Header list of 1fje.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN/RNA 08-AUG-00 1FJE
TITLE SOLUTION STRUCTURE OF NUCLEOLIN RBD12 IN COMPLEX WITH SNRE RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SNRE RNA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: IN VITRO SELECTED RNA;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NUCLEOLIN RBD12;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: TWO N-TERMINAL RBD DOMAINS;
COMPND 10 SYNONYM: PROTEIN C23;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: IN VITRO TRANSCRIPTION BY T7 RNA POLYMERASE;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: MESOCRICETUS AURATUS;
SOURCE 6 ORGANISM_COMMON: GOLDEN HAMSTER;
SOURCE 7 ORGANISM_TAXID: 10036;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15-B
KEYWDS RNP, RBD, RRM, RNA BINDING DOMAIN, RNA-PROTEIN COMPLEX, NUCLEOLUS,
KEYWDS 2 STRUCTURAL PROTEIN-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR F.H.T.ALLAIN,P.BOUVET,T.DIECKMANN,J.FEIGON
REVDAT 4 23-FEB-22 1FJE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1FJE 1 VERSN
REVDAT 2 01-APR-03 1FJE 1 JRNL
REVDAT 1 03-JAN-01 1FJE 0
JRNL AUTH F.H.ALLAIN,P.BOUVET,T.DIECKMANN,J.FEIGON
JRNL TITL MOLECULAR BASIS OF SEQUENCE-SPECIFIC RECOGNITION OF
JRNL TITL 2 PRE-RIBOSOMAL RNA BY NUCLEOLIN.
JRNL REF EMBO J. V. 19 6870 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 11118222
JRNL DOI 10.1093/EMBOJ/19.24.6870
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.H.T.ALLAIN,D.E.GILBERT,P.BOUVET,J.FEIGON
REMARK 1 TITL SOLUTION STRUCTURE OF THE TWO N-TERMINAL RNA-BINDING DOMAINS
REMARK 1 TITL 2 OF NUCLEOLIN AND NMR STUDY OF THE INTERACTION WITH ITS RNA
REMARK 1 TITL 3 TARGET
REMARK 1 REF J.MOL.BIOL. V. 303 227 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.4118
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.841
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 3246
REMARK 3 CONSTRAINTS, 3010 ARE NOE-DERIVED INCLUDING 150 INTERMOLECULAR
REMARK 4
REMARK 4 1FJE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011638.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 318
REMARK 210 PH : 6.2; 6.2
REMARK 210 IONIC STRENGTH : 150; 150
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM U-15N,13C NUCLEOLIN RBD12 IN
REMARK 210 COMPLEX WITH UNLABELED RNA; 1MM
REMARK 210 U-15N NUCLEOLIN RBD12 IN COMPLEX
REMARK 210 WITH UNLABELED RNA; 1MM U-15N
REMARK 210 NUCLEOLIN RBD12 IN COMPLEX WITH
REMARK 210 UNLABELED RNA; 1MM U-15N-13C RNA
REMARK 210 IN COMPLEX WITH U-15N NUCLEOLIN
REMARK 210 RBD12
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 13C-12C
REMARK 210 FILTERED 3D; 3D_15N-SEPARATED_
REMARK 210 NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.841
REMARK 210 METHOD USED : SIMULATED ANNEALING USING XPLOR
REMARK 210 3.841
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: A, B
