Header list of 1m58.pdb file
Complete list - c 21 2 Bytes
HEADER HYDROLASE 09-JUL-02 1M58
TITLE SOLUTION STRUCTURE OF CYTOTOXIC RC-RNASE2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RC-RNASE2 RIBONUCLEASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RANA CATESBEIANA;
SOURCE 3 ORGANISM_COMMON: BULLFROG;
SOURCE 4 ORGANISM_TAXID: 8400;
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 BULLFROG, CYTOTOXICITY, RIBONUCLEASE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.-H.HSU,Y.-D.LIAO,S.-H.WU,C.CHEN
REVDAT 4 21-DEC-22 1M58 1 SEQADV
REVDAT 3 23-FEB-22 1M58 1 REMARK
REVDAT 2 24-FEB-09 1M58 1 VERSN
REVDAT 1 09-JAN-03 1M58 0
JRNL AUTH C.H.HSU,L.W.CHEN,Y.D.LIAO,S.H.WU,C.CHEN
JRNL TITL 1H, 15N AND 13C RESONANCE ASSIGNMENTS AND SECONDARY
JRNL TITL 2 STRUCTURE DETERMINATION OF THE RC-RNASE 2 FROM OOCYTES OF
JRNL TITL 3 BULLFROG RANA CATESBEIANA.
JRNL REF J.BIOMOL.NMR V. 19 87 2001
JRNL REFN ISSN 0925-2738
JRNL PMID 11246862
JRNL DOI 10.1023/A:1008348302036
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 1M58 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016613.
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 : 1.5 MM RRC-RNASE2 U-15N,13C;
REMARK 210 50MM PHOSPHATE BUFFER; 1.5 MM
REMARK 210 RRC-RNASE2 U-15N; 50MM PHOSPHATE
REMARK 210 BUFFER
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 : 600
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 HETERONUCLEAR 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: 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 GLN A 2 -41.43 -131.98
REMARK 500 1 ASP A 17 50.58 -98.77
REMARK 500 1 ASP A 30 49.29 74.07
REMARK 500 1 LYS A 50 42.00 -100.51
REMARK 500 1 LYS A 73 99.90 -171.80
REMARK 500 1 LEU A 74 161.88 -43.86
REMARK 500 1 PRO A 75 -76.48 -79.02
REMARK 500 1 VAL A 97 -17.86 -140.38
REMARK 500 1 ALA A 101 -157.33 -167.33
REMARK 500 1 VAL A 102 -139.46 -109.19
REMARK 500 2 ASN A 3 -167.83 -129.83
REMARK 500 2 ASP A 17 37.03 -99.36
REMARK 500 2 ALA A 27 16.89 55.40
REMARK 500 2 LYS A 32 -173.45 -67.17
REMARK 500 2 LYS A 50 44.92 -97.77
REMARK 500 2 ASN A 51 -45.10 -141.53
REMARK 500 2 LYS A 73 107.53 177.75
REMARK 500 2 LEU A 74 169.26 -49.25
REMARK 500 2 GLU A 92 131.07 -173.56
REMARK 500 2 LYS A 94 -7.96 83.43
REMARK 500 2 ALA A 101 -163.76 -163.90
REMARK 500 2 VAL A 102 -152.19 -90.23
REMARK 500 3 ASP A 17 50.49 -91.96
REMARK 500 3 LYS A 32 -174.33 -55.67
