Header list of 1aud.pdb file
Complete list - v 3 2 Bytes
HEADER RNA BINDING PROTEIN/RNA 22-AUG-97 1AUD
TITLE U1A-UTRRNA, NMR, 31 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA 3UTR;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: UUCG TETRALOOP, ONLY BOX 1 OF 3'UTR RNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: U1A 102;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: RESIDUES 1 - 102 OF U1A;
COMPND 10 SYNONYM: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 STRAIN: BL21 (DE3);
SOURCE 8 CELL_LINE: BL21;
SOURCE 9 GENE: U1A 1-102;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET13A;
SOURCE 14 EXPRESSION_SYSTEM_GENE: T7
KEYWDS COMPLEX (RIBONUCLEOPROTEIN-RNA), RNP DOMAIN, RNA BINDING PROTEIN-RNA
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 31
AUTHOR F.H.-T.ALLAIN,C.C.GUBSER,P.W.A.HOWE,K.NAGAI,D.NEUHAUS,G.VARANI
REVDAT 3 03-NOV-21 1AUD 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1AUD 1 VERSN
REVDAT 1 25-FEB-98 1AUD 0
SPRSDE 25-FEB-98 1AUD 1NUM
JRNL AUTH F.H.ALLAIN,P.W.HOWE,D.NEUHAUS,G.VARANI
JRNL TITL STRUCTURAL BASIS OF THE RNA-BINDING SPECIFICITY OF HUMAN U1A
JRNL TITL 2 PROTEIN.
JRNL REF EMBO J. V. 16 5764 1997
JRNL REFN ISSN 0261-4189
JRNL PMID 9312034
JRNL DOI 10.1093/EMBOJ/16.18.5764
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.W.A.HOWE,F.H.T.ALLAIN,G.VARANI,D.NEUHAUS
REMARK 1 TITL DETERMINATION OF THE NMR STRUCTURE OF THE COMPLEX BETWEEN
REMARK 1 TITL 2 U1A PROTEIN AND ITS RNA POLYADENYLATION INHIBITION ELEMENT
REMARK 1 REF J.BIOMOL.NMR V. 11 59 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.H.ALLAIN,C.C.GUBSER,P.W.HOWE,K.NAGAI,D.NEUHAUS,G.VARANI
REMARK 1 TITL SPECIFICITY OF RIBONUCLEOPROTEIN INTERACTION DETERMINED BY
REMARK 1 TITL 2 RNA FOLDING DURING COMPLEX FORMULATION
REMARK 1 REF NATURE V. 380 646 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.OUBRIDGE,N.ITO,P.R.EVANS,C.H.TEO,K.NAGAI
REMARK 1 TITL CRYSTAL STRUCTURE AT 1.92 A RESOLUTION OF THE RNA-BINDING
REMARK 1 TITL 2 DOMAIN OF THE U1A SPLICEOSOMAL PROTEIN COMPLEXED WITH AN RNA
REMARK 1 TITL 3 HAIRPIN
REMARK 1 REF NATURE V. 372 432 1994
REMARK 1 REFN ISSN 0028-0836
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: STARTING WITH 50 STRUCTURES WITH
REMARK 3 RANDOMISED BACKBONE TORSION ANGLES ON BOTH THE RNA AND THE
REMARK 3 PROTEIN COMPONENTS, 31 STRUCTURES WERE FOUND TO HAVE CONVERGED.
REMARK 3 THE X-PLOR PROTOCOL START WITH A PERIOD OF SIMULATED ANNEALING
REMARK 3 WITH ONLY DISTANCE CONSTRAINTS (249 1 INCLUDING 123
REMARK 3 INTERMOLECULAR) FOLLOWED BY A PERIOD OF REFINEMENT WHERE 110
REMARK 3 DIHEDRAL CONSTRAINTS DERIVED FROM J COUPLING ANALYSIS AND
REMARK 3 PHOSPHORUS CHEMICAL SHIFT VALUE WERE ADDED (IN THE RNA ONLY). NO
REMARK 3 DIHEDRAL ANGLE VIOLATIONS AND AN AVERAGE OF 4 NOE VIOLA TIONS
REMARK 3 BETWEEN 0.2 - 0.5 A WERE FOUND IN THE 31 CONVERGED STRUCTURES.
