Header list of 2adb.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN/RNA 20-JUL-05 2ADB
TITLE SOLUTION STRUCTURE OF POLYPYRIMIDINE TRACT BINDING PROTEIN RBD2
TITLE 2 COMPLEXED WITH CUCUCU RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*CP*UP*CP*UP*CP*U)-3';
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: POLYPYRIMIDINE TRACT-BINDING PROTEIN 1;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: RBD2;
COMPND 9 SYNONYM: PTB, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN I, HNRNP I, 57
COMPND 10 KDA RNA-BINDING PROTEIN PPTB-1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 ORGANISM_TAXID: 9606;
SOURCE 8 GENE: PTB-1;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+RIL;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS RBD, RRM, PROTEIN-RNA COMPLEX, RNA BINDING PROTEIN-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.C.OBERSTRASS,S.D.AUWETER,M.ERAT,Y.HARGOUS,A.HENNING,P.WENTER,
AUTHOR 2 L.REYMOND,S.PITSCH,D.L.BLACK,F.H.T.ALLAIN
REVDAT 3 09-MAR-22 2ADB 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ADB 1 VERSN
REVDAT 1 04-OCT-05 2ADB 0
JRNL AUTH F.C.OBERSTRASS,S.D.AUWETER,M.ERAT,Y.HARGOUS,A.HENNING,
JRNL AUTH 2 P.WENTER,L.REYMOND,B.AMIR-AHMADY,S.PITSCH,D.L.BLACK,
JRNL AUTH 3 F.H.T.ALLAIN
JRNL TITL STRUCTURE OF PTB BOUND TO RNA: SPECIFIC BINDING AND
JRNL TITL 2 IMPLICATIONS FOR SPLICING REGULATION
JRNL REF SCIENCE V. 309 2054 2005
JRNL REFN ISSN 0036-8075
JRNL PMID 16179478
JRNL DOI 10.1126/SCIENCE.1114066
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ADB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033761.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : 30MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM PTB RBD2 15N, 13C; 1.5MM
REMARK 210 CUCUCU-RNA; 20MM PHOSPHATE
REMARK 210 BUFFER; 10MM NACL; 1.5MM PTB
REMARK 210 RBD2 15N; 1.5MM CUCUCU-RNA; 20MM
REMARK 210 PHOSPHATE BUFFER; 10MM NACL;
REMARK 210 1.5MM PTB RBD2 15N; 1.5MM CUCUCU-
REMARK 210 RNA; 20MM PHOSPHATE BUFFER; 10MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.0, DYANA 3.02
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 151
REMARK 465 GLY A 152
REMARK 465 SER A 153
REMARK 465 SER A 154
REMARK 465 HIS A 155
REMARK 465 HIS A 156
REMARK 465 HIS A 157
REMARK 465 HIS A 158
REMARK 465 HIS A 159
REMARK 465 HIS A 160
REMARK 465 SER A 161
REMARK 465 SER A 162
REMARK 465 GLY A 163
REMARK 465 LEU A 164
REMARK 465 VAL A 165
REMARK 465 PRO A 166
REMARK 465 ARG A 167
REMARK 465 GLY A 168
REMARK 465 SER A 169
REMARK 465 HIS A 170
REMARK 465 MET A 171
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 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 C B 301 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 U B 304 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 ARG A 273 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 C B 303 N3 - C2 - O2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 C B 299 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 4 U B 302 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 4 ARG A 185 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 5 U B 300 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 5 C B 301 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 5 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 C B 303 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 ARG A 185 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 6 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 U B 304 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 