Header list of 1e17.pdb file
Complete list - r 25 2 Bytes
HEADER DNA BINDING DOMAIN 25-APR-00 1E17 TITLE SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF THE HUMAN TITLE 2 FORKHEAD TRANSCRIPTION FACTOR AFX (FOXO4) COMPND MOL_ID: 1; COMPND 2 MOLECULE: AFX; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DNA BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELLULAR_LOCATION: NUCLEUS & CYTOPLASM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS DNA BINDING DOMAIN, WINGED HELIX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.WEIGELT,I.CLIMENT,K.DAHLMAN-WRIGHT,M.WIKSTROM REVDAT 2 24-FEB-09 1E17 1 VERSN REVDAT 1 18-AUG-00 1E17 0 JRNL AUTH J.WEIGELT,I.CLIMENT,K.DAHLMAN-WRIGHT,M.WIKSTROM JRNL TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF THE DNA JRNL TITL 2 BINDING DOMAIN OF THE HUMAN FORKHEAD TRANSCRIPTION JRNL TITL 3 FACTOR AFX JRNL REF J.BIOMOL.NMR V. 17 181 2000 JRNL REFN ISSN 0925-2738 JRNL PMID 10921784 JRNL DOI 10.1023/A:1008358816478 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.85 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 1E17 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-APR-00. REMARK 100 THE PDBE ID CODE IS EBI-4870. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 304 REMARK 210 PH : 6.3 REMARK 210 IONIC STRENGTH : 100 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600; 800 REMARK 210 SPECTROMETER MODEL : UNITY; INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING IN REMARK 210 TORSION ANGLE SPACE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 85 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST X-PLOR ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: EXPERIMENTAL DETAILS CAN BE FOUND IN THE JRNL REMARK 210 CITATION ABOVE REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. 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 GLY A 58 REMARK 465 SER A 59 REMARK 465 SER A 60 REMARK 465 HIS A 61 REMARK 465 HIS A 62 REMARK 465 HIS A 63 REMARK 465 HIS A 64 REMARK 465 HIS A 65 REMARK 465 HIS A 66 REMARK 465 SER A 67 REMARK 465 SER A 68 REMARK 465 GLY A 69 REMARK 465 LEU A 70 REMARK 465 VAL A 71 REMARK 465 PRO A 72 REMARK 465 ARG A 73 REMARK 465 GLY A 74 REMARK 465 SER A 75 REMARK 465 HIS A 76 REMARK 465 MET A 77 REMARK 465 LEU A 78 REMARK 465 GLU A 79 REMARK 465 ASP A 80 REMARK 465 PRO A 81 REMARK 465 GLY A 82 REMARK 465 ALA A 83 REMARK 465 VAL A 84 REMARK 465 THR A 85 REMARK 465 GLY A 86 REMARK 465 PRO A 87 REMARK 465 ARG A 88 REMARK 465 LYS A 89 REMARK 465 GLY A 90 REMARK 465 GLY A 91 REMARK 465 LYS A 182 REMARK 465 SER A 183 REMARK 465 GLY A 184 REMARK 465 LYS A 185 REMARK 465 ALA A 186 REMARK 465 PRO A 187 REMARK 465 ARG A 188 REMARK 465 ARG A 189 REMARK 465 ARG A 190 REMARK 465 ALA A 191 REMARK 465 ALA A 192 REMARK 465 SER A 193 REMARK 465 MET A 194 REMARK 465 ASP A 195 REMARK 465 SER A 196 REMARK 465 SER A 197 REMARK 465 SER A 198 REMARK 465 LYS A 199 REMARK 