Header list of 1bc4.pdb file
Complete list - c 25 2 Bytes
HEADER HYDROLASE 05-MAY-98 1BC4
TITLE THE SOLUTION STRUCTURE OF A CYTOTOXIC RIBONUCLEASE FROM THE OOCYTES OF
TITLE 2 RANA CATESBEIANA (BULLFROG), NMR, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RC RNASE;
COMPND 5 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RANA CATESBEIANA;
SOURCE 3 ORGANISM_COMMON: BULLFROG;
SOURCE 4 ORGANISM_TAXID: 8400
KEYWDS HYDROLASE, PHOSPHORIC DIESTER, RC-RNASE, CYTOTOXIC PROTEIN, SIALIC
KEYWDS 2 ACID BINDING LECTIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR C.-F.CHANG,C.CHEN,Y.-C.CHEN,K.HOM,R.-F.HUANG,T.HUANG
REVDAT 5 25-DEC-19 1BC4 1 REMARK SEQRES LINK
REVDAT 4 24-FEB-09 1BC4 1 VERSN
REVDAT 3 01-APR-03 1BC4 1 JRNL
REVDAT 2 28-OCT-98 1BC4 1 REMARK JRNL
REVDAT 1 14-OCT-98 1BC4 0
JRNL AUTH C.F.CHANG,C.CHEN,Y.C.CHEN,K.HOM,R.F.HUANG,T.H.HUANG
JRNL TITL THE SOLUTION STRUCTURE OF A CYTOTOXIC RIBONUCLEASE FROM THE
JRNL TITL 2 OOCYTES OF RANA CATESBEIANA (BULLFROG).
JRNL REF J.MOL.BIOL. V. 283 231 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9761686
JRNL DOI 10.1006/JMBI.1998.2082
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.CHEN,K.HOM,R.F.HUANG,P.J.CHOU,Y.D.LIAO,T.HUANG
REMARK 1 TITL THE SECONDARY STRUCTURE OF A PYRIMIDINE-GUANINE
REMARK 1 TITL 2 SEQUENCE-SPECIFIC RIBONUCLEASE POSSESSING CYTOTOXIC ACTIVITY
REMARK 1 TITL 3 FROM THE OOCYTES OF RANA CATESBEIANA
REMARK 1 REF J.BIOMOL.NMR V. 8 331 1996
REMARK 1 REFN ISSN 0925-2738
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1BC4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171577.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL 1H NMR.
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 ILE A 11 65.64 -102.93
REMARK 500 1 PRO A 15 37.16 -81.51
REMARK 500 1 ILE A 17 33.99 -97.29
REMARK 500 1 ASP A 24 91.76 -60.35
REMARK 500 1 VAL A 30 -168.61 -109.73
REMARK 500 1 GLN A 33 -65.44 -165.22
REMARK 500 1 ASN A 57 110.50 171.47
REMARK 500 1 SER A 62 97.27 -59.16
REMARK 500 1 THR A 64 -92.02 -56.65
REMARK 500 1 ARG A 65 103.10 177.87
REMARK 500 1 PHE A 66 44.51 -98.25
REMARK 500 1 GLN A 67 107.39 18.17
REMARK 500 1 THR A 74 -92.88 -105.87
REMARK 500 1 ILE A 76 139.55 63.79
REMARK 500 1 GLU A 88 -172.12 -172.24
REMARK 500 1 ASN A 98 15.91 56.93
REMARK 500 1 GLN A 99 -15.36 78.29
REMARK 500 1 PRO A 101 91.25 -63.23
REMARK 500 1 ILE A 107 178.65 -56.43
REMARK 500 2 ASN A 13 80.79 -68.25
REMARK 500 2 THR A 14 59.79 -150.60
REMARK 500 2 ILE A 16 -169.17 -124.94
