Header list of 1rl1.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN DEGRADATION 24-NOV-03 1RL1 TITLE SOLUTION STRUCTURE OF HUMAN SGT1 CS DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUPPRESSOR OF G2 ALLELE OF SKP1 HOMOLOG; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CS DOMAIN; COMPND 5 SYNONYM: SGT1, PUTATIVE 40-6-3 PROTEIN; COMPND 6 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: SUGT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS BETA SANDWICH, 7 BETA STRANDS, SIMILAR TO P23, LACKING LAST BETA KEYWDS 2 STRAND SEEN IN P23, PROTEIN DEGRADATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.-T.LEE,J.JACOB,W.MICHOWSKI,M.NOWOTNY,J.KUZNICKI,W.J.CHAZIN REVDAT 3 02-MAR-22 1RL1 1 REMARK SEQADV REVDAT 2 24-FEB-09 1RL1 1 VERSN REVDAT 1 04-MAY-04 1RL1 0 JRNL AUTH Y.-T.LEE,J.JACOB,W.MICHOWSKI,M.NOWOTNY,J.KUZNICKI,W.J.CHAZIN JRNL TITL HUMAN SGT1 BINDS HSP90 THROUGH THE CHORD-SGT1 DOMAIN AND NOT JRNL TITL 2 THE TETRATRICOPEPTIDE REPEAT DOMAIN JRNL REF J.BIOL.CHEM. V. 279 16511 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 14761955 JRNL DOI 10.1074/JBC.M400215200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, AMBER 7 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), PEARLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RL1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020853. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : 40 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2 MM SGT1 CS DOMAIN U-15N, 20 REMARK 210 MM ACETIC ACID, 5 MM DTT, 93% REMARK 210 H2O, 7% D2O; 1-2 MM SGT1 CS REMARK 210 DOMAIN U-15N,U-13C, 20 MM ACETIC REMARK 210 ACID, 5 MM DTT, 93% H2O, 7% D2O; REMARK 210 1-2 MM SGT1 CS DOMAIN U-13C, 20 REMARK 210 MM ACETIC ACID, 5 MM DTT, 100% REMARK 210 D2O; 1-2 MM SGT1 CS DOMAIN, 10%- REMARK 210 13C, 20 MM ACETIC ACID PH 4.5, 5 REMARK 210 MM DTT, 100% D2O; 1-2 MM SGT1 CS REMARK 210 DOMAIN, 20 MM ACETIC ACID, 5 MM REMARK 210 DTT, 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 15N-1H HSQC; 3D 15N-EDITED REMARK 210 NOESY; 3D HNCACB; 3D CBCA(CO)NH; REMARK 210 3D HNCO; 3D C(CCO)NH; 3D H(CCO) REMARK 210 NH; 3D HBHA(CCO)NH; 2D 13C-1H CT- REMARK 210 HSQC; 3D HCCH-TOCSY; 3D 13C- REMARK 210 EDITED NOESY; 2D 1H-TOCSY; 2D DQ REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY, PIPP 4.3.2.SGI, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED REMARK 210 MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19 REMARK 210 REMARK 210 REMARK: NULL 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 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: 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 GLY A 131 REMARK 465 SER A 132 REMARK 465 HIS A 133 REMARK 465 MET A 134 REMARK 465 THR A 135 REMARK 465 HIS A 136 REMARK 465 GLN A 137 REMARK 465 ASP A 230 REMARK 465 VAL A 231 REMARK 465 PRO A 232 REMARK 465 THR A 233 REMARK 465 PRO A 234 REMARK 465 LYS A 235 REMARK 465 GLN A 236 REMARK 465 PHE A 237 REMARK 465 VAL A 238 REMARK 465 ALA A 239 REMARK 465 ASP A 240 REMARK 465 VAL A 241 REMARK 465 LYS A 242 REMARK 465 ASN A 243 REMARK 465 LEU A 244 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 18 TYR A 186 CB - CG - CD2 ANGL. DEV. = -4.3 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 1 SER A 149 -53.77 165.32 REMARK 500 1 SER A 170 59.46 -147.57 REMARK 500 1 LYS A 172 -135.89 -144.93 REMARK 500 1 SER A 182 33.14 -69.48 REMARK 500 1 SER A 207 -64.77 147.19 REMARK 500 2 ASN A 159 62.64 64.94 REMARK 500 2 SER A 170 49.20 -151.26 REMARK 500 2 GLU A 171 -60.94 66.45 REMARK 500 2 LYS A 172 -72.45 -21.98 REMARK 500 2 GLU A 191 87.44 -68.91 REMARK 500 2 GLU A 223 -54.21 70.67 REMARK 500 2 LEU A 225 -63.99 66.03 REMARK 500 3 ILE A 157 86.45 -160.25 REMARK 500 3 ASN A 159 104.13 141.42 REMARK 500 3 SER A 170 48.14 -151.47 REMARK 500 3 GLU A 171 -61.62 70.67 REMARK 500 