Header list of 2hr9.pdb file
Complete list - r 9 2 Bytes
HEADER APOPTOSIS, METAL BINDING PROTEIN 20-JUL-06 2HR9 TITLE SOLUTION STRUCTURE OF HUMAN TRANSLATIONALLY CONTROLLED TUMOR PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSLATIONALLY-CONTROLLED TUMOR PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: TCTP, P23, HISTAMINE-RELEASING FACTOR, HRF, FORTILIN; 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 GENE: TPT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B KEYWDS TUMOR PROTEIN, APOPTOSIS, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.FENG,D.LIU,H.YAO,J.WANG REVDAT 4 09-MAR-22 2HR9 1 REMARK SEQADV REVDAT 3 24-FEB-09 2HR9 1 VERSN REVDAT 2 06-NOV-07 2HR9 1 JRNL REVDAT 1 08-AUG-06 2HR9 0 SPRSDE 08-AUG-06 2HR9 1Y41 JRNL AUTH Y.FENG,D.LIU,H.YAO,J.WANG JRNL TITL SOLUTION STRUCTURE AND MAPPING OF A VERY WEAK JRNL TITL 2 CALCIUM-BINDING SITE OF HUMAN TRANSLATIONALLY CONTROLLED JRNL TITL 3 TUMOR PROTEIN BY NMR JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 48 57 2007 JRNL REFN ISSN 0003-9861 JRNL PMID 17897616 JRNL DOI 10.1016/J.ABB.2007.08.021 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 98.0, CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2HR9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-06. REMARK 100 THE DEPOSITION ID IS D_1000038668. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 7.8 REMARK 210 IONIC STRENGTH : 200MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2MM TCTP U-15N,13C; 200MM REMARK 210 POTASSIUM PHOSPHATE BUFFER; 10MM REMARK 210 EDTA; 0.01% DSS; 0.01% NAN3; 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 3.5, CNS 1.1, FELIX 98.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 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 : 1 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 HIS A 175 REMARK 465 HIS A 176 REMARK 465 HIS A 177 REMARK 465 HIS A 178 REMARK 465 HIS A 179 REMARK 465 HIS A 180 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 GLU A 12 94.84 -58.18 REMARK 500 1 LYS A 34 125.55 -174.56 REMARK 500 1 THR A 39 40.02 179.86 REMARK 500 1 ASN A 42 78.74 -65.93 REMARK 500 1 ILE A 43 112.89 -167.25 REMARK 500 1 ALA A 54 -46.26 -155.61 REMARK 500 1 THR A 62 113.03 63.53 REMARK 500 1 GLN A 106 -62.95 -105.18 REMARK 500 1 ARG A 152 -178.66 -55.56 REMARK 500 1 THR A 157 109.17 -56.95 REMARK 500 2 GLU A 12 89.84 -56.93 REMARK 500 2 ASP A 16 31.87 -95.76 REMARK 500 2 LYS A 34 123.23 -174.49 REMARK 500 2 GLU A 40 127.10 -176.97 REMARK 500 2 ILE A 48 92.40 52.28 REMARK 500 2 ASN A 51 89.29 60.34 REMARK 500 2 ALA A 52 38.16 -97.27 REMARK 500 2 GLU A 55 -47.25 -134.04 REMARK 500 2 GLU A 58 -54.68 -160.30 REMARK 500 2 GLU A 63 -60.46 -143.31 REMARK 500 2 THR A 65 -168.28 -78.57 REMARK 500 2 PHE A 83 149.94 -171.70 REMARK 500 2 GLN A 106 -62.30 -107.36 REMARK 500 2 ASN A 128 32.10 -142.93 REMARK 500 2 ARG A 152 -178.01 -66.66 REMARK 500 2 CYS A 172 -48.46 -139.72 REMARK 500 3 GLU A 12 94.07 -56.79 REMARK 500 3 ASP A 16 36.24 -95.52 REMARK 500 3 TYR