REMARK 500 2 ILE A 17 34.58 -97.88
REMARK 500 2 GLN A 33 -71.87 -166.31
REMARK 500 2 LYS A 35 171.27 -56.18
REMARK 500 2 VAL A 37 114.04 -164.72
REMARK 500 2 SER A 43 151.12 177.71
REMARK 500 2 VAL A 55 -164.80 -160.54
REMARK 500 2 ASN A 57 116.16 172.10
REMARK 500 2 SER A 62 95.81 -62.18
REMARK 500 2 THR A 64 -94.65 -52.16
REMARK 500 2 ARG A 65 101.90 173.66
REMARK 500 2 PHE A 66 44.42 -96.87
REMARK 500 2 GLN A 67 106.24 19.48
REMARK 500 2 THR A 74 -95.72 -125.55
REMARK 500 2 SER A 75 121.21 -171.34
REMARK 500 2 GLN A 99 9.58 52.69
REMARK 500 2 PRO A 101 90.08 -60.79
REMARK 500 2 ILE A 107 -171.20 -69.15
REMARK 500 2 ARG A 109 73.63 -160.88
REMARK 500 3 ILE A 17 41.15 -93.71
REMARK 500 3 ASP A 24 90.88 -62.49
REMARK 500 3 GLN A 33 -75.45 -166.24
REMARK 500 3 VAL A 37 117.55 -162.04
REMARK 500 3 SER A 43 151.23 178.33
REMARK 500 3 VAL A 55 -164.47 -161.12
REMARK 500 3 ASN A 57 117.43 172.44
REMARK 500 3 SER A 62 93.08 -59.12
REMARK 500 3 THR A 64 -90.45 -52.34
REMARK 500 3 ARG A 65 101.06 171.48
REMARK 500
REMARK 500 THIS ENTRY HAS 286 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 36 0.23 SIDE CHAIN
REMARK 500 1 ARG A 65 0.32 SIDE CHAIN
REMARK 500 1 ARG A 73 0.30 SIDE CHAIN
REMARK 500 1 ARG A 79 0.25 SIDE CHAIN
REMARK 500 1 ARG A 86 0.28 SIDE CHAIN
REMARK 500 1 ARG A 109 0.31 SIDE CHAIN
REMARK 500 2 ARG A 36 0.32 SIDE CHAIN
REMARK 500 2 ARG A 65 0.25 SIDE CHAIN
REMARK 500 2 ARG A 73 0.23 SIDE CHAIN
REMARK 500 2 ARG A 79 0.27 SIDE CHAIN
REMARK 500 2 ARG A 86 0.22 SIDE CHAIN
REMARK 500 2 ARG A 109 0.32 SIDE CHAIN
REMARK 500 3 ARG A 36 0.27 SIDE CHAIN
REMARK 500 3 ARG A 65 0.25 SIDE CHAIN
REMARK 500 3 ARG A 73 0.22 SIDE CHAIN
REMARK 500 3 ARG A 79 0.32 SIDE CHAIN
REMARK 500 3 ARG A 86 0.29 SIDE CHAIN
REMARK 500 3 ARG A 109 0.26 SIDE CHAIN
REMARK 500 4 ARG A 36 0.32 SIDE CHAIN
REMARK 500 4 ARG A 65 0.27 SIDE CHAIN
REMARK 500 4 ARG A 73 0.31 SIDE CHAIN
REMARK 500 4 ARG A 79 0.25 SIDE CHAIN
REMARK 500 4 ARG A 86 0.30 SIDE CHAIN
REMARK 500 4 ARG A 109 0.31 SIDE CHAIN
REMARK 500 5 ARG A 36 0.22 SIDE CHAIN
REMARK 500 5 ARG A 65 0.32 SIDE CHAIN
REMARK 500 5 ARG A 73 0.31 SIDE CHAIN
REMARK 500 5 ARG A 79 0.22 SIDE CHAIN
REMARK 500 5 ARG A 86 0.29 SIDE CHAIN
REMARK 500 5 ARG A 109 0.28 SIDE CHAIN
REMARK 500 6 ARG A 36 0.29 SIDE CHAIN
REMARK 500 6 ARG A 65 0.32 SIDE CHAIN
REMARK 500 6 ARG A 73 0.32 SIDE CHAIN
REMARK 500 6 ARG A 79 0.23 SIDE CHAIN
REMARK 500 6 ARG A 86 0.31 SIDE CHAIN
REMARK 500 6 ARG A 109 0.30 SIDE CHAIN
REMARK 500 7 ARG A 36 0.32 SIDE CHAIN
