Header list of 1mv0.pdb file
Complete list - b 23 2 Bytes
HEADER ENDOCYTOSIS/EXOCYTOSIS, TRANSCRIPTION 24-SEP-02 1MV0 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 PROTO-ONCOGENE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 55-68; COMPND 5 SYNONYM: C-MYC, TRANSCRIPTION FACTOR P64; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MYC BOX-DEPENDENT-INTERACTING PROTEIN 1; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: RESIDUES 513-593; COMPND 11 SYNONYM: BRIDGING INTEGRATOR 1, AMPHIPHYSIN-LIKE PROTEIN, AMPHIPHYSIN COMPND 12 II, BOX-DEPENDENT; 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS TUMOR SUPPRESSOR/ONCOPROTEIN, ENDOCYTOSIS/EXOCYTOSIS, TRANSCRIPTION KEYWDS 2 COMPLEX, ENDOCYTOSIS-EXOCYTOSIS EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.PINEDA-LUCENA,C.H.ARROWSMITH REVDAT 5 23-FEB-22 1MV0 1 REMARK REVDAT 4 08-DEC-09 1MV0 1 COMPND REVDAT 3 24-FEB-09 1MV0 1 VERSN REVDAT 2 07-OCT-03 1MV0 1 ATOM REVDAT 1 30-SEP-03 1MV0 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 1MV0 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_1000017204. 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 : 1.4 MM BIN1(402-482)/C-MYC(55 REMARK 210 -68) U-15N, 13C, 25 MM SODIUM REMARK 210 PHOSPHATE, 150 MM NACL, 1 MM DTT, REMARK 210 95% H2O, 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 1.3.13 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: 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: 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 B 462 H LYS B 465 1.47 REMARK 500 H VAL B 414 O VAL B 436 1.48 REMARK 500 H LEU B 437 O VAL B 455 1.49 REMARK 500 H GLN B 415 O GLU B 479 1.52 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 B 410 146.10 -36.97 REMARK 500 1 MET B 411 -71.38 -106.94 REMARK 500 1 ASP B 426 37.91 -162.74 REMARK 500 1 ALA B 432 100.86 -31.69 REMARK 500 1 PHE B 441 -179.23 -58.00 REMARK 500 1 ASN B 443 150.94 172.73 REMARK 500 2 PHE B 410 146.66 -36.14 REMARK 500 2 MET B 411 -71.84 -106.79 REMARK 500 2 ASP B 426 35.94 -168.56 REMARK 500 2 ALA B 432 102.35 -36.34 REMARK 500 2 PHE B 441 -178.97 -57.24 REMARK 500 2 ASN B 443 150.00 171.36 REMARK 500 3 ARG B 403 -175.35 -66.10 REMARK 500 3 PHE B 410 149.70 -36.47 REMARK 500 3 MET B 411 -71.09 -110.74 REMARK 500 3 ASP B 426 40.15 -171.55 REMARK 500 3 ALA B 432 101.99 -36.01 REMARK 500 3 PHE B 441 -172.52 -56.17 REMARK 500 3 ASN B 443 148.28 -174.44 REMARK 500 4 ARG B 403 -171.72 -66.03 REMARK 500 4 PHE B 410 148.23 -36.39 REMARK 500 4 MET B 411 -71.19 -107.97 REMARK 500 4 ASP B 426 39.90 -153.69 REMARK 500 4 ALA B 432 97.66 -39.02 REMARK 500 4 PHE B 441 -173.68 -57.65 REMARK 500 5 ARG B 403 -170.33 -57.37 REMARK 500 5 PHE B 410 146.75 -36.09 REMARK 500 5 MET B 411 -71.08 -105.72 REMARK 500 5 ASP B 426 39.25 -156.93 REMARK 500 5 ALA B 432 97.26 -38.94 REMARK 500 5 PHE B 441 -177.55 -56.73 REMARK 500 5 ASN B 443 147.79 -171.43 REMARK 500 6 PHE B 410 147.43 -36.50 REMARK 500 6 MET B 411 -70.89 -104.55 REMARK 500 6 ASP B 426 59.85 -177.64 REMARK 500 6 ALA B 432 99.16 -33.76 REMARK 500 6 PHE B 441 177.98 -57.38 REMARK 500 6 ASN B 443 150.60 170.81 REMARK 500 6 LYS B 465 49.96 -140.81 REMARK 500 7 ARG B 403 -174.21 -67.76 REMARK 500 7 PHE B 410 151.17 -36.87 REMARK 500 7 MET B 411 -70.73 -111.27 REMARK 500 7 ASP B 426 32.27 -164.22 REMARK 500 7 ALA B 432 108.83 -30.15 REMARK 500 7 PHE B 441 178.75 -56.84 REMARK 500 7 ASN B 443 149.59 168.04 REMARK 500 8 SER A 67 -61.09 -93.30 REMARK 500 8 PHE B 410 147.00 -36.88 REMARK 500 8 MET B 411 -68.57 -107.75 REMARK 500 8 ASP B 426 41.45 -156.06 REMARK 500 REMARK 500 THIS ENTRY HAS 133 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 513-593) REMARK 900 RELATED ID: 1MV3 RELATED DB: PDB REMARK 900 NMR STRUCTURE OF THE TUMOR SUPPRESSOR ISOFORM BIN1 +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 1MV0 A 55 68 UNP P01106 MYC_HUMAN 55 68 DBREF 1MV0 B 402 482 UNP O00499 BIN1_HUMAN 513 593 SEQADV 1MV0 LYS B 465 UNP O00499 GLU 576 SEE REMARK 999 SEQRES 1 A 14 LEU LEU PRO THR PRO PRO LEU SER PRO SER ARG ARG SER SEQRES 2 A 14 GLY SEQRES 1 B 81 GLY ARG LEU ASP LEU PRO PRO GLY PHE MET PHE LYS VAL SEQRES 2 B 81 GLN ALA GLN HIS ASP TYR THR ALA THR ASP THR ASP GLU SEQRES 3 B 81 LEU GLN LEU LYS ALA GLY ASP VAL VAL LEU VAL ILE PRO SEQRES 4 B 81 PHE GLN ASN PRO GLU GLU GLN ASP GLU GLY TRP LEU MET SEQRES 5 B 81 GLY VAL LYS GLU SER ASP TRP ASN GLN HIS LYS LYS LEU SEQRES 6 B 81 GLU LYS CYS ARG GLY VAL PHE PRO GLU ASN PHE THR GLU SEQRES 7 B 81 ARG VAL PRO HELIX 1 1 GLU B 457 GLN B 462 1 6 HELIX 2 2 HIS B 463 CYS B 469 5 7 SHEET 1 A 5 GLY B 471 PRO B 474 0 SHEET 2 A 5 TRP B 451 LYS B 456 -1 N LEU B 452 O PHE B 473 SHEET 3 A 5 VAL B 435 VAL B 438 -1 N LEU B 437 O VAL B 455 SHEET 4 A 5 PHE B 412 ALA B 416 -1 N VAL B 414 O VAL B 436 SHEET 5 A 5 THR B 478 VAL B 481 -1 O GLU B 479 N GLN B 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