3 LYS A 172 -84.32 -10.22 REMARK 500 3 SER A 182 34.80 -67.02 REMARK 500 3 GLU A 191 87.55 -68.72 REMARK 500 3 GLU A 223 -69.34 68.45 REMARK 500 3 LEU A 225 -74.53 58.33 REMARK 500 3 GLN A 228 62.05 -150.65 REMARK 500 4 SER A 149 -66.48 171.48 REMARK 500 4 LYS A 158 40.62 -78.20 REMARK 500 4 ASN A 159 88.06 -178.02 REMARK 500 4 SER A 170 49.10 -153.52 REMARK 500 4 GLU A 171 -62.02 68.74 REMARK 500 4 LYS A 172 -85.24 -14.85 REMARK 500 4 GLU A 191 88.08 -68.43 REMARK 500 4 SER A 207 -74.60 55.01 REMARK 500 4 GLU A 223 -62.75 71.38 REMARK 500 4 LEU A 225 -61.39 -156.40 REMARK 500 5 ASN A 159 59.31 102.50 REMARK 500 5 SER A 170 52.02 -151.30 REMARK 500 5 GLU A 171 -61.94 67.81 REMARK 500 5 LYS A 172 -80.67 -20.53 REMARK 500 5 PRO A 181 -37.39 -38.30 REMARK 500 5 SER A 182 35.00 -66.81 REMARK 500 5 GLU A 191 88.46 -68.61 REMARK 500 5 GLN A 228 -60.48 101.85 REMARK 500 6 SER A 170 48.79 -151.76 REMARK 500 6 GLU A 171 -60.02 67.28 REMARK 500 6 LYS A 172 -73.06 -26.35 REMARK 500 6 LYS A 179 99.90 -65.15 REMARK 500 6 PRO A 181 -39.78 -36.02 REMARK 500 6 SER A 182 35.08 -66.53 REMARK 500 7 ILE A 157 85.40 -163.78 REMARK 500 7 ASN A 159 45.94 -75.17 REMARK 500 7 SER A 170 50.53 -151.95 REMARK 500 7 GLU A 171 -56.73 68.78 REMARK 500 REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS. 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 1 TYR A 145 0.07 SIDE CHAIN REMARK 500 2 PHE A 169 0.15 SIDE CHAIN REMARK 500 2 TYR A 186 0.06 SIDE CHAIN REMARK 500 4 PHE A 169 0.10 SIDE CHAIN REMARK 500 5 PHE A 169 0.08 SIDE CHAIN REMARK 500 7 TYR A 145 0.09 SIDE CHAIN REMARK 500 7 PHE A 169 0.08 SIDE CHAIN REMARK 500 7 TYR A 186 0.17 SIDE CHAIN REMARK 500 8 PHE A 169 0.10 SIDE CHAIN REMARK 500 8 TYR A 186 0.08 SIDE CHAIN REMARK 500 10 PHE A 169 0.14 SIDE CHAIN REMARK 500 11 TYR A 142 0.08 SIDE CHAIN REMARK 500 11 PHE A 169 0.11 SIDE CHAIN REMARK 500 12 TYR A 145 0.07 SIDE CHAIN REMARK 500 12 PHE A 169 0.11 SIDE CHAIN REMARK 500 12 TYR A 186 0.09 SIDE CHAIN REMARK 500 13 TYR A 142 0.13 SIDE CHAIN REMARK 500 13 TYR A 145 0.06 SIDE CHAIN REMARK 500 13 PHE A 169 0.10 SIDE CHAIN REMARK 500 14 TYR A 145 0.07 SIDE CHAIN REMARK 500 14 PHE A 169 0.09 SIDE CHAIN REMARK 500 15 PHE A 169 0.14 SIDE CHAIN REMARK 500 15 TYR A 186 0.15 SIDE CHAIN REMARK 500 17 PHE A 169 0.11 SIDE CHAIN REMARK 500 18 PHE A 169 0.11 SIDE CHAIN REMARK 500 18 TYR A 186 0.08 SIDE CHAIN REMARK 500 19 PHE A 169 0.08 SIDE CHAIN REMARK 500 20 TYR A 186 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1RL1 A 135 244 UNP Q9Y2Z0 SUGT1_HUMAN 135 244 SEQADV 1RL1 GLY A 131 UNP Q9Y2Z0 CLONING ARTIFACT SEQADV 1RL1 SER A 132 UNP Q9Y2Z0 CLONING ARTIFACT SEQADV 1RL1 HIS A 133 UNP Q9Y2Z0 CLONING ARTIFACT SEQADV 1RL1 MET A 134 UNP Q9Y2Z0 CLONING ARTIFACT SEQRES 1 A 114 GLY SER HIS MET THR HIS GLN SER LYS ILE LYS TYR ASP SEQRES 2 A 114 TRP TYR GLN THR GLU SER GLN VAL VAL ILE THR LEU MET SEQRES 3 A 114 ILE LYS ASN VAL GLN LYS ASN ASP VAL ASN VAL GLU PHE SEQRES 4 A 114 SER GLU LYS GLU LEU SER ALA LEU VAL LYS LEU PRO SER SEQRES 5 A 114 GLY GLU ASP TYR ASN LEU LYS LEU GLU LEU LEU HIS PRO SEQRES 6 A 114 ILE ILE PRO GLU GLN SER THR PHE LYS VAL LEU SER THR SEQRES 7 A 114 LYS ILE GLU ILE LYS LEU LYS LYS PRO GLU ALA VAL ARG SEQRES 8 A 114 TRP GLU LYS LEU GLU GLY GLN GLY ASP VAL PRO THR PRO SEQRES 9 A 114 LYS GLN PHE VAL ALA ASP VAL LYS ASN LEU HELIX 1 1 GLN A 161 ASN A 163 5 3 HELIX 2 2 ILE A 197 GLU A 199 5 3 SHEET 1 A 4 TYR A 142 GLN A 146 0 SHEET 2 A 4 GLN A 150 LEU A 155 -1 O VAL A 152 N TYR A 145 SHEET 3 A 4 ILE A 210 LYS A 215 -1 O ILE A 212 N ILE A 153 SHEET 4 A 4 SER A 201 VAL A 205 -1 N THR A 202 O LYS A 213 SHEET 1 B 3 VAL A 165 GLU A 168 0 SHEET 2 B 3 LEU A 174 LYS A 179 -1 O LEU A 177 N ASN A 166 SHEET 3 B 3 ASP A 185 LEU A 190 -1 O LEU A 190 N LEU A 174 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 2 2 Bytes