Header list of 1kvz.pdb file
Complete list - c 21 2 Bytes
HEADER HYDROLASE 28-JAN-02 1KVZ TITLE SOLUTION STRUCTURE OF CYTOTOXIC RC-RNASE4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RC-RNASE4; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RANA CATESBEIANA; SOURCE 3 ORGANISM_COMMON: BULLFROG; SOURCE 4 ORGANISM_TAXID: 8400; SOURCE 5 GENE: OOCYTES; 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: PET-11D KEYWDS ANTITUMOR, BULLFROG, CYTOTOXICITY, RIBONUCLEASE, STRUCTURE FROM KEYWDS 2 MOLMOL, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR C.-H.HSU,Y.-D.LIAO,L.-W.CHEN,S.-H.WU,C.CHEN REVDAT 5 21-DEC-22 1KVZ 1 SEQADV REVDAT 4 23-FEB-22 1KVZ 1 REMARK REVDAT 3 24-FEB-09 1KVZ 1 VERSN REVDAT 2 03-JUN-03 1KVZ 1 JRNL REMARK REVDAT 1 28-JUL-02 1KVZ 0 JRNL AUTH C.-H.HSU,Y.-D.LIAO,Y.-R.PAN,L.-W.CHEN,S.-H.WU,Y.-J.LEU, JRNL AUTH 2 C.CHEN JRNL TITL SOLUTION STRUCTURE OF THE CYTOTOXIC RNASE 4 FROM THE OOCYTES JRNL TITL 2 OF BULLFROG RANA CATESBEIANA JRNL REF J.MOL.BIOL. V. 326 1189 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12589762 JRNL DOI 10.1016/S0022-2836(02)01472-9 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 98 REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015390. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310; 310 REMARK 210 PH : 3.5; 3.5 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : 1 ATM; 1 ATM REMARK 210 SAMPLE CONTENTS : 1.5MM RRC-RNASE4 U-15N, 13C; REMARK 210 50MM PHOSPHATE BUFFER; 90% H2O, REMARK 210 10%; 1.5MM RRC-RNASE4 U-15N; REMARK 210 50MM PHOSPHATE BUFFER; 90% H2O, REMARK 210 10% REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 2.6, X-PLOR 98 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D REMARK 210 HETREONUCLEAR TECHNIQUES. 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 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 CYS A 31 72.21 63.66 REMARK 500 1 ARG A 50 93.59 -55.06 REMARK 500 1 CYS A 77 72.63 50.12 REMARK 500 2 ASP A 30 49.01 39.81 REMARK 500 2 LYS A 32 -176.18 -65.85 REMARK 500 2 ARG A 50 93.37 -56.80 REMARK 500 2 PRO A 76 -163.84 -71.29 REMARK 500 3 GLN A 2 -64.84 -143.02 REMARK 500 3 LYS A 32 -178.58 -55.05 REMARK 500 3 ARG A 50 91.52 -57.76 REMARK 500 3 GLU A 95 37.87 76.45 REMARK 500 4 THR A 26 -173.11 -67.77 REMARK 500 4 CYS A 31 69.91 60.82 REMARK 500 4 ARG A 50 96.58 -57.99 REMARK 500 5 LYS A 32 -178.91 -58.18 REMARK 500 5 ARG A 50 91.69 -57.87 REMARK 500 5 PRO A 76 -163.52 -71.31 REMARK 500 6 ARG A 50 92.18 -57.67 REMARK 500 7 LYS A 32 -173.50 -54.70 REMARK 500 7 ARG A 50 89.05 -61.32 REMARK 500 8 LYS A 32 -174.06 -57.84 REMARK 500 8 ARG A 50 93.67 -57.08 REMARK 500 8 GLU A 95 34.85 74.70 REMARK 500 9 LYS A 32 -175.36 -61.07 REMARK 500 9 ARG A 50 91.53 -57.93 REMARK 500 9 PRO A 76 -162.22 -72.63 REMARK 500 10 LYS A 32 -166.76 -61.61 REMARK 500 10 ARG A 50 93.23 -54.06 REMARK 500 10 ASN A 86 -178.95 -171.33 REMARK 500 11 LYS A 32 -176.22 -55.52 REMARK 500 11 ARG A 50 93.71 -56.70 REMARK 500 12 THR A 26 -179.91 -69.30 REMARK 500 12 LYS A 32 174.19 -54.74 REMARK 500 12 ARG A 50 95.13 -58.62 REMARK 500 13 THR A 15 144.71 -177.46 REMARK 500 13 LYS A 32 -173.52 -67.26 REMARK 500 13 ASP A 33 -72.70 -81.87 REMARK 500 13 ARG A 50 95.54 -55.67 REMARK 500 14 ARG A 50 89.88 -60.90 REMARK 500 14 ILE A 53 -41.81 -133.14 REMARK 500 14 SER A 60 150.69 -49.60 REMARK 500 14 LYS A 72 156.02 -49.04 REMARK 500 15 CYS A 31 75.76 64.70 REMARK 500 15 ARG A 50 92.48 -55.85 