HEADER RNA BINDING PROTEIN/RNA 23-JUN-10 3NNA
TITLE CRYSTAL STRUCTURE OF CUGBP1 RRM1/2-RNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUGBP ELAV-LIKE FAMILY MEMBER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM1-RRM2 DOMAIN (UNP RESIDUES 14-187);
COMPND 5 SYNONYM: CELF-1, CUG-BP- AND ETR-3-LIKE FACTOR 1, BRUNO-LIKE PROTEIN
COMPND 6 2, RNA-BINDING PROTEIN BRUNOL-2, CUG TRIPLET REPEAT RNA-BINDING
COMPND 7 PROTEIN 1, CUG-BP1, DEADENYLATION FACTOR CUG-BP, 50 KDA NUCLEAR
COMPND 8 POLYADENYLATED RNA-BINDING PROTEIN, EMBRYO DEADENYLATION ELEMENT-
COMPND 9 BINDING PROTEIN HOMOLOG, EDEN-BP HOMOLOG;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: RNA (5'-R(*GP*UP*UP*GP*UP*UP*UP*UP*GP*UP*UP*U)-3');
COMPND 13 CHAIN: B;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRUNOL2, CELF1, CUGBP, CUGBP1, NAB50;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
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: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS RRM, RNA BINDING, RNA, RNA BINDING PROTEIN-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TEPLOVA,J.SONG,H.GAW,A.TEPLOV,D.J.PATEL
REVDAT 3 27-DEC-23 3NNA 1 DBREF SEQADV LINK
REVDAT 2 08-OCT-14 3NNA 1 AUTHOR VERSN
REVDAT 1 27-OCT-10 3NNA 0
JRNL AUTH M.TEPLOVA,J.SONG,H.Y.GAW,A.TEPLOV,D.J.PATEL
JRNL TITL STRUCTURAL INSIGHTS INTO RNA RECOGNITION BY THE
JRNL TITL 2 ALTERNATE-SPLICING REGULATOR CUG-BINDING PROTEIN 1.
JRNL REF STRUCTURE V. 18 1364 2010
JRNL REFN ISSN 0969-2126
JRNL PMID 20947024
JRNL DOI 10.1016/J.STR.2010.06.018
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16774
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 897
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1174
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1375
REMARK 3 NUCLEIC ACID ATOMS : 103
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.85000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 1.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.314
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.225
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1515 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1313 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2058 ; 1.268 ; 2.041
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3077 ; 0.666 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ;10.911 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;37.291 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 259 ;15.542 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;20.777 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 228 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1601 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 299 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 872 ; 0.922 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 354 ; 0.307 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1405 ; 1.615 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 643 ; 2.509 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 653 ; 3.824 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2828 ; 1.205 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 98 ; 5.218 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2792 ; 1.887 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3NNA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000060040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920, 0.97880, 0.96360
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33331
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.899
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 45% MPD, 0.1 M
REMARK 280 TRIS PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.68350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.03050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.85300
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.68350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.03050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.85300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.68350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.03050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.85300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.68350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.03050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.85300
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 12 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 G B 0
REMARK 465 U B 6
REMARK 465 U B 7
REMARK 465 G B 8
REMARK 465 U B 9
REMARK 465 U B 10
REMARK 465 U B 11
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 GLU A 44 140.27 -177.03
REMARK 500 ASN A 102 -81.61 -111.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NMR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH GUUGUUUUGUUU.
REMARK 900 RELATED ID: 3NNC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1-RRM2 DOMAIN COMPLEXED WITH UGUGUGUUGUGUG.
REMARK 900 RELATED ID: 3NNH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RRM1 DOMAIN COMPLEXED WITH GUUGUUUUGUUU.
