Header list of 2adc.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN/RNA 20-JUL-05 2ADC
TITLE SOLUTION STRUCTURE OF POLYPYRIMIDINE TRACT BINDING PROTEIN RBD34
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, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: POLYPYRIMIDINE TRACT-BINDING PROTEIN 1;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: RBD34;
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 BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
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 2ADC 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ADC 1 VERSN
REVDAT 1 04-OCT-05 2ADC 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 2ADC 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_1000033762.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 30MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM PTB RBD34 15N, 13C; 3MM
REMARK 210 CUCUCU-RNA; 20MM PHOSPHATE
REMARK 210 BUFFER; 10MM NACL; 1.5MM PTB
REMARK 210 RBD34 15N; 3MM CUCUCU-RNA; 20MM
REMARK 210 PHOSPHATE BUFFER; 10MM NACL;
REMARK 210 1.5MM PTB RBD34 15N; 3MM 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 303
REMARK 465 GLY A 304
REMARK 465 SER A 305
REMARK 465 SER A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 SER A 313
REMARK 465 SER A 314
REMARK 465 GLY A 315
REMARK 465 LEU A 316
REMARK 465 VAL A 317
REMARK 465 PRO A 318
REMARK 465 ARG A 319
REMARK 465 GLY A 320
REMARK 465 SER A 321
REMARK 465 HIS A 322
REMARK 465 MET A 323
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 532 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 U B 533 O4' - C1' - N1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 U B 533 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 C B 534 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 C B 536 C3' - C2' - C1' ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 C C 538 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 C C 540 C3' - C2' - C1' ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 C C 540 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 C C 542 N3 - C2 - O2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 1 PHE A 487 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 C B 532 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 U B 533 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 C B 534 O4' - C1' - N1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 C B 534 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 C B 536 C3' - C2' - C1' ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 C C 538 O4' - C1' - N1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 2 C C 538 N1 - C2 - O2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 C C 538 N3 - C2 - O2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 C C 540 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 C C 540 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 U C 541 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 C C 542 N3 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 2 ARG A 491 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 C B 532 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 C B 532 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 C B 532 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 3 C B 534 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 C B 536 C3' - C2' - C1' ANGL. DEV. = 5.6 DEGREES