A 18 -166.85 -109.41 REMARK 500 3 LYS A 34 125.89 -174.48 REMARK 500 3 THR A 39 -56.28 -136.65 REMARK 500 3 GLU A 40 61.83 62.55 REMARK 500 3 ASP A 45 -62.66 71.31 REMARK 500 3 ALA A 52 -43.03 -169.50 REMARK 500 3 SER A 64 -173.58 -177.19 REMARK 500 3 THR A 65 -43.81 -165.79 REMARK 500 3 PHE A 83 148.56 -171.66 REMARK 500 3 ARG A 152 -177.66 -66.71 REMARK 500 4 GLU A 12 104.06 -58.03 REMARK 500 4 LYS A 34 125.98 -174.46 REMARK 500 4 GLU A 40 160.41 59.67 REMARK 500 4 ILE A 43 133.38 69.30 REMARK 500 4 ALA A 54 33.10 -98.40 REMARK 500 4 PRO A 57 43.43 -86.07 REMARK 500 4 GLU A 58 113.34 60.62 REMARK 500 4 GLU A 60 -47.91 -130.43 REMARK 500 4 ASN A 128 31.68 -142.47 REMARK 500 4 CYS A 172 140.84 -171.27 REMARK 500 5 GLU A 12 96.84 -57.12 REMARK 500 5 GLU A 40 -73.86 66.15 REMARK 500 REMARK 500 THIS ENTRY HAS 265 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 2HR9 A 1 172 UNP P13693 TCTP_HUMAN 1 172 SEQADV 2HR9 LEU A 173 UNP P13693 EXPRESSION TAG SEQADV 2HR9 GLU A 174 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 175 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 176 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 177 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 178 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 179 UNP P13693 EXPRESSION TAG SEQADV 2HR9 HIS A 180 UNP P13693 EXPRESSION TAG SEQRES 1 A 180 MET ILE ILE TYR ARG ASP LEU ILE SER HIS ASP GLU MET SEQRES 2 A 180 PHE SER ASP ILE TYR LYS ILE ARG GLU ILE ALA ASP GLY SEQRES 3 A 180 LEU CYS LEU GLU VAL GLU GLY LYS MET VAL SER ARG THR SEQRES 4 A 180 GLU GLY ASN ILE ASP ASP SER LEU ILE GLY GLY ASN ALA SEQRES 5 A 180 SER ALA GLU GLY PRO GLU GLY GLU GLY THR GLU SER THR SEQRES 6 A 180 VAL ILE THR GLY VAL ASP ILE VAL MET ASN HIS HIS LEU SEQRES 7 A 180 GLN GLU THR SER PHE THR LYS GLU ALA TYR LYS LYS TYR SEQRES 8 A 180 ILE LYS ASP TYR MET LYS SER ILE LYS GLY LYS LEU GLU SEQRES 9 A 180 GLU GLN ARG PRO GLU ARG VAL LYS PRO PHE MET THR GLY SEQRES 10 A 180 ALA ALA GLU GLN ILE LYS HIS ILE LEU ALA ASN PHE LYS SEQRES 11 A 180 ASN TYR GLN PHE PHE ILE GLY GLU ASN MET ASN PRO ASP SEQRES 12 A 180 GLY MET VAL ALA LEU LEU ASP TYR ARG GLU ASP GLY VAL SEQRES 13 A 180 THR PRO TYR MET ILE PHE PHE LYS ASP GLY LEU GLU MET SEQRES 14 A 180 GLU LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 ASP A 71 HIS A 76 1 6 HELIX 2 2 THR A 84 ARG A 107 1 24 HELIX 3 3 ARG A 110 ALA A 127 1 18 SHEET 1 A 3 GLU A 12 SER A 15 0 SHEET 2 A 3 ILE A 2 ASP A 6 -1 N TYR A 4 O PHE A 14 SHEET 3 A 3 LEU A 167 LYS A 171 -1 O GLU A 168 N ARG A 5 SHEET 1 B 6 LYS A 19 ILE A 23 0 SHEET 2 B 6 CYS A 28 GLU A 32 -1 O GLU A 30 N ARG A 21 SHEET 3 B 6 PRO A 158 PHE A 163 -1 O PHE A 162 N LEU A 29 SHEET 4 B 6 ALA A 147 TYR A 151 -1 N ASP A 150 O TYR A 159 SHEET 5 B 6 GLN A 133 ILE A 136 -1 N PHE A 135 O ALA A 147 SHEET 6 B 6 GLN A 79 THR A 81 -1 N GLN A 79 O ILE A 136 SHEET 1 C 2 MET A 35 VAL A 36 0 SHEET 2 C 2 GLY A 69 VAL A 70 -1 O GLY A 69 N VAL A 36 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 9 2 Bytes