Header list of 1dz5.pdb file
Complete list - n 12 2 Bytes
HEADER RIBONUCLEOPROTEIN/RNA 16-FEB-00 1DZ5
TITLE THE NMR STRUCTURE OF THE 38KDA U1A PROTEIN-PIE RNA COMPLEX
TITLE 2 REVEALS THE BASIS OF COOPERATIVITY IN REGULATION OF
TITLE 3 POLYADENYLATION BY HUMAN U1A PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-102;
COMPND 5 SYNONYM: U1 SNRNP A, U1-A, U1A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PIE, RNA (5'-R(*GP*AP*GP*AP*CP*AP*UP*UP*GP*CP*AP*CP*CP*
COMPND 10 CP*GP*GP*AP*GP*UP*CP*UP*C)-3');
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: 3' UTR POLYADENYLATION INHIBITION ELEMENT;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET13A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
SOURCE 14 OTHER_DETAILS: PRODUCED BY IN VITRO TRANSCRIPTION;
KEYWDS RIBONUCLEOPROTEIN-RNA COMPLEX, POLYADENYLATION,
KEYWDS 2 PROTEIN PROTEIN INTERACTION, RNA PROTEIN INTERACTION
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR L.VARANI,S.I.GUNDERSON,I.W.MATTAJ,L.E.KAY,D.NEUHAUS,G.VARANI
REVDAT 10 15-MAY-13 1DZ5 1 COMPND SOURCE KEYWDS JRNL
REVDAT 10 2 REMARK VERSN SHEET ATOM
REVDAT 10 3 TER MASTER
REVDAT 9 24-FEB-09 1DZ5 1 VERSN
REVDAT 8 14-JUL-05 1DZ5 1 ATOM TER
REVDAT 7 03-MAY-05 1DZ5 1 ATOM
REVDAT 6 03-JUL-02 1DZ5 1 SEQADV
REVDAT 5 02-APR-02 1DZ5 1 JRNL
REVDAT 4 21-JUL-00 1DZ5 1 ATOM
REVDAT 3 09-JUN-00 1DZ5 1 JRNL
REVDAT 2 22-APR-00 1DZ5 1 ENDMDL
REVDAT 1 29-MAR-00 1DZ5 0
JRNL AUTH L.VARANI,S.I.GUNDERSON,I.W.MATTAJ,L.E.KAY,D.NEUHAUS,G.VARANI
JRNL TITL THE NMR STRUCTURE OF THE 38KDA U1A PROTEIN-PIE RNA COMPLEX
JRNL TITL 2 REVEALS THE BASIS OF COOPERATIVITY IN REGULATION OF
JRNL TITL 3 POLYADENYLATION BY HUMAN U1A PROTEIN
JRNL REF NAT.STRUCT.BIOL. V. 7 329 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10742179
JRNL DOI 10.1038/74101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DETAILS CAN BE FOUND IN THE JOURNAL
REMARK 3 CITATION ABOVE
REMARK 4
REMARK 4 1DZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-00.
REMARK 100 THE PDBE ID CODE IS EBI-4599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D FILTERED NOESY, HSQCS,
REMARK 210 HALF-FILTER EXPERIMENTS,
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.8.1
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13
REMARK 210 CONFORMERS, SELECTION CRITERIA : AGREEMENT WITH EXPERIMENTAL DATA
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 15N, 13C AND 2D
REMARK 210 LABELED SAMPLES. DIFFERENT LABELLED SPECIES WERE MIXED IN
REMARK 210 DIFFERENT EXPERIMENTS. TRIPLE RESONANCE EXPERIMENTS COULD
REMARK 210 NOT BE USED DUE TO THE SIZE OF THE COMPLEX; TROSY WAS NOT
REMARK 210 AVAILABLE WHEN MOST OF THE ASSIGNMENT WAS COMPLETED.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 MUTATIONS IN CHAIN A,B: Y31H, Q36R
REMARK 400 MUTATIONS IN CHAIN C: U18C, A21G
REMARK 400 MUTATIONS IN CHAIN D: U47C
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 5 ALA A 1 N
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 O MET A 96 HG1 THR A 99 1.50
REMARK 500 O MET B 96 HG1 THR B 99 1.50
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 G C 8 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G C 8 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A C 9 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 G C 10 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G C 10 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 A C 11 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A C 13 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G C 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G C 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A C 18 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 G C 22 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G C 22 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G C 23 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G C 23 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A C 24 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G C 25 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G C 25 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G