REMARK 500 3 C C 538 O4' - C1' - N1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 3 C C 538 N1 - C2 - O2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 C C 538 N3 - C2 - O2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 C C 540 N3 - C2 - O2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 C C 542 N3 - C2 - O2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 4 C B 532 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 4 C B 536 C3' - C2' - C1' ANGL. DEV. = 5.9 DEGREES
REMARK 500 4 C C 538 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 4 C C 538 N1 - C2 - O2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 C C 538 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 4 C C 540 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 C C 542 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 ARG A 366 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 C B 532 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 C B 534 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 5 C B 536 C3' - C2' - C1' ANGL. DEV. = 4.9 DEGREES
REMARK 500 5 C C 540 C5' - C4' - O4' ANGL. DEV. = 5.6 DEGREES
REMARK 500 5 U C 541 O4' - C1' - N1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 C C 542 N3 - C2 - O2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 ARG A 405 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 6 C B 532 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 6 C B 532 N1 - C2 - O2 ANGL. DEV. = 4.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 177 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 A 337 -17.85 59.28
REMARK 500 1 ASN A 343 -4.18 64.08
REMARK 500 1 LEU A 357 -72.53 -60.69
REMARK 500 1 ASP A 363 91.35 71.53
REMARK 500 1 HIS A 400 -11.19 56.32
REMARK 500 1 LEU A 408 6.94 -67.72
REMARK 500 1 SER A 409 -171.75 61.87
REMARK 500 1 GLN A 412 -40.33 -148.59
REMARK 500 1 LEU A 416 103.97 57.25
REMARK 500 1 PRO A 417 -70.42 -43.12
REMARK 500 1 GLU A 422 -29.97 65.87
REMARK 500 1 LEU A 435 -7.00 -151.55
REMARK 500 1 LYS A 439 -168.20 -126.63
REMARK 500 1 VAL A 481 99.86 -68.12
REMARK 500 1 PHE A 484 115.93 174.11
REMARK 500 1 HIS A 514 105.32 -58.37
REMARK 500 1 LYS A 528 -51.89 -19.54
REMARK 500 2 ILE A 326 -36.89 -150.57
REMARK 500 2 PRO A 351 -39.61 -39.17
REMARK 500 2 ASP A 363 161.16 75.71
REMARK 500 2 PHE A 371 120.16 -14.46
REMARK 500 2 ASN A 372 -85.26 23.72
REMARK 500 2 PRO A 403 108.49 -52.87
REMARK 500 2 LEU A 426 -66.73 45.09
REMARK 500 2 HIS A 436 94.55 -53.35
REMARK 500 2 ASN A 445 59.73 -104.96
REMARK 500 2 PHE A 446 96.85 -61.95
REMARK 500 2 VAL A 480 46.32 -92.04
REMARK 500 2 PHE A 484 121.36 -178.20
REMARK 500 2 LYS A 489 -166.73 -69.00
REMARK 500 2 ASP A 490 174.85 -59.21