REMARK 500 15 CYS A 77 79.47 44.35 REMARK 500 15 GLU A 95 37.79 73.46 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 50 0.29 SIDE CHAIN REMARK 500 1 ARG A 74 0.22 SIDE CHAIN REMARK 500 1 ARG A 87 0.32 SIDE CHAIN REMARK 500 1 ARG A 91 0.28 SIDE CHAIN REMARK 500 2 ARG A 50 0.26 SIDE CHAIN REMARK 500 2 ARG A 74 0.28 SIDE CHAIN REMARK 500 2 ARG A 87 0.32 SIDE CHAIN REMARK 500 2 ARG A 91 0.29 SIDE CHAIN REMARK 500 3 ARG A 50 0.20 SIDE CHAIN REMARK 500 3 ARG A 74 0.29 SIDE CHAIN REMARK 500 3 ARG A 87 0.27 SIDE CHAIN REMARK 500 3 ARG A 91 0.27 SIDE CHAIN REMARK 500 4 ARG A 50 0.23 SIDE CHAIN REMARK 500 4 ARG A 74 0.30 SIDE CHAIN REMARK 500 4 ARG A 87 0.25 SIDE CHAIN REMARK 500 4 ARG A 91 0.23 SIDE CHAIN REMARK 500 5 ARG A 50 0.29 SIDE CHAIN REMARK 500 5 ARG A 74 0.28 SIDE CHAIN REMARK 500 5 ARG A 87 0.20 SIDE CHAIN REMARK 500 5 ARG A 91 0.31 SIDE CHAIN REMARK 500 6 ARG A 50 0.22 SIDE CHAIN REMARK 500 6 ARG A 74 0.32 SIDE CHAIN REMARK 500 6 ARG A 87 0.26 SIDE CHAIN REMARK 500 6 ARG A 91 0.26 SIDE CHAIN REMARK 500 7 ARG A 50 0.32 SIDE CHAIN REMARK 500 7 ARG A 74 0.28 SIDE CHAIN REMARK 500 7 ARG A 87 0.24 SIDE CHAIN REMARK 500 7 ARG A 91 0.22 SIDE CHAIN REMARK 500 8 ARG A 50 0.23 SIDE CHAIN REMARK 500 8 ARG A 74 0.31 SIDE CHAIN REMARK 500 8 ARG A 87 0.21 SIDE CHAIN REMARK 500 8 ARG A 91 0.31 SIDE CHAIN REMARK 500 9 ARG A 50 0.21 SIDE CHAIN REMARK 500 9 ARG A 74 0.28 SIDE CHAIN REMARK 500 9 ARG A 87 0.31 SIDE CHAIN REMARK 500 9 ARG A 91 0.32 SIDE CHAIN REMARK 500 10 ARG A 50 0.31 SIDE CHAIN REMARK 500 10 ARG A 74 0.27 SIDE CHAIN REMARK 500 10 ARG A 87 0.27 SIDE CHAIN REMARK 500 10 ARG A 91 0.25 SIDE CHAIN REMARK 500 11 ARG A 50 0.24 SIDE CHAIN REMARK 500 11 ARG A 74 0.24 SIDE CHAIN REMARK 500 11 ARG A 87 0.26 SIDE CHAIN REMARK 500 11 ARG A 91 0.21 SIDE CHAIN REMARK 500 12 ARG A 50 0.31 SIDE CHAIN REMARK 500 12 ARG A 74 0.27 SIDE CHAIN REMARK 500 12 ARG A 87 0.22 SIDE CHAIN REMARK 500 12 ARG A 91 0.30 SIDE CHAIN REMARK 500 13 ARG A 50 0.32 SIDE CHAIN REMARK 500 13 ARG A 74 0.28 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1KVZ A 1 107 UNP Q9DFY6 Q9DFY6_RANCA 23 129 SEQADV 1KVZ MET A 1 UNP Q9DFY6 INITIATING METHIONINE SEQRES 1 A 107 MET GLN ASP TRP ALA THR PHE LYS LYS LYS HIS LEU THR SEQRES 2 A 107 ASP THR TRP ASP VAL ASP CYS ASP ASN LEU MET PRO THR SEQRES 3 A 107 SER LEU PHE ASP CYS LYS ASP LYS ASN THR PHE ILE TYR SEQRES 4 A 107 SER LEU PRO GLY PRO VAL LYS ALA LEU CYS ARG GLY VAL SEQRES 5 A 107 ILE PHE SER ALA ASP VAL LEU SER ASN SER GLU PHE TYR SEQRES 6 A 107 LEU ALA GLU CYS ASN VAL LYS PRO ARG LYS PRO CYS LYS SEQRES 7 A 107 TYR LYS LEU LYS LYS SER SER ASN ARG ILE CYS ILE ARG SEQRES 8 A 107 CYS GLU HIS GLU LEU PRO VAL HIS PHE ALA GLY VAL GLY SEQRES 9 A 107 ILE CYS PRO HELIX 1 1 ASP A 3 HIS A 11 1 9 HELIX 2 2 ASP A 19 MET A 24 1 6 HELIX 3 3 LEU A 41 ARG A 50 1 10 SHEET 1 A 2 LEU A 12 THR A 13 0 SHEET 2 A 2 ILE A 38 TYR A 39 1 O ILE A 38 N THR A 13 SHEET 1 B 3 LYS A 34 THR A 36 0 SHEET 2 B 3 PHE A 64 VAL A 71 -1 O CYS A 69 N ASN A 35 SHEET 3 B 3 TYR A 79 ASN A 86 -1 O SER A 84 N LEU A 66 SHEET 1 C 3 ALA A 56 LEU A 59 0 SHEET 2 C 3 ILE A 88 GLU A 93 -1 O CYS A 92 N ALA A 56 SHEET 3 C 3 LEU A 96 VAL A 103 -1 O GLY A 102 N CYS A 89 SSBOND 1 CYS A 20 CYS A 69 1555 1555 2.02 SSBOND 2 CYS A 31 CYS A 77 1555 1555 2.02 SSBOND 3 CYS A 49 CYS A 92 1555 1555 2.02 SSBOND 4 CYS A 89 CYS A 106 1555 1555 2.02 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 - c 21 2 Bytes