REMARK 4
REMARK 4 1AUD 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_1000171269.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.1
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 1 G B 19 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G B 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G B 20 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G B 20 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A B 22 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 G B 23 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 23 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A B 24 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G B 25 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 25 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G B 34 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G B 34 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G B 35 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 35 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 1 G B 36 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 36 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A B 37 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A B 39 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G B 42 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 42 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 1 A B 44 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G B 48 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G B 48 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G B 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G B 20 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 20 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A B 22 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G B 23 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 23 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 A B 24 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G B 25 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 25 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G B 34 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G B 34 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G B 35 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G B 35 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G B 36 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G B 36 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A B 37 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A B 39 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G B 42 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 42 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 2 A B 44 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G B 48 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G B 48 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G B 19 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G B 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G B 20 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G B 20 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 714 ANGLE DEVIATIONS.
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 THR A 5 104.39 60.09
REMARK 500 1 LYS A 19 34.94 -149.51
REMARK 500 1 MET A 50 56.65 -94.10
REMARK 500 1 ARG A 51 47.56 -101.53
REMARK 500 1 PHE A 76 -59.73 -126.19
REMARK 500 1 TYR A 77 67.44 -118.98
REMARK 500 1 THR A 99 46.29 38.67
REMARK 500 1 PHE A 100 91.08 45.10
REMARK 500 2 GLU A 18 42.09 -105.50
REMARK 500 2 LYS A 19 34.91 -148.17
REMARK 500 2 ASP A 41 141.96 -173.17
REMARK 500 2 PHE A 76 -59.73 -123.59
REMARK 500 2 TYR A 77 65.66 -113.53
REMARK 500 2 TYR A 85 176.10 -51.00
REMARK 500 2 THR A 99 49.99 179.69
REMARK 500 3 GLU A 4 -178.72 -58.31
REMARK 500 3 GLU A 18 56.98 -101.96
REMARK 500 3 LYS A 19 32.58 -147.37
REMARK 500 3 ALA A 31 -70.41 -83.30
REMARK 500 3 ASP A 41 159.64 179.44
REMARK 500 3 ARG A 46 35.70 -146.55
REMARK 500 3 MET A 50 53.08 -96.44
REMARK 500 3 PHE A 76 -59.24 -122.63
REMARK 500 3 LYS A 79 142.52 -173.03
REMARK 500 3 ALA A 86 -172.76 -63.15
REMARK 500 3 THR A 99 74.41 40.16
REMARK 500 4 ARG A 6 153.52 62.73
