Header list of 1qwq.pdb file
Complete list - v 10 2 Bytes
HEADER HYDROLASE 03-SEP-03 1QWQ TITLE SOLUTION STRUCTURE OF THE MONOMERIC N67D MUTANT OF BOVINE SEMINAL TITLE 2 RIBONUCLEASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBONUCLEASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SEMINAL RIBONUCLEASE; COMPND 5 EC: 3.1.27.5; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: SRN; 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-22B+ KEYWDS ALPHA-BETA-PROTEIN, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR F.AVITABILE,C.ALFANO,R.SPADACCINI,O.CRESCENZI,A.M.D'URSI,G.D'ALESSIO, AUTHOR 2 T.TANCREDI,D.PICONE REVDAT 4 10-NOV-21 1QWQ 1 SEQADV REVDAT 3 26-FEB-20 1QWQ 1 REMARK REVDAT 2 24-FEB-09 1QWQ 1 VERSN REVDAT 1 16-SEP-03 1QWQ 0 SPRSDE 16-SEP-03 1QWQ 1O0G JRNL AUTH F.AVITABILE,C.ALFANO,R.SPADACCINI,O.CRESCENZI,A.M.D'URSI, JRNL AUTH 2 G.D'ALESSIO,T.TANCREDI,D.PICONE JRNL TITL THE SWAPPING OF TERMINAL ARMS IN RIBONUCLEASES: COMPARISON JRNL TITL 2 OF THE SOLUTION STRUCTURE OF MONOMERIC BOVINE SEMINAL AND JRNL TITL 3 PANCREATIC RIBONUCLEASES JRNL REF BIOCHEMISTRY V. 42 8704 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12873130 JRNL DOI 10.1021/BI0342517 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH O.CRESCENZI,A.CAROTENUTO,A.M.D'URSI,T.TANCREDI,G.D'ALESSIO, REMARK 1 AUTH 2 F.AVITABILE,D.PICONE REMARK 1 TITL 1H AND 15N SEQUENTIAL ASSIGNMENT AND SECONDARY STRUCTURE OF REMARK 1 TITL 2 THE MONOMERIC N67D MUTANT OF BOVINE SEMINAL RIBONUCLEASE. REMARK 1 REF J.BIOMOL.NMR V. 20 289 2001 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1011294812364 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, AMBER 6.0 REMARK 3 AUTHORS : REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH, REMARK 3 WEINER,KOLLMAN (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QWQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020160. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 5.65 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2.0MM MONOMERIC BOVINE SEMINAL REMARK 210 RIBONUCLEASE U-97% 15N; 2.0MM REMARK 210 MONOMERIC BOVINE SEMINAL REMARK 210 RIBONUCLEASE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_TOCSY; HNHA; HNHB; 2D REMARK 210 NOESY; 2D TOCSY; 2D COSY; 2D REMARK 210 NHSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 400 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 4.0.3, DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 5 CYS A 65 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 9 CYS A 40 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 11 ARG A 33 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES 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 SER A 3 -165.70 -123.27 REMARK 500 1 ALA A 4 -74.93 62.10 REMARK 500 1 HIS A 12 -51.95 -131.50 REMARK 500 1 THR A 45 62.31 -102.36 REMARK 500 1 HIS A 48 59.39 -90.41 REMARK 500 1 GLN A 60 -110.15 -94.72 REMARK 500 1 ASP A 67 -44.36 -150.95 REMARK 500 1 GLN A 69 -61.03 -154.39 REMARK 500 1 GLU A 86 84.15 -64.03 REMARK 500 1 LYS A 91 89.39 -151.32 REMARK 500 1 TYR A 92 125.05 -34.09 REMARK 500 1 ALA A 122 -170.06 -172.96 REMARK 500 2 ALA A 4 -67.22 -175.23 REMARK 500 2 SER A 15 71.26 -69.93 REMARK 500 2 SER A 22 -114.30 -89.28 REMARK 500 2 LYS A 39 -151.72 -86.29 REMARK 500 2 HIS A 48 -117.49 -82.52 REMARK 500 2 GLU A 49 -148.95 58.17 REMARK 500 2 SER A 59 48.41 -109.22 REMARK 500 2 GLN A 60 -126.74 -114.76 REMARK 500 2 GLN A 69 -69.27 -153.22 REMARK 500 2 GLU A 86 108.47 -43.61 REMARK 500 2 SER A 89 -48.23 -179.87 REMARK 500 2 SER A 90 109.82 -25.41 REMARK 500 2 LYS A 113 124.39 -34.39 REMARK 500 3 SER A 3 36.98 -144.75 REMARK 500 3 ALA A 4 -61.92 66.75 REMARK 500 3 ASP A 14 119.57 -169.07 REMARK 500 3 ASN A 17 150.90 66.80 REMARK 500 3 SER A 18 141.21 75.20 REMARK 500 3 SER A 21 68.79 -66.77 REMARK 500 3 PRO A 42 -71.40 -64.44 REMARK 500 3 PHE A 46 98.97 -65.48 REMARK 500 3 ASP A 67 -27.10 -146.99 REMARK 500 3 GLN A 69 -73.09 -159.73 REMARK 500 3 SER A 75 30.31 -69.27 REMARK 500 3 LYS A 76 -28.64 61.75 REMARK 500 3 GLU A 86 74.48 -68.42 REMARK 500 3 SER A 89 27.65 -164.09 REMARK 500 3 LYS A 91 80.06 -151.95 REMARK 500 3 TYR A 92 126.90 -36.59 REMARK 500 3 LYS A 113 123.63 -34.36 REMARK 500 4 GLU A 2 150.28 -48.81 REMARK 500 4 ALA A 4 -73.13 71.25 REMARK 500 4 SER A 15 65.30 -68.63 REMARK 500 4 SER A 18 140.94 69.73 REMARK 500 4 SER A 20 -90.98 -78.76 REMARK 500 4 SER A 22 -74.97 -97.65 REMARK 500 4 HIS A 48 -111.92 -82.34 REMARK 500 4 GLU A 49 -154.93 61.30 REMARK 500 REMARK 500 THIS ENTRY HAS 212 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 TYR A 25 0.06 SIDE CHAIN REMARK 500 1 PHE A 46 0.09 SIDE CHAIN REMARK 500 1 TYR A 92 0.11 SIDE CHAIN REMARK 500 2 ARG A 10 0.18 SIDE CHAIN REMARK 500 4 TYR A 73 0.09 SIDE CHAIN REMARK 500 4 TYR A 92 0.15 SIDE CHAIN REMARK 500 4 TYR A 97 0.07 SIDE CHAIN REMARK 500 5 TYR A 25 0.10 SIDE CHAIN REMARK 500 6 TYR A 25 0.15 SIDE CHAIN REMARK 500 6 TYR A 73 0.08 SIDE CHAIN REMARK 500 7 TYR A 73 0.07 SIDE CHAIN REMARK 500 7 TYR A 97 0.09 SIDE CHAIN REMARK 500 8 TYR A 73 0.06 SIDE CHAIN REMARK 500 8 TYR A 97 0.17 SIDE CHAIN REMARK 500 9 TYR A 92 0.07 SIDE CHAIN REMARK 500 9 TYR A 97 0.12 SIDE CHAIN REMARK 500 10 TYR A 97 0.21 SIDE CHAIN REMARK 500 11 TYR A 25 0.08 SIDE CHAIN REMARK 500 11 PHE A 46 0.09 SIDE CHAIN REMARK 500 11 TYR A 92 0.11 SIDE CHAIN REMARK 500 11 TYR A 97 0.07 SIDE CHAIN REMARK 500 12 ARG A 80 0.08 SIDE CHAIN REMARK 500 13 TYR A 73 0.10 SIDE CHAIN REMARK 500 13 TYR A 92 0.07 SIDE CHAIN REMARK 500 13 TYR A 97 0.08 SIDE CHAIN REMARK 500 15 TYR A 25 0.17 SIDE CHAIN REMARK 500 16 TYR A 25 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4980 RELATED DB: BMRB REMARK 900 1H AND 15N SEQUENTIAL ASSIGNMENT AND SECONDARY STRUCTURE OF THE REMARK 900 SAME PROTEIN REMARK 900 RELATED