Header list of 1pu3.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 24-JUN-03 1PU3 TITLE THE SOLUTION NMR STRUCTURE AND DYNAMICS OF A RECOMBINANT ONCONASE WITH TITLE 2 ALTERED N-TERMINAL AND MET23 RESIDUES COMPND MOL_ID: 1; COMPND 2 MOLECULE: P-30 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ONCONASE; COMPND 5 EC: 3.1.27.-; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RANA PIPIENS; SOURCE 3 ORGANISM_COMMON: NORTHERN LEOPARD FROG; SOURCE 4 ORGANISM_TAXID: 8404; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11D KEYWDS BOWL-SHAPED FOLDING OF THE TWO SHEETS, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 20 MDLTYP MINIMIZED AVERAGE AUTHOR V.Y.GORBATYUK,C.K.TSAI,C.F.CHANG,T.H.HUANG REVDAT 3 27-OCT-21 1PU3 1 REMARK SEQADV REVDAT 2 24-FEB-09 1PU3 1 VERSN REVDAT 1 16-MAR-04 1PU3 0 JRNL AUTH V.Y.GORBATYUK,C.K.TSAI,C.F.CHANG,T.H.HUANG JRNL TITL EFFECT OF N-TERMINAL AND MET23 MUTATIONS ON THE STRUCTURE JRNL TITL 2 AND DYNAMICS OF ONCONASE JRNL REF J.BIOL.CHEM. V. 279 5772 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 14645226 JRNL DOI 10.1074/JBC.M311233200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA 1.2, CNS 1.1 REMARK 3 AUTHORS : NILGES (ARIA), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1802 RESTRAINTS, 1550 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 4 DISULFIDE BONDS, 150 DIHEDRAL ANGLE REMARK 3 RESTRAINTS, 98 DISTANCE RESTRAINTS REMARK 3 FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1PU3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000019565. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 4.1 REMARK 210 IONIC STRENGTH : 0.3 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5 MM (M-1, Q1, M23L)RONC [U REMARK 210 -15N; U-13C] REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY; REMARK 210 3D_13C-SEPARATED_NOESY; 2D TOCSY; REMARK 210 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING, MATRIX REMARK 210 RELAXATION, TORSION ANGLE REMARK 210 DYMANICS 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 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 OD2 ASP A 17 HZ1 LYS A 82 1.58 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 ASN A 35 115.79 -161.56 REMARK 500 1 SER A 55 105.02 -51.81 REMARK 500 1 THR A 72 -136.64 -89.24 REMARK 500 1 VAL A 100 -65.57 -95.54 REMARK 500 2 PHE A 29 -30.13 -136.01 REMARK 500 2 SER A 40 148.17 -175.17 REMARK 500 2 SER A 55 105.99 -51.44 REMARK 500 2 THR A 72 -145.59 -93.90 REMARK 500 3 ASN A 27 25.43 -76.74 REMARK 500 3 PHE A 29 -36.02 -133.98 REMARK 500 3 SER A 55 105.57 -51.56 REMARK 500 3 THR A 72 -82.32 -114.52 REMARK 500 3 SER A 73 -63.53 -94.71 REMARK 500 3 VAL A 100 -79.48 -80.13 REMARK 500 4 SER A 55 104.13 -51.93 REMARK 500 4 THR A 72 -99.17 -97.50 REMARK 500 4 VAL A 100 -72.39 -90.64 REMARK 500 5 PHE A 29 -33.91 -135.63 REMARK 500 5 CYS A 31 62.72 38.78 REMARK 500 5 THR A 72 -140.72 -87.26 REMARK 