REMARK 500 3 ASN A 51 -38.04 -132.44
REMARK 500 3 GLU A 92 132.41 -172.85
REMARK 500 3 LYS A 94 17.53 59.60
REMARK 500 3 ALA A 101 -163.56 -169.25
REMARK 500 3 VAL A 102 -141.39 -108.40
REMARK 500 4 VAL A 18 154.13 -47.76
REMARK 500 4 ASP A 30 48.19 70.17
REMARK 500 4 LYS A 32 -179.93 -66.52
REMARK 500 4 ASN A 51 26.52 -142.27
REMARK 500 4 LYS A 73 117.58 -173.24
REMARK 500 4 LEU A 74 169.35 -48.28
REMARK 500 4 ALA A 101 -163.14 -166.58
REMARK 500 4 VAL A 102 -147.25 -101.09
REMARK 500 5 ASP A 17 40.82 -97.27
REMARK 500 5 GLN A 33 -70.20 -58.46
REMARK 500 5 ALA A 40 176.74 179.51
REMARK 500 5 LYS A 50 42.55 -107.08
REMARK 500 5 ILE A 72 -47.82 -137.44
REMARK 500 5 LEU A 74 167.93 -48.18
REMARK 500 5 GLU A 92 135.10 -173.06
REMARK 500 5 VAL A 97 17.73 -150.14
REMARK 500 5 ALA A 101 -164.15 -169.37
REMARK 500 5 VAL A 102 -152.19 -92.37
REMARK 500 6 GLN A 2 -65.49 -145.82
REMARK 500 6 ASP A 17 46.42 -95.64
REMARK 500 6 LYS A 32 -172.10 -60.00
REMARK 500
REMARK 500 THIS ENTRY HAS 127 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 16 0.25 SIDE CHAIN
REMARK 500 1 ARG A 41 0.25 SIDE CHAIN
REMARK 500 1 ARG A 44 0.32 SIDE CHAIN
REMARK 500 1 ARG A 71 0.32 SIDE CHAIN
REMARK 500 2 ARG A 16 0.32 SIDE CHAIN
REMARK 500 2 ARG A 41 0.27 SIDE CHAIN
REMARK 500 2 ARG A 44 0.31 SIDE CHAIN
REMARK 500 2 ARG A 71 0.19 SIDE CHAIN
REMARK 500 3 ARG A 16 0.26 SIDE CHAIN
REMARK 500 3 ARG A 41 0.32 SIDE CHAIN
REMARK 500 3 ARG A 44 0.32 SIDE CHAIN
REMARK 500 3 ARG A 71 0.20 SIDE CHAIN
REMARK 500 4 ARG A 16 0.21 SIDE CHAIN
REMARK 500 4 ARG A 41 0.30 SIDE CHAIN
REMARK 500 4 ARG A 44 0.28 SIDE CHAIN
REMARK 500 4 ARG A 71 0.31 SIDE CHAIN
REMARK 500 5 ARG A 16 0.24 SIDE CHAIN
REMARK 500 5 ARG A 41 0.31 SIDE CHAIN
REMARK 500 5 ARG A 44 0.30 SIDE CHAIN
REMARK 500 5 ARG A 71 0.18 SIDE CHAIN
REMARK 500 6 ARG A 16 0.20 SIDE CHAIN
REMARK 500 6 ARG A 41 0.27 SIDE CHAIN
REMARK 500 6 ARG A 44 0.28 SIDE CHAIN
REMARK 500 6 ARG A 71 0.32 SIDE CHAIN
REMARK 500 7 ARG A 16 0.31 SIDE CHAIN
REMARK 500 7 ARG A 41 0.23 SIDE CHAIN
REMARK 500 7 ARG A 44 0.22 SIDE CHAIN
REMARK 500 7 ARG A 71 0.31 SIDE CHAIN
REMARK 500 8 ARG A 16 0.26 SIDE CHAIN
REMARK 500 8 ARG A 41 0.20 SIDE CHAIN
REMARK 500 8 ARG A 44 0.29 SIDE CHAIN
REMARK 500 8 ARG A 71 0.23 SIDE CHAIN
REMARK 500 9 ARG A 16 0.29 SIDE CHAIN
REMARK 500 9 ARG A 41 0.31 SIDE CHAIN
REMARK 500 9 ARG A 44 0.23 SIDE CHAIN
REMARK 500 9 ARG A 71 0.22 SIDE CHAIN
