Header list of 1wel.pdb file
Complete list - c 21 2 Bytes
HEADER RNA BINDING PROTEIN 25-MAY-04 1WEL TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN NP_006038 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA-BINDING PROTEIN 12; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA BINDING DOMAIN; COMPND 5 SYNONYM: RNA BINDING MOTIF PROTEIN 12, SH3/WW DOMAIN ANCHOR PROTEIN COMPND 6 IN THE NUCLEUS, SWAN, HRIHFB2091; COMPND 7 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: RIKEN CDNA HK04803S1; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040126-04; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA BINDING PROTEIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.SOMEYA,Y.MUTO,T.NAGATA,S.SUZUKI,M.INOUE,T.KIGAWA,T.TERADA, AUTHOR 2 M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 3 INITIATIVE (RSGI) REVDAT 4 21-DEC-22 1WEL 1 SEQADV REVDAT 3 02-MAR-22 1WEL 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WEL 1 VERSN REVDAT 1 23-AUG-05 1WEL 0 JRNL AUTH T.SOMEYA,Y.MUTO,T.NAGATA,S.SUZUKI,M.INOUE,T.KIGAWA,T.TERADA, JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN NP_006038 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.1, CYANA 2.0 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), GUENTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WEL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1000023493. 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 : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.08MM PROTEIN U-15N,13C; 20MM REMARK 210 TRIS-HCL; 100MM NACL; 1MM DTT; REMARK 210 0.02% NAN3; 90% H2O; 10% D2O 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 : NMRVIEW 5.0.4, KUJIRA 0.8992, REMARK 210 CYANA 2.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, 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 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: 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 417 39.11 37.04 REMARK 500 1 ALA A 428 141.00 -174.40 REMARK 500 1 LEU A 437 152.38 -42.80 REMARK 500 1 ALA A 441 153.28 -44.01 REMARK 500 1 ASN A 443 -37.48 -37.04 REMARK 500 1 PHE A 450 44.74 -104.06 REMARK 500 1 VAL A 456 96.65 -68.56 REMARK 500 1 GLU A 457 -31.26 -38.12 REMARK 500 1 ILE A 460 103.66 -38.58 REMARK 500 1 ARG A 490 54.41 -106.17 REMARK 500 1 MET A 495 81.09 -67.75 REMARK 500 2 SER A 415 143.77 -170.38 REMARK 500 2 GLU A 427 48.33 -90.51 REMARK 500 2 ALA A 428 33.43 38.22 REMARK 500 2 LEU A 437 150.47 -36.54 REMARK 500 2 VAL A 456 105.41 -57.99 REMARK 500 2 ILE A 460 106.28 -37.73 REMARK 500 2 GLN A 522 37.30 -97.87 REMARK 500 2 SER A 523 164.38 -42.80 REMARK 500 3 LEU A 437 143.89 -37.29 REMARK 500 3 PHE A 450 48.14 -103.33 REMARK 500 3 GLU A 457 -32.03 -36.05 REMARK 500 3 ARG A 490 40.76 -96.05 REMARK 500 3 GLN A 522 140.27 -39.93 REMARK 500 3 SER A 526 99.21 -59.13 REMARK 500 4 SER A 413 142.23 -173.93 REMARK 500 4 PRO A 425 89.30 -69.81 REMARK 500 4 HIS A 426 139.06 -171.00 REMARK 500 4 LEU A 437 147.93 -38.29 REMARK 500 4 ASN A 443 -34.21 -38.65 REMARK 500 4 VAL A 456 93.30 -60.10 REMARK 500 4 GLU A 457 -30.29 -37.76 REMARK 500 4 ILE A 460 104.40 -34.43 REMARK 500 4 ASN A 467 35.01 -86.41 REMARK 500 4 ARG A 490 51.09 -102.21 REMARK 500 5 LYS A 412 151.71 -45.99 REMARK 500 5 SER A 415 -75.01 -46.45 REMARK 500 5 ARG A 419 38.78 38.90 REMARK 500 5 HIS A 426 161.07 -43.72 REMARK 500 5 LEU A 437 149.57 -35.17 REMARK 500 5 PHE A 450 47.45 -103.44 REMARK 500 5 GLU A 457 -30.21 -38.99 REMARK 500 5 ILE A 460 104.45 -35.68 REMARK 500 5 PRO A 525 -179.90 -69.80 REMARK 500 5 SER A 526 42.25 -97.95 REMARK 500 5 SER A 527 42.12 38.12 REMARK 500 6 LYS A 412 100.98 -43.15 REMARK 500 6 LEU A 437 151.02 -36.83 REMARK 500 6 PHE A 450 50.91 -114.99 REMARK 500 6 VAL A 456 92.54 -48.00 REMARK 500 REMARK 500 THIS ENTRY HAS 170 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK002100747.1 RELATED DB: TARGETDB DBREF 1WEL A 412 522 UNP Q9NTZ6 RBM12_HUMAN 412 522 SEQADV 1WEL GLY A 405 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 406 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 407 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL GLY A 408 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 409 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 410 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL GLY A 411 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 523 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL GLY A 524 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL PRO A 525 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 526 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL SER A 527 UNP Q9NTZ6 CLONING ARTIFACT SEQADV 1WEL GLY A 528 UNP Q9NTZ6 CLONING ARTIFACT SEQRES 1 A 124 GLY SER SER GLY SER SER GLY LYS SER PRO SER GLY GLN SEQRES 2 A 124 LYS ARG SER ARG SER ARG SER PRO HIS GLU ALA GLY PHE SEQRES 3 A 124 CYS VAL TYR LEU LYS GLY LEU PRO PHE GLU ALA GLU ASN SEQRES 4 A 124 LYS HIS VAL ILE ASP PHE PHE LYS LYS LEU ASP ILE VAL SEQRES 5 A 124 GLU ASP SER ILE TYR ILE ALA TYR GLY PRO ASN GLY LYS SEQRES 6 A 124 ALA THR GLY GLU GLY PHE VAL GLU PHE ARG ASN GLU ALA SEQRES 7 A 124 ASP TYR LYS ALA ALA LEU CYS ARG HIS LYS GLN TYR MET SEQRES 8 A 124 GLY ASN ARG PHE ILE GLN VAL HIS PRO ILE THR LYS LYS SEQRES 9 A 124 GLY MET LEU GLU LYS ILE ASP MET ILE ARG LYS ARG LEU SEQRES 10 A 124 GLN SER GLY PRO SER SER GLY HELIX 1 1 GLU A 442 PHE A 450 1 9 HELIX 2 2 GLU A 481 CYS A 489 1 9 HELIX 3 3 THR A 506 GLN A 522 1 17 SHEET 1 A 4 TYR A 461 TYR A 464 0 SHEET 2 A 4 ALA A 470 GLU A 477 -1 O PHE A 475 N TYR A 461 SHEET 3 A 4 CYS A 431 LYS A 435 -1 N VAL A 432 O VAL A 476 SHEET 4 A 4 GLN A 501 ILE A 505 -1 O HIS A 503 N TYR A 433 SHEET 1 B 2 GLN A 493 MET A 495 0 SHEET 2 B 2 ARG A 498 ILE A 500 -1 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 - c 21 2 Bytes