Header list of 1k4u.pdb file
Complete list - v 10 2 Bytes
HEADER HORMONE/GROWTH FACTOR 08-OCT-01 1K4U
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL SH3 DOMAIN OF P67PHOX COMPLEXED
TITLE 2 WITH THE C-TERMINAL TAIL REGION OF P47PHOX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHAGOCYTE NADPH OXIDASE SUBUNIT P67PHOX;
COMPND 3 CHAIN: S;
COMPND 4 FRAGMENT: C-TERMINAL SH3 DOMAIN (RESIDUES 455-516);
COMPND 5 SYNONYM: NEUTROPHIL CYTOSOL FACTOR 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PHAGOCYTE NADPH OXIDASE SUBUNIT P47PHOX;
COMPND 10 CHAIN: P;
COMPND 11 FRAGMENT: TAIL PEPTIDE (RESIDUES 359-390);
COMPND 12 SYNONYM: NEUTROPHIL CYTOSOL FACTOR 1;
COMPND 13 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: NCF2;
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: PGEX-2T;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: NCF1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS P67PHOX, P47PHOX, SH3-PEPTIDE COMPLEX, HELIX-TURN-HELIX, HORMONE-
KEYWDS 2 GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR K.KAMI,R.TAKEYA,H.SUMIMOTO,D.KOHDA
REVDAT 5 10-NOV-21 1K4U 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1K4U 1 VERSN
REVDAT 3 01-APR-03 1K4U 1 JRNL
REVDAT 2 21-AUG-02 1K4U 1 JRNL
REVDAT 1 08-APR-02 1K4U 0
JRNL AUTH K.KAMI,R.TAKEYA,H.SUMIMOTO,D.KOHDA
JRNL TITL DIVERSE RECOGNITION OF NON-PXXP PEPTIDE LIGANDS BY THE SH3
JRNL TITL 2 DOMAINS FROM P67(PHOX), GRB2 AND PEX13P.
JRNL REF EMBO J. V. 21 4268 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12169629
JRNL DOI 10.1093/EMBOJ/CDF428
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, CNS 1.0
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 693 RESTRAINTS, 611 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 82
REMARK 3 DIHEDRAL ANGLE RESTRAINTS. NO HYDROGEN BOND RESTRAINT WAS USED.
REMARK 4
REMARK 4 1K4U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014562.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : 100MM KCL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.7MM P67SH3(C) U-15N,13C;
REMARK 210 0.77MM P47 TAIL PEPTIDE; 5MM
REMARK 210 MOPSO BUFFER; 30 MM D10-DTT;
REMARK 210 100MM KCL; 0.5MM P47 TAIL
REMARK 210 PEPTIDE U-15N,13C; 0.55MM
REMARK 210 P67SH3(C); 5MM MOPSO BUFFER;
REMARK 210 30MM D10-DTT; 100MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HN(CO)CA, CBCA(CO)NH,
REMARK 210 HNCACB, HBHA(CO)NH, HCCH-COSY,
REMARK 210 HCCH-TOCSY, CCH-COSY, 15N-
REMARK 210 RESOLVED NOESY, 15-RESOLVED
REMARK 210 TOCSY, HNHA, HNHB, 3D_F1 13C-
REMARK 210 FILTERED-F3 13C-RESOLVED NOESY,
REMARK 210 3D_F1 15N-FILTERED-F3 15N-
REMARK 210 RESOLVED NOESY, 2D_SPIN-ECHO
REMARK 210 DIFFERENCE EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
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: S, P
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: 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 H LEU S 476 O ILE S 505 1.55
REMARK 500 O GLY S 497 H GLY S 504 1.58
REMARK 500 H SER S 460 O VAL S 486 1.58
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 S 460 -166.32 -166.36