DBREF 3NNA A 14 187 UNP Q92879 CELF1_HUMAN 14 187
DBREF 3NNA B 0 11 PDB 3NNA 3NNA 0 11
SEQADV 3NNA SER A 13 UNP Q92879 EXPRESSION TAG
SEQRES 1 A 175 SER ASP ALA ILE LYS MSE PHE VAL GLY GLN VAL PRO ARG
SEQRES 2 A 175 THR TRP SER GLU LYS ASP LEU ARG GLU LEU PHE GLU GLN
SEQRES 3 A 175 TYR GLY ALA VAL TYR GLU ILE ASN VAL LEU ARG ASP ARG
SEQRES 4 A 175 SER GLN ASN PRO PRO GLN SER LYS GLY CYS CYS PHE VAL
SEQRES 5 A 175 THR PHE TYR THR ARG LYS ALA ALA LEU GLU ALA GLN ASN
SEQRES 6 A 175 ALA LEU HIS ASN MSE LYS VAL LEU PRO GLY MSE HIS HIS
SEQRES 7 A 175 PRO ILE GLN MSE LYS PRO ALA ASP SER GLU LYS ASN ASN
SEQRES 8 A 175 ALA VAL GLU ASP ARG LYS LEU PHE ILE GLY MSE ILE SER
SEQRES 9 A 175 LYS LYS CYS THR GLU ASN ASP ILE ARG VAL MSE PHE SER
SEQRES 10 A 175 SER PHE GLY GLN ILE GLU GLU CYS ARG ILE LEU ARG GLY
SEQRES 11 A 175 PRO ASP GLY LEU SER ARG GLY CYS ALA PHE VAL THR PHE
SEQRES 12 A 175 THR THR ARG ALA MSE ALA GLN THR ALA ILE LYS ALA MSE
SEQRES 13 A 175 HIS GLN ALA GLN THR MSE GLU GLY CYS SER SER PRO MSE
SEQRES 14 A 175 VAL VAL LYS PHE ALA ASP
SEQRES 1 B 12 G U U G U U U U G U U U
MODRES 3NNA MSE A 18 MET SELENOMETHIONINE
MODRES 3NNA MSE A 82 MET SELENOMETHIONINE
MODRES 3NNA MSE A 88 MET SELENOMETHIONINE
MODRES 3NNA MSE A 94 MET SELENOMETHIONINE
MODRES 3NNA MSE A 114 MET SELENOMETHIONINE
MODRES 3NNA MSE A 127 MET SELENOMETHIONINE
MODRES 3NNA MSE A 160 MET SELENOMETHIONINE
MODRES 3NNA MSE A 168 MET SELENOMETHIONINE
MODRES 3NNA MSE A 174 MET SELENOMETHIONINE
MODRES 3NNA MSE A 181 MET SELENOMETHIONINE
HET MSE A 18 8
HET MSE A 82 8
HET MSE A 88 8
HET MSE A 94 8
HET MSE A 114 8
HET MSE A 127 8
HET MSE A 160 8
HET MSE A 168 8
HET MSE A 174 8
HET MSE A 181 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 3 HOH *91(H2 O)
HELIX 1 1 SER A 28 GLU A 37 1 10
HELIX 2 2 THR A 68 HIS A 80 1 13
HELIX 3 3 ASP A 98 LYS A 101 5 4
HELIX 4 4 ALA A 104 ASP A 107 5 4
HELIX 5 5 THR A 120 SER A 129 1 10
HELIX 6 6 SER A 130 GLY A 132 5 3
HELIX 7 7 THR A 157 HIS A 169 1 13
SHEET 1 A 4 VAL A 42 ASP A 50 0
SHEET 2 A 4 GLN A 57 PHE A 66 -1 O THR A 65 N TYR A 43
SHEET 3 A 4 ILE A 16 GLY A 21 -1 N MSE A 18 O VAL A 64
SHEET 4 A 4 GLN A 93 PRO A 96 -1 O LYS A 95 N PHE A 19
SHEET 1 B 4 ILE A 134 ARG A 141 0
SHEET 2 B 4 SER A 147 PHE A 155 -1 O THR A 154 N GLU A 136
SHEET 3 B 4 LYS A 109 GLY A 113 -1 N LEU A 110 O VAL A 153
SHEET 4 B 4 VAL A 182 PHE A 185 -1 O LYS A 184 N PHE A 111
LINK C LYS A 17 N MSE A 18 1555 1555 1.33
LINK C MSE A 18 N PHE A 19 1555 1555 1.33
LINK C ASN A 81 N MSE A 82 1555 1555 1.33
LINK C MSE A 82 N LYS A 83 1555 1555 1.33
LINK C GLY A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N HIS A 89 1555 1555 1.33
LINK C GLN A 93 N MSE A 94 1555 1555 1.32
LINK C MSE A 94 N LYS A 95 1555 1555 1.33
LINK C GLY A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N ILE A 115 1555 1555 1.33
LINK C VAL A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N PHE A 128 1555 1555 1.33
LINK C ALA A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N ALA A 161 1555 1555 1.33
LINK C ALA A 167 N MSE A 168 1555 1555 1.33
LINK C MSE A 168 N HIS A 169 1555 1555 1.33
LINK C THR A 173 N MSE A 174 1555 1555 1.32
LINK C MSE A 174 N GLU A 175 1555 1555 1.33
LINK C PRO A 180 N MSE A 181 1555 1555 1.33
LINK C MSE A 181 N VAL A 182 1555 1555 1.33
CISPEP 1 ASN A 54 PRO A 55 0 -0.35
CRYST1 47.367 70.061 131.706 90.00 90.00 90.00 I 2 2 2 8
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 0.021112 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014273 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007593 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