REMARK 500 2 ARG A 491 -112.33 55.89
REMARK 500 2 LYS A 492 45.38 -157.77
REMARK 500 2 ASN A 519 -6.88 -141.65
REMARK 500 2 LYS A 528 -0.62 -58.18
REMARK 500 2 SER A 529 -157.80 -138.16
REMARK 500 3 ALA A 327 -153.83 -136.55
REMARK 500 3 ALA A 332 -114.22 -147.49
REMARK 500 3 ASN A 336 3.70 -64.89
REMARK 500 3 ASN A 343 19.27 57.68
REMARK 500 3 ASP A 363 163.86 87.40
REMARK 500 3 LYS A 373 20.43 -66.22
REMARK 500 3 ASN A 395 108.98 -58.69
REMARK 500 3 LEU A 399 -75.87 -40.88
REMARK 500 3 HIS A 436 102.22 -54.32
REMARK 500 3 PHE A 484 152.43 166.55
REMARK 500 3 ASP A 490 74.05 -150.89
REMARK 500 3 LYS A 492 10.65 -145.66
REMARK 500 3 ASN A 513 37.64 70.91
REMARK 500 3 HIS A 514 91.03 -66.54
REMARK 500
REMARK 500 THIS ENTRY HAS 398 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 LYS A 492 MET A 493 1 -148.56
REMARK 500 SER A 527 LYS A 528 1 138.43
REMARK 500 GLY A 478 GLY A 479 2 143.59
REMARK 500 SER A 527 LYS A 528 3 145.45
REMARK 500 LYS A 492 MET A 493 5 -146.84
REMARK 500 HIS A 520 HIS A 521 5 148.90
REMARK 500 SER A 527 LYS A 528 6 135.71
REMARK 500 LYS A 492 MET A 493 7 -146.50
REMARK 500 LYS A 485 PHE A 486 8 148.58
REMARK 500 LYS A 489 ASP A 490 9 144.01
REMARK 500 LYS A 492 MET A 493 9 -147.71
REMARK 500 SER A 527 LYS A 528 9 142.67
REMARK 500 ILE A 369 LEU A 370 10 -145.35
REMARK 500 LYS A 492 MET A 493 10 -149.53
REMARK 500 LYS A 492 MET A 493 11 -143.75
REMARK 500 HIS A 521 LEU A 522 11 -135.53
REMARK 500 SER A 527 LYS A 528 11 132.94
REMARK 500 LYS A 492 MET A 493 12 -148.52
REMARK 500 ALA A 494 LEU A 495 12 149.27
REMARK 500 SER A 527 LYS A 528 12 138.46
REMARK 500 ILE A 449 PHE A 450 13 145.06
REMARK 500 GLN A 415 LEU A 416 14 -148.47
REMARK 500 ILE A 449 PHE A 450 14 -146.09
REMARK 500 LYS A 492 MET A 493 14 -143.94
REMARK 500 LEU A 399 HIS A 400 15 141.02
REMARK 500 GLY A 478 GLY A 479 15 146.50
REMARK 500 ALA A 494 LEU A 495 15 146.83
REMARK 500 SER A 527 LYS A 528 15 140.32
REMARK 500 GLY A 483 PHE A 484 16 -33.12
REMARK 500 SER A 527 LYS A 528 16 135.74
REMARK 500 LYS A 428 ASP A 429 17 143.10
REMARK 500 PRO A 434 LEU A 435 17 -148.33
REMARK 500 ILE A 449 PHE A 450 17 -137.30
REMARK 500 LEU A 522 ARG A 523 17 138.42
REMARK 500 SER A 525 PHE A 526 17 147.32
REMARK 500 LEU A 370 PHE A 371 18 -142.80
REMARK 500 SER A 527 LYS A 528 18 134.70
REMARK 500 GLY A 478 GLY A 479 19 147.15
REMARK 500 LYS A 492 MET A 493 20 -144.13
REMARK 500 SER A 527 LYS A 528 20 139.89
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 C B 536 0.07 SIDE CHAIN
REMARK 500 1 U B 537 0.08 SIDE CHAIN
REMARK 500 1 C C 540 0.14 SIDE CHAIN
REMARK 500 1 C C 542 0.06 SIDE CHAIN
REMARK 500 1 PHE A 450 0.12 SIDE CHAIN
REMARK 500 1 ARG A 523 0.09 SIDE CHAIN
REMARK 500 2 C B 534 0.07 SIDE CHAIN
REMARK 500 2 C B 536 0.10 SIDE CHAIN
REMARK 500 2 U C 539 0.07 SIDE CHAIN
REMARK 500 2 C C 540 0.14 SIDE CHAIN
REMARK 500 2 TYR A 361 0.07 SIDE CHAIN
REMARK 500 3 C B 536 0.08 SIDE CHAIN
REMARK 500 3 C C 540 0.14 SIDE CHAIN
REMARK 500 3 PHE A 450 0.09 SIDE CHAIN
REMARK 500 4 U B 537 0.08 SIDE CHAIN