D 34 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G D 34 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 A D 35 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 G D 36 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G D 36 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A D 37 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A D 39 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G D 42 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G D 42 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A D 44 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G D 48 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G D 48 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G D 49 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G D 49 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 A D 50 N7 - C8 - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 G D 51 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G D 51 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G C 8 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G C 8 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 A C 9 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G C 10 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G C 10 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 A C 11 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A C 13 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G C 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G C 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 A C 18 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G C 22 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G C 22 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G C 23 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G C 23 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 A C 24 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G C 25 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 444 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 VAL A 2 91.73 59.62
REMARK 500 1 PRO A 3 -168.02 -78.31
REMARK 500 1 ARG A 6 155.30 62.45
REMARK 500 1 HIS A 9 -80.24 60.88
REMARK 500 1 THR A 10 -154.50 -123.74
REMARK 500 1 LEU A 16 -179.56 -59.37
REMARK 500 1 LYS A 19 26.90 -145.78
REMARK 500 1 LYS A 22 -56.66 72.16
REMARK 500 1 ASP A 41 162.83 179.23
REMARK 500 1 SER A 45 -167.24 -123.32
REMARK 500 1 MET A 50 48.07 -100.33
REMARK 500 1 ALA A 54 100.99 -176.28
REMARK 500 1 PHE A 58 -89.07 -120.05
REMARK 500 1 LYS A 59 -40.16 178.43
REMARK 500 1 GLN A 72 103.04 -57.94
REMARK 500 1 PHE A 76 -80.47 -91.50
REMARK 500 1 ASP A 78 36.31 -178.98
REMARK 500 1 LYS A 79 148.02 -171.72
REMARK 500 1 ASP A 89 -169.12 46.28
REMARK 500 1 PHE A 100 -32.19 177.07
REMARK 500 1 VAL B 2 91.82 59.56
REMARK 500 1 PRO B 3 -167.99 -78.33
REMARK 500 1 ARG B 6 155.32 62.42
REMARK 500 1 HIS B 9 -80.26 60.83
REMARK 500 1 THR B 10 -154.53 -123.72
REMARK 500 1 LEU B 16 -179.74 -59.41
REMARK 500 1 LYS B 19 26.83 -145.73
REMARK 500 1 LYS B 22 -56.78 72.25
REMARK 500 1 ASP B 41 162.95 179.38
REMARK 500 1 SER B 45 -167.36 -123.41
REMARK 500 1 MET B 50 48.02 -100.27
REMARK 500 1 ALA B 54 101.03 -176.26
REMARK 500 1 PHE B 58 -89.08 -119.99
REMARK 500 1 LYS B 59 -40.08 178.39
REMARK 500 1 GLN B 72 102.99 -57.85
REMARK 500 1 PHE B 76 -80.57 -91.48
REMARK 500 1 ASP B 78 36.33 -179.03
REMARK 500 1 LYS B 79 148.01 -171.66
REMARK 500 1 ASP B 89 -169.02 46.26
REMARK 500 1 PHE B 100 -32.26 177.00
REMARK 500 2 VAL A 2 90.85 59.44
REMARK 500 2 HIS A 9 -73.73 62.53
REMARK 500 2 THR A 10 -159.60 -135.38
REMARK 500 2 ASN A 15 39.29 177.21
REMARK 500 2 GLU A 18 41.45 -104.89
REMARK 500 2 LYS A 22 -55.01 71.84
REMARK 500 2 ASP A 41 151.38 179.90
REMARK 500 2 ARG A 46 35.46 -178.14
REMARK 500 2 MET A 50 51.00 -103.50
REMARK 500 2 GLN A 53 141.84 -172.90
REMARK 500
REMARK 500 THIS ENTRY HAS 425 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 0.23 SIDE CHAIN
REMARK 500 1 ARG A 46 0.29 SIDE CHAIN
REMARK 500 1 ARG A 51 0.28 SIDE CHAIN
REMARK 500 1 ARG A 69 0.32 SIDE CHAIN
