HEADER OXIDOREDUCTASE 11-DEC-24 9HO6 TITLE CRYSTAL STRUCTURE OF THE HUMAN FRATAXIN PROTEIN IN COMPLEX WITH A TITLE 2 TAILORED CAMELID NANOBODY 16C10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRATAXIN MATURE FORM; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: FRATAXIN(81-210),M81-FXN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CAMELID NANOBODY 16C10; COMPND 8 CHAIN: D, 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 9HO6 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. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_4958 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.75 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 74.0 REMARK 3 NUMBER OF REFLECTIONS : 25977 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 1327 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 64.7500 - 4.1500 1.00 3902 209 0.1466 0.1852 REMARK 3 2 4.1500 - 3.3000 1.00 3735 219 0.1518 0.2010 REMARK 3 3 3.3000 - 2.8800 1.00 3736 179 0.1918 0.2479 REMARK 3 4 2.8800 - 2.6200 1.00 3658 206 0.2099 0.2927 REMARK 3 5 2.6200 - 2.4300 1.00 3686 183 0.2220 0.2636 REMARK 3 6 2.4300 - 2.2900 0.87 3178 187 0.2346 0.2394 REMARK 3 7 2.2900 - 2.1700 0.47 1699 95 0.2492 0.3351 REMARK 3 8 2.1700 - 2.0800 0.26 932 45 0.2563 0.3406 REMARK 3 9 2.0800 - 2.0000 0.03 124 4 0.2833 0.2836 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) : 0.221 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.684 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.76 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.28 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 : 0.007 3858 REMARK 3 ANGLE : 0.996 5246 REMARK 3 CHIRALITY : 0.054 580 REMARK 3 PLANARITY : 0.012 680 REMARK 3 DIHEDRAL : 17.202 1386 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESSEQ 1:121) REMARK 3 ORIGIN FOR THE GROUP (A): 37.5247 6.4685 3.4841 REMARK 3 T TENSOR REMARK 3 T11: 0.2252 T22: 0.1948 REMARK 3 T33: 0.2832 T12: -0.0444 REMARK 3 T13: -0.1089 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 1.2584 L22: 1.3503 REMARK 3 L33: 1.3083 L12: -0.3911 REMARK 3 L13: -0.2044 L23: -0.1127 REMARK 3 S TENSOR REMARK 3 S11: -0.1382 S12: -0.0274 S13: 0.2287 REMARK 3 S21: -0.1260 S22: 0.0779 S23: -0.0566 REMARK 3 S31: -0.1099 S32: 0.0113 S33: -0.0028 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN D AND RESSEQ 1:123) REMARK 3 ORIGIN FOR THE GROUP (A): 7.4261 -1.9463 -2.4955 REMARK 3 T TENSOR REMARK 3 T11: 0.2220 T22: 0.1571 REMARK 3 T33: 0.2202 T12: 0.0105 REMARK 3 T13: -0.0812 T23: -0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.4057 L22: 1.6189 REMARK 3 L33: 1.7234 L12: 0.7961 REMARK 3 L13: 0.3035 L23: 0.5827 REMARK 3 S TENSOR REMARK 3 S11: -0.2692 S12: 0.0533 S13: 0.3248 REMARK 3 S21: -0.2216 S22: 0.0595 S23: 0.1823 REMARK 3 S31: -0.2357 S32: 0.0042 S33: -0.0141 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN B AND RESSEQ 1:121) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9338 -13.4313 25.9570 REMARK 3 T TENSOR REMARK 3 T11: 0.1365 T22: 0.2269 REMARK 3 T33: 0.1559 T12: 0.0686 REMARK 3 T13: 0.0234 T23: -0.0463 REMARK 3 L TENSOR REMARK 3 L11: 