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PDBsum entry 1w70

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Top Page protein ligands Protein-protein interface(s) links
Sh3 domain PDB id
1w70
Jmol
Contents
Protein chains
60 a.a.
14 a.a.
12 a.a.
Ligands
SO4 ×4
TFA ×2
Waters ×227
HEADER    SH3 DOMAIN                              26-AUG-04   1W70
TITLE     SH3 DOMAIN OF P40PHOX COMPLEXED WITH C-TERMINAL POLYPROLINE
TITLE    2 REGION OF P47PHOX
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 4;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: SH3 DOMAIN, RESIDUES 174-228;
COMPND   5 SYNONYM: NCF-4, NEUTROPHIL NADPH OXIDASE FACTOR 4,
COMPND   6  P40PHOX, P40-PHOX;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: NEUTROPHIL CYTOSOL FACTOR 1;
COMPND  10 CHAIN: C, D;
COMPND  11 FRAGMENT: POLYPROLINE MOTIF, RESIDUES 360-372;
COMPND  12 SYNONYM: NCF-1,NEUTROPHIL NADPH OXIDASE FACTOR 1,47 KDA
COMPND  13  NEUTROPHIL OXIDASE FACTOR, P47-PHOX
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL: NEUTROPHIL;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PIVEX2.4;
SOURCE  10 MOL_ID: 2;
SOURCE  11 SYNTHETIC: YES;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 CELL: NEUTROPHIL
KEYWDS    NADPH OXIDASE, P40PHOX, P47PHOX, SH3 DOMAIN, POLYPROLINE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.MASSENET,S.CHENAVAS,C.COHEN-ADDAD,M.-C.DAGHER,G.BRANDOLIN,
AUTHOR   2 E.PEBAY-PEYROULA,F.FIESCHI
REVDAT   3   24-FEB-09 1W70    1       VERSN
REVDAT   2   04-APR-05 1W70    1       JRNL
REVDAT   1   18-JAN-05 1W70    0
JRNL        AUTH   C.MASSENET,S.CHENAVAS,C.COHEN-ADDAD,M.-C.DAGHER,
JRNL        AUTH 2 G.BRANDOLIN,E.PEBAY-PEYROULA,F.FIESCHI
JRNL        TITL   EFFECTS OF P47PHOX C-TERMINUS PHOSPHORYLATION ON
JRNL        TITL 2 BINDING INTERACTIONS WITH P40PHOX AND P67PHOX:
JRNL        TITL 3 STRUCTURAL AND FUNCTIONAL COMPARISON OF P40PHOX
JRNL        TITL 4 P67PHOX SH3 DOMAINS
JRNL        REF    J.BIOL.CHEM.                  V. 280 13752 2005
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   15657040
JRNL        DOI    10.1074/JBC.M412897200
REMARK   2
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.7
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7
REMARK   3   NUMBER OF REFLECTIONS             : 23121
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.1811
REMARK   3   FREE R VALUE                     : 0.2073
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.8
REMARK   3   FREE R VALUE TEST SET COUNT      : 1168
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.46
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.51
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.47
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1820
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2308
REMARK   3   BIN FREE R VALUE                    : 0.2602
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.51
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 108
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1169
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 227
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.91
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.939
REMARK   3    B22 (A**2) : 1.290
REMARK   3    B33 (A**2) : -3.229
REMARK   3    B12 (A**2) : 0.000
REMARK   3    B13 (A**2) : 0.000
REMARK   3    B23 (A**2) : 0.000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.15
REMARK   3   ESD FROM SIGMAA              (A) : 0.08
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.17
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.09
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008391
REMARK   3   BOND ANGLES            (DEGREES) : 1.49521
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50055
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.05772
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.541566
REMARK   3   BSOL        : 76.2164
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : SULF.PARAM
REMARK   3  PARAMETER FILE  5  : TFA.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1W70 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-AUG-04.