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 HO2' C A 4 O4' G A 5 1.30
REMARK 500 O2 C A 4 H21 G A 19 1.32
REMARK 500 O6 G A 2 H41 C A 21 1.34
REMARK 500 O LEU B 103 H TYR B 169 1.45
REMARK 500 O GLY B 158 H VAL B 166 1.46
REMARK 500 O ARG B 127 H TYR B 140 1.47
REMARK 500 O2' U A 9 H6 C A 10 1.47
REMARK 500 H ALA B 104 O ALA B 139 1.48
REMARK 500 H LYS B 105 O SER B 167 1.49
REMARK 500 OE1 GLN B 157 H LEU B 168 1.50
REMARK 500 O PHE B 14 H PHE B 61 1.51
REMARK 500 O ILE B 161 H ARG B 164 1.52
REMARK 500 H4' C A 4 OP1 G A 5 1.52
REMARK 500 O GLU B 113 H LYS B 117 1.53
REMARK 500 O SER B 93 H LYS B 95 1.54
REMARK 500 O ASP B 92 H LYS B 94 1.55
REMARK 500 O ASN B 106 HE ARG B 164 1.57
REMARK 500 HD21 ASN B 15 OD1 ASP B 60 1.57
REMARK 500 H22 G A 5 N7 A A 18 1.58
REMARK 500 O LEU B 116 H PHE B 120 1.59
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 A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 7 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 A A 8 N7 - C8 - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 G A 13 N7 - C8 - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 G A 13 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 14 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 18 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 20 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 20 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 2 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 2 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 7 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 8 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 G A 13 N7 - C8 - N9 ANGL. DEV. = 5.1 DEGREES
REMARK 500 2 G A 13 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 2 A A 14 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 G A 16 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 16 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A A 18 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G A 20 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 20 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 3 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 3 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 A A 6 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 3 A A 7 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 A A 8 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 G A 13 N7 - C8 - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 381 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 SER B 2 48.18 -107.56
REMARK 500 1 SER B 8 -80.98 168.12
REMARK 500 1 GLU B 9 34.21 -165.86
REMARK 500 1 ASN B 20 66.03 62.40
REMARK 500 1 LEU B 21 -88.65 -84.60
REMARK 500 1 ASN B 22 95.86 176.89
REMARK 500 1 LYS B 25 -157.54 -143.20
REMARK 500 1 ASP B 42 35.46 95.18
REMARK 500 1 LEU B 43 -147.83 -95.31
REMARK 500 1 ALA B 44 60.32 -172.65
REMARK 500 1 ARG B 49 -162.57 -127.98
