Header list of 1h3z.pdb file
Complete list - n 24 2 Bytes
HEADER NUCLEAR PROTEIN 23-SEP-02 1H3Z TITLE SOLUTION STRUCTURE OF A PWWP DOMAIN FROM SCHIZOSACCHAROMYCES POMBE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL 62.8 KDA PROTEIN C215.07C; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PWWP DOMAIN, RESIDUES 118-225; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE; SOURCE 3 ORGANISM_COMMON: FISSION YEAST; SOURCE 4 ORGANISM_TAXID: 4896; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41; SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PRSETA-GROEL; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSETA-GROEL; SOURCE 10 OTHER_DETAILS: SYNTHETIC GENE KEYWDS NUCLEAR PROTEIN, PWWP, CHROMATIN, BETA-BARREL EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR L.M.SLATER,M.D.ALLEN,M.BYCROFT REVDAT 4 24-JAN-18 1H3Z 1 SOURCE REVDAT 3 17-JAN-18 1H3Z 1 JRNL REVDAT 2 24-FEB-09 1H3Z 1 VERSN REVDAT 1 10-JUL-03 1H3Z 0 JRNL AUTH L.M.SLATER,M.D.ALLEN,M.BYCROFT JRNL TITL STRUCTURAL VARIATION IN PWWP DOMAINS JRNL REF J.MOL.BIOL. V. 330 571 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12842472 JRNL DOI 10.1016/S0022-2836(03)00470-4 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1H3Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1290011350. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 0.2 REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : STANDARD REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ANSIG 3.3 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATION GREATER THAN 0.25A REMARK 210 AND NO VIOLATIONS GREATER THAN 5 REMARK 210 DEGREES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS ASSIGNED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELLED PWWP. 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 400 REMARK 400 COMPOUND REMARK 400 THE PWWP DOMAIN IS NAMED AFTER A CONSERVED PRO-TRP-TRP-PRO MOTIF. REMARK 400 IT IS PRESENT IN PROTEINS OF NUCLEAR ORIGIN AND PLAYS A ROLE IN CEL REMARK 400 GROWTH AND DIFFERENTIATION. 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 1-23 REMARK 465 RES C SSSEQI REMARK 465 GLY A 117 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 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 ARG A 120 152.37 -47.99 REMARK 500 1 VAL A 144 -167.89 -116.79 REMARK 500 1 THR A 150 -156.43 -64.51 REMARK 500 1 PRO A 171 -155.10 -91.42 REMARK 500 1 ASN A 172 10.88 59.73 REMARK 500 1 LYS A 173 84.45 38.69 REMARK 500 1 GLU A 174 -168.84 -100.88 REMARK 500 1 PRO A 200 -161.80 -72.05 REMARK 500 2 VAL A 144 -168.53 -109.32 REMARK 500 2 THR A 150 -170.81 -55.85 REMARK 500 2 PRO A 171 -154.38 -97.12 REMARK 500 2 PRO A 200 -166.64 -72.02 REMARK 500 3 ARG A 120 168.56 -46.90 REMARK 500 3 VAL A 144 -168.37 -118.12 REMARK 500 3 THR A 150 -171.12 -53.79 REMARK 500 3 PRO A 171 -156.58 -92.29 REMARK 500 3 LYS A 173 48.08 27.95 REMARK 500 3 GLU A 174 -176.51 -60.74 REMARK 500 3 PRO A 200 -168.90 -73.27 REMARK 500 4 GLU A 119 78.33 43.40 REMARK 500 4 PRO A 140 98.05 -67.76 REMARK 500 4 VAL A 144 -168.10 -110.05 REMARK 500 4 THR A 150 -172.97 -65.74 REMARK 500 4 PRO A 171 -154.11 -93.93 REMARK 500 4 LYS A 173 46.39 39.44 REMARK 500 4 PRO A 200 -156.71 -71.91 REMARK 500 5 GLU A 119 172.29 53.55 REMARK 500 5 ARG A 120 80.01 52.11 REMARK 500 5 VAL A 144 -168.86 -106.65 REMARK 500 5 THR A 150 -167.86 -53.43 REMARK 500 5 PRO A 171 -152.44 -93.95 REMARK 500 5 GLU A 174 -179.55 -64.91 REMARK 500 5 PRO A 200 -169.68 -73.08 REMARK 500 6 VAL A 144 -168.64 -119.01 REMARK 500 6 THR A 150 -157.25 -67.29 REMARK 500 6 PRO A 171 -154.35 -92.70 REMARK 500 6 LYS A 173 47.46 33.05 REMARK 500 6 GLU A 174 -178.15 -58.44 REMARK 500 6 PRO A 200 -160.25 -72.11 REMARK 500 7 VAL A 144 -168.34 -117.14 REMARK 500 7 THR A 150 -166.32 -53.86 REMARK 500 7 PRO A 171 -154.81 -91.91 REMARK 500 7 LYS A 173 46.47 29.71 REMARK 500 7 GLU A 174 -176.33 -60.84 REMARK 500 7 PRO A 200 -156.49 -74.89 REMARK 500 7 PRO A 216 -81.78 -71.68 REMARK 500 8 PRO A 171 -156.34 -93.68 REMARK 500 8 LYS A 173 52.52 30.64 REMARK 500 8 GLU A 174 -177.07 -68.16 REMARK 500 8 PRO A 200 -159.09 -72.11 REMARK 500 REMARK 500 THIS ENTRY HAS 150 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 ARG A 120 0.25 SIDE CHAIN REMARK 500 1 ARG A 128 0.23 SIDE CHAIN REMARK 500 1 ARG A 154 0.23 SIDE CHAIN REMARK 500 1 ARG A 160 0.31 SIDE CHAIN REMARK 500 2 ARG A 120 0.30 SIDE CHAIN REMARK 500 2 ARG A 128 0.28 SIDE CHAIN REMARK 500 2 ARG A 154 0.24 SIDE CHAIN REMARK 500 2 ARG A 160 0.12 SIDE CHAIN REMARK 500 3 ARG A 120 0.24 SIDE CHAIN REMARK 500 3 ARG A 154 0.17 SIDE CHAIN REMARK 500 3 ARG A 160 0.16 SIDE CHAIN REMARK 500 4 ARG A 120 0.31 SIDE CHAIN REMARK 500 4 ARG A 128 0.20 SIDE CHAIN REMARK 500 4 ARG A 154 0.23 SIDE CHAIN REMARK 500 4 ARG A 160 0.13 SIDE CHAIN REMARK 500 5 ARG A 120 0.32 SIDE CHAIN REMARK 500 5 ARG A 128 0.26 SIDE CHAIN REMARK 500 5 ARG A 154 0.19 SIDE CHAIN REMARK 500 6 ARG A 120 0.24 SIDE CHAIN REMARK 500 6 ARG A 128 0.25 SIDE CHAIN REMARK 500 6 ARG A 154 0.32 SIDE CHAIN REMARK 500 6 ARG A 160 0.14 SIDE CHAIN REMARK 500 7 ARG A 120 0.22 SIDE CHAIN REMARK 500 7 ARG A 128 0.32 SIDE CHAIN REMARK 500 7 ARG A 154 0.31 SIDE CHAIN REMARK 500 7 ARG A 160 0.31 SIDE CHAIN REMARK 500 8 ARG A 120 0.14 SIDE CHAIN REMARK 500 8 ARG A 128 0.23 SIDE CHAIN REMARK 500 8 ARG A 154 0.23 SIDE CHAIN REMARK 500 8 ARG A 160 0.18 SIDE CHAIN REMARK 500 9 ARG A 120 0.20 SIDE CHAIN REMARK 500 9 ARG A 128 0.20 SIDE CHAIN REMARK 500 9 ARG A 154 0.13 SIDE CHAIN REMARK 500 9 ARG A 160 0.32 SIDE CHAIN REMARK 500 10 ARG A 120 0.15 SIDE CHAIN REMARK 500 10 ARG A 128 0.26 SIDE CHAIN REMARK 500 10 ARG A 154 0.31 SIDE CHAIN REMARK 500 10 ARG A 160 0.31 SIDE CHAIN REMARK 500 11 ARG A 120 0.24 SIDE CHAIN REMARK 500 11 ARG A 128 0.21 SIDE CHAIN REMARK 500 11 ARG A 154 0.27 SIDE CHAIN REMARK 500 11 ARG A 160 0.19 SIDE CHAIN REMARK 500 12 ARG A 120 0.11 SIDE CHAIN REMARK 500 12 ARG A 128 0.09 SIDE CHAIN REMARK 500 12 ARG A 154 0.19 SIDE CHAIN REMARK 500 12 ARG A 160 0.31 SIDE CHAIN REMARK 500 13 ARG A 120 0.30 SIDE CHAIN REMARK 500 13 ARG A 128 0.27 SIDE CHAIN REMARK 500 13 ARG A 154 0.28 SIDE CHAIN REMARK 500 13 ARG A 160 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 