REMARK 100 THE PDBE ID CODE IS EBI-20877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM30A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23121
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.700
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.03000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1W6X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION AT 20 DEGRE C
REMARK 280  AT 14MG/ML OF P40PHOX SH3 WITH A1/5 RATIO WITH POLYPROLINE
REMARK 280  PEPTIDE, 20 MM HEPES PH 7.5, 150 MM NACL MIXED WITH 100 MM
REMARK 280  NA-CITRATE/CITRIC ACID PH5, 2.4 M SA
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       19.82000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.09000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.24500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       34.09000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.82000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.24500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300
REMARK 300 DETAILS:CHAINS A AND B ARE ISOLATED FRAGMENTS OF
REMARK 300 P40PHOXAND THERE IS NO BIOLOGICAL EVIDENCE OF
REMARK 300 THEIRDIMERIZATION. HOWEVER, SINCE EACH CHAIN IS
REMARK 300 INCOMPLEX WITH A PEPTIDE IN THIS ENTRY, THE
REMARK 300 BIOLOGICALUNIT IS CLASSIFIED AS DIMERIC.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 400
REMARK 400 COMPOUND
REMARK 400  COMPONENT OF THE NADPH-OXIDASE, A MULTICOMPONENT ENZYME
REMARK 400  SYSTEM RESPONSIBLE FOR TRANSPORT OF ELECTRONS FROM
REMARK 400  NADPH TO MOLECULAR OXYGEN, GENERATING REACTIVE
REMARK 400  OXIDANT INTERMEDIATES. P40-PHOX ASSOCIATES PRIMARILY
REMARK 400  WITH P67-PHOX TO FORM A COMPLEX WITH P47-PHOX.
REMARK 400  NCF2, NCF1, AND A MEMBRANE BOUND CYTOCHROME B558 ARE
REMARK 400  REQUIRED FOR ACTIVATION OF THE LATENT NADPH OXIDASE
REMARK 400 (NECESSARY FOR SUPEROXIDE PRODUCTION).
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA D   371
REMARK 465     ASP D   372
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS D 360    CG   CD   CE   NZ
REMARK 470     SER D 370    CA   C    O    CB   OG
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 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    ASN A 204     -168.41   -160.78
REMARK 500    ASN B 204     -167.30   -161.30
REMARK 500    ALA C 371       38.88   -145.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFA B1232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFA B1233
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H6H   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE PX DOMAIN FROM P40PHOX
REMARK 900  BOUND TO PHOSPHATIDYLINOSITOL 3-PHOSPHATE
REMARK 900 RELATED ID: 1OEY   RELATED DB: PDB
REMARK 900  HETERODIMER OF P40PHOX AND P67PHOX PB1
REMARK 900  DOMAINS FROM HUMAN NADPH OXIDASE
REMARK 900 RELATED ID: 1W6X   RELATED DB: PDB
REMARK 900  SH3 DOMAIN OF P40PHOX, COMPONENT OF THE
REMARK 900  NADPH OXIDASE
REMARK 900 RELATED ID: 1GD5   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF THE PX DOMAIN FROM
REMARK 900  HUMAN P47PHOXNADPH OXIDASE
REMARK 900 RELATED ID: 1K4U   RELATED DB: PDB
REMARK 900  SOLUTION STRUCTURE OF THE C-TERMINAL SH3
REMARK 900  DOMAIN OF P67PHOXCOMPLEXED WITH THE C-
REMARK 900  TERMINAL TAIL REGION OF P47PHOX
REMARK 900 RELATED ID: 1KQ6   RELATED DB: PDB
REMARK 900  P47PHOX PX DOMAIN
REMARK 900 RELATED ID: 1NG2   RELATED DB: PDB
REMARK 900  STRUCTURE OF AUTOINHIBITED P47PHOX
REMARK 900 RELATED ID: 1O7K   RELATED DB: PDB
REMARK 900  HUMAN P47 PX DOMAIN COMPLEX WITH SULPHATES
REMARK 900 RELATED ID: 1OV3   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE P22PHOX-P47PHOX COMPLEX
REMARK 900 RELATED ID: 1UEC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF AUTOINHIBITED FORM OF
REMARK 900  TANDEM SH3DOMAIN OF P47PHOX