REMARK 500 4 GLU A 18 59.32 -100.40
REMARK 500 4 LYS A 19 33.60 -148.51
REMARK 500 4 MET A 50 51.87 -107.41
REMARK 500 4 GLU A 60 156.47 71.69
REMARK 500 4 PHE A 76 -59.94 -129.68
REMARK 500 4 LYS A 79 140.91 -176.79
REMARK 500 4 TYR A 85 169.22 -47.91
REMARK 500 4 THR A 99 45.05 38.52
REMARK 500 4 PHE A 100 91.76 45.53
REMARK 500 5 GLU A 4 179.52 -57.34
REMARK 500 5 ASN A 15 71.67 71.16
REMARK 500 5 LYS A 19 38.42 -154.29
REMARK 500 5 ASP A 41 146.32 -179.98
REMARK 500 5 MET A 50 -52.01 -170.51
REMARK 500 5 PHE A 76 -61.19 -135.75
REMARK 500 5 TYR A 77 70.54 -115.99
REMARK 500 5 ALA A 86 179.71 -53.26
REMARK 500 5 THR A 99 49.24 -179.92
REMARK 500 5 PHE A 100 79.07 44.12
REMARK 500 6 ARG A 6 84.55 55.92
REMARK 500 6 THR A 10 110.82 -167.92
REMARK 500 6 GLU A 18 42.54 -101.27
REMARK 500 6 LYS A 19 33.93 -148.24
REMARK 500
REMARK 500 THIS ENTRY HAS 336 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 6 0.31 SIDE CHAIN
REMARK 500 1 ARG A 35 0.26 SIDE CHAIN
REMARK 500 1 ARG A 46 0.32 SIDE CHAIN
REMARK 500 1 ARG A 51 0.31 SIDE CHAIN
REMARK 500 1 ARG A 69 0.25 SIDE CHAIN
REMARK 500 1 ARG A 82 0.26 SIDE CHAIN
REMARK 500 2 ARG A 6 0.31 SIDE CHAIN
REMARK 500 2 ARG A 35 0.30 SIDE CHAIN
REMARK 500 2 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG A 51 0.28 SIDE CHAIN
REMARK 500 2 ARG A 69 0.25 SIDE CHAIN
REMARK 500 2 ARG A 82 0.32 SIDE CHAIN
REMARK 500 3 ARG A 6 0.28 SIDE CHAIN
REMARK 500 3 ARG A 35 0.26 SIDE CHAIN
REMARK 500 3 ARG A 46 0.29 SIDE CHAIN
REMARK 500 3 ARG A 51 0.26 SIDE CHAIN
REMARK 500 3 ARG A 69 0.31 SIDE CHAIN
REMARK 500 3 ARG A 82 0.31 SIDE CHAIN
REMARK 500 4 ARG A 6 0.30 SIDE CHAIN
REMARK 500 4 ARG A 35 0.27 SIDE CHAIN
REMARK 500 4 ARG A 46 0.22 SIDE CHAIN
REMARK 500 4 ARG A 51 0.27 SIDE CHAIN
REMARK 500 4 ARG A 69 0.32 SIDE CHAIN
REMARK 500 4 ARG A 82 0.26 SIDE CHAIN
REMARK 500 5 ARG A 6 0.26 SIDE CHAIN
REMARK 500 5 ARG A 35 0.32 SIDE CHAIN
REMARK 500 5 ARG A 46 0.22 SIDE CHAIN
REMARK 500 5 ARG A 51 0.32 SIDE CHAIN
REMARK 500 5 ARG A 69 0.32 SIDE CHAIN
REMARK 500 5 ARG A 82 0.23 SIDE CHAIN
REMARK 500 6 ARG A 6 0.31 SIDE CHAIN
REMARK 500 6 ARG A 35 0.32 SIDE CHAIN
REMARK 500 6 ARG A 46 0.27 SIDE CHAIN
REMARK 500 6 ARG A 51 0.30 SIDE CHAIN
REMARK 500 6 ARG A 69 0.31 SIDE CHAIN
REMARK 500 6 ARG A 82 0.25 SIDE CHAIN
REMARK 500 7 ARG A 6 0.21 SIDE CHAIN
REMARK 500 7 ARG A 35 0.31 SIDE CHAIN
REMARK 500 7 ARG A 46 0.29 SIDE CHAIN
REMARK 500 7 ARG A 51 0.31 SIDE CHAIN
REMARK 500 7 ARG A 69 0.24 SIDE CHAIN
REMARK 500 7 ARG A 82 0.31 SIDE CHAIN
REMARK 500 8 ARG A 6 0.25 SIDE CHAIN
REMARK 500 8 ARG A 35 0.28 SIDE CHAIN
REMARK 500 8 ARG A 46 0.24 SIDE CHAIN
REMARK 500 8 ARG A 51 0.26 SIDE CHAIN
REMARK 500 8 ARG A 69 0.21 SIDE CHAIN
REMARK 500 8 ARG A 82 0.25 SIDE CHAIN
REMARK 500 9 ARG A 6 0.31 SIDE CHAIN
REMARK 500 9 ARG A 35 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 187 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AUD A 1 101 UNP P09012 SNRPA_HUMAN 2 102
DBREF 1AUD B 19 50 PDB 1AUD 1AUD 19 50
SEQADV 1AUD HIS A 30 UNP P09012 TYR 31 ENGINEERED MUTATION
SEQADV 1AUD ARG A 35 UNP P09012 GLN 36 ENGINEERED MUTATION
SEQRES 1 B 30 G G C A G A G U C C U U C
SEQRES 2 B 30 G G G A C A U U G C A C C
SEQRES 3 B 30 U G C C
SEQRES 1 A 101 ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR ILE
SEQRES 2 A 101 ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU LYS
SEQRES 3 A 101 LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN ILE
SEQRES 4 A 101 LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG GLY
SEQRES 5 A 101 GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA THR
SEQRES 6 A 101 ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR ASP
SEQRES 7 A 101 LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER ASP
SEQRES 8 A 101 ILE ILE ALA LYS MET LYS GLY THR PHE VAL
HELIX 1 1 LEU A 25 ILE A 32 1 8
HELIX 2 2 GLU A 60 ARG A 69 1 10
HELIX 3 3 ASP A 91 LYS A 97 1 7
SHEET 1 A 3 GLN A 53 VAL A 56 0
SHEET 2 A 3 ILE A 11 ASN A 14 -1 N ILE A 13 O ALA A 54
SHEET 3 A 3 ILE A 83 TYR A 85 -1 N GLN A 84 O TYR A 12
SHEET 1 B 2 PHE A 74 PHE A 76 0
SHEET 2 B 2 LYS A 79 MET A 81 -1 N MET A 81 O PHE A 74
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 3 2 Bytes