REMARK 500 7 ARG A 65 0.25 SIDE CHAIN
REMARK 500 7 ARG A 73 0.24 SIDE CHAIN
REMARK 500 7 ARG A 79 0.32 SIDE CHAIN
REMARK 500 7 ARG A 86 0.28 SIDE CHAIN
REMARK 500 7 ARG A 109 0.30 SIDE CHAIN
REMARK 500 8 ARG A 36 0.27 SIDE CHAIN
REMARK 500 8 ARG A 65 0.31 SIDE CHAIN
REMARK 500 8 ARG A 73 0.26 SIDE CHAIN
REMARK 500 8 ARG A 79 0.31 SIDE CHAIN
REMARK 500 8 ARG A 86 0.25 SIDE CHAIN
REMARK 500 8 ARG A 109 0.27 SIDE CHAIN
REMARK 500 9 ARG A 36 0.29 SIDE CHAIN
REMARK 500 9 ARG A 65 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 90 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BC4 A 2 111 UNP P11916 RNASO_RANCA 2 111
SEQRES 1 A 111 PCA ASN TRP ALA THR PHE GLN GLN LYS HIS ILE ILE ASN
SEQRES 2 A 111 THR PRO ILE ILE ASN CYS ASN THR ILE MET ASP ASN ASN
SEQRES 3 A 111 ILE TYR ILE VAL GLY GLY GLN CYS LYS ARG VAL ASN THR
SEQRES 4 A 111 PHE ILE ILE SER SER ALA THR THR VAL LYS ALA ILE CYS
SEQRES 5 A 111 THR GLY VAL ILE ASN MET ASN VAL LEU SER THR THR ARG
SEQRES 6 A 111 PHE GLN LEU ASN THR CYS THR ARG THR SER ILE THR PRO
SEQRES 7 A 111 ARG PRO CYS PRO TYR SER SER ARG THR GLU THR ASN TYR
SEQRES 8 A 111 ILE CYS VAL LYS CYS GLU ASN GLN TYR PRO VAL HIS PHE
SEQRES 9 A 111 ALA GLY ILE GLY ARG CYS PRO
MODRES 1BC4 PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA C5 H7 N O3
HELIX 1 AL1 TRP A 3 ILE A 11 1 9
HELIX 2 AL2 ASN A 18 MET A 23 1 6
HELIX 3 AL3 ALA A 45 THR A 53 1 9
SHEET 1 S1 3 VAL A 37 ILE A 42 0
SHEET 2 S1 3 PHE A 66 ARG A 73 -1 O GLN A 67 N ILE A 42
SHEET 3 S1 3 TYR A 83 ASN A 90 -1 O GLU A 88 N LEU A 68
SHEET 1 S2 3 ASN A 57 SER A 62 0
SHEET 2 S2 3 ILE A 92 GLU A 97 -1 O ILE A 92 N SER A 62
SHEET 3 S2 3 TYR A 100 GLY A 106 -1 N TYR A 100 O GLU A 97
SSBOND 1 CYS A 19 CYS A 71 1555 1555 2.02
SSBOND 2 CYS A 34 CYS A 81 1555 1555 2.02
SSBOND 3 CYS A 52 CYS A 96 1555 1555 2.02
SSBOND 4 CYS A 93 CYS A 110 1555 1555 2.02
LINK C PCA A 1 N ASN A 2 1555 1555 1.32
CISPEP 1 ARG A 79 PRO A 80 1 -3.08
CISPEP 2 ARG A 79 PRO A 80 2 0.17
CISPEP 3 ARG A 79 PRO A 80 3 1.27
CISPEP 4 ARG A 79 PRO A 80 4 0.71
CISPEP 5 ARG A 79 PRO A 80 5 0.25
CISPEP 6 ARG A 79 PRO A 80 6 0.14
CISPEP 7 ARG A 79 PRO A 80 7 0.86
CISPEP 8 ARG A 79 PRO A 80 8 -1.34
CISPEP 9 ARG A 79 PRO A 80 9 1.39
CISPEP 10 ARG A 79 PRO A 80 10 2.07
CISPEP 11 ARG A 79 PRO A 80 11 0.12
CISPEP 12 ARG A 79 PRO A 80 12 1.13
CISPEP 13 ARG A 79 PRO A 80 13 1.27
CISPEP 14 ARG A 79 PRO A 80 14 0.72
CISPEP 15 ARG A 79 PRO A 80 15 -2.45
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 25 2 Bytes