Header list of 2b7v.pdb file
Complete list - r 9 2 Bytes
HEADER HYDROLASE 05-OCT-05 2B7V
TITLE STRUCTURE OF ADAR2 DSRBM2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLE-STRANDED RNA-SPECIFIC EDITASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOUBLE-STRANDED RNA-BINDING DOMAIN;
COMPND 5 SYNONYM: DSRNA ADENOSINE DEAMINASE, RNA EDITING DEAMINASE 1, RNA
COMPND 6 EDITING ENZYME 1;
COMPND 7 EC: 3.5.-.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ADARB1, RED1;
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: PET16
KEYWDS RNA EDITING, RNA-BINDING PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.STEFL,M.XU,L.SKRISOVSKA,R.B.EMESON,F.H.-T.ALLAIN
REVDAT 3 09-MAR-22 2B7V 1 REMARK
REVDAT 2 24-FEB-09 2B7V 1 VERSN
REVDAT 1 14-MAR-06 2B7V 0
JRNL AUTH R.STEFL,M.XU,L.SKRISOVSKA,R.B.EMESON,F.H.-T.ALLAIN
JRNL TITL STRUCTURE AND SPECIFIC RNA BINDING OF ADAR2 DOUBLE-STRANDED
JRNL TITL 2 RNA BINDING MOTIFS.
JRNL REF STRUCTURE V. 14 345 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16472753
JRNL DOI 10.1016/J.STR.2005.11.013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, SPARKY, AMBER 7
REMARK 3 AUTHORS : CASE, D.A., ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B7V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034784.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 8.0
REMARK 210 IONIC STRENGTH : 250MM TOTAL SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N; 200MM NACL; 50 MM
REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10%
REMARK 210 D2O; 1MM U-13C,15N; 200MM NACL;
REMARK 210 50 MM PHOSPHATE BUFFER, 90% H2O,
REMARK 210 10% D2O; 1MM U-15N; 200MM NACL;
REMARK 210 50 MM PHOSPHATE BUFFER, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D 15N-SEPARATED
REMARK 210 NOESY; 3D 13C-SEPARATED NOESY;
REMARK 210 15N-HSQC; 13C-HSQC; HNCA; HNCO;
REMARK 210 CBCA(CO)NH; 3D HCCH-TOCSY; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULTED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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
REMARK 500 REMARK: NULL
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 1 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 PRO A 1 CA - N - CD ANGL. DEV. = -8.6 DEGREES
REMARK 500 2 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 PRO A 1 CA - N - CD ANGL. DEV. = -9.4 DEGREES
REMARK 500 3 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 PRO A 1 CA - N - CD ANGL. DEV. = -8.6 DEGREES
REMARK 500 7 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 PHE A 33 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 8 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 11 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 PRO A 1 CA - N - CD ANGL. DEV. = -9.3 DEGREES
REMARK 500 13 PRO A 1 CA - N - CD ANGL. DEV. = -9.4 DEGREES
REMARK 500 13 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 15 PRO A 1 CA - N - CD ANGL. DEV. = -8.9 DEGREES
REMARK 500 15 LEU A 10 CB - CG - CD1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 17 PRO A 1 CA - N - CD ANGL. DEV. = -8.6 DEGREES
REMARK 500 17 LEU A 10 CB - CG - CD1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 18 PRO A 1 CA - N - CD ANGL. DEV. = -9.3 DEGREES
REMARK 500 19 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.0 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 ARG A 14 75.92 -9.21
REMARK 500 1 GLU A 24 80.34 100.04
REMARK 500 1 HIS A 29 -38.40 -130.34
REMARK 500 1 LYS A 31 149.14 84.73
REMARK 500 1 VAL A 39 -110.97 -126.74
REMARK 500 1 ASP A 40 45.22 -81.14
REMARK 500 1 THR A 65 -70.35 -55.25
REMARK 500 2 SER A 2 29.97 -67.99
REMARK 500 2 ARG A 14 65.39 24.11
REMARK 500 2 GLU A 24 78.04 85.54
REMARK 500 2 SER A 28 10.12 -62.33
REMARK 500 2 ALA A 30 -59.29 -159.50
REMARK 500 2 ASP A 40 -79.92 56.65
REMARK 500 2 THR A 65 -71.35 -55.24
REMARK 500 2 HIS A 70 43.40 99.56