88 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5902 RELATED DB: BMRB DBREF 1H3Z A 117 117 PDB 1H3Z 1H3Z 117 117 DBREF 1H3Z A 118 225 UNP O94312 O94312 118 225 SEQRES 1 A 109 GLY SER GLU ARG VAL ASN TYR LYS PRO GLY MET ARG VAL SEQRES 2 A 109 LEU THR LYS MET SER GLY PHE PRO TRP TRP PRO SER MET SEQRES 3 A 109 VAL VAL THR GLU SER LYS MET THR SER VAL ALA ARG LYS SEQRES 4 A 109 SER LYS PRO LYS ARG ALA GLY THR PHE TYR PRO VAL ILE SEQRES 5 A 109 PHE PHE PRO ASN LYS GLU TYR LEU TRP THR GLY SER ASP SEQRES 6 A 109 SER LEU THR PRO LEU THR SER GLU ALA ILE SER GLN PHE SEQRES 7 A 109 LEU GLU LYS PRO LYS PRO LYS THR ALA SER LEU ILE LYS SEQRES 8 A 109 ALA TYR LYS MET ALA GLN SER THR PRO ASP LEU ASP SER SEQRES 9 A 109 LEU SER VAL PRO SER HELIX 1 1 GLU A 146 LYS A 148 5 3 HELIX 2 2 SER A 151 SER A 156 1 6 HELIX 3 3 SER A 180 SER A 182 5 3 HELIX 4 4 SER A 188 GLU A 196 1 9 HELIX 5 5 ALA A 203 SER A 214 1 12 HELIX 6 6 LEU A 218 SER A 220 5 3 SHEET 1 AA 5 LEU A 176 THR A 178 0 SHEET 2 AA 5 TYR A 165 PHE A 169 -1 O TYR A 165 N THR A 178 SHEET 3 AA 5 PHE A 136 VAL A 143 -1 O MET A 142 N ILE A 168 SHEET 4 AA 5 ARG A 128 MET A 133 -1 O VAL A 129 N SER A 141 SHEET 5 AA 5 LEU A 183 PRO A 185 -1 O THR A 184 N LEU A 130 CISPEP 1 PHE A 170 PRO A 171 1 -0.08 CISPEP 2 LYS A 199 PRO A 200 1 -0.24 CISPEP 3 PHE A 170 PRO A 171 2 -1.32 CISPEP 4 LYS A 199 PRO A 200 2 -0.22 CISPEP 5 PHE A 170 PRO A 171 3 -0.77 CISPEP 6 LYS A 199 PRO A 200 3 -0.47 CISPEP 7 PHE A 170 PRO A 171 4 -1.08 CISPEP 8 LYS A 199 PRO A 200 4 -0.54 CISPEP 9 PHE A 170 PRO A 171 5 -1.30 CISPEP 10 LYS A 199 PRO A 200 5 -0.47 CISPEP 11 PHE A 170 PRO A 171 6 -0.97 CISPEP 12 LYS A 199 PRO A 200 6 -1.24 CISPEP 13 PHE A 170 PRO A 171 7 -0.99 CISPEP 14 LYS A 199 PRO A 200 7 -0.62 CISPEP 15 PHE A 170 PRO A 171 8 -0.69 CISPEP 16 LYS A 199 PRO A 200 8 -0.65 CISPEP 17 PHE A 170 PRO A 171 9 -0.66 CISPEP 18 LYS A 199 PRO A 200 9 -0.20 CISPEP 19 PHE A 170 PRO A 171 10 -0.52 CISPEP 20 LYS A 199 PRO A 200 10 -0.69 CISPEP 21 PHE A 170 PRO A 171 11 -1.19 CISPEP 22 LYS A 199 PRO A 200 11 -0.13 CISPEP 23 PHE A 170 PRO A 171 12 -0.78 CISPEP 24 LYS A 199 PRO A 200 12 -0.68 CISPEP 25 PHE A 170 PRO A 171 13 -0.60 CISPEP 26 LYS A 199 PRO A 200 13 -0.54 CISPEP 27 PHE A 170 PRO A 171 14 -0.95 CISPEP 28 LYS A 199 PRO A 200 14 -0.43 CISPEP 29 PHE A 170 PRO A 171 15 -1.32 CISPEP 30 LYS A 199 PRO A 200 15 -0.52 CISPEP 31 PHE A 170 PRO A 171 16 -0.83 CISPEP 32 LYS A 199 PRO A 200 16 -0.31 CISPEP 33 PHE A 170 PRO A 171 17 -0.74 CISPEP 34 LYS A 199 PRO A 200 17 -0.60 CISPEP 35 PHE A 170 PRO A 171 18 -0.83 CISPEP 36 LYS A 199 PRO A 200 18 -0.16 CISPEP 37 PHE A 170 PRO A 171 19 -0.82 CISPEP 38 LYS A 199 PRO A 200 19 -0.02 CISPEP 39 PHE A 170 PRO A 171 20 -0.74 CISPEP 40 LYS A 199 PRO A 200 20 -0.38 CISPEP 41 PHE A 170 PRO A 171 21 -1.44 CISPEP 42 LYS A 199 PRO A 200 21 -0.49 CISPEP 43 PHE A 170 PRO A 171 22 -0.22 CISPEP 44 LYS A 199 PRO A 200 22 -0.03 CISPEP 45 PHE A 170 PRO A 171 23 -0.10 CISPEP 46 LYS A 199 PRO A 200 23 -0.30 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 - n 24 2 Bytes