465 LEU A 200 REMARK 465 LEU A 201 REMARK 465 ARG A 202 REMARK 465 GLY A 203 REMARK 465 ARG A 204 REMARK 465 SER A 205 REMARK 465 LYS A 206 REMARK 465 ALA A 207 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 HD23 LEU A 120 - HH TYR A 124 1.59 REMARK 500 O TRP A 126 - H THR A 130 1.54 REMARK 500 HG SER A 143 - HE1 TRP A 146 1.47 REMARK 500 OD1 ASN A 165 - HE1 TRP A 173 1.57 REMARK 500 HD21 ASN A 165 - H SER A 171 1.49 REMARK 500 O GLU A 166 - H THR A 168 1.56 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 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 1 ASN A 95 -163.02 -173.64 REMARK 500 1 ALA A 96 -124.34 82.52 REMARK 500 1 ASN A 99 36.55 -72.21 REMARK 500 1 SER A 142 -13.63 -44.20 REMARK 500 1 HIS A 157 95.00 61.52 REMARK 500 1 SER A 158 6.70 -57.41 REMARK 500 1 ALA A 167 34.64 -65.95 REMARK 500 2 ALA A 96 -126.15 45.24 REMARK 500 2 ASN A 99 -11.47 -168.95 REMARK 500 2 HIS A 157 95.76 67.84 REMARK 500 2 ALA A 167 66.27 -68.24 REMARK 500 3 ASN A 95 0.77 -51.71 REMARK 500 3 HIS A 157 100.07 53.77 REMARK 500 3 ALA A 167 60.42 -64.48 REMARK 500 3 PRO A 178 -16.80 -44.09 REMARK 500 4 ALA A 96 -78.37 174.24 REMARK 500 4 ASN A 99 21.73 33.71 REMARK 500 4 ALA A 167 75.13 -67.53 REMARK 500 5 ALA A 96 -114.93 131.49 REMARK 500 5 ASN A 99 1.94 85.72 REMARK 500 5 PRO A 132 -13.51 -45.86 REMARK 500 5 TRP A 146 -17.24 -49.82 REMARK 500 5 HIS A 157 106.89 65.29 REMARK 500 5 ALA A 167 -0.85 -57.30 REMARK 500 6 ALA A 167 67.73 -63.53 REMARK 500 7 ALA A 96 -115.54 175.83 REMARK 500 7 ASN A 99 21.18 -71.16 REMARK 500 7 LYS A 116 37.41 70.28 REMARK 500 7 ASP A 139 20.82 -79.11 REMARK 500 7 SER A 143 29.15 -142.64 REMARK 500 7 HIS A 157 126.43 59.92 REMARK 500 7 ALA A 167 73.44 -68.67 REMARK 500 7 PRO A 178 2.39 -48.39 REMARK 500 8 ALA A 96 -128.58 50.49 REMARK 500 8 ALA A 167 69.23 -66.67 REMARK 500 8 PRO A 178 31.52 -58.03 REMARK 500 9 ASN A 95 6.76 -56.95 REMARK 500 9 ASN A 99 53.36 34.72 REMARK 500 9 LYS A 147 -70.48 -39.33 REMARK 500 9 HIS A 157 114.78 58.27 REMARK 500 9 SER A 158 -4.77 -59.74 REMARK 500 9 ALA A 167 66.97 -68.94 REMARK 500 10 ARG A 93 34.18 -74.41 REMARK 500 10 ALA A 96 -154.33 -112.09 REMARK 500 10 PRO A 132 -19.84 -43.89 REMARK 500 10 ALA A 167 44.96 -62.98 REMARK 500 10 SER A 171 127.68 172.97 REMARK 500 11 ALA A 96 -147.54 47.16 REMARK 500 11 HIS A 157 78.49 57.23 REMARK 500 11 SER A 158 -7.72 -49.26 REMARK 500 11 ALA A 167 55.36 -62.40 REMARK 500 12 ALA A 96 -135.08 -140.33 REMARK 500 12 ASN A 99 0.03 -65.92 REMARK 500 12 LYS A 116 53.21 75.57 REMARK 500 12 HIS A 157 90.48 71.42 REMARK 500 12 SER A 158 -8.55 -51.72 REMARK 500 12 ALA A 167 72.06 -67.55 REMARK 500 12 PRO A 178 9.17 -62.04 REMARK 500 13 ALA A 96 -83.30 -47.06 REMARK 500 13 ASN A 99 26.91 44.67 REMARK 500 13 HIS A 157 101.05 59.39 REMARK 500 13 SER A 158 -6.58 -55.76 REMARK 500 13 ALA A 167 59.17 -62.07 REMARK 500 13 ASN A 177 126.30 65.13 REMARK 500 14 ALA A 96 -128.44 