6 U B 304 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 6 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 U B 302 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 7 U B 302 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 7 C B 303 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 7 U B 304 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 8 U B 302 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 8 ARG A 273 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 C B 299 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 9 U B 302 C5' - C4' - O4' ANGL. DEV. = 6.3 DEGREES
REMARK 500 9 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 9 C B 303 C5' - C4' - O4' ANGL. DEV. = 6.3 DEGREES
REMARK 500 10 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 10 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 11 C B 299 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 11 C B 301 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 11 U B 302 C5' - C4' - O4' ANGL. DEV. = 5.8 DEGREES
REMARK 500 11 U B 302 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 11 U B 304 O4' - C1' - N1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 11 U B 304 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 11 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 C B 301 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 12 U B 302 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 12 U B 304 O4' - C1' - N1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 12 U B 304 N3 - C2 - O2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 13 C B 299 N3 - C2 - O2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 13 U B 302 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 82 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 ASN A 190 14.96 -66.19
REMARK 500 1 PHE A 192 -33.97 -141.36
REMARK 500 1 PRO A 194 79.46 -64.10
REMARK 500 1 VAL A 195 -40.59 -142.36
REMARK 500 1 THR A 196 -62.25 -17.48
REMARK 500 1 THR A 209 75.33 -111.80
REMARK 500 1 LEU A 211 -64.42 -121.66
REMARK 500 1 ASN A 219 -73.39 55.36
REMARK 500 1 LEU A 239 -71.78 -31.11
REMARK 500 1 ASN A 248 25.70 43.87
REMARK 500 1 SER A 262 86.41 -152.31
REMARK 500 1 LYS A 266 -67.47 -124.19
REMARK 500 1 TYR A 267 130.66 179.87
REMARK 500 1 ASN A 268 8.19 -61.90
REMARK 500 1 ASP A 270 -6.44 -146.77
REMARK 500 1 LYS A 271 -44.87 -131.83
REMARK 500 1 SER A 272 136.17 -170.97
REMARK 500 1 ASP A 279 -5.50 -166.04
REMARK 500 1 LEU A 280 163.26 12.93
REMARK 500 1 PRO A 287 174.36 -54.65
REMARK 500 1 GLN A 291 -22.68 -148.66
REMARK 500 1 THR A 292 -71.30 -98.62
REMARK 500 1 ALA A 296 -52.82 -141.04
REMARK 500 1 PHE A 297 -8.73 47.41
REMARK 500 2 ALA A 176 -62.07 61.58
REMARK 500 2 GLN A 180 0.18 80.94
REMARK 500 2 GLU A 189 -171.06 -68.37
REMARK 500 2 PHE A 192 -42.03 -132.32
REMARK 500 2 PRO A 194 71.88 -55.34
REMARK 500 2 VAL A 195 -34.44 -149.19
REMARK 500 2 LEU A 211 -56.33 -124.68
REMARK 500 2 LYS A 218 -153.21 -77.59
REMARK 500 2 ASN A 220 -16.93 -146.31
REMARK 500 2 LEU A 239 -75.96 -21.40
REMARK 500 2 ASN A 245 -161.49 -79.20
REMARK 500 2 TYR A 247 -82.82 -146.51
REMARK 500 2 ALA A 249 15.44 58.37
REMARK 500 2 LYS A 266 -68.58 -109.54
REMARK 500 2 TYR A 267 119.02 -166.96
REMARK 500 2 ASN A 268 1.14 -40.51
REMARK 500 2 ASP A 270 -17.87 -157.40
REMARK 500 2 ASP A 279 -37.33 164.26
REMARK 500 2 LEU A 280 121.83 106.28
REMARK 500 2 SER A 282 -6.37 71.96
REMARK 500 2 LEU A 289 4.44 -65.07
REMARK 500 2 GLN A 291 -45.99 -146.93
REMARK 500 2 THR A 292 -70.67 -78.15