REMARK 500 10 ARG A 16 0.23 SIDE CHAIN
REMARK 500 10 ARG A 41 0.30 SIDE CHAIN
REMARK 500 10 ARG A 44 0.23 SIDE CHAIN
REMARK 500 10 ARG A 71 0.30 SIDE CHAIN
REMARK 500 11 ARG A 16 0.31 SIDE CHAIN
REMARK 500 11 ARG A 41 0.32 SIDE CHAIN
REMARK 500 11 ARG A 44 0.22 SIDE CHAIN
REMARK 500 11 ARG A 71 0.29 SIDE CHAIN
REMARK 500 12 ARG A 16 0.19 SIDE CHAIN
REMARK 500 12 ARG A 41 0.31 SIDE CHAIN
REMARK 500 12 ARG A 44 0.31 SIDE CHAIN
REMARK 500 12 ARG A 71 0.32 SIDE CHAIN
REMARK 500 13 ARG A 16 0.29 SIDE CHAIN
REMARK 500 13 ARG A 41 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M58 A 2 106 UNP Q9DFY8 Q9DFY8_RANCA 24 128
SEQADV 1M58 MET A 1 UNP Q9DFY8 INITIATING METHIONINE
SEQRES 1 A 106 MET GLN ASN TRP GLU THR PHE GLN LYS LYS HIS LEU THR
SEQRES 2 A 106 ASP THR ARG ASP VAL LYS CYS ASP ALA GLU MET LYS LYS
SEQRES 3 A 106 ALA LEU PHE ASP CYS LYS GLN LYS ASN THR PHE ILE TYR
SEQRES 4 A 106 ALA ARG PRO GLY ARG VAL GLN ALA LEU CYS LYS ASN ILE
SEQRES 5 A 106 ILE VAL SER LYS ASN VAL LEU SER THR ASP GLU PHE TYR
SEQRES 6 A 106 LEU SER ASP CYS ASN ARG ILE LYS LEU PRO CYS HIS TYR
SEQRES 7 A 106 LYS LEU LYS LYS SER SER ASN THR ILE CYS ILE THR CYS
SEQRES 8 A 106 GLU ASN LYS LEU PRO VAL HIS PHE VAL ALA VAL GLU GLU
SEQRES 9 A 106 CYS PRO
HELIX 1 1 ASN A 3 HIS A 11 1 9
HELIX 2 2 LYS A 19 LYS A 25 1 7
HELIX 3 3 ARG A 41 ALA A 47 1 7
SHEET 1 A 4 LEU A 12 THR A 13 0
SHEET 2 A 4 ASN A 35 TYR A 39 1 O ILE A 38 N THR A 13
SHEET 3 A 4 PHE A 64 LYS A 73 -1 O CYS A 69 N ASN A 35
SHEET 4 A 4 HIS A 77 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 CYS A 88 GLU A 92 -1 O ILE A 89 N VAL A 58
SHEET 3 B 3 LEU A 95 ALA A 101 -1 O ALA A 101 N CYS A 88
SSBOND 1 CYS A 20 CYS A 69 1555 1555 2.02
SSBOND 2 CYS A 31 CYS A 76 1555 1555 2.02
SSBOND 3 CYS A 49 CYS A 91 1555 1555 2.02
SSBOND 4 CYS A 88 CYS A 105 1555 1555 2.02
CISPEP 1 LEU A 74 PRO A 75 1 0.61
CISPEP 2 LEU A 74 PRO A 75 2 -0.49
CISPEP 3 LEU A 74 PRO A 75 3 -1.53
CISPEP 4 LEU A 74 PRO A 75 4 0.13
CISPEP 5 LEU A 74 PRO A 75 5 -0.15
CISPEP 6 LEU A 74 PRO A 75 6 -0.49
CISPEP 7 LEU A 74 PRO A 75 7 -0.09
CISPEP 8 LEU A 74 PRO A 75 8 -0.57
CISPEP 9 LEU A 74 PRO A 75 9 -0.17
CISPEP 10 LEU A 74 PRO A 75 10 0.41
CISPEP 11 LEU A 74 PRO A 75 11 -0.28
CISPEP 12 LEU A 74 PRO A 75 12 -0.65
CISPEP 13 LEU A 74 PRO A 75 13 0.32
CISPEP 14 LEU A 74 PRO A 75 14 -0.47
CISPEP 15 LEU A 74 PRO A 75 15 -1.19
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