500 6 CYS A 31 74.15 60.19 REMARK 500 6 SER A 55 108.61 -51.56 REMARK 500 6 THR A 72 -105.48 -114.60 REMARK 500 6 PRO A 96 106.40 -59.94 REMARK 500 6 VAL A 100 -72.96 -79.81 REMARK 500 7 ASN A 27 25.25 -78.50 REMARK 500 7 ASN A 35 117.78 -162.41 REMARK 500 7 SER A 55 105.95 -51.13 REMARK 500 7 THR A 72 -98.31 -92.67 REMARK 500 8 CYS A 31 79.42 40.40 REMARK 500 8 SER A 40 -177.26 -176.59 REMARK 500 8 SER A 55 105.51 -50.29 REMARK 500 8 THR A 72 -113.05 -114.32 REMARK 500 9 GLN A 2 112.76 64.57 REMARK 500 9 SER A 55 106.96 -51.30 REMARK 500 9 THR A 72 -152.69 -88.89 REMARK 500 10 ASP A 3 -177.72 -170.05 REMARK 500 10 SER A 40 -177.50 -170.45 REMARK 500 10 SER A 55 102.43 -50.85 REMARK 500 10 THR A 72 -106.53 -90.69 REMARK 500 11 CYS A 31 72.15 41.26 REMARK 500 11 SER A 55 108.60 -50.68 REMARK 500 11 THR A 72 -144.54 -88.29 REMARK 500 12 SER A 55 109.60 -51.39 REMARK 500 12 THR A 72 -133.53 -97.67 REMARK 500 13 HIS A 11 -13.79 -140.77 REMARK 500 13 SER A 40 -172.36 -177.14 REMARK 500 13 SER A 55 106.19 -51.89 REMARK 500 13 THR A 72 -142.88 -95.58 REMARK 500 14 THR A 72 -108.63 -114.36 REMARK 500 REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4371 RELATED DB: BMRB REMARK 900 1H,13C,15N CHEMICAL SHIFTS ASSIGNMENTS OF THE SAME PROTEIN REMARK 900 RELATED ID: 5835 RELATED DB: BMRB REMARK 900 HNHA COUPLING CONSTANTS OF THE SAME PROTEIN REMARK 900 RELATED ID: 1ONC RELATED DB: PDB REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE NATIVE ONCONASE DBREF 1PU3 A 2 105 UNP P22069 RN30_RANPI 1 104 SEQADV 1PU3 MET A 1 UNP P22069 CLONING ARTIFACT SEQADV 1PU3 LEU A 24 UNP P22069 MET 23 ENGINEERED MUTATION SEQRES 1 A 105 MET GLN ASP TRP LEU THR PHE GLN LYS LYS HIS ILE THR SEQRES 2 A 105 ASN THR ARG ASP VAL ASP CYS ASP ASN ILE LEU SER THR SEQRES 3 A 105 ASN LEU PHE HIS CYS LYS ASP LYS ASN THR PHE ILE TYR SEQRES 4 A 105 SER ARG PRO GLU PRO VAL LYS ALA ILE CYS LYS GLY ILE SEQRES 5 A 105 ILE ALA SER LYS ASN VAL LEU THR THR SER GLU PHE TYR SEQRES 6 A 105 LEU SER ASP CYS ASN VAL THR SER ARG PRO CYS LYS TYR SEQRES 7 A 105 LYS LEU LYS LYS SER THR ASN LYS PHE CYS VAL THR CYS SEQRES 8 A 105 GLU ASN GLN ALA PRO VAL HIS PHE VAL GLY VAL GLY SER SEQRES 9 A 105 CYS HELIX 1 1 ASP A 3 HIS A 11 1 9 HELIX 2 2 ASP A 19 LEU A 24 1 6 HELIX 3 3 ARG A 41 ALA A 47 1 7 HELIX 4 4 ILE A 48 LYS A 50 5 3 SHEET 1 A 4 ILE A 12 THR A 13 0 SHEET 2 A 4 LYS A 34 TYR A 39 1 O ILE A 38 N THR A 13 SHEET 3 A 4 PHE A 64 VAL A 71 -1 O TYR A 65 N TYR A 39 SHEET 4 A 4 TYR A 78 ASN A 85 -1 O LYS A 81 N ASP A 68 SHEET 1 B 3 LYS A 56 LEU A 59 0 SHEET 2 B 3 PHE A 87 GLU A 92 -1 O CYS A 91 N LYS A 56 SHEET 3 B 3 ALA A 95 VAL A 102 -1 O HIS A 98 N THR A 90 SSBOND 1 CYS A 20 CYS A 69 1555 1555 2.03 SSBOND 2 CYS A 31 CYS A 76 1555 1555 2.03 SSBOND 3 CYS A 49 CYS A 91 1555 1555 2.02 SSBOND 4 CYS A 88 CYS A 105 1555 1555 2.03 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 - t 27 2 Bytes