REMARK 500 1 THR B 52 102.27 29.33
REMARK 500 1 ASN B 53 24.38 90.64
REMARK 500 1 PHE B 56 -150.12 -131.14
REMARK 500 1 PHE B 79 36.46 33.73
REMARK 500 1 GLU B 82 97.74 -52.80
REMARK 500 1 GLU B 86 169.84 163.87
REMARK 500 1 ARG B 91 -73.09 -153.38
REMARK 500 1 SER B 93 57.98 -66.82
REMARK 500 1 LYS B 94 -65.23 53.70
REMARK 500 1 ILE B 111 170.13 -45.55
REMARK 500 1 PHE B 120 61.06 -101.25
REMARK 500 1 SER B 130 -158.90 -116.21
REMARK 500 1 GLN B 131 55.67 -103.08
REMARK 500 1 LYS B 134 115.86 163.75
REMARK 500 1 SER B 135 136.20 -38.79
REMARK 500 1 SER B 145 -168.23 -165.73
REMARK 500 1 LYS B 156 -64.71 -109.27
REMARK 500 1 GLN B 157 90.20 29.65
REMARK 500 1 ALA B 159 93.96 35.31
REMARK 500 1 GLU B 160 99.80 -66.54
REMARK 500 1 ASP B 162 39.05 37.64
REMARK 500 1 TYR B 170 -168.96 -51.36
REMARK 500 2 HIS B 3 43.75 -144.94
REMARK 500 2 SER B 8 -51.48 -124.70
REMARK 500 2 SER B 10 160.13 -37.57
REMARK 500 2 LEU B 16 -177.87 -177.65
REMARK 500 2 ASN B 20 39.29 71.79
REMARK 500 2 LEU B 21 -97.66 -64.57
REMARK 500 2 ASN B 22 99.17 173.84
REMARK 500 2 LYS B 25 -159.51 -144.02
REMARK 500 2 ASP B 42 33.07 96.15
REMARK 500 2 LEU B 43 -149.66 -98.64
REMARK 500 2 ALA B 44 62.39 -172.82
REMARK 500 2 ARG B 49 -164.87 -120.02
REMARK 500 2 THR B 52 101.04 31.25
REMARK 500 2 ASN B 53 29.38 88.84
REMARK 500 2 ARG B 54 17.05 57.91
REMARK 500 2 PHE B 56 -145.45 -129.87
REMARK 500 2 VAL B 78 -141.27 -53.87
REMARK 500
REMARK 500 THIS ENTRY HAS 644 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 B 49 0.12 SIDE CHAIN
REMARK 500 1 ARG B 91 0.31 SIDE CHAIN
REMARK 500 1 ARG B 97 0.21 SIDE CHAIN
REMARK 500 1 ARG B 100 0.17 SIDE CHAIN
REMARK 500 1 ARG B 127 0.21 SIDE CHAIN
REMARK 500 1 ARG B 164 0.20 SIDE CHAIN
REMARK 500 2 A A 14 0.05 SIDE CHAIN
REMARK 500 2 ARG B 49 0.32 SIDE CHAIN
REMARK 500 2 ARG B 54 0.31 SIDE CHAIN
REMARK 500 2 ARG B 91 0.12 SIDE CHAIN
REMARK 500 2 ARG B 97 0.28 SIDE CHAIN
REMARK 500 2 ARG B 100 0.32 SIDE CHAIN
REMARK 500 2 ARG B 127 0.21 SIDE CHAIN
REMARK 500 2 ARG B 164 0.26 SIDE CHAIN
REMARK 500 3 ARG B 49 0.31 SIDE CHAIN
REMARK 500 3 ARG B 54 0.32 SIDE CHAIN
REMARK 500 3 ARG B 91 0.31 SIDE CHAIN
REMARK 500 3 ARG B 97 0.19 SIDE CHAIN
REMARK 500 3 ARG B 100 0.32 SIDE CHAIN
REMARK 500 3 ARG B 127 0.25 SIDE CHAIN
REMARK 500 3 ARG B 164 0.14 SIDE CHAIN
REMARK 500 4 ARG B 49 0.31 SIDE CHAIN
REMARK 500 4 ARG B 54 0.11 SIDE CHAIN
REMARK 500 4 ARG B 91 0.23 SIDE CHAIN
REMARK 500 4 ARG B 97 0.18 SIDE CHAIN
REMARK 500 4 ARG B 100 0.21 SIDE CHAIN
REMARK 500 4 ARG B 127 0.21 SIDE CHAIN
REMARK 500 4 ARG B 164 0.31 SIDE CHAIN
REMARK 500 5 ARG B 49 0.32 SIDE CHAIN
REMARK 500 5 ARG B 54 0.13 SIDE CHAIN
REMARK 500 5 ARG B 91 0.27 SIDE CHAIN
REMARK 500 5 ARG B 97 0.10 SIDE CHAIN
REMARK 500 5 ARG B 100 0.31 SIDE CHAIN
REMARK 500 5 ARG B 127 0.24 SIDE CHAIN
REMARK 500 5 ARG B 164 0.32 SIDE CHAIN
REMARK 500 6 ARG B 49 0.25 SIDE CHAIN