REMARK 500 1 LEU S 465 -32.28 -142.85
REMARK 500 1 PRO S 473 -75.83 -61.66
REMARK 500 1 ILE S 483 78.69 -111.82
REMARK 500 1 SER S 488 177.16 169.02
REMARK 500 1 ASN S 491 31.01 -175.51
REMARK 500 1 GLU S 492 -57.48 75.03
REMARK 500 1 LYS S 500 77.88 71.02
REMARK 500 1 VAL S 511 80.09 -155.52
REMARK 500 1 GLU S 512 0.98 -63.21
REMARK 500 1 ASP S 513 160.08 66.38
REMARK 500 1 SER S 514 -41.71 -136.19
REMARK 500 1 ALA S 515 108.00 -161.62
REMARK 500 1 GLN P 362 156.29 -48.36
REMARK 500 1 ALA P 364 100.15 -51.29
REMARK 500 1 PRO P 367 91.57 -66.04
REMARK 500 1 ARG P 368 140.98 -39.53
REMARK 500 1 PRO P 369 149.71 -33.16
REMARK 500 1 ALA P 371 -45.82 -28.18
REMARK 500 1 LEU P 386 -81.51 -97.61
REMARK 500 1 ALA P 389 -178.45 57.70
REMARK 500 2 LYS S 458 -170.07 -57.98
REMARK 500 2 SER S 460 -163.08 -74.62
REMARK 500 2 ALA S 470 110.27 -39.52
REMARK 500 2 PRO S 473 -70.66 -68.39
REMARK 500 2 ILE S 483 76.79 -103.61
REMARK 500 2 SER S 488 162.74 171.53
REMARK 500 2 ASN S 491 32.10 -174.71
REMARK 500 2 GLU S 492 -58.44 75.26
REMARK 500 2 SER S 499 -142.83 -89.14
REMARK 500 2 LYS S 500 -86.62 -37.16
REMARK 500 2 VAL S 511 56.80 -157.47
REMARK 500 2 SER S 514 -159.19 77.80
REMARK 500 2 ALA S 515 82.70 75.48
REMARK 500 2 GLN P 362 154.31 -46.67
REMARK 500 2 ALA P 364 101.68 -50.05
REMARK 500 2 PRO P 369 151.34 -25.57
REMARK 500 2 SER P 370 34.17 -73.97
REMARK 500 2 ALA P 371 -63.70 65.38
REMARK 500 2 ALA P 389 -69.59 68.55
REMARK 500 3 LEU S 456 179.49 -59.36
REMARK 500 3 LYS S 458 -72.47 -104.86
REMARK 500 3 SER S 460 -160.43 -73.46
REMARK 500 3 VAL S 462 118.10 -160.33
REMARK 500 3 PRO S 473 -77.70 -62.00
REMARK 500 3 GLU S 474 -37.65 -39.74
REMARK 500 3 SER S 488 167.17 167.47
REMARK 500 3 ASN S 491 34.38 -176.58
REMARK 500 3 GLU S 492 -56.68 69.37
REMARK 500 3 LYS S 500 91.18 59.32
REMARK 500
REMARK 500 THIS ENTRY HAS 423 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K4U S 455 516 UNP P19878 NCF2_HUMAN 455 516
DBREF 1K4U P 359 390 UNP P14598 NCF1_HUMAN 359 390
SEQADV 1K4U SER S 499 UNP P19878 CYS 499 ENGINEERED MUTATION
SEQADV 1K4U SER S 514 UNP P19878 CYS 514 ENGINEERED MUTATION
SEQRES 1 S 62 GLN LEU LYS LYS GLY SER GLN VAL GLU ALA LEU PHE SER
SEQRES 2 S 62 TYR GLU ALA THR GLN PRO GLU ASP LEU GLU PHE GLN GLU
SEQRES 3 S 62 GLY ASP ILE ILE LEU VAL LEU SER LYS VAL ASN GLU GLU
SEQRES 4 S 62 TRP LEU GLU GLY GLU SER LYS GLY LYS VAL GLY ILE PHE
SEQRES 5 S 62 PRO LYS VAL PHE VAL GLU ASP SER ALA THR
SEQRES 1 P 32 SER LYS PRO GLN PRO ALA VAL PRO PRO ARG PRO SER ALA
SEQRES 2 P 32 ASP LEU ILE LEU ASN ARG CYS SER GLU SER THR LYS ARG
SEQRES 3 P 32 LYS LEU ALA SER ALA VAL
HELIX 1 1 PRO S 507 VAL S 511 5 5
HELIX 2 2 SER P 370 ARG P 377 1 8
HELIX 3 3 SER P 379 LEU P 386 1 8
SHEET 1 A 4 SER S 460 GLU S 463 0
SHEET 2 A 4 ILE S 483 LYS S 489 -1 O VAL S 486 N SER S 460
SHEET 3 A 4 LEU S 495 GLU S 498 -1 O GLU S 496 N SER S 488
SHEET 4 A 4 VAL S 503 PHE S 506 -1 O GLY S 504 N GLY S 497
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 - v 10 2 Bytes