REMARK 500 4 U C 539 0.07 SIDE CHAIN
REMARK 500 4 C C 540 0.12 SIDE CHAIN
REMARK 500 4 PHE A 450 0.08 SIDE CHAIN
REMARK 500 5 C C 540 0.14 SIDE CHAIN
REMARK 500 6 C B 534 0.10 SIDE CHAIN
REMARK 500 6 U B 537 0.07 SIDE CHAIN
REMARK 500 6 C C 540 0.15 SIDE CHAIN
REMARK 500 7 U B 533 0.09 SIDE CHAIN
REMARK 500 7 C C 540 0.15 SIDE CHAIN
REMARK 500 7 C C 542 0.07 SIDE CHAIN
REMARK 500 7 PHE A 450 0.08 SIDE CHAIN
REMARK 500 8 U B 533 0.06 SIDE CHAIN
REMARK 500 8 C B 534 0.12 SIDE CHAIN
REMARK 500 8 C C 540 0.11 SIDE CHAIN
REMARK 500 8 U C 541 0.10 SIDE CHAIN
REMARK 500 9 U B 533 0.09 SIDE CHAIN
REMARK 500 9 C B 534 0.08 SIDE CHAIN
REMARK 500 9 U B 535 0.09 SIDE CHAIN
REMARK 500 9 U B 537 0.10 SIDE CHAIN
REMARK 500 9 C C 540 0.14 SIDE CHAIN
REMARK 500 9 U C 541 0.09 SIDE CHAIN
REMARK 500 9 PHE A 450 0.08 SIDE CHAIN
REMARK 500 10 C C 540 0.13 SIDE CHAIN
REMARK 500 10 PHE A 450 0.08 SIDE CHAIN
REMARK 500 11 C B 536 0.07 SIDE CHAIN
REMARK 500 11 U B 537 0.11 SIDE CHAIN
REMARK 500 11 C C 540 0.14 SIDE CHAIN
REMARK 500 11 ARG A 437 0.09 SIDE CHAIN
REMARK 500 11 PHE A 450 0.08 SIDE CHAIN
REMARK 500 12 C C 540 0.14 SIDE CHAIN
REMARK 500 12 PHE A 450 0.10 SIDE CHAIN
REMARK 500 13 C B 536 0.12 SIDE CHAIN
REMARK 500 13 U B 537 0.06 SIDE CHAIN
REMARK 500 13 C C 540 0.15 SIDE CHAIN
REMARK 500 14 U B 535 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 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: 2ADB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN RBD2 COMPLEXED WITH CUCUCU RNA
DBREF 2ADC A 324 531 UNP P26599 PTBP1_HUMAN 324 531
DBREF 2ADC B 532 537 PDB 2ADC 2ADC 532 537
DBREF 2ADC C 538 543 PDB 2ADC 2ADC 538 543
SEQADV 2ADC MET A 303 UNP P26599 EXPRESSION TAG
SEQADV 2ADC GLY A 304 UNP P26599 EXPRESSION TAG
SEQADV 2ADC SER A 305 UNP P26599 EXPRESSION TAG
SEQADV 2ADC SER A 306 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 307 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 308 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 309 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 310 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 311 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 312 UNP P26599 EXPRESSION TAG
SEQADV 2ADC SER A 313 UNP P26599 EXPRESSION TAG
SEQADV 2ADC SER A 314 UNP P26599 EXPRESSION TAG
SEQADV 2ADC GLY A 315 UNP P26599 EXPRESSION TAG
SEQADV 2ADC LEU A 316 UNP P26599 EXPRESSION TAG
SEQADV 2ADC VAL A 317 UNP P26599 EXPRESSION TAG
SEQADV 2ADC PRO A 318 UNP P26599 EXPRESSION TAG
SEQADV 2ADC ARG A 319 UNP P26599 EXPRESSION TAG
SEQADV 2ADC GLY A 320 UNP P26599 EXPRESSION TAG
SEQADV 2ADC SER A 321 UNP P26599 EXPRESSION TAG
SEQADV 2ADC HIS A 322 UNP P26599 EXPRESSION TAG
SEQADV 2ADC MET A 323 UNP P26599 EXPRESSION TAG
SEQRES 1 B 6 C U C U C U
SEQRES 1 C 6 C U C U C U
SEQRES 1 A 229 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 229 LEU VAL PRO ARG GLY SER HIS MET GLY ARG ILE ALA ILE
SEQRES 3 A 229 PRO GLY LEU ALA GLY ALA GLY ASN SER VAL LEU LEU VAL
SEQRES 4 A 229 SER ASN LEU ASN PRO GLU ARG VAL THR PRO GLN SER LEU
SEQRES 5 A 229 PHE ILE LEU PHE GLY VAL TYR GLY ASP VAL GLN ARG VAL