REMARK 500 2 ALA A 294 -29.14 -39.28
REMARK 500 2 ALA A 296 -39.10 -142.15
REMARK 500 2 PHE A 297 -3.31 50.03
REMARK 500
REMARK 500 THIS ENTRY HAS 497 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 LEU A 184 ARG A 185 1 132.44
REMARK 500 VAL A 195 THR A 196 1 148.64
REMARK 500 LEU A 253 ARG A 254 1 146.22
REMARK 500 THR A 276 ARG A 277 1 145.81
REMARK 500 ASP A 279 LEU A 280 1 -101.24
REMARK 500 GLY A 179 GLN A 180 2 142.42
REMARK 500 LEU A 191 PHE A 192 2 -142.85
REMARK 500 LEU A 253 ARG A 254 2 141.00
REMARK 500 GLY A 179 GLN A 180 3 148.10
REMARK 500 PRO A 194 VAL A 195 3 -149.15
REMARK 500 GLY A 179 GLN A 180 4 144.75
REMARK 500 ASN A 190 LEU A 191 4 -149.94
REMARK 500 VAL A 195 THR A 196 4 147.61
REMARK 500 LEU A 253 ARG A 254 4 144.40
REMARK 500 LYS A 266 TYR A 267 4 148.91
REMARK 500 SER A 272 ARG A 273 4 134.40
REMARK 500 GLY A 179 GLN A 180 5 143.32
REMARK 500 VAL A 183 LEU A 184 5 -149.69
REMARK 500 VAL A 188 GLU A 189 5 145.44
REMARK 500 ASN A 190 LEU A 191 5 -143.60
REMARK 500 PRO A 194 VAL A 195 5 -130.69
REMARK 500 GLN A 223 ALA A 224 5 147.57
REMARK 500 LYS A 238 LEU A 239 5 145.36
REMARK 500 VAL A 265 LYS A 266 5 149.29
REMARK 500 GLY A 179 GLN A 180 6 145.29
REMARK 500 GLN A 180 SER A 181 6 149.73
REMARK 500 VAL A 195 THR A 196 6 128.64
REMARK 500 THR A 209 VAL A 210 6 -149.48
REMARK 500 GLN A 223 ALA A 224 6 144.76
REMARK 500 LEU A 253 ARG A 254 6 135.54
REMARK 500 ASP A 279 LEU A 280 6 -114.03
REMARK 500 LYS A 238 LEU A 239 7 149.61
REMARK 500 ASP A 279 LEU A 280 7 -98.10
REMARK 500 LEU A 253 ARG A 254 8 148.47
REMARK 500 LYS A 271 SER A 272 8 -144.41
REMARK 500 ASP A 279 LEU A 280 8 -105.89
REMARK 500 GLY A 179 GLN A 180 9 148.90
REMARK 500 LEU A 184 ARG A 185 9 139.29
REMARK 500 VAL A 195 THR A 196 9 146.46
REMARK 500 LEU A 253 ARG A 254 9 143.69
REMARK 500 ASP A 279 LEU A 280 9 -112.98
REMARK 500 VAL A 195 THR A 196 10 139.86
REMARK 500 ASP A 270 LYS A 271 10 -148.08
REMARK 500 GLY A 179 GLN A 180 11 141.23
REMARK 500 GLN A 180 SER A 181 11 142.06
REMARK 500 LEU A 184 ARG A 185 11 142.09
REMARK 500 VAL A 195 THR A 196 11 145.91
REMARK 500 LEU A 253 ARG A 254 11 149.39
REMARK 500 ASP A 279 LEU A 280 11 -108.51
REMARK 500 SER A 272 ARG A 273 12 143.77
REMARK 500
REMARK 500 THIS ENTRY HAS 94 NON CIS, NON-TRANS OMEGA 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 U B 300 0.17 SIDE CHAIN
REMARK 500 1 C B 301 0.15 SIDE CHAIN
REMARK 500 1 TYR A 228 0.10 SIDE CHAIN
REMARK 500 2 U B 300 0.14 SIDE CHAIN
REMARK 500 2 C B 303 0.06 SIDE CHAIN
REMARK 500 2 TYR A 228 0.07 SIDE CHAIN
REMARK 500 3 C B 299 0.06 SIDE CHAIN
REMARK 500 3 U B 300 0.17 SIDE CHAIN
REMARK 500 3 C B 301 0.08 SIDE CHAIN
REMARK 500 3 C B 303 0.09 SIDE CHAIN
REMARK 500 3 TYR A 228 0.09 SIDE CHAIN
REMARK 500 4 U B 300 0.08 SIDE CHAIN
REMARK 500 4 C B 303 0.07 SIDE CHAIN
REMARK 500 4 TYR A 228 0.08 SIDE CHAIN
REMARK 500 5 C B 301 0.07 SIDE CHAIN
REMARK 500 5 C B 303 0.06 SIDE CHAIN
REMARK 500 5 TYR A 228 0.07 SIDE CHAIN
REMARK 500 6 C B 301 0.12 SIDE CHAIN
REMARK 500 6 U B 304 0.08 SIDE CHAIN
REMARK 500 6 TYR A 228 0.07 SIDE CHAIN
REMARK 500 7 U B 300 0.15 SIDE CHAIN
REMARK 500 7 C B 303 0.07 SIDE CHAIN
REMARK 500 7 TYR A 228 0.10 SIDE CHAIN
REMARK 500 8 U B 300 0.17 SIDE CHAIN
REMARK 500 8 C B 301 0.11 SIDE CHAIN
REMARK 500 8 C B 303 0.11 SIDE CHAIN
REMARK 500 8 TYR A 228 0.09 SIDE CHAIN
REMARK 500 9 U B 300 0.17 SIDE CHAIN
REMARK 500 9 C B 301 0.10 SIDE CHAIN
REMARK 500 9 C B 303 0.06 SIDE CHAIN
REMARK 500 10 U B 300 0.24 SIDE CHAIN
REMARK 500 10 C B 301 0.06 SIDE CHAIN
