Header list of 1iyy.pdb file
Complete list - l 25 2 Bytes
HEADER HYDROLASE 12-SEP-02 1IYY TITLE NMR STRUCTURE OF GLN25-RIBONUCLEASE T1, 24 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBONUCLEASE T1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GUANYLORIBONUCLEASE, RNASE T1; COMPND 5 EC: 3.1.27.3; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE; SOURCE 3 ORGANISM_COMMON: YELLOW KOJI MOLD; SOURCE 4 ORGANISM_TAXID: 5062; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RIBONUCLEASE, ENDONUCLEASE, ENDORIBONUCLEASE, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 24 AUTHOR K.HATANO,M.KOJIMA,E.SUZUKI,M.TANOKURA,K.TAKAHASHI REVDAT 3 25-JUL-18 1IYY 1 COMPND SOURCE JRNL REMARK REVDAT 3 2 1 DBREF SEQADV REVDAT 2 24-FEB-09 1IYY 1 VERSN REVDAT 1 07-OCT-03 1IYY 0 JRNL AUTH K.HATANO,M.KOJIMA,E.SUZUKI,M.TANOKURA,K.TAKAHASHI JRNL TITL DETERMINATION OF THE NMR STRUCTURE OF GLN25-RIBONUCLEASE T1. JRNL REF BIOL. CHEM. V. 384 1173 2003 JRNL REFN ISSN 1431-6730 JRNL PMID 12974386 JRNL DOI 10.1515/BC.2003.130 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.KOJIMA,H.MIYANO,E.SUZUKI,M.TANOKURA,K.TAKAHASHI REMARK 1 TITL EFFECTS OF REPLACEMENT OF LYS25 WITH GLN ON THE CONFORMATION REMARK 1 TITL 2 OF RIBONUCLEASE T1: SEQUENCE-SPECIFIC 1H NMR RESONANCE REMARK 1 TITL 3 ASSIGNMENTS OF GLN25 RIBONUCLEASE T1 BY TWO-DIMENSIONAL NMR REMARK 1 TITL 4 SPECTROSCOPY. REMARK 1 REF J. BIOCHEM. V. 118 710 1995 REMARK 1 REFN ISSN 0021-924X REMARK 1 PMID 8576083 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IYY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1000005422. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM RIBONUCLEASE T1 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: STRUCTURES WERE REFINED BY 1340 NOES (392 INTRARESIDUE, REMARK 210 384 SEQUENTIAL AND 564 LONG-RANGE NOES) USING A DG/SA PROTOCOL. REMARK 210 37 ASSIGNMENTS FOR 14 CHI-1 ANGLE, 21 PHI ANGLE AND 2 OMEGA REMARK 210 ANGLE CONSTRAINTS WERE INCLUDED DURING THE COURSE OF THE REMARK 210 REFINEMENT. 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: 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 2 94.20 38.93 REMARK 500 1 TYR A 4 65.73 -115.07 REMARK 500 1 SER A 8 43.84 70.44 REMARK 500 1 CYS A 10 88.26 -54.90 REMARK 500 1 GLU A 31 -154.81 -63.01 REMARK 500 1 SER A 35 32.61 171.04 REMARK 500 1 ASN A 36 25.29 -152.64 REMARK 500 1 SER A 37 92.75 47.95 REMARK 500 1 ASN A 44 135.59 77.20 REMARK 500 1 TYR A 45 -38.11 -159.50 REMARK 500 1 GLU A 46 -73.02 -38.72 REMARK 500 1 ASP A 49 26.59 -145.05 REMARK 500 1 PHE A 50 173.08 -45.60 REMARK 500 1 SER A 51 30.30 -146.53 REMARK 500 1 VAL A 52 -92.13 -96.28 REMARK 500 1 SER A 64 -54.20 -148.25 REMARK 500 1 ASP A 66 -162.84 175.49 REMARK 500 1 SER A 69 74.14 -177.19 REMARK 500 1 SER A 72 101.63 -166.29 REMARK 500 1 PRO A 73 -81.71 -77.82 REMARK 500 1 ALA A 75 -122.03 56.47 REMARK 500 1 ARG A 77 90.12 -176.37 REMARK 500 1 ASN A 81 -81.15 -124.07 REMARK 500 1 GLU A 82 21.55 -158.74 REMARK 500 1 ASN A 83 23.89 -140.39 REMARK 500 1 ASN A 84 19.92 