1.1700 L22: 1.4788 REMARK 3 L33: 1.8309 L12: 0.4482 REMARK 3 L13: -0.5124 L23: 0.2263 REMARK 3 S TENSOR REMARK 3 S11: -0.0559 S12: -0.1644 S13: 0.0838 REMARK 3 S21: 0.0352 S22: -0.0427 S23: -0.0518 REMARK 3 S31: 0.1819 S32: 0.1683 S33: -0.0174 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN C AND RESSEQ 1:123) REMARK 3 ORIGIN FOR THE GROUP (A): 39.2283 -20.2360 18.6231 REMARK 3 T TENSOR REMARK 3 T11: 0.2346 T22: 0.2027 REMARK 3 T33: 0.1575 T12: 0.0670 REMARK 3 T13: -0.0170 T23: -0.0165 REMARK 3 L TENSOR REMARK 3 L11: 1.6632 L22: 1.8110 REMARK 3 L33: 1.8177 L12: 0.1472 REMARK 3 L13: -0.5060 L23: 0.2705 REMARK 3 S TENSOR REMARK 3 S11: -0.2127 S12: -0.2141 S13: 0.0149 REMARK 3 S21: 0.2083 S22: 0.1510 S23: 0.0851 REMARK 3 S31: 0.1871 S32: 0.0398 S33: -0.0024 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 9HO6 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_1292143926. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUL-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 : 25980 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.997 REMARK 200 RESOLUTION RANGE LOW (A) : 64.752 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7 REMARK 200 DATA REDUNDANCY : 11.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 10K 0.1M AMMONIUM ACETATE 0.1M REMARK 280 BIS-TRIS PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K 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 28.94950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.77300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.55000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.77300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.94950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.55000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 0 REMARK 465 TYR D 124 REMARK 465 PRO D 125 REMARK 465 TYR D 126 REMARK 465 ASP D 127 REMARK 465 VAL D 128 REMARK 465 PRO D 129 REMARK 465 ASP D 130 REMARK 465 TYR D 131 REMARK 465 GLY D 132 REMARK 465 SER D 133 REMARK 465 HIS D 134 REMARK 465 HIS D 135 REMARK 465 HIS D 136 REMARK 465 HIS D 137 REMARK 465 HIS D 138 REMARK 465 HIS D 139 REMARK 465 MET B 0 REMARK 465 TYR C 124 REMARK 465 PRO C 125 REMARK 465 TYR C 126 REMARK 465 ASP C 127 REMARK 465 VAL C 128 REMARK 465 PRO C 129 REMARK 465 ASP C 130 REMARK 465 TYR C 131 REMARK 465 GLY C 132 REMARK 465 SER C 133 REMARK 465 HIS C 134 REMARK 465 HIS C 135 REMARK 465 HIS C 136 REMARK 465 HIS C 137 REMARK 465 HIS C 138 REMARK 465 HIS C 139 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 ALA C 123 O HOH C 201 1.65 REMARK 500 O HOH A 239 O HOH A 255 1.74 REMARK 500 O HOH C 256 O HOH C 262 1.92 REMARK 500 O HOH B 242 O HOH B 243 2.01 REMARK 500 OE1 GLU B 7 O HOH B 201 2.07 REMARK 500 N GLN D 13 O HOH D 201 2.10 REMARK 500 O GLU C 88 O HOH C 202 2.10 REMARK 500 O HOH D 253 O HOH B 246 2.10 REMARK 500 OD2 ASP D 108 O HOH D 202 2.11 REMARK 500 O HOH B 247 O HOH B 254 2.13 REMARK 500 OE2 GLU B 19 O HOH B 202 2.13 REMARK 500 O HOH C 230 O HOH C 263 2.15 REMARK 500 O HOH C 212 O HOH C 259 2.16 REMARK 500 O HOH B 239 O HOH B 244 2.17 REMARK 500 O HOH A 257 O HOH A 258 