Header list of 1muz.pdb file
Complete list - b 23 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 24-SEP-02 1MUZ
TITLE NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN
TITLE 2 MELANOMA AND INTERACTION WITH C-MYC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYC BOX DEPENDENT INTERACTING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 513-593;
COMPND 5 SYNONYM: BIN1, BRIDGING INTEGRATOR 1, AMPHIPHYSIN-LIKE PROTEIN,
COMPND 6 AMPHIPHYSIN II, BOX-DEPENDENT MYC-INTERACTING PROTEIN-1;
COMPND 7 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: PET15B
KEYWDS TUMOR SUPPRESSOR, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.PINEDA-LUCENA,C.H.ARROWSMITH
REVDAT 3 23-FEB-22 1MUZ 1 REMARK
REVDAT 2 24-FEB-09 1MUZ 1 VERSN
REVDAT 1 30-SEP-03 1MUZ 0
JRNL AUTH A.PINEDA-LUCENA,C.S.HO,D.Y.MAO,Y.SHENG,R.C.LAISTER,
JRNL AUTH 2 R.MUHANDIRAM,Y.LU,B.T.SEET,S.KATZ,T.SZYPERSKI,L.Z.PENN,
JRNL AUTH 3 C.H.ARROWSMITH
JRNL TITL A STRUCTURE-BASED MODEL OF THE C-MYC/BIN1 PROTEIN
JRNL TITL 2 INTERACTION SHOWS ALTERNATIVE SPLICING OF BIN1 AND C-MYC
JRNL TITL 3 PHOSPHORYLATION ARE KEY BINDING DETERMINANTS.
JRNL REF J.MOL.BIOL. V. 351 182 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15992821
JRNL DOI 10.1016/J.JMB.2005.05.046
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, DYANA 1.5
REMARK 3 AUTHORS : DELAGIO ET AL. (NMRPIPE), GUNTERT ET AL. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000017203.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 300E-3
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM BIN1(402-482) U-15N, 13C
REMARK 210 25 MM SODIUM PHOSPHATE BUFFER,
REMARK 210 150 MM NACL, 1 MM DTT, 95% H2O,
REMARK 210 5% D2O PH=6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 1.3.14
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR NMR TECHNIQUES
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 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 462 H LYS A 465 1.48
REMARK 500 H VAL A 414 O VAL A 436 1.48
REMARK 500 H LEU A 437 O VAL A 455 1.51
REMARK 500 H GLN A 415 O GLU A 479 1.53
REMARK 500 O LEU A 466 H CYS A 469 1.56
REMARK 500 O TRP A 460 H HIS A 463 1.60
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 PHE A 410 151.75 -36.99
REMARK 500 1 MET A 411 -72.94 -110.66
REMARK 500 1 ASP A 426 45.14 -171.89
REMARK 500 1 ALA A 432 97.49 -37.53
REMARK 500 1 PHE A 441 -172.42 -59.75
REMARK 500 2 PHE A 410 149.68 -36.87
REMARK 500 2 MET A 411 -69.88 -109.59
REMARK 500 2 ASP A 426 46.73 -172.16
REMARK 500 2 ALA A 432 100.23 -39.90
REMARK 500 2 PHE A 441 -174.20 -61.34
REMARK 500 2 LYS A 465 52.09 -148.81
REMARK 500 3 ARG A 403 173.39 -56.63
REMARK 500 3 PHE A 410 152.18 -36.78
REMARK 500 3 ASP A 426 56.62 -174.49
REMARK 500 3 ALA A 432 97.17 -37.74
REMARK 500 3 PHE A 441 -171.81 -58.80