SEQRES 6 A 229 LYS ILE LEU PHE ASN LYS LYS GLU ASN ALA LEU VAL GLN
SEQRES 7 A 229 MET ALA ASP GLY ASN GLN ALA GLN LEU ALA MET SER HIS
SEQRES 8 A 229 LEU ASN GLY HIS LYS LEU HIS GLY LYS PRO ILE ARG ILE
SEQRES 9 A 229 THR LEU SER LYS HIS GLN ASN VAL GLN LEU PRO ARG GLU
SEQRES 10 A 229 GLY GLN GLU ASP GLN GLY LEU THR LYS ASP TYR GLY ASN
SEQRES 11 A 229 SER PRO LEU HIS ARG PHE LYS LYS PRO GLY SER LYS ASN
SEQRES 12 A 229 PHE GLN ASN ILE PHE PRO PRO SER ALA THR LEU HIS LEU
SEQRES 13 A 229 SER ASN ILE PRO PRO SER VAL SER GLU GLU ASP LEU LYS
SEQRES 14 A 229 VAL LEU PHE SER SER ASN GLY GLY VAL VAL LYS GLY PHE
SEQRES 15 A 229 LYS PHE PHE GLN LYS ASP ARG LYS MET ALA LEU ILE GLN
SEQRES 16 A 229 MET GLY SER VAL GLU GLU ALA VAL GLN ALA LEU ILE ASP
SEQRES 17 A 229 LEU HIS ASN HIS ASP LEU GLY GLU ASN HIS HIS LEU ARG
SEQRES 18 A 229 VAL SER PHE SER LYS SER THR ILE
HELIX 1 1 ILE A 328 GLY A 333 5 6
HELIX 2 2 THR A 350 GLY A 362 1 13
HELIX 3 3 ASP A 383 ASN A 395 1 13
HELIX 4 4 SER A 443 GLN A 447 5 5
HELIX 5 5 SER A 466 SER A 476 1 11
HELIX 6 6 SER A 500 HIS A 512 1 13
SHEET 1 A 5 ARG A 405 THR A 407 0
SHEET 2 A 5 VAL A 338 SER A 342 -1 N SER A 342 O ARG A 405
SHEET 3 A 5 ALA A 377 MET A 381 -1 O VAL A 379 N LEU A 339
SHEET 4 A 5 VAL A 364 ILE A 369 -1 N GLN A 365 O GLN A 380
SHEET 5 A 5 THR A 427 ASP A 429 -1 O LYS A 428 N VAL A 367
SHEET 1 B 4 VAL A 481 PHE A 486 0
SHEET 2 B 4 ALA A 494 MET A 498 -1 O LEU A 495 N LYS A 485
SHEET 3 B 4 THR A 455 SER A 459 -1 N LEU A 456 O ILE A 496
SHEET 4 B 4 ARG A 523 PHE A 526 -1 O SER A 525 N HIS A 457
CISPEP 1 GLY A 478 GLY A 479 1 8.11
CISPEP 2 ARG A 325 ILE A 326 3 -5.51
CISPEP 3 GLY A 478 GLY A 479 3 13.37
CISPEP 4 GLY A 333 ALA A 334 4 1.89
CISPEP 5 GLY A 335 ASN A 336 4 -1.98
CISPEP 6 GLY A 479 VAL A 480 4 -6.77
CISPEP 7 ASP A 490 ARG A 491 5 -9.12
CISPEP 8 GLY A 517 GLU A 518 5 -9.46
CISPEP 9 GLN A 424 GLY A 425 6 -3.61
CISPEP 10 GLY A 335 ASN A 336 7 0.31
CISPEP 11 ASN A 372 LYS A 373 7 1.12
CISPEP 12 GLY A 478 GLY A 479 7 12.67
CISPEP 13 ARG A 491 LYS A 492 7 -10.86
CISPEP 14 GLY A 479 VAL A 480 8 -11.55
CISPEP 15 GLY A 479 VAL A 480 9 -9.55
CISPEP 16 ARG A 491 LYS A 492 10 -11.81
CISPEP 17 ALA A 334 GLY A 335 11 -5.85
CISPEP 18 GLU A 419 GLY A 420 11 -1.22
CISPEP 19 SER A 443 LYS A 444 11 -4.15
CISPEP 20 GLY A 478 GLY A 479 11 10.30
CISPEP 21 ARG A 491 LYS A 492 11 -20.36
CISPEP 22 GLY A 478 GLY A 479 12 7.92
CISPEP 23 ALA A 334 GLY A 335 13 -3.74
CISPEP 24 ASN A 336 SER A 337 13 -3.86
CISPEP 25 GLY A 478 GLY A 479 13 12.01
CISPEP 26 GLY A 478 GLY A 479 14 12.84
CISPEP 27 ARG A 491 LYS A 492 14 5.65
CISPEP 28 GLY A 483 PHE A 484 15 -14.88
CISPEP 29 LYS A 440 PRO A 441 16 -10.01
CISPEP 30 GLY A 479 VAL A 480 16 -5.57
CISPEP 31 ASN A 372 LYS A 373 17 -2.00
CISPEP 32 GLY A 431 ASN A 432 17 4.57
CISPEP 33 GLY A 478 GLY A 479 18 8.37
CISPEP 34 ASP A 490 ARG A 491 18 7.37
CISPEP 35 GLY A 431 ASN A 432 19 1.48
CISPEP 36 ILE A 328 PRO A 329 20 -12.47
CISPEP 37 GLY A 478 GLY A 479 20 11.00
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