK 3 B22 (A**2) : 0.89500 REMARK 3 B33 (A**2) : -2.90500 REMARK 3 B12 (A**2) : 0.44800 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): 0.087 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.191 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 991 ; 0.013 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 892 ; 0.001 ; 0.014 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1346 ; 1.841 ; 1.651 REMARK 3 BOND ANGLES OTHERS (DEGREES): 2057 ; 1.467 ; 1.582 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 134 ; 6.902 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;25.672 ;20.577 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 153 ;12.954 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;18.567 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 127 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1199 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 257 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 139 ; 0.210 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 31 ; 0.200 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 459 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 72 ; 0.185 ; 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): 497 ; 3.024 ; 2.839 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 496 ; 2.987 ; 2.835 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 620 ; 4.616 ; 4.217 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 621 ; 4.613 ; 4.221 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 494 ; 4.186 ; 3.314 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 495 ; 4.182 ; 3.316 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 718 ; 6.201 ; 4.750 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 718 ; 6.201 ; 4.750 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 7QCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292119392. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-JUL-21 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801 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 : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21730 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700 REMARK 200 RESOLUTION RANGE LOW (A) : 44.382 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 39.50 REMARK 200 R MERGE (I) : 0.20200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 9.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 44.34 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 28.90 REMARK 200 R MERGE FOR SHELL (I) : 0.06500 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: 1OL0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM SULFATE, 25.5% PEG REMARK 280 4000, 15% GLYCEROL, PH 7.4, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 23.71933 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 11.85967 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 17.78950 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 5.92983 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 29.64917 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 23.71933 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 11.85967 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 5.92983 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 17.78950 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 29.64917 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 APPLY THE FOLLOWING TO CHAINS: AAA, BBB 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 A 366 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 383 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLU A 3 REMARK 465 VAL A 4 REMARK 465 GLN A 5 REMARK 465 LEU A 6 REMARK 465 GLN A 7 REMARK 465 ALA A 8 REMARK 465 SER A 9 REMARK 465 ASP A 111 REMARK 465 SER A 112 REMARK 465 TYR A 113 REMARK 465 GLY A 114 REMARK 465 GLY A 115 REMARK 465 ALA A 125 REMARK 465 ALA A 126 REMARK 465 ALA A 127 REMARK 465 HIS A 128 REMARK 465 HIS A 129 REMARK 465 HIS A 130 REMARK 465 HIS A 131 REMARK 465 HIS A 132 REMARK 465 HIS A 133 REMARK 465 PRO B 301 REMARK 465 GLY B 302 REMARK 465 GLY B 303 REMARK 465 LYS B 314 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 GLN A 116 CG CD OE1 NE2 REMARK 470 LYS B 313 CG CD CE NZ 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 SERAA 59 -153.19 -73.73 REMARK 500 SERAA 59 -154.21 -71.62 REMARK 500 ALAAA 95 169.56 178.19 REMARK 500 REMARK 500 REMARK: NULL DBREF 7QCQAA 1 133 PDB 7QCQ 7QCQ 1 133 DBREF 7QCQBB 301 314 PDB 7QCQ 7QCQ 301 314 SEQRES 1AA 133 MET ALA GLU VAL GLN LEU GLN ALA SER GLY GLY VAL PHE SEQRES 2AA 133 VAL GLN SER GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3AA 133 SER GLY ALA THR SER THR PHE ASP GLY MET GLY TRP PHE SEQRES 4AA 133 ARG GLN ALA PRO GLY LYS GLU ARG GLU PHE VAL SER ALA SEQRES 5AA 133 ILE SER TYR GLU GLN GLY SER TYR THR TYR TYR ALA ASP SEQRES 6AA 133 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SER SEQRES 7AA 133 LYS ASN MET VAL TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8AA 133 GLU ASP THR ALA THR TYR TYR CYS ALA PRO ALA TYR GLU SEQRES 9AA 133 GLY ASP LEU TYR ALA PHE ASP SER TYR GLY GLY GLN GLY SEQRES 10AA 133 THR GLN VAL THR VAL SER SER ALA ALA ALA HIS HIS HIS SEQRES 11AA 133 HIS HIS HIS SEQRES 1BB 14 PRO GLY GLY GLY SER VAL GLN ILE VAL TYR LYS PRO LYS SEQRES 2BB 14 LYS HET GOL AA 201 14 HET GOL AA 202 14 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 2(C3 H8 O3) FORMUL 5 HOH *109(H2 O) HELIX 1 AA1 ASPAA 65 LYSAA 68 5 4 HELIX 2 AA2 ARGAA 90 THRAA 94 5 5 SHEET 1 AA1 6 VALAA 12 GLNAA 15 0 SHEET 2 AA1 6 THRAA 118 SERAA 123 1 O GLNAA 119 N VALAA 12 SHEET 3 AA1 6 ALAAA 95 TYRAA 103 -1 N TYRAA 97 O THRAA 118 SHEET 4 AA1 6 GLYAA 35 GLNAA 41 -1 N GLYAA 37 O ALAAA 100 SHEET 5 AA1 6 GLUAA 48 SERAA 54 -1 O ILEAA 53 N METAA 36 SHEET 6 AA1 6 THRAA 61 TYRAA 63 -1 O TYRAA 62 N ALAAA 52 SHEET 1 AA2 5 VALAA 12 GLNAA 15 0 SHEET 2 AA2 5 THRAA 118 SERAA 123 1 O GLNAA 119 N VALAA 12 SHEET 3 AA2 5 ALAAA 95 TYRAA 103 -1 N TYRAA 97 O THRAA 118 SHEET 4 AA2 5 ASPAA 106 ALAAA 109 -1 O TYRAA 108 N PROAA 101 SHEET 5 AA2 5 GLNBB 307 VALBB 309 -1 O GLNBB 307 N ALAAA 109 SHEET 1 AA3 3 LEUAA 20 ALAAA 25 0 SHEET 2 AA3 3 METAA 81 METAA 86 -1 O METAA 86 N LEUAA 20 SHEET 3 AA3 3 PHEAA 71 ASPAA 76 -1 N THRAA 72 O GLNAA 85 SSBOND 1 CYSAA 24 CYSAA 99 1555 1555 2.12 CRYST1 135.469 135.469 35.579 90.00 90.00 120.00 P 65 2 2 12 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 0.007382 0.004262 0.000000 0.00000 SCALE2 0.000000 0.008524 0.000000 0.00000 SCALE3 0.000000 0.000000 0.028106 0.00000