REMARK 500 1 ARG A 82 0.29 SIDE CHAIN
REMARK 500 1 ARG B 6 0.31 SIDE CHAIN
REMARK 500 1 ARG B 35 0.23 SIDE CHAIN
REMARK 500 1 ARG B 46 0.29 SIDE CHAIN
REMARK 500 1 ARG B 51 0.28 SIDE CHAIN
REMARK 500 1 ARG B 69 0.32 SIDE CHAIN
REMARK 500 1 ARG B 82 0.29 SIDE CHAIN
REMARK 500 2 ARG A 6 0.32 SIDE CHAIN
REMARK 500 2 ARG A 35 0.29 SIDE CHAIN
REMARK 500 2 ARG A 46 0.30 SIDE CHAIN
REMARK 500 2 ARG A 51 0.31 SIDE CHAIN
REMARK 500 2 ARG A 69 0.31 SIDE CHAIN
REMARK 500 2 ARG A 82 0.24 SIDE CHAIN
REMARK 500 2 ARG B 6 0.32 SIDE CHAIN
REMARK 500 2 ARG B 35 0.29 SIDE CHAIN
REMARK 500 2 ARG B 46 0.30 SIDE CHAIN
REMARK 500 2 ARG B 51 0.31 SIDE CHAIN
REMARK 500 2 ARG B 69 0.31 SIDE CHAIN
REMARK 500 2 ARG B 82 0.24 SIDE CHAIN
REMARK 500 3 ARG A 6 0.31 SIDE CHAIN
REMARK 500 3 ARG A 35 0.21 SIDE CHAIN
REMARK 500 3 ARG A 46 0.28 SIDE CHAIN
REMARK 500 3 ARG A 51 0.23 SIDE CHAIN
REMARK 500 3 ARG A 69 0.32 SIDE CHAIN
REMARK 500 3 ARG A 82 0.32 SIDE CHAIN
REMARK 500 3 ARG B 6 0.31 SIDE CHAIN
REMARK 500 3 ARG B 35 0.21 SIDE CHAIN
REMARK 500 3 ARG B 46 0.29 SIDE CHAIN
REMARK 500 3 ARG B 51 0.23 SIDE CHAIN
REMARK 500 3 ARG B 69 0.32 SIDE CHAIN
REMARK 500 3 ARG B 82 0.32 SIDE CHAIN
REMARK 500 4 ARG A 6 0.32 SIDE CHAIN
REMARK 500 4 ARG A 35 0.32 SIDE CHAIN
REMARK 500 4 ARG A 46 0.21 SIDE CHAIN
REMARK 500 4 ARG A 51 0.31 SIDE CHAIN
REMARK 500 4 ARG A 69 0.30 SIDE CHAIN
REMARK 500 4 ARG A 82 0.31 SIDE CHAIN
REMARK 500 4 ARG B 6 0.32 SIDE CHAIN
REMARK 500 4 ARG B 35 0.32 SIDE CHAIN
REMARK 500 4 ARG B 46 0.21 SIDE CHAIN
REMARK 500 4 ARG B 51 0.31 SIDE CHAIN
REMARK 500 4 ARG B 69 0.30 SIDE CHAIN
REMARK 500 4 ARG B 82 0.31 SIDE CHAIN
REMARK 500 5 ARG A 6 0.23 SIDE CHAIN
REMARK 500 5 ARG A 35 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 156 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AUD RELATED DB: PDB
REMARK 900 U1A-UTRRNA, NMR, 31 STRUCTURES
REMARK 900 RELATED ID: 1FHT RELATED DB: PDB
REMARK 900 RNA-BINDING DOMAIN OF THE U1A SPLICEOSOMAL PROTEIN
REMARK 900 RELATED ID: 1URN RELATED DB: PDB
REMARK 900 U1A/RNA COMPLEX
DBREF 1DZ5 A 1 101 UNP P09012 RU1A_HUMAN 2 102
DBREF 1DZ5 B 1 101 UNP P09012 RU1A_HUMAN 2 102
DBREF 1DZ5 C 8 29 PDB 1DZ5 1DZ5 8 29
DBREF 1DZ5 D 34 55 PDB 1DZ5 1DZ5 34 55
SEQADV 1DZ5 HIS A 30 UNP P09012 TYR 31 ENGINEERED MUTATION
SEQADV 1DZ5 ARG A 35 UNP P09012 GLN 36 ENGINEERED MUTATION
SEQADV 1DZ5 HIS B 30 UNP P09012 TYR 31 ENGINEERED MUTATION
SEQADV 1DZ5 ARG B 35 UNP P09012 GLN 36 ENGINEERED MUTATION
SEQRES 1 C 22 G A G A C A U U G C A C C
SEQRES 2 C 22 C G G A G U C U C
SEQRES 1 D 22 G A G A C A U U G C A C C
SEQRES 2 D 22 C G G A G U C U 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
SEQRES 1 B 101 ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR ILE
SEQRES 2 B 101 ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU LYS
SEQRES 3 B 101 LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN ILE
SEQRES 4 B 101 LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG GLY
SEQRES 5 B 101 GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA THR
SEQRES 6 B 101 ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR ASP
SEQRES 7 B 101 LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER ASP
SEQRES 8 B 101 ILE ILE ALA LYS MET LYS GLY THR PHE VAL
HELIX 1 1 LYS A 22 PHE A 33 1 12
HELIX 2 2 GLU A 60 ARG A 69 1 10
HELIX 3 3 SER A 90 LYS A 95 5 6
HELIX 4 4 LYS A 95 PHE A 100 5 6
HELIX 5 5 LYS B 22 PHE B 33 1 12
HELIX 6 6 GLU B 60 ARG B 69 1 10
HELIX 7 7 SER B 90 LYS B 95 5 6
HELIX 8 8 LYS B 95 PHE B 100 5 6
SHEET 1 AA 5 ASP A 41 LEU A 43 0
SHEET 2 AA 5 GLN A 53 ILE A 57 -1 O PHE A 55 N LEU A 43
SHEET 3 AA 5 THR A 10 ASN A 14 -1 O ILE A 11 N VAL A 56
SHEET 4 AA 5 PRO A 80 ALA A 86 -1 O ARG A 82 N ASN A 14
SHEET 5 AA 5 PHE A 74 PRO A 75 -1 O PHE A 74 N MET A 81
SHEET 1 BA 5 ASP B 41 LEU B 43 0
SHEET 2 BA 5 GLN B 53 ILE B 57 -1 O PHE B 55 N LEU B 43
SHEET 3 BA 5 THR B 10 ASN B 14 -1 O ILE B 11 N VAL B 56
SHEET 4 BA 5 PRO B 80 ALA B 86 -1 O ARG B 82 N ASN B 14
SHEET 5 BA 5 PHE B 74 PRO B 75 -1 O PHE B 74 N MET B 81
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 - n 12 2 Bytes