Header list of 1mv3.pdb file
Complete list - b 23 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS 24-SEP-02 1MV3 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: ISOFORM BIN1+12A (RESIDUES 301-377, 458-594); 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 1MV3 1 REMARK REVDAT 2 24-FEB-09 1MV3 1 VERSN REVDAT 1 30-SEP-03 1MV3 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 : DELAGLIO ET AL. (NMRPIPE), GUNTERT ET AL. (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MV3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-02. REMARK 100 THE DEPOSITION ID IS D_1000017207. 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 : 1.3 MM BIN1(270-482,+12A) U-15N, REMARK 210 13C, 25 MM SODIUM PHOSPHATE, 150 REMARK 210 MM NACL, 1 MM DTT, 95 % H2O, 5% REMARK 210 D2O 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 1.3.13 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 H LEU A 437 O VAL A 455 1.44 REMARK 500 O GLN A 462 H LYS A 465 1.48 REMARK 500 H GLN A 415 O GLU A 479 1.49 REMARK 500 H VAL A 414 O VAL A 436 1.51 REMARK 500 O LEU A 466 H CYS A 469 1.55 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 A 272 115.30 -161.85 REMARK 500 1 LEU A 297 70.90 -151.70 REMARK 500 1 HIS A 316 -70.69 -125.89 REMARK 500 1 THR A 317 112.62 -166.76 REMARK 500 1 GLN A 326 149.81 -173.51 REMARK 500 1 ASP A 333 165.95 174.38 REMARK 500 1 THR A 334 145.21 -172.47 REMARK 500 1 PHE A 335 -173.94 -177.56 REMARK 500 1 VAL A 336 99.69 56.45 REMARK 500 1 SER A 340 124.29 175.97 REMARK 500 1 GLN A 346 114.12 -177.68 REMARK 500 1 PRO A 347 -162.48 -75.00 REMARK 500 1 GLU A 349 173.55 179.28 REMARK 500 1 VAL A 353 -64.93 -137.45 REMARK 500 1 ALA A 354 165.27 65.42 REMARK 500 1 THR A 357 63.55 39.97 REMARK 500 1 GLN A 358 92.75 -178.40 REMARK 500 1 ALA A 361 -61.54 -156.41 REMARK 500 1 GLU A 368 141.51 61.12 REMARK 500 1 SER A 376 165.79 174.78 REMARK 500 1 SER A 377 177.14 174.15 REMARK 500 1 LEU A 379 90.96 -170.92 REMARK 500 1 PRO A 380 -169.41 -75.01 REMARK 500 1 PRO A 388 -165.81 -75.04 REMARK 500 1 ALA A 389 134.88 177.18 REMARK 500 1 VAL A 391 136.22 -170.71 REMARK 500 1 GLU A 396 83.40 -178.18 REMARK 500 1 SER A 399 87.21 56.30 REMARK 500 1 ALA A 401 131.95 -172.03 REMARK 500 1 PHE A 410 147.11 -36.54 REMARK 500 1 ASP A 426 42.31 -170.19 REMARK 500 1 ALA A 432 97.94 -38.26 REMARK 500 1 PHE A 441 -176.15 -59.00 REMARK 500 1 LYS A 465 42.86 -140.33 REMARK 500 2 PRO A 285 -166.34 -74.99 REMARK 500 2 THR A 292 111.33 -162.63 REMARK 500 2 ALA A 295 174.27 179.91 REMARK 500 2 THR A 296 158.09 62.57 REMARK 500 2 LEU A 297 69.20 69.30 REMARK 500 2 SER A 302 69.02 -106.99 REMARK 500 2 LEU A 304 89.56 -170.54 REMARK 500 2 LYS A 306 151.00 75.45 REMARK 500 2 THR A 317 114.27 61.21 REMARK 500 2 GLU A 321 114.60 -161.37 REMARK 500 2 LYS A 323 68.07 -152.39 REMARK 500 2 GLN A 326 89.77 -167.85 REMARK 500 2 GLU A 338 -167.39 -58.20 REMARK 500 2 ILE A 339 -48.51 -149.34 REMARK 500 2 SER A 340 106.14 64.88 REMARK 500 2 THR A 342 80.06 40.61 REMARK 500 REMARK 500 THIS ENTRY HAS 767 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MUZ RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1 (RESIDUES 513-193) REMARK 900 RELATED ID: 1MV0 RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1 (RESIDUES 513-193) AND REMARK 900 THE ONCOPROTEIN C-MYC (RESIDUES 55-68) REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE BIN1(-10,+12A) ISOFORM CRYSTALLIZED BY THE AUTHOR CONTAINS REMARK 999 RESIDUES 301-377 AND 458-594 OF THE BIN1 SEQUENCE PRESENT REMARK 999 IN THE SWISS-PROT REFERENCE DATABASE (ACCESION O00499). REMARK 999 THIS ISOFORM IS MISSING RESIDUES 378 TO 457 OF THE BIN1 REMARK 999 SEQUENCE AND THEREFORE THE BIN1(-10,+12A) SEQUENCE MATCHES REMARK 999 DISCONTINUOUSLY WITH THE REFERENCE DATABASE. DBREF 1MV3 A 270 346 UNP O00499 BIN1_HUMAN 301 377 DBREF 1MV3 A 347 482 UNP O00499 BIN1_HUMAN 458 593 SEQRES 1 A 213 ASP GLY SER PRO ALA ALA THR PRO GLU ILE ARG VAL ASN SEQRES 2 A 213 HIS GLU PRO GLU PRO ALA GLY GLY ALA THR PRO GLY ALA SEQRES 3 A 213 THR LEU PRO LYS SER PRO SER GLN LEU ARG LYS GLY PRO SEQRES 4 A 213 PRO VAL PRO PRO PRO PRO LYS HIS THR PRO SER LYS GLU SEQRES 5 A 213 VAL LYS GLN GLU GLN ILE LEU SER LEU PHE GLU ASP THR SEQRES 6 A 213 PHE VAL PRO GLU ILE SER VAL THR THR PRO SER GLN PRO SEQRES 7 A 213 ALA GLU ALA SER GLU VAL ALA GLY GLY THR GLN PRO ALA SEQRES 8 A 213 ALA GLY ALA GLN GLU PRO GLY GLU THR ALA ALA SER GLU SEQRES 9 A 213 ALA ALA SER SER SER LEU PRO ALA VAL VAL VAL GLU THR SEQRES 10 A 213 PHE PRO ALA THR VAL ASN GLY THR VAL GLU GLY GLY SER SEQRES 11 A 213 GLY ALA GLY ARG LEU ASP LEU PRO PRO GLY PHE MET PHE SEQRES 12 A 213 LYS VAL GLN ALA GLN HIS ASP TYR THR ALA THR ASP THR SEQRES 13 A 213 ASP GLU LEU GLN LEU LYS ALA GLY ASP VAL VAL LEU VAL SEQRES 14 A 213 ILE PRO PHE GLN ASN PRO GLU GLU GLN ASP GLU GLY TRP SEQRES 15 A 213 LEU MET GLY VAL LYS GLU SER ASP TRP ASN GLN HIS LYS SEQRES 16 A 213 LYS LEU GLU LYS CYS ARG GLY VAL PHE PRO GLU ASN PHE SEQRES 17 A 213 THR GLU 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 VAL A 481 -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