HEADER OXIDOREDUCTASE 11-DEC-24 9HO4 TITLE CRYSTAL STRUCTURE OF THE HUMAN FRATAXIN PROTEIN IN COMPLEX WITH A TITLE 2 TAILORED CAMELID NANOBODY 6B1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRATAXIN MATURE FORM; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FRATAXIN(81-210),M81-FXN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAMELID NANOBODY 6B1; COMPND 8 CHAIN: C; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FXN, FRDA, X25; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_COMMON: LLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, NANOBODY, MITOCHONDRIAL REGULATION, FRIEDREICH ATAXIA, KEYWDS 2 OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR A.GARAY-ALVAREZ,R.MOLINA,J.A.HERMOSO REVDAT 1 24-DEC-25 9HO4 0 JRNL AUTH M.F.PIGNATARO,N.B.FRENANDEZ,M.F.PAVAN,A.GARAY-ALVAREZ, JRNL AUTH 2 R.MOLINA,J.GROSSI,M.NOGUERA,A.VILA,A.GARCIA,H.GENTILI, JRNL AUTH 3 N.A.RODRIGUEZ,M.ARAN,J.A.HERMOSO,L.I.IBANEZ,J.SANTOS JRNL TITL FRATAXIN STABILITY AND FUNCTION MODULATION BY NANOBODY JRNL TITL 2 INTERACTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.76 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0430 (REFMACAT 0.4.105) REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.22 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 36124 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) : 0.151 REMARK 3 FREE R VALUE : 0.175 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.784 REMARK 3 FREE R VALUE TEST SET COUNT : 1728 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.76 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2521 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.1320 REMARK 3 BIN FREE R VALUE SET COUNT : 120 REMARK 3 BIN FREE R VALUE : 0.1630 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1875 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 153 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.44 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.06 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.54500 REMARK 3 B22 (A**2) : -0.54500 REMARK 3 B33 (A**2) : 1.76700 REMARK 3 B12 (A**2) : -0.27200 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): 0.096 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.076 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.292 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1939 ; 0.013 ; 0.016 REMARK 3 BOND LENGTHS OTHERS (A): 1747 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2638 ; 1.362 ; 1.777 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4034 ; 0.500 ; 1.565 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 251 ; 8.312 ; 5.179 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;12.984 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 280 ; 0.081 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2279 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 457 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 335 ; 0.200 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 53 ; 0.224 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 968 ; 0.179 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 133 ; 0.169 ; 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): 971 ; 8.702 ; 2.082 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 971 ; 8.679 ; 2.081 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1212 ;11.597 ; 3.735 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1213 ;11.628 ; 3.738 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 968 ;11.783 ; 2.509 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 968 ;11.778 ; 2.510 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1426 ;16.005 ; 4.416 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1427 ;15.999 ; 4.417 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): 3686 ; 3.388 ; 3.000 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 : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 4 A 114 REMARK 3 ORIGIN FOR THE GROUP (A): 9.9050 -38.0570 16.3910 REMARK 3 T TENSOR REMARK 3 T11: 0.1062 T22: 0.3780 REMARK 3 T33: 0.1495 T12: -0.0433 REMARK 3 T13: 0.0067 T23: -0.0637 REMARK 3 L TENSOR REMARK 3 L11: 5.9722 L22: 1.2548 REMARK 3 L33: 2.0438 L12: 0.7438 REMARK 3 L13: 0.3873 L23: -0.0329 REMARK 3 S TENSOR REMARK 3 S11: 0.0632 S12: -0.6455 S13: 0.1292 REMARK 3 S21: 0.1921 S22: -0.0862 S23: 0.3247 REMARK 3 S31: -0.0024 S32: -0.6987 S33: 0.0230 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 2 C 128 REMARK 3 ORIGIN FOR THE GROUP (A): 39.4220 -39.1610 13.2630 REMARK 3 T TENSOR REMARK 3 T11: 0.0467 T22: 0.0246 REMARK 3 T33: 0.0164 T12: -0.0128 REMARK 3 T13: 0.0085 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 1.7273 L22: 1.7128 REMARK 3 L33: 2.4547 L12: -0.1322 REMARK 3 L13: -0.0108 L23: 0.7733 REMARK 3 S TENSOR REMARK 3 S11: -0.0050 S12: 0.0019 S13: -0.1306 REMARK 3 S21: 0.0061 S22: -0.0536 S23: 0.0625 REMARK 3 S31: 0.3089 S32: -0.0642 S33: 0.0585 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 : 1.00 REMARK 3 ION PROBE RADIUS : 0.70 REMARK 3 SHRINKAGE RADIUS : 0.70 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9HO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292143924. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-SEP-23 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 : ALBA REMARK 200 BEAMLINE : XALOC REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50815 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480 REMARK 200 RESOLUTION RANGE LOW (A) : 84.224 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : 20.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5 REMARK 200 DATA REDUNDANCY IN SHELL : 21.70 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0 0.8M POTASSIUM REMARK 280 SODIUM TARTRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 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 REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z+1/2 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-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 -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 0.00000 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 0.00000 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 64.05250 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 64.05250 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 64.05250 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 0.00000 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 0.00000 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 64.05250 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 64.05250 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 64.05250 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: A, 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 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 C 305 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 306 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 309 LIES ON A SPECIAL POSITION. 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 O HOH C 312 O HOH C 313 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 8 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9HO4 A 4 117 UNP Q16595 FRDA_HUMAN 93 206 DBREF 9HO4 C 2 129 PDB 9HO4 9HO4 2 129 SEQRES 1 A 114 THR THR TYR GLU ARG LEU ALA GLU GLU THR LEU ASP SER SEQRES 2 A 114 LEU ALA GLU PHE PHE GLU ASP LEU ALA ASP LYS PRO TYR SEQRES 3 A 114 THR PHE GLU ASP TYR ASP VAL SER PHE GLY SER GLY VAL SEQRES 4 A 114 LEU THR VAL LYS LEU GLY GLY ASP LEU GLY THR TYR VAL SEQRES 5 A 114 ILE ASN LYS GLN THR PRO ASN LYS GLN ILE TRP LEU SER SEQRES 6 A 114 SER PRO SER SER GLY PRO LYS ARG TYR ASP TRP THR GLY SEQRES 7 A 114 LYS ASN TRP VAL TYR SER HIS ASP GLY VAL SER LEU HIS SEQRES 8 A 114 GLU LEU LEU ALA ALA GLU LEU THR LYS ALA LEU LYS THR SEQRES 9 A 114 LYS LEU ASP LEU SER SER LEU ALA TYR SER SEQRES 1 C 128 VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN PRO SEQRES 2 C 128 GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SER SEQRES 3 C 128 ILE PHE SER THR ASP ALA MET GLY TRP TYR ARG GLN PHE SEQRES 4 C 128 PRO GLY LYS ASN ARG LYS LEU VAL ALA ARG ILE SER SER SEQRES 5 C 128 GLY ASP TYR GLY ASP TYR THR ASN TYR ALA ASP SER VAL SEQRES 6 C 128 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 C 128 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 C 128 THR ALA VAL TYR TYR CYS ASN SER VAL PRO PRO ALA PRO SEQRES 9 C 128 GLY GLU TYR GLY ARG ASP TYR TRP GLY ALA GLY THR GLN SEQRES 10 C 128 VAL THR VAL SER SER ALA ALA ALA TYR PRO TYR FORMUL 3 HOH *153(H2 O) HELIX 1 AA1 THR A 4 ALA A 25 1 22 HELIX 2 AA2 SER A 92 LYS A 106 1 15 HELIX 3 AA3 SER C 25 SER C 30 1 6 HELIX 4 AA4 LYS C 89 THR C 93 5 5 SHEET 1 AA1 6 ASP A 35 GLY A 39 0 SHEET 2 AA1 6 VAL A 42 LYS A 46 -1 O LYS A 46 N ASP A 35 SHEET 3 AA1 6 THR A 53 GLN A 59 -1 O ILE A 56 N LEU A 43 SHEET 4 AA1 6 GLN A 64 SER A 69 -1 O TRP A 66 N ASN A 57 SHEET 5 AA1 6 GLY A 73 TRP A 79 -1 O TYR A 77 N ILE A 65 SHEET 6 AA1 6 TRP A 84 VAL A 85 -1 O VAL A 85 N ASP A 78 SHEET 1 AA2 4 LEU C 4 SER C 7 0 SHEET 2 AA2 4 LEU C 18 ALA C 24 -1 O SER C 21 N SER C 7 SHEET 3 AA2 4 THR C 80 MET C 85 -1 O MET C 85 N LEU C 18 SHEET 4 AA2 4 PHE C 70 ASP C 75 -1 N SER C 73 O TYR C 82 SHEET 1 AA3 6 GLY C 10 VAL C 12 0 SHEET 2 AA3 6 THR C 117 VAL C 121 1 O THR C 120 N GLY C 10 SHEET 3 AA3 6 ALA C 94 SER C 100 -1 N TYR C 96 O THR C 117 SHEET 4 AA3 6 ALA C 33 GLN C 39 -1 N TYR C 37 O TYR C 97 SHEET 5 AA3 6 LYS C 46 SER C 52 -1 O VAL C 48 N TRP C 36 SHEET 6 AA3 6 TYR C 59 TYR C 62 -1 O TYR C 59 N SER C 52 SSBOND 1 CYS C 22 CYS C 98 1555 1555 1.99 CISPEP 1 VAL C 101 PRO C 102 0 -5.05 CRYST1 97.253 97.253 128.105 90.00 90.00 120.00 P 63 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 0.010282 0.005937 0.000000 0.00000 SCALE2 0.000000 0.011873 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007806 0.00000