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 253 O HOH C 265 1455 1.91 REMARK 500 O HOH D 238 O HOH C 250 4445 2.08 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 PRO D 99 C - N - CD ANGL. DEV. = -23.9 DEGREES REMARK 500 PRO C 99 C - N - CD ANGL. DEV. = -23.3 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 ASP A 89 11.02 -142.17 REMARK 500 ASP A 120 47.60 -71.82 REMARK 500 ASN D 32 -155.02 -133.01 REMARK 500 PRO D 99 131.37 16.23 REMARK 500 LYS B 82 -16.59 -150.69 REMARK 500 ASP B 120 66.19 -62.13 REMARK 500 ASN C 32 -155.37 -128.73 REMARK 500 PRO C 99 128.26 18.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 VAL D 98 PRO D 99 -92.56 REMARK 500 VAL C 98 PRO C 99 -92.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 VAL D 98 -10.24 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HO6 A 1 121 UNP Q16595 FRDA_HUMAN 90 210 DBREF 9HO6 D 1 139 PDB 9HO6 9HO6 1 139 DBREF 9HO6 B 1 121 UNP Q16595 FRDA_HUMAN 90 210 DBREF 9HO6 C 1 139 PDB 9HO6 9HO6 1 139 SEQADV 9HO6 MET A 0 UNP Q16595 INITIATING METHIONINE SEQADV 9HO6 MET B 0 UNP Q16595 INITIATING METHIONINE SEQRES 1 A 122 MET LEU ASP GLU THR THR TYR GLU ARG LEU ALA GLU GLU SEQRES 2 A 122 THR LEU ASP SER LEU ALA GLU PHE PHE GLU ASP LEU ALA SEQRES 3 A 122 ASP LYS PRO TYR THR PHE GLU ASP TYR ASP VAL SER PHE SEQRES 4 A 122 GLY SER GLY VAL LEU THR VAL LYS LEU GLY GLY ASP LEU SEQRES 5 A 122 GLY THR TYR VAL ILE ASN LYS GLN THR PRO ASN LYS GLN SEQRES 6 A 122 ILE TRP LEU SER SER PRO SER SER GLY PRO LYS ARG TYR SEQRES 7 A 122 ASP TRP THR GLY LYS ASN TRP VAL TYR SER HIS ASP GLY SEQRES 8 A 122 VAL SER LEU HIS GLU LEU LEU ALA ALA GLU LEU THR LYS SEQRES 9 A 122 ALA LEU LYS THR LYS LEU ASP LEU SER SER LEU ALA TYR SEQRES 10 A 122 SER GLY LYS ASP ALA SEQRES 1 D 139 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 139 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA THR GLY SEQRES 3 D 139 SER ILE PHE SER ILE ASN ASN MET GLY TRP TYR ARG GLN SEQRES 4 D 139 PRO PRO GLY LYS GLY ARG HIS LEU VAL ALA ARG LEU ASN SEQRES 5 D 139 ASP ASP GLY SER THR ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 D 139 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU SEQRES 7 D 139 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 139 VAL TYR TYR CYS ASN ALA VAL PRO PRO ILE VAL THR VAL SEQRES 9 D 139 ASN ALA THR ASP TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 D 139 VAL SER SER ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP SEQRES 11 D 139 TYR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 122 MET LEU ASP GLU THR THR TYR GLU ARG LEU ALA GLU GLU SEQRES 2 B 122 THR LEU ASP SER LEU ALA GLU PHE PHE GLU ASP LEU ALA SEQRES 3 B 122 ASP LYS PRO TYR THR PHE GLU ASP TYR ASP VAL SER PHE SEQRES 4 B 122 GLY SER GLY VAL LEU THR VAL LYS LEU GLY GLY ASP LEU SEQRES 5 B 122 GLY THR TYR VAL ILE ASN LYS GLN THR PRO ASN LYS GLN SEQRES 6 B 122 ILE TRP LEU SER SER PRO SER SER GLY PRO LYS ARG TYR SEQRES 7 B 122 ASP TRP THR GLY LYS ASN TRP VAL TYR SER HIS ASP GLY SEQRES 8 B 122 VAL SER LEU HIS GLU LEU LEU ALA ALA GLU LEU THR LYS SEQRES 9 B 122 ALA LEU LYS THR LYS LEU ASP LEU SER SER LEU ALA TYR SEQRES 10 