REMARK 500 10 ARG A 185 0.08 SIDE CHAIN
REMARK 500 10 TYR A 228 0.08 SIDE CHAIN
REMARK 500 11 U B 300 0.20 SIDE CHAIN
REMARK 500 11 C B 301 0.09 SIDE CHAIN
REMARK 500 11 U B 304 0.07 SIDE CHAIN
REMARK 500 11 TYR A 228 0.10 SIDE CHAIN
REMARK 500 12 C B 301 0.10 SIDE CHAIN
REMARK 500 12 ARG A 185 0.08 SIDE CHAIN
REMARK 500 12 TYR A 228 0.09 SIDE CHAIN
REMARK 500 13 C B 301 0.07 SIDE CHAIN
REMARK 500 13 TYR A 228 0.09 SIDE CHAIN
REMARK 500 14 U B 300 0.21 SIDE CHAIN
REMARK 500 14 TYR A 228 0.10 SIDE CHAIN
REMARK 500 15 C B 301 0.06 SIDE CHAIN
REMARK 500 15 TYR A 228 0.07 SIDE CHAIN
REMARK 500 16 U B 300 0.17 SIDE CHAIN
REMARK 500 16 ARG A 185 0.08 SIDE CHAIN
REMARK 500 16 TYR A 228 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 63 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AD9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RBD1 COMPLEXED WITH CUCUCU RNA
REMARK 900 RELATED ID: 2ADC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RBD34 COMPLEXED WITH CUCUCU RNA
DBREF 2ADB A 172 298 UNP P26599 PTBP1_HUMAN 172 298
DBREF 2ADB B 299 304 PDB 2ADB 2ADB 299 304
SEQADV 2ADB MET A 151 UNP P26599 EXPRESSION TAG
SEQADV 2ADB GLY A 152 UNP P26599 EXPRESSION TAG
SEQADV 2ADB SER A 153 UNP P26599 EXPRESSION TAG
SEQADV 2ADB SER A 154 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 155 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 156 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 157 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 158 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 159 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 160 UNP P26599 EXPRESSION TAG
SEQADV 2ADB SER A 161 UNP P26599 EXPRESSION TAG
SEQADV 2ADB SER A 162 UNP P26599 EXPRESSION TAG
SEQADV 2ADB GLY A 163 UNP P26599 EXPRESSION TAG
SEQADV 2ADB LEU A 164 UNP P26599 EXPRESSION TAG
SEQADV 2ADB VAL A 165 UNP P26599 EXPRESSION TAG
SEQADV 2ADB PRO A 166 UNP P26599 EXPRESSION TAG
SEQADV 2ADB ARG A 167 UNP P26599 EXPRESSION TAG
SEQADV 2ADB GLY A 168 UNP P26599 EXPRESSION TAG
SEQADV 2ADB SER A 169 UNP P26599 EXPRESSION TAG
SEQADV 2ADB HIS A 170 UNP P26599 EXPRESSION TAG
SEQADV 2ADB MET A 171 UNP P26599 EXPRESSION TAG
SEQRES 1 B 6 C U C U C U
SEQRES 1 A 148 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 148 LEU VAL PRO ARG GLY SER HIS MET ASP ALA GLY MET ALA
SEQRES 3 A 148 MET ALA GLY GLN SER PRO VAL LEU ARG ILE ILE VAL GLU
SEQRES 4 A 148 ASN LEU PHE TYR PRO VAL THR LEU ASP VAL LEU HIS GLN
SEQRES 5 A 148 ILE PHE SER LYS PHE GLY THR VAL LEU LYS ILE ILE THR
SEQRES 6 A 148 PHE THR LYS ASN ASN GLN PHE GLN ALA LEU LEU GLN TYR
SEQRES 7 A 148 ALA ASP PRO VAL SER ALA GLN HIS ALA LYS LEU SER LEU
SEQRES 8 A 148 ASP GLY GLN ASN ILE TYR ASN ALA CYS CYS THR LEU ARG
SEQRES 9 A 148 ILE ASP PHE SER LYS LEU THR SER LEU ASN VAL LYS TYR
SEQRES 10 A 148 ASN ASN ASP LYS SER ARG ASP TYR THR ARG PRO ASP LEU
SEQRES 11 A 148 PRO SER GLY ASP SER GLN PRO SER LEU ASP GLN THR MET
SEQRES 12 A 148 ALA ALA ALA PHE GLY
HELIX 1 1 VAL A 195 SER A 205 1 11
HELIX 2 2 ASP A 230 GLY A 243 1 14
SHEET 1 A 5 ARG A 254 PHE A 257 0
SHEET 2 A 5 VAL A 183 ILE A 187 -1 N ARG A 185 O ASP A 256
SHEET 3 A 5 GLN A 221 TYR A 228 -1 O LEU A 226 N LEU A 184
SHEET 4 A 5 VAL A 210 LYS A 218 -1 N LEU A 211 O GLN A 227
SHEET 5 A 5 SER A 272 ASP A 274 -1 O ARG A 273 N ILE A 213
CISPEP 1 ALA A 295 ALA A 296 12 10.33
CISPEP 2 MET A 175 ALA A 176 15 -0.33
CISPEP 3 SER A 258 LYS A 259 18 -0.49
CISPEP 4 THR A 252 LEU A 253 19 -22.66
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