Header list of 1z9q.pdb file
Complete list - r 2 2 Bytes
HEADER OXIDOREDUCTASE ACTIVATOR 04-APR-05 1Z9Q TITLE SOLUTION STRUCTURE OF SH3 DOMAIN OF P40PHOX COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SH3 DOMAIN; COMPND 5 SYNONYM: P40PHOX, NCF-4, NEUTROPHIL NADPH OXIDASE FACTOR 4, P40-PHOX; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOLD2 KEYWDS OXIDOREDUCTASE ACTIVATOR EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.ADACHI,K.OGURA,Y.FUJIOKA,F.INAGAKI REVDAT 3 02-MAR-22 1Z9Q 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Z9Q 1 VERSN REVDAT 1 21-MAR-06 1Z9Q 0 JRNL AUTH S.ADACHI,K.OGURA,Y.FUJIOKA,F.INAGAKI JRNL TITL SOLUTION STRUCTURE OF SH3 DOMAIN OF P40PHOX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0 REMARK 3 AUTHORS : WELCH (VNMR), GUNTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z9Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-APR-05. REMARK 100 THE DEPOSITION ID IS D_1000032475. 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 : 150MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM P40PHOXSH3 U-13C, 15N; REMARK 210 50MM NAPI PH7.0; 150MM NACL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 23, SPARKY 3.11, CYANA REMARK 210 2.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS 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: 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 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 -12 REMARK 465 ASN A -11 REMARK 465 HIS A -10 REMARK 465 LYS A -9 REMARK 465 VAL A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 MET A 0 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 MET A 3 -42.01 -140.47 REMARK 500 1 ARG A 7 131.91 -172.75 REMARK 500 1 ASN A 17 -64.36 -91.75 REMARK 500 1 ALA A 26 98.42 -57.61 REMARK 500 1 VAL A 29 115.31 65.83 REMARK 500 1 LEU A 32 116.11 64.79 REMARK 500 1 ASN A 37 -67.65 -145.40 REMARK 500 1 LYS A 38 -38.72 -167.83 REMARK 500 1 ILE A 59 98.04 -58.30 REMARK 500 1 PRO A 64 85.59 -69.76 REMARK 500 2 MET A 3 38.28 -94.97 REMARK 500 2 ALA A 4 25.02 -160.62 REMARK 500 2 ARG A 7 131.57 -171.35 REMARK 500 2 ALA A 26 96.10 -60.07 REMARK 500 2 VAL A 29 114.65 65.82 REMARK 500 2 LEU A 32 113.26 64.20 REMARK 500 2 ASN A 37 -71.61 -150.32 REMARK 500 2 LYS A 38 -39.71 -163.21 REMARK 500 2 ILE A 59 97.80 -58.64 REMARK 500 2 PRO A 64 85.28 -69.77 REMARK 500 3 MET A 3 40.28 -94.18 REMARK 500 3 ALA A 4 30.31 -170.83 REMARK 500 3 ARG A 7 131.22 -171.87 REMARK 500 3 ALA A 26 98.16 -57.95 REMARK 500 3 VAL A 29 114.32 65.53 REMARK 500 3 LEU A 32 112.47 64.13 REMARK 500 3 ASN A 37 -71.17 -149.22 REMARK 500 3 LYS A 38 -38.92 -163.88 REMARK 500 3 ILE A 59 97.91 -58.46 REMARK 500 3 PRO A 64 79.96 -69.79 REMARK 500 4 ALA A 4 25.68 -140.02 REMARK 500 4 ARG A 7 131.75 -172.90 REMARK 500 4 ASN A 17 -61.85 -92.74 REMARK 500 4 ALA A 26 96.73 -59.20 REMARK 500 4 VAL A 29 114.88 65.79 REMARK 500 4 LEU A 32 115.25 64.71 REMARK 500 4 ASN A 37 -70.92 -153.45 REMARK 500 4 LYS A 38 -39.61 -163.87 REMARK 500 4 ILE A 59 98.02 -58.20 REMARK 500 4 PRO A 64 86.21 -69.80 REMARK 500 5 ALA A 4 24.81 -160.06 REMARK 500 5 ARG A 7 131.76 -172.17 REMARK 500 5 ALA A 26 97.77 -58.11 REMARK 500 5 VAL A 29 113.54 65.55 REMARK 500 5 LEU A 32 113.14 64.18 REMARK 500 5 ASN A 37 -69.55 -153.04 REMARK 500 5 LYS A 38 -39.33 -165.26 REMARK 500 5 ILE A 59 97.81 -58.37 REMARK 500 5 PRO A 64 83.54 -69.79 REMARK 500 6 ALA A 4 29.82 -169.85 REMARK 500 REMARK 500 THIS ENTRY HAS 199 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z9Q A 1 66 UNP Q15080 NCF4_HUMAN 168 233 SEQADV 1Z9Q MET A -12 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q ASN A -11 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -10 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q LYS A -9 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q VAL A -8 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -7 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -6 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -5 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -4 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -3 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -2 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q HIS A -1 UNP Q15080 CLONING ARTIFACT SEQADV 1Z9Q MET A 0 UNP Q15080 CLONING ARTIFACT SEQRES 1 A 79 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS HIS MET SEQRES 2 A 79 ASP ARG MET ALA ALA PRO ARG ALA GLU ALA LEU PHE ASP SEQRES 3 A 79 PHE THR GLY ASN SER LYS LEU GLU LEU ASN PHE LYS ALA SEQRES 4 A 79 GLY ASP VAL ILE PHE LEU LEU SER ARG ILE ASN LYS ASP SEQRES 5 A 79 TRP LEU GLU GLY THR VAL ARG GLY ALA THR GLY ILE PHE SEQRES 6 A 79 PRO LEU SER PHE VAL LYS ILE LEU LYS ASP PHE PRO GLU SEQRES 7 A 79 GLU SHEET 1 A 2 ALA A 8 ALA A 10 0 SHEET 2 A 2 VAL A 57 ILE A 59 -1 O LYS A 58 N GLU A 9 SHEET 1 B 3 SER A 34 ARG A 35 0 SHEET 2 B 3 TRP A 40 VAL A 45 -1 O GLU A 42 N SER A 34 SHEET 3 B 3 ALA A 48 PRO A 53 -1 O PHE A 52 N LEU A 41 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 2 2 Bytes