ID: 1BSR RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF BOVINE SEMINAL RIBONUCLEASE DBREF 1QWQ A 1 124 UNP P00669 RNS_BOVIN 27 150 SEQADV 1QWQ ASP A 67 UNP P00669 ASN 93 ENGINEERED MUTATION SEQRES 1 A 124 LYS GLU SER ALA ALA ALA LYS PHE GLU ARG GLN HIS MET SEQRES 2 A 124 ASP SER GLY ASN SER PRO SER SER SER SER ASN TYR CYS SEQRES 3 A 124 ASN LEU MET MET CYS CYS ARG LYS MET THR GLN GLY LYS SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA SEQRES 5 A 124 ASP VAL LYS ALA VAL CYS SER GLN LYS LYS VAL THR CYS SEQRES 6 A 124 LYS ASP GLY GLN THR ASN CYS TYR GLN SER LYS SER THR SEQRES 7 A 124 MET ARG ILE THR ASP CYS ARG GLU THR GLY SER SER LYS SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN VAL GLU LYS SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLY GLY LYS PRO SER VAL PRO SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL HELIX 1 1 ALA A 4 HIS A 12 1 9 HELIX 2 2 SER A 21 LYS A 34 1 14 HELIX 3 3 SER A 50 SER A 59 1 10 SHEET 1 A 5 VAL A 43 VAL A 47 0 SHEET 2 A 5 MET A 79 ARG A 85 -1 O CYS A 84 N ASN A 44 SHEET 3 A 5 LYS A 98 GLY A 111 -1 O LYS A 98 N ARG A 85 SHEET 4 A 5 ASN A 71 GLN A 74 -1 N TYR A 73 O VAL A 108 SHEET 5 A 5 LYS A 61 THR A 64 -1 N VAL A 63 O CYS A 72 SHEET 1 B 4 VAL A 43 VAL A 47 0 SHEET 2 B 4 MET A 79 ARG A 85 -1 O CYS A 84 N ASN A 44 SHEET 3 B 4 LYS A 98 GLY A 111 -1 O LYS A 98 N ARG A 85 SHEET 4 B 4 VAL A 116 VAL A 124 -1 O ALA A 122 N ILE A 107 SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.07 SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.07 SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.08 SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.08 CISPEP 1 TYR A 92 PRO A 93 1 6.63 CISPEP 2 LYS A 113 PRO A 114 1 -2.22 CISPEP 3 TYR A 92 PRO A 93 2 7.49 CISPEP 4 LYS A 113 PRO A 114 2 4.19 CISPEP 5 TYR A 92 PRO A 93 3 10.14 CISPEP 6 LYS A 113 PRO A 114 3 3.98 CISPEP 7 TYR A 92 PRO A 93 4 5.85 CISPEP 8 LYS A 113 PRO A 114 4 4.96 CISPEP 9 TYR A 92 PRO A 93 5 8.09 CISPEP 10 LYS A 113 PRO A 114 5 -2.21 CISPEP 11 TYR A 92 PRO A 93 6 3.89 CISPEP 12 LYS A 113 PRO A 114 6 -7.28 CISPEP 13 TYR A 92 PRO A 93 7 6.66 CISPEP 14 LYS A 113 PRO A 114 7 3.44 CISPEP 15 TYR A 92 PRO A 93 8 10.00 CISPEP 16 LYS A 113 PRO A 114 8 2.46 CISPEP 17 TYR A 92 PRO A 93 9 7.61 CISPEP 18 LYS A 113 PRO A 114 9 -4.82 CISPEP 19 TYR A 92 PRO A 93 10 2.80 CISPEP 20 LYS A 113 PRO A 114 10 3.82 CISPEP 21 TYR A 92 PRO A 93 11 8.29 CISPEP 22 LYS A 113 PRO A 114 11 5.08 CISPEP 23 TYR A 92 PRO A 93 12 5.15 CISPEP 24 LYS A 113 PRO A 114 12 -2.47 CISPEP 25 TYR A 92 PRO A 93 13 7.63 CISPEP 26 LYS A 113 PRO A 114 13 -3.33 CISPEP 27 TYR A 92 PRO A 93 14 5.62 CISPEP 28 LYS A 113 PRO A 114 14 -1.58 CISPEP 29 TYR A 92 PRO A 93 15 -0.97 CISPEP 30 LYS A 113 PRO A 114 15 -3.55 CISPEP 31 TYR A 92 PRO A 93 16 1.35 CISPEP 32 LYS A 113 PRO A 114 16 -4.42 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 - v 10 2 Bytes