REMARK 500 3 ASN A 443 148.39 -176.09
REMARK 500 3 LYS A 465 49.16 -142.75
REMARK 500 4 PHE A 410 152.84 -36.87
REMARK 500 4 MET A 411 -72.53 -110.23
REMARK 500 4 ASP A 426 47.40 -165.32
REMARK 500 4 ALA A 432 97.64 -40.28
REMARK 500 4 PHE A 441 -173.15 -58.90
REMARK 500 4 LYS A 465 55.60 -155.82
REMARK 500 5 PHE A 410 151.63 -36.56
REMARK 500 5 MET A 411 -70.07 -111.79
REMARK 500 5 ASP A 426 46.28 -172.26
REMARK 500 5 ALA A 432 97.67 -38.24
REMARK 500 5 PHE A 441 -176.39 -58.74
REMARK 500 5 LYS A 465 49.32 -147.56
REMARK 500 6 PHE A 410 154.62 -36.47
REMARK 500 6 ASP A 426 44.96 -171.37
REMARK 500 6 ALA A 432 100.87 -39.06
REMARK 500 6 PHE A 441 -172.95 -56.33
REMARK 500 6 ASN A 443 148.04 179.52
REMARK 500 7 ARG A 403 165.39 -44.11
REMARK 500 7 PHE A 410 151.60 -36.86
REMARK 500 7 MET A 411 -71.86 -110.96
REMARK 500 7 ASP A 426 62.03 178.11
REMARK 500 7 ALA A 432 101.01 -36.81
REMARK 500 7 PHE A 441 -175.31 -59.16
REMARK 500 8 PHE A 410 153.27 -37.07
REMARK 500 8 MET A 411 -72.35 -113.93
REMARK 500 8 ASP A 426 45.36 -161.18
REMARK 500 8 ALA A 432 98.71 -36.42
REMARK 500 8 PHE A 441 -172.28 -57.05
REMARK 500 8 ASN A 443 147.94 179.01
REMARK 500 8 LYS A 465 52.10 -151.50
REMARK 500 9 PHE A 410 153.27 -36.45
REMARK 500 9 ASP A 426 42.85 -156.44
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MV0 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1 (RESIDUES 513-593) AND
REMARK 900 THE ONCOPROTEIN C-MYC (RESIDUES 55-68)
REMARK 900 RELATED ID: 1MV3 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1 ISOFORM +12A (RESIDUES
REMARK 900 301-377, 458-593)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN CRYSTALLIZED BY THE AUTHOR CONTAINS
REMARK 999 LYS465 WHICH CORRESPONDS TO GLU576 IN THE SWISS-PROT
REMARK 999 ENTRY O00499. THIS RESIDUE CONFLICT IS NOTED IN
REMARK 999 THE DATABASE REFERENCE.
DBREF 1MUZ A 402 482 UNP O00499 BIN1_HUMAN 513 593
SEQADV 1MUZ LYS A 465 UNP O00499 GLU 576 SEE REMARK 999
SEQRES 1 A 81 GLY ARG LEU ASP LEU PRO PRO GLY PHE MET PHE LYS VAL
SEQRES 2 A 81 GLN ALA GLN HIS ASP TYR THR ALA THR ASP THR ASP GLU
SEQRES 3 A 81 LEU GLN LEU LYS ALA GLY ASP VAL VAL LEU VAL ILE PRO
SEQRES 4 A 81 PHE GLN ASN PRO GLU GLU GLN ASP GLU GLY TRP LEU MET
SEQRES 5 A 81 GLY VAL LYS GLU SER ASP TRP ASN GLN HIS LYS LYS LEU
SEQRES 6 A 81 GLU LYS CYS ARG GLY VAL PHE PRO GLU ASN PHE THR GLU
SEQRES 7 A 81 ARG VAL PRO
HELIX 1 1 ASN A 443 GLN A 447 5 5
HELIX 2 2 GLU A 457 GLN A 462 1 6
HELIX 3 3 HIS A 463 CYS A 469 5 7
SHEET 1 A 5 GLY A 471 PRO A 474 0
SHEET 2 A 5 TRP A 451 LYS A 456 -1 N LEU A 452 O PHE A 473
SHEET 3 A 5 VAL A 435 VAL A 438 -1 N LEU A 437 O VAL A 455
SHEET 4 A 5 PHE A 412 ALA A 416 -1 N VAL A 414 O VAL A 436
SHEET 5 A 5 THR A 478 ARG A 480 -1 O GLU A 479 N GLN A 415
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