163.94 REMARK 500 14 ASN A 99 5.07 -69.12 REMARK 500 14 GLU A 115 4.03 55.43 REMARK 500 14 ASP A 139 27.21 -77.41 REMARK 500 14 ALA A 167 57.72 -59.90 REMARK 500 14 PRO A 178 -19.43 -39.19 REMARK 500 15 ALA A 96 -134.25 25.64 REMARK 500 15 LYS A 116 37.30 73.23 REMARK 500 15 HIS A 157 103.54 71.36 REMARK 500 15 SER A 158 -4.75 -56.96 REMARK 500 16 ALA A 96 55.26 -68.35 REMARK 500 16 ASN A 99 39.29 29.27 REMARK 500 16 PRO A 114 -70.19 -40.31 REMARK 500 16 SER A 143 19.98 44.28 REMARK 500 16 HIS A 157 95.11 57.80 REMARK 500 16 SER A 158 -7.09 -56.12 REMARK 500 16 ALA A 167 67.00 -65.69 REMARK 500 17 ALA A 96 -137.17 22.81 REMARK 500 17 GLN A 100 154.51 -38.26 REMARK 500 17 HIS A 157 94.21 72.85 REMARK 500 17 SER A 158 -2.41 -56.94 REMARK 500 17 ALA A 167 59.48 -61.54 REMARK 500 17 ASN A 177 163.10 -36.93 REMARK 500 17 PRO A 178 -95.65 -83.60 REMARK 500 18 ARG A 94 38.24 -96.60 REMARK 500 18 LYS A 116 61.01 67.85 REMARK 500 18 HIS A 157 98.99 60.30 REMARK 500 18 ALA A 167 49.66 -65.26 REMARK 500 18 SER A 171 79.25 47.55 REMARK 500 19 ALA A 96 -133.34 49.98 REMARK 500 19 LYS A 116 64.18 60.73 REMARK 500 19 SER A 140 21.75 82.86 REMARK 500 19 SER A 143 76.75 -58.40 REMARK 500 19 PRO A 178 -73.11 -56.88 REMARK 500 20 ASN A 95 -101.81 -107.50 REMARK 500 20 ALA A 96 -162.76 40.10 REMARK 500 20 GLU A 115 10.69 59.31 REMARK 500 20 LYS A 116 70.71 59.37 REMARK 500 20 HIS A 157 86.31 74.44 REMARK 500 20 SER A 158 -12.98 -48.83 REMARK 500 20 ALA A 167 76.58 -65.55 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4675 RELATED DB: BMRB REMARK 900 1H, 13C AND 15N CHEMICAL SHIFTS REMARK 999 REMARK 999 SEQUENCE REMARK 999 GLY 58 - PRO 81 IN PDB ENTRY BELONG TO ARTIFICIAL HIS-TAG DBREF 1E17 A 58 81 PDB 1E17 1E17 58 81 DBREF 1E17 A 82 207 UNP P98177 AFX1_HUMAN 82 207 SEQADV 1E17 LEU A 105 UNP P98177 PHE 105 CONFLICT SEQRES 1 A 150 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU SEQRES 2 A 150 VAL PRO ARG GLY SER HIS MET LEU GLU ASP PRO GLY ALA SEQRES 3 A 150 VAL THR GLY PRO ARG LYS GLY GLY SER ARG ARG ASN ALA SEQRES 4 A 150 TRP GLY ASN GLN SER TYR ALA GLU LEU ILE SER GLN ALA SEQRES 5 A 150 ILE GLU SER ALA PRO GLU LYS ARG LEU THR LEU ALA GLN SEQRES 6 A 150 ILE TYR GLU TRP MET VAL ARG THR VAL PRO TYR PHE LYS SEQRES 7 A 150 ASP LYS GLY ASP SER ASN SER SER ALA GLY TRP LYS ASN SEQRES 8 A 150 SER ILE ARG HIS ASN LEU SER LEU HIS SER LYS PHE ILE SEQRES 9 A 150 LYS VAL HIS ASN GLU ALA THR GLY LYS SER SER TRP TRP SEQRES 10 A 150 MET LEU ASN PRO GLU GLY GLY LYS SER GLY LYS ALA PRO SEQRES 11 A 150 ARG ARG ARG ALA ALA SER MET ASP SER SER SER LYS LEU SEQRES 12 A 150 LEU ARG GLY ARG SER LYS ALA HELIX 1 1 SER A 101 ALA A 113 1 13 HELIX 2 2 LEU A 120 VAL A 131 1 12 HELIX 3 3 PHE A 134 ASP A 139 1 6 HELIX 4 4 SER A 142 LEU A 156 1 15 SHEET 1 A 2 PHE A 160 VAL A 163 0 SHEET 2 A 2 TRP A 173 LEU A 176 -1 N MET A 175 O ILE A 161 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - r 25 2 Bytes