Header list of 1nyn.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 13-FEB-03 1NYN TITLE SOLUTION NMR STRUCTURE OF PROTEIN YHR087W FROM SACCHAROMYCES TITLE 2 CEREVISIAE. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET YTYST425. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL 12.0 KDA PROTEIN IN NAM8-GAR1 INTERGENIC COMPND 3 REGION; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: YHR087W; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 15B KEYWDS HYPOTHETICAL PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN KEYWDS 3 FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.R.CORT,A.A.YEE,C.H.ARROWSMITH,M.A.KENNEDY,NORTHEAST STRUCTURAL AUTHOR 2 GENOMICS CONSORTIUM (NESG) REVDAT 6 23-FEB-22 1NYN 1 REMARK SEQADV REVDAT 5 24-FEB-09 1NYN 1 VERSN REVDAT 4 06-SEP-05 1NYN 1 AUTHOR REVDAT 3 17-MAY-05 1NYN 1 JRNL REVDAT 2 25-JAN-05 1NYN 1 AUTHOR KEYWDS REMARK REVDAT 1 08-APR-03 1NYN 0 JRNL AUTH A.SAVCHENKO,N.KROGAN,J.R.CORT,E.EVDOKIMOVA,J.M.LEW,A.A.YEE, JRNL AUTH 2 L.SANCHEZ-PULIDO,M.A.ANDRADE,A.BOCHKAREV,J.D.WATSON, JRNL AUTH 3 M.A.KENNEDY,J.GREENBLATT,T.HUGHES,C.H.ARROWSMITH, JRNL AUTH 4 J.M.ROMMENS,A.M.EDWARDS JRNL TITL THE SHWACHMAN-BODIAN-DIAMOND SYNDROME PROTEIN FAMILY IS JRNL TITL 2 INVOLVED IN RNA METABOLISM. JRNL REF J.BIOL.CHEM. V. 280 19213 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 15701634 JRNL DOI 10.1074/JBC.M414421200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NIH-XPLOR 2.0.4 REMARK 3 AUTHORS : BRUNGER, A.T., SCHWIETERS, C.D., KUSZEWSKI, J.J., REMARK 3 TJANDRA, N., CLORE, G.M. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 665 CONFORMATIONALLY- REMARK 3 RESTRICTING NOE-DERIVED DISTANCE RESTRAINTS, REMARK 3 73 DIHEDRAL ANGLE RESTRAINTS, AND 44 HYDROGEN BOND RESTRAINTS REMARK 3 (10.0 RESTRAINTS PER RESIDUE FOR RESIDUES REMARK 3 4-90, EXCLUDING LOOP RESIDUES 51-59). THE 20 RESIDUE N-TERMINAL REMARK 3 TAG (MGSSHHHHHHSSGLVPRGSH) WAS NOT REMARK 3 INCLUDED IN THE STRUCTURE CALCULATION AND IS NOT PRESENT IN THE REMARK 3 COORDINATES. REMARK 4 REMARK 4 1NYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-03. REMARK 100 THE DEPOSITION ID IS D_1000018356. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : 300MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM YHR087W U-13C,15N, 10MM REMARK 210 SODIUM ACETATE, 300MM NACL; 1MM REMARK 210 YHR087W U-13C,15N, 10MM SODIUM REMARK 210 ACETATE, 300MM NACL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 97, NIH-XPLOR 2.0.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 BACKBONE AND SIDECHAIN ASSIGNMENTS WERE DETERMINED MANUALLY FROM REMARK 210 TRIPLE-RESONANCE NMR DATA. NOE DISTANCE REMARK 210 RESTRAINTS WERE DERIVED MANUALLY FROM NOESY DATA. PHI DIHEDRAL REMARK 210 ANGLE RESTRAINTS WERE DERIVED FROM THE REMARK 210 HNHA EXPERIMENT. PSI DIHEDRAL ANGLE RESTRAINTS WERE DERIVED FROM REMARK 210 NOE RATIOS, SECONDARY STRUCTURE REMARK 210 PROPENSITIES EVIDENT IN PRELIMINARY STRUCTURES, AND FROM ALPHA REMARK 210 CARBON 13C CHEMICAL SHIFT TRENDS. RESIDUES REMARK 210 51-59 COMPRISE A POORLY-DEFINED LOOP IN THIS ENSEMBLE OF REMARK 210 STRUCTURES. RESIDUES 92 TO 110 ARE ALSO NOT REMARK 210 WELL-DEFINED IN THE ENSEMBLE. 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 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 -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 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 O GLN A 51 H GLY A 53 1.44 REMARK 500 O SER A 34 H LYS A 37 1.49 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 2 6.72 173.82 REMARK 500 1 ALA A 21 -73.33 -73.96 REMARK 500 1 GLU A 24 -74.72 -65.49 REMARK 500 1 VAL A 26 -70.61 -67.32 REMARK 500 1 ASN A 32 79.43 -175.62 REMARK 500 1 SER A 34 94.41 -164.33 REMARK 500 1 LEU A 38 -31.61 -39.13 REMARK 500 1 VAL A 41 -70.94 -69.17 REMARK 500 1 PRO A 50 -172.38 -45.30 REMARK 500 1 ASP A 52 59.25 -62.94 REMARK 500 1 LEU A 60 150.75 -38.42 REMARK 500 1 GLU A 71 -73.03 -113.75 REMARK 500 1 LYS A 77 -140.87 -114.37 REMARK 500 1 ASN A 88 75.62 -167.87 REMARK 500 1 PRO A 91 165.27 -48.50 REMARK 500 1 THR A 95 56.19 -107.39 REMARK 500 1 SER A 96 172.80 -53.56 REMARK 500 1 SER A 97 -77.06 -171.34 REMARK 500 1 LYS A 99 -160.51 -64.26 REMARK 500 1 LYS A 101 -157.86 -88.13 REMARK 500 1 ASN A 104 -78.86 -158.47 REMARK 500 1 ALA A 109 -94.31 -92.62 REMARK 500 2 VAL A 4 -179.80 -55.27 REMARK 500 2 GLU A 12 -82.55 -42.82 REMARK 500 2 ALA A 21 -87.19 -73.93 REMARK 500 2 GLU A 24 -74.06 -75.14 REMARK 500 2 ASN A 32 70.59 -150.31 REMARK 500 2 SER A 34 -104.84 -171.26 REMARK 500 2 ILE A 35 -20.61 -169.08 REMARK 500 2 GLU A 46 114.22 -166.70 REMARK 500 2 GLN A 51 -32.73 -144.80 REMARK 500 2 ARG A 54 -3.99 57.94 REMARK 500 2 LEU A 60 -170.55 57.54 REMARK 500 2 GLN A 67 -39.23 -35.91 REMARK 500 2 GLU A 71 -70.18 -98.61 REMARK 500 2 PHE A 72 54.20 -160.07 REMARK 500 2 LYS A 74 -61.08 177.81 REMARK 500 2 LYS A 77 -149.13 -71.84 REMARK 500 2 ASN A 88 -86.94 -76.44 REMARK 500 2 PRO A 91 -160.66 -48.81 REMARK 500 2 THR A 95 -170.26 -51.14 REMARK 500 2 LEU A 98 -80.23 -109.85 REMARK 500 2 LYS A 99 93.06 80.34 REMARK 500 2 ASN A 104 104.88 -168.81 REMARK 500 2 ALA A 105 -146.25 -78.74 REMARK 500 2 LYS A 108 -132.59 -76.95 REMARK 500 2 TYR A 110 175.40 70.43 REMARK 500 3 ASN A 13 -35.27 -149.70 REMARK 500 3 ALA A 21 -90.68 -106.05 REMARK 500 3 ASN A 32 71.55 -167.66 REMARK 500 REMARK 500 THIS ENTRY HAS 402 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: YTYST425 RELATED DB: TARGETDB DBREF 1NYN A 1 111 UNP P38804 YHO7_YEAST 1 111 SEQADV 1NYN MET A -19 UNP P38804 EXPRESSION TAG SEQADV 1NYN GLY A -18 UNP P38804 EXPRESSION TAG SEQADV 1NYN SER A -17 UNP P38804 EXPRESSION TAG SEQADV 1NYN SER A -16 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -15 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -14 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -13 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -12 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -11 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A -10 UNP P38804 EXPRESSION TAG SEQADV 1NYN SER A -9 UNP P38804 EXPRESSION TAG SEQADV 1NYN SER A -8 UNP P38804 EXPRESSION TAG SEQADV 1NYN GLY A -7 UNP P38804 EXPRESSION TAG SEQADV 1NYN LEU A -6 UNP P38804 EXPRESSION TAG SEQADV 1NYN VAL A -5 UNP P38804 EXPRESSION TAG SEQADV 1NYN PRO A -4 UNP P38804 EXPRESSION TAG SEQADV 1NYN ARG A -3 UNP P38804 EXPRESSION TAG SEQADV 1NYN GLY A -2 UNP P38804 EXPRESSION TAG SEQADV 1NYN SER A -1 UNP P38804 EXPRESSION TAG SEQADV 1NYN HIS A 0 UNP P38804 EXPRESSION TAG SEQRES 1 A 131 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 131 LEU VAL PRO ARG GLY SER HIS MET SER THR VAL THR LYS SEQRES 3 A 131 TYR PHE TYR LYS GLY GLU ASN THR ASP LEU ILE VAL PHE SEQRES 4 A 131 ALA ALA SER GLU GLU LEU VAL ASP GLU TYR LEU LYS ASN SEQRES 5 A 131 PRO SER ILE GLY LYS LEU SER GLU VAL VAL GLU LEU PHE SEQRES 6 A 131 GLU VAL PHE THR PRO GLN ASP GLY ARG GLY ALA GLU GLY SEQRES 7 A 131 GLU LEU GLY ALA ALA SER LYS ALA GLN VAL GLU ASN GLU SEQRES 8 A 131 PHE GLY LYS GLY LYS LYS ILE GLU GLU VAL ILE ASP LEU SEQRES 9 A 131 ILE LEU ARG ASN GLY LYS PRO ASN SER THR THR SER SER SEQRES 10 A 131 LEU LYS THR LYS GLY GLY ASN ALA GLY THR LYS ALA TYR SEQRES 11 A 131 ASN HELIX 1 1 SER A 22 ASN A 32 1 11 HELIX 2 2 SER A 34 VAL A 42 1 9 HELIX 3 3 SER A 64 GLY A 73 1 10 HELIX 4 4 ILE A 78 ASN A 88 1 11 SHEET 1 A 2 THR A 5 LYS A 10 0 SHEET 2 A 2 ASP A 15 ALA A 20 -1 O VAL A 18 N TYR A 7 SHEET 1 B 2 PHE A 48 THR A 49 0 SHEET 2 B 2 GLY A 61 ALA A 62 -1 O GLY A 61 N THR A 49 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 - b 23 2 Bytes