B 122 SER GLY LYS ASP ALA SEQRES 1 C 139 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 139 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA THR GLY SEQRES 3 C 139 SER ILE PHE SER ILE ASN ASN MET GLY TRP TYR ARG GLN SEQRES 4 C 139 PRO PRO GLY LYS GLY ARG HIS LEU VAL ALA ARG LEU ASN SEQRES 5 C 139 ASP ASP GLY SER THR ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 C 139 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU SEQRES 7 C 139 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 139 VAL TYR TYR CYS ASN ALA VAL PRO PRO ILE VAL THR VAL SEQRES 9 C 139 ASN ALA THR ASP TYR TRP GLY GLN GLY THR GLN VAL THR SEQRES 10 C 139 VAL SER SER ALA ALA ALA TYR PRO TYR ASP VAL PRO ASP SEQRES 11 C 139 TYR GLY SER HIS HIS HIS HIS HIS HIS FORMUL 5 HOH *235(H2 O) HELIX 1 AA1 ASP A 2 ALA A 25 1 24 HELIX 2 AA2 SER A 92 LYS A 106 1 15 HELIX 3 AA3 GLY D 26 ASN D 32 5 7 HELIX 4 AA4 LYS D 86 THR D 90 5 5 HELIX 5 AA5 SER D 120 ALA D 123 5 4 HELIX 6 AA6 ASP B 2 ALA B 25 1 24 HELIX 7 AA7 SER B 92 LYS B 106 1 15 HELIX 8 AA8 GLY C 26 ASN C 32 5 7 HELIX 9 AA9 LYS C 86 THR C 90 5 5 HELIX 10 AB1 SER C 120 ALA C 123 5 4 SHEET 1 AA1 6 ASP A 35 GLY A 39 0 SHEET 2 AA1 6 VAL A 42 LYS A 46 -1 O THR A 44 N SER A 37 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 SER A 68 N VAL A 55 SHEET 5 AA1 6 GLY A 73 TRP A 79 -1 O LYS A 75 N LEU A 67 SHEET 6 AA1 6 TRP A 84 VAL A 85 -1 O VAL A 85 N ASP A 78 SHEET 1 AA2 4 GLN D 3 SER D 7 0 SHEET 2 AA2 4 LEU D 18 THR D 25 -1 O SER D 21 N SER D 7 SHEET 3 AA2 4 THR D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AA2 4 PHE D 67 ASP D 72 -1 N SER D 70 O TYR D 79 SHEET 1 AA3 6 LEU D 11 VAL D 12 0 SHEET 2 AA3 6 THR D 114 VAL D 118 1 O THR D 117 N VAL D 12 SHEET 3 AA3 6 ALA D 91 ALA D 97 -1 N TYR D 93 O THR D 114 SHEET 4 AA3 6 MET D 34 GLN D 39 -1 N TYR D 37 O TYR D 94 SHEET 5 AA3 6 HIS D 46 LEU D 51 -1 O LEU D 51 N MET D 34 SHEET 6 AA3 6 THR D 57 TYR D 59 -1 O ASN D 58 N ARG D 50 SHEET 1 AA4 6 ASP B 35 GLY B 39 0 SHEET 2 AA4 6 VAL B 42 LYS B 46 -1 O LYS B 46 N ASP B 35 SHEET 3 AA4 6 THR B 53 GLN B 59 -1 O TYR B 54 N VAL B 45 SHEET 4 AA4 6 GLN B 64 SER B 69 -1 O TRP B 66 N ASN B 57 SHEET 5 AA4 6 GLY B 73 TRP B 79 -1 O LYS B 75 N LEU B 67 SHEET 6 AA4 6 TRP B 84 VAL B 85 -1 O VAL B 85 N ASP B 78 SHEET 1 AA5 4 GLN C 3 SER C 7 0 SHEET 2 AA5 4 LEU C 18 THR C 25 -1 O SER C 21 N SER C 7 SHEET 3 AA5 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA5 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AA6 6 GLY C 10 VAL C 12 0 SHEET 2 AA6 6 THR C 114 VAL C 118 1 O THR C 117 N VAL C 12 SHEET 3 AA6 6 ALA C 91 ALA C 97 -1 N TYR C 93 O THR C 114 SHEET 4 AA6 6 MET C 34 GLN C 39 -1 N TYR C 37 O TYR C 94 SHEET 5 AA6 6 HIS C 46 LEU C 51 -1 O LEU C 51 N MET C 34 SHEET 6 AA6 6 THR C 57 TYR C 59 -1 O ASN C 58 N ARG C 50 SSBOND 1 CYS D 22 CYS D 95 1555 1555 2.03 SSBOND 2 CYS C 22 CYS C 95 1555 1555 2.05 CRYST1 57.899 81.100 107.546 90.00 90.00 90.00 P 21 21 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 0.017271 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012330 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009298 0.00000