REMARK 500 3 LYS A 4 28.84 -141.89
REMARK 500 3 ARG A 14 67.87 15.04
REMARK 500 3 PRO A 15 43.14 -62.17
REMARK 500 3 GLU A 24 7.34 122.92
REMARK 500 3 SER A 25 32.93 -62.44
REMARK 500 3 SER A 28 40.26 -70.36
REMARK 500 3 HIS A 29 -40.11 -153.50
REMARK 500 3 ASP A 40 -23.66 62.16
REMARK 500 3 ARG A 49 -59.10 -13.63
REMARK 500 3 THR A 65 -73.17 -55.44
REMARK 500 3 HIS A 70 -42.18 -169.30
REMARK 500 4 ARG A 14 65.17 27.38
REMARK 500 4 PRO A 15 74.74 -58.97
REMARK 500 4 GLU A 24 -12.77 -166.19
REMARK 500 4 SER A 25 39.25 -78.04
REMARK 500 4 GLU A 27 -27.68 67.77
REMARK 500 4 HIS A 29 -59.24 -148.89
REMARK 500 4 ASP A 40 -66.34 59.02
REMARK 500 5 SER A 2 176.33 55.03
REMARK 500 5 ARG A 14 90.71 -10.11
REMARK 500 5 PRO A 15 -166.10 -66.98
REMARK 500 5 GLU A 24 60.40 97.90
REMARK 500 5 GLU A 27 -146.74 -82.28
REMARK 500 5 LYS A 31 53.65 29.23
REMARK 500 5 ASP A 40 -65.62 59.83
REMARK 500 5 HIS A 70 39.68 103.90
REMARK 500 6 LYS A 4 25.27 -151.30
REMARK 500 6 ARG A 14 66.40 34.80
REMARK 500 6 PRO A 15 60.64 -68.71
REMARK 500 6 GLU A 24 0.01 -162.27
REMARK 500 6 SER A 28 48.87 -75.06
REMARK 500 6 HIS A 29 -32.12 64.25
REMARK 500 6 ALA A 30 58.90 -69.96
REMARK 500 6 ASP A 40 -79.28 54.97
REMARK 500 6 HIS A 70 45.47 77.25
REMARK 500
REMARK 500 THIS ENTRY HAS 158 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 24 SER A 25 1 148.84
REMARK 500 ARG A 49 ASN A 50 2 147.53
REMARK 500 SER A 23 GLU A 24 3 142.26
REMARK 500 PRO A 1 SER A 2 5 -135.41
REMARK 500 GLU A 24 SER A 25 5 138.99
REMARK 500 PRO A 1 SER A 2 6 139.49
REMARK 500 SER A 23 GLU A 24 7 -45.02
REMARK 500 LEU A 17 LYS A 18 8 145.27
REMARK 500 GLU A 27 SER A 28 8 -148.67
REMARK 500 PRO A 1 SER A 2 9 -129.66
REMARK 500 SER A 23 GLU A 24 9 -43.54
REMARK 500 ASP A 40 GLY A 41 9 -147.28
REMARK 500 ARG A 49 ASN A 50 9 149.91
REMARK 500 LEU A 22 SER A 23 10 149.67
REMARK 500 SER A 23 GLU A 24 11 142.72
REMARK 500 LEU A 17 LYS A 18 14 147.01
REMARK 500 SER A 23 GLU A 24 14 -129.48
REMARK 500 LYS A 4 ASN A 5 15 145.93
REMARK 500 SER A 23 GLU A 24 15 147.83
REMARK 500 ASN A 5 PRO A 6 18 -141.25
REMARK 500 ASP A 40 GLY A 41 18 -142.92
REMARK 500 SER A 23 GLU A 24 19 -143.73
REMARK 500 SER A 25 GLY A 26 19 148.65
REMARK 500 LEU A 22 SER A 23 20 149.14
REMARK 500 SER A 23 GLU A 24 20 119.73
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 5 ARG A 14 0.09 SIDE CHAIN
REMARK 500 5 ARG A 57 0.08 SIDE CHAIN
REMARK 500 7 ARG A 14 0.08 SIDE CHAIN
REMARK 500 9 ARG A 57 0.09 SIDE CHAIN
REMARK 500 12 ARG A 57 0.09 SIDE CHAIN
REMARK 500 20 TYR A 19 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6280 RELATED DB: BMRB
REMARK 900 RELATED ID: 2B7T RELATED DB: PDB
DBREF 2B7V A 1 71 UNP P51400 RED1_RAT 231 301
SEQRES 1 A 71 PRO SER GLY LYS ASN PRO VAL MET ILE LEU ASN GLU LEU
SEQRES 2 A 71 ARG PRO GLY LEU LYS TYR ASP PHE LEU SER GLU SER GLY
SEQRES 3 A 71 GLU SER HIS ALA LYS SER PHE VAL MET SER VAL VAL VAL
SEQRES 4 A 71 ASP GLY GLN PHE PHE GLU GLY SER GLY ARG ASN LYS LYS
SEQRES 5 A 71 LEU ALA LYS ALA ARG ALA ALA GLN SER ALA LEU ALA THR
SEQRES 6 A 71 VAL PHE ASN LEU HIS LEU
HELIX 1 1 ASN A 5 ARG A 14 1 10
HELIX 2 2 ASN A 50 HIS A 70 1 21
SHEET 1 A 3 LYS A 18 SER A 23 0
SHEET 2 A 3 PHE A 33 VAL A 38 -1 O VAL A 34 N LEU A 22
SHEET 3 A 3 PHE A 43 GLY A 48 -1 O GLY A 48 N PHE A 33
CISPEP 1 GLY A 26 GLU A 27 1 -10.14
CISPEP 2 SER A 25 GLY A 26 2 -7.70
CISPEP 3 GLY A 26 GLU A 27 5 1.54
CISPEP 4 GLY A 26 GLU A 27 7 -10.22
CISPEP 5 PRO A 1 SER A 2 11 0.30
CISPEP 6 SER A 28 HIS A 29 12 17.36
CISPEP 7 PRO A 1 SER A 2 14 1.98
CISPEP 8 HIS A 29 ALA A 30 14 -1.97
CISPEP 9 PRO A 1 SER A 2 15 4.31
CISPEP 10 ALA A 30 LYS A 31 15 10.74
CISPEP 11 ALA A 30 LYS A 31 16 4.74
CISPEP 12 GLY A 26 GLU A 27 17 4.10
CISPEP 13 GLY A 3 LYS A 4 18 13.68
CISPEP 14 SER A 2 GLY A 3 20 -7.82
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 - r 9 2 Bytes