Header list of 1wlp.pdb file
Complete list - 2 20 Bytes
HEADER OXIDOREDUCTASE/SIGNALING PROTEIN 29-JUN-04 1WLP
TITLE SOLUTION STRUCTURE OF THE P22PHOX-P47PHOX COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B-245 LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA POLYPEPTIDE (1-25);
COMPND 5 SYNONYM: FLAVOCYTOCHROME B558, P22PHOX;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: TANDEM SH3 DOMAIN;
COMPND 11 SYNONYM: P47PHOX;
COMPND 12 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS SH3 DOMAIN, POLYPROLINE, OXIDOREDUCTASE-SIGNALING PROTEIN COMPLEX
EXPDTA SOLUTION NMR
AUTHOR K.OGURA,S.TORIKAI,K.SAIKAWA,S.YUZAWA,H.SUMIMOTO,F.INAGAKI
REVDAT 4 02-MAR-22 1WLP 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1WLP 1 VERSN
REVDAT 2 17-OCT-06 1WLP 1 JRNL
REVDAT 1 04-OCT-05 1WLP 0
JRNL AUTH K.OGURA,I.NOBUHISA,S.YUZAWA,R.TAKEYA,S.TORIKAI,K.SAIKAWA,
JRNL AUTH 2 H.SUMIMOTO,F.INAGAKI
JRNL TITL NMR SOLUTION STRUCTURE OF THE TANDEM SRC HOMOLOGY 3 DOMAINS
JRNL TITL 2 OF P47PHOX COMPLEXED WITH A P22PHOX-DERIVED PROLINE-RICH
JRNL TITL 3 PEPTIDE
JRNL REF J.BIOL.CHEM. V. 281 3660 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16326715
JRNL DOI 10.1074/JBC.M505193200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURE WAS ALSO REFINED WITH
REMARK 3 ARIA
REMARK 4
REMARK 4 1WLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023715.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 LYS B 169 -147.71 37.50
REMARK 500 THR B 170 -43.15 -175.14
REMARK 500 SER B 171 -156.23 -130.86
REMARK 500 SER B 173 -150.01 -171.17
REMARK 500 GLU B 174 -164.92 58.99
REMARK 500 VAL B 185 129.85 -37.06
REMARK 500 ALA B 200 -81.98 -104.87
REMARK 500 ARG B 202 -166.08 -110.88
REMARK 500 PRO B 212 123.46 -28.83
REMARK 500 ASP B 214 -4.24 177.67
REMARK 500 THR B 219 157.10 65.64
REMARK 500 PRO B 224 93.76 -65.49
REMARK 500 TRP B 263 103.66 -46.64
REMARK 500 TYR B 279 -16.15 -46.75
REMARK 500 SER B 283 62.52 -161.34
REMARK 500 GLN B 285 -154.37 44.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WLP A 6 25 UNP P13498 CY24A_HUMAN 148 167
DBREF 1WLP B 151 286 UNP P14598 NCF1_HUMAN 151 286
SEQADV 1WLP GLY A 1 UNP P13498 CLONING ARTIFACT
SEQADV 1WLP PRO A 2 UNP P13498 CLONING ARTIFACT
SEQADV 1WLP LEU A 3 UNP P13498 CLONING ARTIFACT
SEQADV 1WLP GLY A 4 UNP P13498 CLONING ARTIFACT
SEQADV 1WLP SER A 5 UNP P13498 CLONING ARTIFACT
SEQADV 1WLP GLY B 149 UNP P14598 CLONING ARTIFACT
SEQADV 1WLP SER B 150 UNP P14598 CLONING ARTIFACT
SEQRES 1 A 25 GLY PRO LEU GLY SER LYS GLN PRO PRO SER ASN PRO PRO
SEQRES 2 A 25 PRO ARG PRO PRO ALA GLU ALA ARG LYS LYS PRO SER
SEQRES 1 B 138 GLY SER ASP ILE THR GLY PRO ILE ILE LEU GLN THR TYR
SEQRES 2 B 138 ARG ALA ILE ALA ASP TYR GLU LYS THR SER GLY SER GLU
SEQRES 3 B 138 MET ALA LEU SER THR GLY ASP VAL VAL GLU VAL VAL GLU
SEQRES 4 B 138 LYS SER GLU SER GLY TRP TRP PHE CYS GLN MET LYS ALA
SEQRES 5 B 138 LYS ARG GLY TRP ILE PRO ALA SER PHE LEU GLU PRO LEU
SEQRES 6 B 138 ASP SER PRO ASP GLU THR GLU ASP PRO GLU PRO ASN TYR
SEQRES 7 B 138 ALA GLY GLU PRO TYR VAL ALA ILE LYS ALA TYR THR ALA
SEQRES 8 B 138 VAL GLU GLY ASP GLU VAL SER LEU LEU GLU GLY GLU ALA
SEQRES 9 B 138 VAL GLU VAL ILE HIS LYS LEU LEU ASP GLY TRP TRP VAL
SEQRES 10 B 138 ILE ARG LYS ASP ASP VAL THR GLY TYR PHE PRO SER MET
SEQRES 11 B 138 TYR LEU GLN LYS SER GLY GLN ASP
HELIX 1 1 PRO A 17 LYS A 23 1 7
SHEET 1 A 5 ARG B 202 PRO B 206 0
SHEET 2 A 5 TRP B 193 GLN B 197 -1 N TRP B 194 O ILE B 205
SHEET 3 A 5 VAL B 182 LYS B 188 -1 N GLU B 187 O PHE B 195
SHEET 4 A 5 GLN B 159 ALA B 163 -1 N TYR B 161 O VAL B 183
SHEET 5 A 5 LEU B 210 PRO B 212 -1 O GLU B 211 N ARG B 162
SHEET 1 B 2 TYR B 167 GLU B 168 0
SHEET 2 B 2 ALA B 176 LEU B 177 -1 O LEU B 177 N TYR B 167
SHEET 1 C 5 THR B 272 PHE B 275 0
SHEET 2 C 5 TRP B 264 ARG B 267 -1 N TRP B 264 O PHE B 275
SHEET 3 C 5 ALA B 252 HIS B 257 -1 N GLU B 254 O ARG B 267
SHEET 4 C 5 PRO B 230 ALA B 233 -1 N TYR B 231 O VAL B 253
SHEET 5 C 5 LEU B 280 LYS B 282 -1 O GLN B 281 N VAL B 232
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
Complete list - 2 20 Bytes