REMARK 500 6 ARG B 54 0.22 SIDE CHAIN
REMARK 500 6 ARG B 91 0.09 SIDE CHAIN
REMARK 500 6 ARG B 97 0.17 SIDE CHAIN
REMARK 500 6 ARG B 100 0.18 SIDE CHAIN
REMARK 500 6 ARG B 127 0.25 SIDE CHAIN
REMARK 500 6 ARG B 164 0.26 SIDE CHAIN
REMARK 500 7 ARG B 49 0.20 SIDE CHAIN
REMARK 500 7 ARG B 54 0.32 SIDE CHAIN
REMARK 500 7 ARG B 91 0.29 SIDE CHAIN
REMARK 500 7 ARG B 97 0.18 SIDE CHAIN
REMARK 500 7 ARG B 100 0.20 SIDE CHAIN
REMARK 500 7 ARG B 127 0.23 SIDE CHAIN
REMARK 500 7 ARG B 164 0.28 SIDE CHAIN
REMARK 500 8 ARG B 49 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 131 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FJ7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF NUCLEOLIN RBD1
REMARK 900 RELATED ID: 1FJC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF NUCLEOLIN RBD2
DBREF 1FJE B 1 175 UNP P08199 NUCL_MESAU 295 469
DBREF 1FJE A 1 22 PDB 1FJE 1FJE 1 22
SEQADV 1FJE GLY B 1 UNP P08199 LYS 295 CONFLICT
SEQADV 1FJE SER B 2 UNP P08199 LYS 296 CONFLICT
SEQADV 1FJE HIS B 3 UNP P08199 GLN 297 CONFLICT
SEQADV 1FJE MET B 4 UNP P08199 LYS 298 CONFLICT
SEQADV 1FJE LEU B 37 UNP P08199 PRO 331 CONFLICT
SEQRES 1 A 22 G G C C G A A A U C C C G
SEQRES 2 A 22 A A G U A G G C C
SEQRES 1 B 175 GLY SER HIS MET VAL GLU GLY SER GLU SER THR THR PRO
SEQRES 2 B 175 PHE ASN LEU PHE ILE GLY ASN LEU ASN PRO ASN LYS SER
SEQRES 3 B 175 VAL ALA GLU LEU LYS VAL ALA ILE SER GLU LEU PHE ALA
SEQRES 4 B 175 LYS ASN ASP LEU ALA VAL VAL ASP VAL ARG THR GLY THR
SEQRES 5 B 175 ASN ARG LYS PHE GLY TYR VAL ASP PHE GLU SER ALA GLU
SEQRES 6 B 175 ASP LEU GLU LYS ALA LEU GLU LEU THR GLY LEU LYS VAL
SEQRES 7 B 175 PHE GLY ASN GLU ILE LYS LEU GLU LYS PRO LYS GLY ARG
SEQRES 8 B 175 ASP SER LYS LYS VAL ARG ALA ALA ARG THR LEU LEU ALA
SEQRES 9 B 175 LYS ASN LEU SER PHE ASN ILE THR GLU ASP GLU LEU LYS
SEQRES 10 B 175 GLU VAL PHE GLU ASP ALA LEU GLU ILE ARG LEU VAL SER
SEQRES 11 B 175 GLN ASP GLY LYS SER LYS GLY ILE ALA TYR ILE GLU PHE
SEQRES 12 B 175 LYS SER GLU ALA ASP ALA GLU LYS ASN LEU GLU GLU LYS
SEQRES 13 B 175 GLN GLY ALA GLU ILE ASP GLY ARG SER VAL SER LEU TYR
SEQRES 14 B 175 TYR THR GLY GLU LYS GLY
HELIX 1 1 SER B 26 ASP B 42 1 17
HELIX 2 2 SER B 63 LEU B 73 1 11
HELIX 3 3 VAL B 96 ALA B 99 5 4
HELIX 4 4 THR B 112 PHE B 120 1 9
HELIX 5 5 SER B 145 GLN B 157 1 13
SHEET 1 A 5 ASP B 47 GLY B 51 0
SHEET 2 A 5 PHE B 56 PHE B 61 -1 O PHE B 56 N GLY B 51
SHEET 3 A 5 PHE B 14 GLY B 19 -1 O PHE B 14 N PHE B 61
SHEET 4 A 5 ASN B 81 GLU B 86 -1 N LYS B 84 O GLY B 19
SHEET 5 A 5 LEU B 76 VAL B 78 -1 O LEU B 76 N ILE B 83
SHEET 1 B 5 GLU B 125 VAL B 129 0
SHEET 2 B 5 ILE B 138 GLU B 142 -1 O ILE B 138 N VAL B 129
SHEET 3 B 5 THR B 101 LYS B 105 -1 N LEU B 102 O ILE B 141
SHEET 4 B 5 ARG B 164 TYR B 170 -1 O SER B 167 N LYS B 105
SHEET 5 B 5 GLY B 158 ILE B 161 -1 O GLY B 158 N VAL B 166
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 - b 23 2 Bytes