Header list of 1rg6.pdb file
Complete list - r 2 2 Bytes
HEADER GENE REGULATION 11-NOV-03 1RG6 TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF P63 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SECOND SPLICE VARIANT P63; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 501-575); 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: P63; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEXSX2 KEYWDS P73 SAM-LIKE DOMAIN, GENE REGULATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.CADOT,E.CANDI,D.O.CICERO,A.DESIDERI,S.MELE,G.MELINO,M.PACI REVDAT 3 02-MAR-22 1RG6 1 REMARK SEQADV REVDAT 2 24-FEB-09 1RG6 1 VERSN REVDAT 1 23-NOV-04 1RG6 0 JRNL AUTH B.CADOT,E.CANDI,D.O.CICERO,A.DESIDERI,S.MELE,G.MELINO,M.PACI JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF P63 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR 3.85 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON NOE-DERIVED DISTANCE CONSTRAINTS, REMARK 3 DIHEDRAL ANGLE RESTRAINTS, DISTANCE RESTRAINTS REMARK 3 FROM HYDROGEN BONDS, COSTANT COUPLING CONSTANTS AND RESIDUAL REMARK 3 DIPOLAR COUPLING REMARK 4 REMARK 4 1RG6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020722. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298 REMARK 210 PH : 6; 6; 6; 6 REMARK 210 IONIC STRENGTH : 150MM NACL; 150MM NACL; 150MM REMARK 210 NACL; 150MM NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT REMARK 210 SAMPLE CONTENTS : 0.75MM P63 U-15N, 25MM SODIUM REMARK 210 POSPHATE, 150MM SODIUM CHLORIDE, REMARK 210 1MM AEBSF, 3MM DTT, 95% H20, 5% REMARK 210 D2O; 0.25MM P63 U-15N U-13C, REMARK 210 25MM SODIUM POSPHATE, 150MM REMARK 210 SODIUM CHLORIDE, 1MM AEBSF, 3MM REMARK 210 DTT, 95% H20, 5%D2O; 0.25MM P63 REMARK 210 U-15N U-13C, 25MM SODIUM REMARK 210 POSPHATE, 150MM SODIUM CHLORIDE, REMARK 210 1MM AEBSF, 3MM DTT, 100% D2O; REMARK 210 0.75MM P63 U-15N, 25MM SODIUM REMARK 210 POSPHATE, 150MM SODIUM CHLORIDE, REMARK 210 1MM AEBSF, 3MM DTT, PHAGE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-1H-15N TOCSY, 3D 1H-1H-15N REMARK 210 NOESY, 3D HNHA, 2D 1H-15N HSQC; REMARK 210 3D HNCA, 3D HNCO, 3D CBCA(CO)NH, REMARK 210 3D CBCANH, 3D HBHA(CO)NH, H1 - REMARK 210 C13 HSQC; 3D HACACO, 3D HCCH REMARK 210 TOCSY, 3D HCCH TOCSY, 3D HCCH REMARK 210 COSY, 3D HCCH COSY, 3D C13, N15 REMARK 210 EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 970271256, X-PLOR 3.85, REMARK 210 NMRVIEW 5 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 500 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY AND RESIDUAL DIPOLAR COUPLING EXPERIMENT 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 PRO A 1 REMARK 465 PRO A 2 REMARK 465 PRO A 3 REMARK 465 TYR A 4 REMARK 465 ALA A 72 REMARK 465 ALA A 73 REMARK 465 ALA A 74 REMARK 465 SER A 75 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 20 28.23 -161.13 REMARK 500 2 SER A 20 -34.04 -175.83 REMARK 500 2 SER A 41 -168.15 -109.11 REMARK 500 3 SER A 9 -164.90 -59.17 REMARK 500 3 SER A 20 -37.97 -177.38 REMARK 500 3 LYS A 49 -4.87 85.19 REMARK 500 4 SER A 9 171.08 -56.99 REMARK 500 4 SER A 20 25.49 -160.90 REMARK 500 5 SER A 20 21.75 -153.02 REMARK 500 6 SER A 9 -168.64 -59.22 REMARK 500 6 SER A 20 -35.82 -173.96 REMARK 500 7 SER A 20 24.02 -154.14 REMARK 500 8 SER A 20 -36.08 -173.85 REMARK 500 9 SER A 9 171.31 -57.20 REMARK 500 9 SER A 20 22.87 -158.60 REMARK 500 10 SER A 9 179.71 -56.38 REMARK 500 10 SER A 20 -36.39 -173.14 REMARK 500 11 SER A 9 -171.18 -58.98 REMARK 500 11 SER A 20 -37.62 -176.03 REMARK 500 12 SER A 9 175.90 -56.81 REMARK 500 