Header list of 1m7k.pdb file
Complete list - b 23 2 Bytes
HEADER CHAPERONE 22-JUL-02 1M7K TITLE SOLUTION STRUCTURE OF THE SODD BAG DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SILENCER OF DEATH DOMAINS; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 358-456; COMPND 5 SYNONYM: BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-4; COMPND 6 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 BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1 KEYWDS THREE HELIX BUNDLE, CHAPERONE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.BROCKMANN,D.LEITNER,D.LABUDDE,A.DIEHL,V.SIEVERT,K.BUESSOW, AUTHOR 2 H.OSCHKINAT REVDAT 5 23-FEB-22 1M7K 1 REMARK REVDAT 4 24-FEB-09 1M7K 1 VERSN REVDAT 3 08-FEB-05 1M7K 1 JRNL REVDAT 2 18-SEP-02 1M7K 1 AUTHOR REVDAT 1 07-AUG-02 1M7K 0 JRNL AUTH C.BROCKMANN,D.LEITNER,D.LABUDDE,A.DIEHL,V.SIEVERT,K.BUESSOW, JRNL AUTH 2 R.KUHNE,H.OSCHKINAT JRNL TITL THE SOLUTION STRUCTURE OF THE SODD BAG DOMAIN REVEALS JRNL TITL 2 ADDITIONAL ELECTROSTATIC INTERACTIONS IN THE HSP70 COMPLEXES JRNL TITL 3 OF SODD SUBFAMILY BAG DOMAINS JRNL REF FEBS LETT. V. 558 101 2004 JRNL REFN ISSN 0014-5793 JRNL PMID 14759524 JRNL DOI 10.1016/S0014-5793(03)01490-X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, ADAMS, CLORE, DELANO, REMARK 3 GROS, GROSSE-KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, REMARK 3 PANNU, READ, RICE, SIMONSON, WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CALCULATED FROM 723 NOE RESTRAINTS, 52 REMARK 3 FROM HYDROGEN BONDS AND 140 DIHEDRAL RESTRAINTS REMARK 4 REMARK 4 1M7K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-02. REMARK 100 THE DEPOSITION ID IS D_1000016694. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.4MM SODD U-15N,13C; 20MM REMARK 210 PHOSPHATE BUFFER, PH6.0; 50MM REMARK 210 NACL;; 1.4MM SODD U-15N,13C; REMARK 210 20MM PHOSPHATE BUFFER, NA; 50MM REMARK 210 NACL; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D_13C-METHYL_ REMARK 210 SELECTIVE_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, SPARKY 3.1 REMARK 210 METHOD USED : TORSION ANGLE SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 400 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: 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: 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 ASN A 358 REMARK 465 GLN A 359 REMARK 465 ASP A 360 REMARK 465 GLN A 361 REMARK 465 SER A 362 REMARK 465 SER A 363 REMARK 465 SER A 364 REMARK 465 LEU A 365 REMARK 465 PRO A 366 REMARK 465 GLU A 367 REMARK 465 GLU A 368 REMARK 465 CYS A 369 REMARK 465 VAL A 370 REMARK 465 PRO A 371 REMARK 465 SER A 372 REMARK 465 ASP A 373 REMARK 465 GLU A 374 REMARK 465 SER A 375 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 PRO A 377 101.20 -45.23 REMARK 500 1 ILE A 380 -32.34 -37.59 REMARK 500 1 SER A 425 37.96 -96.05 REMARK 500 2 PRO A 377 -177.16 -53.44 REMARK 500 2 LYS A 404 47.11 -90.55 REMARK 500 2 LEU A 412 -70.83 -56.36 REMARK 500 2 GLU A 427 74.01 -66.84 REMARK 500 3 SER A 425 38.02 -93.72 REMARK 500 4 PRO A 377 -175.06 -52.61 REMARK 500 4 LEU A 412 -71.33 -57.46 REMARK 500 4 SER A 425 38.20 -95.89 REMARK 500 4 GLU A 427 79.81 -114.84 REMARK 500 5 SER A 425 37.94 -96.99 REMARK 500 6 GLN A 431 96.43 -59.77 REMARK 500 7 SER A 425 38.07 -97.43 REMARK 500 7 THR A 428 76.18 -165.46 REMARK 500 8 PRO A 377 102.50 -47.36 REMARK 500 9 PRO A 377 105.09 -48.87 REMARK 500 9 PHE A 400 158.75 -46.46 REMARK 500 9 SER A 425 38.27 -86.94 REMARK 500 9 THR A 428 -48.94 -131.82 REMARK 500 10 PRO A 377 170.71 -52.33 REMARK 500 10 THR A 405 -31.24 -131.92 REMARK 500 10 SER A 425 38.08 -94.38 REMARK 500 11 LEU A 412 -71.68 -51.58 REMARK 500 11 SER A 425 38.15 -89.90 REMARK 500 12 ILE A 380 -33.44 -37.80 REMARK 500 12 SER A 425 38.09 -94.12 REMARK 500 12 GLN A 431 108.40 -59.14 REMARK 500 13 PRO A 377 106.53 -57.50 REMARK 500 13 ILE A 380 -32.32 -38.09 REMARK 500 13 SER A 425 38.12 -95.59 REMARK 500 13 GLU A 427 72.34 -108.30 REMARK 500 14 PRO A 377 106.72 -56.74 REMARK 500 14 PRO A 378 96.82 -64.08 REMARK 500 14 LYS A 404 62.70 -68.82 REMARK 500 15 LEU A 412 -71.48 -53.61 REMARK 500 16 PRO A 378 70.27 -65.48 REMARK 500 16 GLN A 431 105.87 -160.36 REMARK 500 17 PRO A 378 57.75 -68.09 REMARK 500 17 GLU A 427 -74.37 -67.00 REMARK 500 17 THR A 428 80.31 56.06 REMARK 500 18 PRO A 377 106.29 -51.93 REMARK 500 18 ILE A 380 -32.13 -39.52 REMARK 500 18 GLU A 427 -64.06 -132.45 REMARK 500 18 THR A 428 -75.67 64.76 REMARK 500 19 PRO A 377 -173.91 -51.57 REMARK 500 19 PRO A 378 40.71 -81.94 REMARK 500 19 SER A 425 38.12 -94.88 REMARK 500 20 LEU A 412 -70.37 -58.27 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1M7K A 358 456 UNP O95429 BAG4_HUMAN 358 456 SEQRES 1 A 99 ASN GLN ASP GLN SER SER SER LEU PRO GLU GLU CYS VAL SEQRES 2 A 99 PRO SER ASP GLU SER THR PRO PRO SER ILE LYS LYS ILE SEQRES 3 A 99 ILE HIS VAL LEU GLU LYS VAL GLN TYR LEU GLU GLN GLU SEQRES 4 A 99 VAL GLU GLU PHE VAL GLY LYS LYS THR ASP LYS ALA TYR SEQRES 5 A 99 TRP LEU LEU GLU GLU MET LEU THR LYS GLU LEU LEU GLU SEQRES 6 A 99 LEU ASP SER VAL GLU THR GLY GLY GLN ASP SER VAL ARG SEQRES 7 A 99 GLN ALA ARG LYS GLU ALA VAL CYS LYS ILE GLN ALA ILE SEQRES 8 A 99 LEU GLU LYS LEU GLU LYS LYS GLY HELIX 1 1 SER A 379 PHE A 400 1 22 HELIX 2 2 ASP A 406 ASP A 424 1 19 HELIX 3 3 GLN A 431 LYS A 455 1 25 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