52.83 REMARK 500 1 GLN A 85 -111.75 -60.62 REMARK 500 1 LEU A 86 110.16 172.84 REMARK 500 1 HIS A 92 66.05 -116.76 REMARK 500 1 THR A 93 -29.65 178.42 REMARK 500 1 ASN A 98 41.66 34.71 REMARK 500 2 CYS A 2 137.25 173.27 REMARK 500 2 CYS A 6 14.98 -143.98 REMARK 500 2 TYR A 24 -70.65 -72.11 REMARK 500 2 VAL A 33 -126.36 -100.30 REMARK 500 2 SER A 35 -34.88 163.99 REMARK 500 2 SER A 37 121.78 69.29 REMARK 500 2 ASN A 43 21.66 -74.77 REMARK 500 2 ASN A 44 148.63 60.42 REMARK 500 2 TYR A 45 -57.85 -174.39 REMARK 500 2 ASP A 49 44.90 -150.49 REMARK 500 2 SER A 51 56.68 -153.22 REMARK 500 2 SER A 53 162.90 167.55 REMARK 500 2 SER A 69 20.36 -155.91 REMARK 500 2 ALA A 75 -174.06 51.01 REMARK 500 2 ASP A 76 143.16 -37.89 REMARK 500 2 GLU A 82 -21.54 161.21 REMARK 500 2 GLN A 85 -160.32 -60.66 REMARK 500 2 THR A 93 -28.56 177.36 REMARK 500 2 SER A 96 157.02 -40.95 REMARK 500 REMARK 500 THIS ENTRY HAS 584 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 77 0.30 SIDE CHAIN REMARK 500 2 ARG A 77 0.31 SIDE CHAIN REMARK 500 4 ARG A 77 0.28 SIDE CHAIN REMARK 500 5 ARG A 77 0.11 SIDE CHAIN REMARK 500 6 ARG A 77 0.27 SIDE CHAIN REMARK 500 7 ARG A 77 0.10 SIDE CHAIN REMARK 500 9 ARG A 77 0.12 SIDE CHAIN REMARK 500 10 ARG A 77 0.25 SIDE CHAIN REMARK 500 11 ARG A 77 0.30 SIDE CHAIN REMARK 500 12 ARG A 77 0.11 SIDE CHAIN REMARK 500 13 ARG A 77 0.30 SIDE CHAIN REMARK 500 14 ARG A 77 0.15 SIDE CHAIN REMARK 500 15 ARG A 77 0.29 SIDE CHAIN REMARK 500 16 ARG A 77 0.32 SIDE CHAIN REMARK 500 17 ARG A 77 0.19 SIDE CHAIN REMARK 500 18 ARG A 77 0.32 SIDE CHAIN REMARK 500 19 ARG A 77 0.31 SIDE CHAIN REMARK 500 20 ARG A 77 0.30 SIDE CHAIN REMARK 500 21 ARG A 77 0.29 SIDE CHAIN REMARK 500 22 ARG A 77 0.14 SIDE CHAIN REMARK 500 23 ARG A 77 0.28 SIDE CHAIN REMARK 500 24 ARG A 77 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1YGW RELATED DB: PDB REMARK 900 1YGW CONTAINS NMR STRUCTURE OF THE ISOZYME, 34 STRUCTURES DBREF 1IYY A 1 104 UNP A2NUJ9 A2NUJ9_ASPOZ 1 104 SEQADV 1IYY GLN A 25 UNP A2NUJ9 LYS 25 ENGINEERED MUTATION SEQRES 1 A 104 ALA CYS ASP TYR THR CYS GLY SER ASN CYS TYR SER SER SEQRES 2 A 104 SER ASP VAL SER THR ALA GLN ALA ALA GLY TYR GLN LEU SEQRES 3 A 104 HIS GLU ASP GLY GLU THR VAL GLY SER ASN SER TYR PRO SEQRES 4 A 104 HIS LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE SER VAL SEQRES 5 A 104 SER SER PRO TYR TYR GLU TRP PRO ILE LEU SER SER GLY SEQRES 6 A 104 ASP VAL TYR SER GLY GLY SER PRO GLY ALA ASP ARG VAL SEQRES 7 A 104 VAL PHE ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE THR SEQRES 8 A 104 HIS THR GLY ALA SER GLY ASN ASN PHE VAL GLU CYS THR HELIX 1 1 SER A 12 GLY A 30 1 19 HELIX 2 2 ALA A 95 ASN A 99 5 5 SHEET 1 A 2 TYR A 4 CYS A 6 0 SHEET 2 A 2 ASN A 9 TYR A 11 -1 O TYR A 11 N TYR A 4 SHEET 1 B 3 TYR A 57 GLU A 58 0 SHEET 2 B 3 ARG A 77 PHE A 80 -1 O PHE A 80 N TYR A 57 SHEET 3 B 3 GLY A 88 ILE A 90 -1 O GLY A 88 N VAL A 79 SSBOND 1 CYS A 2 CYS A 10 1555 1555 2.02 SSBOND 2 CYS A 6 CYS A 103 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 - l 25 2 Bytes