12 SER A 20 26.74 -158.34 REMARK 500 12 LYS A 49 -0.16 79.97 REMARK 500 13 SER A 20 -34.40 -173.01 REMARK 500 14 SER A 9 175.48 -55.75 REMARK 500 14 SER A 20 31.75 -171.03 REMARK 500 15 SER A 9 -165.15 -61.78 REMARK 500 15 SER A 20 -35.83 -171.18 REMARK 500 16 SER A 20 28.24 -167.15 REMARK 500 17 SER A 9 171.47 -58.17 REMARK 500 17 SER A 20 32.48 -168.73 REMARK 500 17 LYS A 49 -0.16 78.32 REMARK 500 18 CYS A 8 49.89 -155.76 REMARK 500 18 SER A 9 170.13 -59.39 REMARK 500 18 SER A 20 -36.80 -172.57 REMARK 500 18 LYS A 49 -0.91 79.55 REMARK 500 19 ASP A 7 83.73 49.32 REMARK 500 19 SER A 20 21.70 -151.87 REMARK 500 19 LYS A 49 5.61 80.01 REMARK 500 20 SER A 9 -169.54 -61.91 REMARK 500 20 SER A 20 34.33 -166.29 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 16 0.32 SIDE CHAIN REMARK 500 1 ARG A 55 0.19 SIDE CHAIN REMARK 500 1 ARG A 66 0.25 SIDE CHAIN REMARK 500 2 ARG A 16 0.23 SIDE CHAIN REMARK 500 2 ARG A 55 0.21 SIDE CHAIN REMARK 500 2 ARG A 66 0.32 SIDE CHAIN REMARK 500 3 ARG A 16 0.27 SIDE CHAIN REMARK 500 3 ARG A 55 0.27 SIDE CHAIN REMARK 500 3 ARG A 66 0.25 SIDE CHAIN REMARK 500 4 ARG A 16 0.32 SIDE CHAIN REMARK 500 4 ARG A 55 0.29 SIDE CHAIN REMARK 500 4 ARG A 66 0.30 SIDE CHAIN REMARK 500 5 ARG A 16 0.24 SIDE CHAIN REMARK 500 5 ARG A 55 0.20 SIDE CHAIN REMARK 500 5 ARG A 66 0.29 SIDE CHAIN REMARK 500 6 ARG A 16 0.24 SIDE CHAIN REMARK 500 6 ARG A 55 0.26 SIDE CHAIN REMARK 500 6 ARG A 66 0.32 SIDE CHAIN REMARK 500 7 ARG A 16 0.21 SIDE CHAIN REMARK 500 7 ARG A 55 0.25 SIDE CHAIN REMARK 500 7 ARG A 66 0.23 SIDE CHAIN REMARK 500 8 ARG A 16 0.32 SIDE CHAIN REMARK 500 8 ARG A 55 0.22 SIDE CHAIN REMARK 500 8 ARG A 66 0.31 SIDE CHAIN REMARK 500 9 ARG A 16 0.21 SIDE CHAIN REMARK 500 9 ARG A 55 0.22 SIDE CHAIN REMARK 500 9 ARG A 66 0.31 SIDE CHAIN REMARK 500 10 ARG A 16 0.29 SIDE CHAIN REMARK 500 10 ARG A 55 0.28 SIDE CHAIN REMARK 500 10 ARG A 66 0.25 SIDE CHAIN REMARK 500 11 ARG A 16 0.31 SIDE CHAIN REMARK 500 11 ARG A 55 0.25 SIDE CHAIN REMARK 500 11 ARG A 66 0.26 SIDE CHAIN REMARK 500 12 ARG A 16 0.32 SIDE CHAIN REMARK 500 12 ARG A 55 0.32 SIDE CHAIN REMARK 500 12 ARG A 66 0.19 SIDE CHAIN REMARK 500 13 ARG A 16 0.24 SIDE CHAIN REMARK 500 13 ARG A 55 0.20 SIDE CHAIN REMARK 500 13 ARG A 66 0.30 SIDE CHAIN REMARK 500 14 ARG A 16 0.29 SIDE CHAIN REMARK 500 14 ARG A 55 0.29 SIDE CHAIN REMARK 500 14 ARG A 66 0.28 SIDE CHAIN REMARK 500 15 ARG A 16 0.25 SIDE CHAIN REMARK 500 15 ARG A 55 0.32 SIDE CHAIN REMARK 500 15 ARG A 66 0.25 SIDE CHAIN REMARK 500 16 ARG A 16 0.21 SIDE CHAIN REMARK 500 16 ARG A 55 0.26 SIDE CHAIN REMARK 500 16 ARG A 66 0.31 SIDE CHAIN REMARK 500 17 ARG A 16 0.32 SIDE CHAIN REMARK 500 17 ARG A 55 0.28 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1RG6 A 1 75 UNP Q9H3D4 P73L_HUMAN 501 575 SEQADV 1RG6 ALA A 72 UNP Q9H3D4 SER 572 CLONING ARTIFACT SEQADV 1RG6 ALA A 73 UNP Q9H3D4 SER 573 CLONING ARTIFACT SEQADV 1RG6 ALA A 74 UNP Q9H3D4 PRO 574 CLONING ARTIFACT SEQRES 1 A 75 PRO PRO PRO TYR PRO THR ASP CYS SER ILE VAL SER PHE SEQRES 2 A 75 LEU ALA ARG LEU GLY CYS SER SER CYS LEU ASP TYR PHE SEQRES 3 A 75 THR THR GLN GLY LEU THR THR ILE TYR GLN ILE GLU HIS SEQRES 4 A 75 TYR SER MET ASP ASP LEU ALA SER LEU LYS ILE PRO GLU SEQRES 5 A 75 GLN PHE ARG HIS ALA ILE TRP LYS GLY ILE LEU ASP HIS SEQRES 6 A 75 ARG GLN LEU HIS GLU PHE ALA ALA ALA SER HELIX 1 1 SER A 9 LEU A 17 1 9 HELIX 2 2 CYS A 22 GLY A 30 1 9 HELIX 3 3 THR A 33 GLU A 38 5 6 HELIX 4 4 SER A 41 SER A 47 1 7 HELIX 5 5 GLU A 52 HIS A 69 1 18 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