DBREF  1W70 A  169   173  PDB    1W70     1W70           169    173
DBREF  1W70 A  174   228  UNP    Q15080   NCF4_HUMAN     174    228
DBREF  1W70 B  169   173  PDB    1W70     1W70           169    173
DBREF  1W70 B  174   228  UNP    Q15080   NCF4_HUMAN     174    228
DBREF  1W70 C  359   359  PDB    1W70     1W70           359    359
DBREF  1W70 C  360   372  UNP    P14598   NCF1_HUMAN     360    372
DBREF  1W70 D  359   359  PDB    1W70     1W70           359    359
DBREF  1W70 D  360   372  UNP    P14598   NCF1_HUMAN     360    372
SEQRES   1 A   60  LEU ILE LYS HIS MET ARG ALA GLU ALA LEU PHE ASP PHE
SEQRES   2 A   60  THR GLY ASN SER LYS LEU GLU LEU ASN PHE LYS ALA GLY
SEQRES   3 A   60  ASP VAL ILE PHE LEU LEU SER ARG ILE ASN LYS ASP TRP
SEQRES   4 A   60  LEU GLU GLY THR VAL ARG GLY ALA THR GLY ILE PHE PRO
SEQRES   5 A   60  LEU SER PHE VAL LYS ILE LEU LYS
SEQRES   1 B   60  LEU ILE LYS HIS MET ARG ALA GLU ALA LEU PHE ASP PHE
SEQRES   2 B   60  THR GLY ASN SER LYS LEU GLU LEU ASN PHE LYS ALA GLY
SEQRES   3 B   60  ASP VAL ILE PHE LEU LEU SER ARG ILE ASN LYS ASP TRP
SEQRES   4 B   60  LEU GLU GLY THR VAL ARG GLY ALA THR GLY ILE PHE PRO
SEQRES   5 B   60  LEU SER PHE VAL LYS ILE LEU LYS
SEQRES   1 C   14  ACE LYS PRO GLN PRO ALA VAL PRO PRO ARG PRO SER ALA
SEQRES   2 C   14  ASP
SEQRES   1 D   14  ACE LYS PRO GLN PRO ALA VAL PRO PRO ARG PRO SER ALA
SEQRES   2 D   14  ASP
HET    SO4  A1229       5
HET    SO4  B1229       5
HET    SO4  B1230       5
HET    SO4  B1231       5
HET    ACE  C 359       3
HET    ACE  D 359       3
HET    TFA  B1232       7
HET    TFA  B1233       7
HETNAM     SO4 SULFATE ION
HETNAM     ACE ACETYL GROUP
HETNAM     TFA TRIFLUOROACETYL GROUP
FORMUL   5  SO4    4(O4 S 2-)
FORMUL   9  ACE    2(C2 H4 O)
FORMUL  11  TFA    2(C2 H F3 O2)
FORMUL  13  HOH   *227(H2 O1)
SHEET    1  AA 5 ALA A 215  PRO A 220  0
SHEET    2  AA 5 TRP A 207  VAL A 212 -1  O  LEU A 208   N  PHE A 219
SHEET    3  AA 5 VAL A 196  ARG A 202 -1  O  PHE A 198   N  THR A 211
SHEET    4  AA 5 ARG A 174  ALA A 177 -1  O  ALA A 175   N  ILE A 197
SHEET    5  AA 5 VAL A 224  ILE A 226 -1  O  LYS A 225   N  GLU A 176
SHEET    1  BA 5 ALA B 215  PRO B 220  0
SHEET    2  BA 5 TRP B 207  VAL B 212 -1  O  LEU B 208   N  PHE B 219
SHEET    3  BA 5 VAL B 196  ARG B 202 -1  O  PHE B 198   N  THR B 211
SHEET    4  BA 5 ARG B 174  ALA B 177 -1  O  ALA B 175   N  ILE B 197
SHEET    5  BA 5 VAL B 224  ILE B 226 -1  O  LYS B 225   N  GLU B 176
SHEET    1  BB 2 PHE B 181  THR B 182  0
SHEET    2  BB 2 ASN B 190  PHE B 191 -1  O  PHE B 191   N  PHE B 181
LINK         C   ACE C 359                 N   LYS C 360     1555   1555  1.33
LINK         C   ACE D 359                 N   LYS D 360     1555   1555  1.33
SITE     1 AC1  5 LYS A 171  HIS A 172  HOH A2083  HOH A2084
SITE     2 AC1  5 HOH A2085
SITE     1 AC2  4 ARG B 202  ASN B 204  LYS B 205  HOH B2081
SITE     1 AC3 11 ILE B 170  LYS B 171  HIS B 172  ARG B 174
SITE     2 AC3 11 PHE B 198  HOH B2045  HOH B2082  HOH B2083
SITE     3 AC3 11 HOH B2084  HOH B2086  HOH B2087
SITE     1 AC4  5 LYS A 192  LYS A 205  ARG B 174  PHE B 198
SITE     2 AC4  5 HOH B2088
SITE     1 AC5  9 LEU A 187  ILE A 203  ILE A 218  LEU B 169
SITE     2 AC5  9 ILE B 170  SER B 201  ARG B 202  HOH B2089
SITE     3 AC5  9 PRO C 369
SITE     1 AC6  7 ILE A 170  ARG A 202  LEU B 187  ILE B 218
SITE     2 AC6  7 HOH B2090  PRO D 369  SER D 370
CRYST1   39.640   50.490   68.180  90.00  90.00  90.00 P 21 21 21    8
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      0.025227  0.000000  0.000000        0.00000
SCALE2      0.000000  0.019806  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014667        0.00000
      
PROCHECK
Go to PROCHECK summary
 References