Header list of 2cph.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-MAY-05 2CPH TITLE SOLUTION STRUCTURE OF THE C-TERMINAL RNA RECOGNITION MOTIF OF TITLE 2 HYPOTHETICAL RNA-BINDING PROTEIN RBM19 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA BINDING MOTIF PROTEIN 19; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RBM19; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-04; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, RRM, RNP, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN KEYWDS 4 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CPH 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CPH 1 VERSN REVDAT 1 19-NOV-05 2CPH 0 JRNL AUTH T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL RNA RECOGNITION MOTIF JRNL TITL 2 OF HYPOTHETICAL RNA-BINDING PROTEIN RBM19 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CPH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024479. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.20MM 13C/15N-PROTEIN; 20MM D REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL; REMARK 210 1MM D-DTT; 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE : 20030801/20031121, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.925, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LOWEST ENERGY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLN A 454 178.69 -49.30 REMARK 500 1 LEU A 481 -38.49 -37.78 REMARK 500 1 THR A 498 95.08 -39.81 REMARK 500 1 ALA A 502 -74.97 -95.03 REMARK 500 1 ARG A 504 -178.66 -64.79 REMARK 500 1 SER A 527 106.88 -166.20 REMARK 500 1 SER A 548 -64.66 -101.41 REMARK 500 1 PRO A 550 -177.20 -69.81 REMARK 500 2 GLN A 454 140.27 -173.28 REMARK 500 2 ARG A 479 -70.41 -48.82 REMARK 500 2 THR A 490 136.57 -174.86 REMARK 500 2 MET A 497 -61.59 -103.69 REMARK 500 2 SER A 548 168.97 -44.38 REMARK 500 3 SER A 452 91.87 -50.61 REMARK 500 3 GLN A 454 150.87 -42.49 REMARK 500 3 LYS A 457 121.05 -34.82 REMARK 500 3 THR A 484 -36.25 -39.71 REMARK 500 3 THR A 490 140.67 -174.51 REMARK 500 3 ALA A 502 -55.45 -121.00 REMARK 500 3 LYS A 519 -70.34 -40.20 REMARK 500 3 SER A 527 109.83 -173.84 REMARK 500 4 PRO A 470 -166.09 -69.78 REMARK 500 4 THR A 498 74.94 -64.72 REMARK 500 4 CYS A 525 -32.52 -35.99 REMARK 500 4 SER A 527 109.40 -170.19 REMARK 500 4 ASP A 541 78.00 -106.18 REMARK 500 5 THR A 490 131.14 -173.03 REMARK 500 5 THR A 498 62.07 -112.27 REMARK 500 5 CYS A 525 -39.66 -38.23 REMARK 500 5 SER A 527 105.91 -170.83 REMARK 500 6 SER A 451 47.74 -83.61 REMARK 500 6 THR A 460 82.84 -67.74 REMARK 500 6 ALA A 473 124.07 -39.13 REMARK 500 6 THR A 498 40.94 34.41 REMARK 500 6 THR A 500 108.32 -45.88 REMARK 500 6 SER A 527 116.50 -167.68 REMARK 500 6 ALA A 540 154.21 -39.93 REMARK 500 7 SER A 448 114.51 -173.64 REMARK 500 7 SER A 483 -35.67 -37.25 REMARK 500 7 THR A 490 148.83 -174.00 REMARK 500 7 THR A 500 102.90 -54.60 REMARK 500 7 HIS A 503 170.84 -54.84 REMARK 500 7 VAL A 546 39.81 35.83 REMARK 500 7 SER A 548 -44.69 -132.05 REMARK 500 7 SER A 551 -61.43 -97.87 REMARK 500 8 SER A 451 -52.45 -127.69 REMARK 500 8 ASN A 468 32.36 70.39 REMARK 500 8 SER A 483 -34.10 -38.51 REMARK 500 8 THR A 498 94.79 -41.14 REMARK 500 8 SER A 527 105.91 -160.72 REMARK 500 REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007011210.11 RELATED DB: TARGETDB DBREF 2CPH A 454 547 UNP Q8R3C6 RBM19_MOUSE 816 909 SEQADV 2CPH GLY A 447 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 448 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 449 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH GLY A 450 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 451 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 452 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH GLY A 453 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 548 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH GLY A 549 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH PRO A 550 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 551 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH SER A 552 UNP Q8R3C6 CLONING ARTIFACT SEQADV 2CPH GLY A 553 UNP Q8R3C6 CLONING ARTIFACT SEQRES 1 A 107 GLY SER SER GLY SER SER GLY GLN VAL PRO LYS LYS GLN SEQRES 2 A 107 THR THR SER LYS ILE LEU VAL ARG ASN ILE PRO PHE GLN SEQRES 3 A 107 ALA ASN GLN ARG GLU ILE ARG GLU LEU PHE SER THR PHE SEQRES 4 A 107 GLY GLU LEU LYS THR VAL ARG LEU PRO LYS LYS MET THR SEQRES 5 A 107 GLY THR GLY ALA HIS ARG GLY PHE GLY PHE VAL ASP PHE SEQRES 6 A 107 ILE THR LYS GLN ASP ALA LYS LYS ALA PHE ASN ALA LEU SEQRES 7 A 107 CYS HIS SER THR HIS LEU TYR GLY ARG ARG LEU VAL LEU SEQRES 8 A 107 GLU TRP ALA ASP SER GLU VAL THR VAL GLN SER GLY PRO SEQRES 9 A 107 SER SER GLY HELIX 1 1 GLN A 475 PHE A 482 1 8 HELIX 2 2 LYS A 514 LEU A 524 1 11 SHEET 1 A 4 LEU A 488 ARG A 492 0 SHEET 2 A 4 PHE A 506 PHE A 511 -1 O PHE A 508 N ARG A 492 SHEET 3 A 4 ILE A 464 ARG A 467 -1 N ILE A 464 O VAL A 509 SHEET 4 A 4 VAL A 536 TRP A 539 -1 O VAL A 536 N ARG A 467 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