Header list of 1hn6.pdb file
Complete list - b 23 2 Bytes
HEADER MEMBRANE PROTEIN 07-DEC-00 1HN6 TITLE SOLUTION STRUCTURE OF PLASMODIUM FALCIPARUM APICAL MEMBRANE ANTIGEN 1 TITLE 2 (RESIDUES 436-545) COMPND MOL_ID: 1; COMPND 2 MOLECULE: APICAL MEMBRANE ANTIGEN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DOMAIN III (RESIDUES 436-545); COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM; SOURCE 3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM; SOURCE 4 ORGANISM_TAXID: 5833; SOURCE 5 GENE: PF83; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DISULPHIDE CONNECTIVITIES, MEMBRANE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.NAIR REVDAT 3 23-FEB-22 1HN6 1 REMARK REVDAT 2 24-FEB-09 1HN6 1 VERSN REVDAT 1 09-OCT-02 1HN6 0 JRNL AUTH M.NAIR,M.G.HINDS,A.M.COLEY,A.N.HODDER,M.FOLEY,R.F.ANDERS, JRNL AUTH 2 R.S.NORTON JRNL TITL STRUCTURE OF DOMAIN III OF THE BLOOD-STAGE MALARIA VACCINE JRNL TITL 2 CANDIDATE, PLASMODIUM FALCIPARUM APICAL MEMBRANE ANTIGEN 1 JRNL TITL 3 (AMA1). JRNL REF J.MOL.BIOL. V. 322 741 2002 JRNL REFN ISSN 0022-2836 JRNL PMID 12270711 JRNL DOI 10.1016/S0022-2836(02)00806-9 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, CNS 1.0 REMARK 3 AUTHORS : GUENTERT (DYANA), BRUENGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 668 NOE DERIVED RESTRAINTS, SIX HYDROGEN BOND RESTRAINTS AND 172 REMARK 3 DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1HN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-00. REMARK 100 THE DEPOSITION ID IS D_1000012459. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 3.4 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM PF AMA1 U-15N, 1MM PF AMA1 U REMARK 210 -15N, 13C; 1MM PF AMA1 U-15N, 13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 1.3, XEASY 1.3.13, TALOS REMARK 210 1999 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 256 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ANGLE INFORMATION DERIVED FROM ANALYSIS OF HNHA, HNHB AND REMARK 210 3D NOE DATA RECORDED AT SHORT MIXING TIMES. 1H,13C AND 15N REMARK 210 CHEMICAL SHIFT DATA USED IN SOFTWARE PROGRAM TALOS TO CALCULATE REMARK 210 ADDITIONAL ANGLES. 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 OD2 ASP A 467 HZ1 LYS A 473 1.55 REMARK 500 OE2 GLU A 495 HZ1 LYS A 508 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 ARG A 456 -108.25 -82.47 REMARK 500 1 GLU A 457 -140.61 -81.48 REMARK 500 1 LYS A 459 -120.75 -84.22 REMARK 500 1 ASP A 465 -48.84 72.72 REMARK 500 1 ASP A 467 -32.99 -167.61 REMARK 500 1 ASN A 471 -77.12 -130.25 REMARK 500 1 CYS A 490 112.42 -165.33 REMARK 500 1 PRO A 491 30.90 -85.31 REMARK 500 1 ASP A 493 122.35 71.23 REMARK 500 1 ASN A 499 -92.51 55.82 REMARK 500 1 THR A 501 -13.45 -156.45 REMARK 500 1 LYS A 508 16.58 -155.07 REMARK 500 1 ARG A 512 -76.16 -150.53 REMARK 500 1 ASN A 519 108.30 -169.60 REMARK 500 1 ASN A 520 -64.25 -109.00 REMARK 500 1 GLU A 521 48.86 -145.73 REMARK 500 1 ALA A 533 49.14 -84.84 REMARK 500 1 LYS A 539 160.96 69.25 REMARK 500 1 PRO A 540 -132.92 -91.13 REMARK 500 1 TYR A 542 98.85 -59.90 REMARK 500 1 ASP A 543 -141.73 -97.24 REMARK 500 1 LYS A 544 -65.22 73.11 REMARK 500 2 VAL A 437 -111.08 -142.29 REMARK 500 2 ASN A 439 42.36 -82.62 REMARK 500 2 CYS A 443 -68.95 -90.83 REMARK 500 2 GLU A 453 -73.37 -85.61 REMARK 500 2 ILE A 454 -149.43 171.11 REMARK 500 2 ASP A 465 -139.38 62.30 REMARK 500 2 ASN A 466 -158.03 -138.78 REMARK 500 2 ILE A 481 -39.96 -130.22 REMARK 500 2 CYS A 490 113.25 -163.76 REMARK 500 2 PRO A 491 33.24 -84.78 REMARK 500 2 ASP A 493 155.20 68.17 REMARK 500 2 PRO A 494 68.65 -100.15 REMARK 500 2 ASN A 499 -91.72 64.10 REMARK 500 2 LYS A 508 15.31 -143.54 REMARK 500 2 GLU A 511 -140.41 -144.63 REMARK 500 2 ASP A 530 -34.10 -133.79 REMARK 500 2 HIS A 538 -65.89 -149.83 REMARK 500 2 LYS A 539 133.20 72.24 REMARK 500 2 THR A 541 -154.52 -164.30 REMARK 500 2 LYS A 544 79.76 -108.89 REMARK 500 3 ASN A 439 -70.81 -168.05 REMARK 500 3 CYS A 443 -73.62 -93.27 REMARK 500 3 ASP A 448 -162.45 -178.95 REMARK 500 3 GLU A 455 -94.12 -90.54 REMARK 500 3 GLU A 457 102.14 -49.29 REMARK 500 3 LEU A 463 -129.76 -140.54 REMARK 500 3 ASN A 466 -40.90 177.00 REMARK 500 3 ASP A 467 68.03 32.50 REMARK 500 REMARK 500 THIS ENTRY HAS 455 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4787 RELATED DB: BMRB REMARK 900 4787 IS CHEMICAL SHIFT DATA DBREF 1HN6 A 436 545 UNP Q94661 Q94661_PLAFA 436 545 SEQRES 1 A 110 GLU VAL GLU ASN ASN PHE PRO CYS SER LEU TYR LYS ASP SEQRES 2 A 110 GLU ILE MET LYS GLU ILE GLU ARG GLU SER LYS ARG ILE SEQRES 3 A 110 LYS LEU ASN ASP ASN ASP ASP GLU GLY ASN LYS LYS ILE SEQRES 4 A 110 ILE ALA PRO ARG ILE PHE ILE SER ASP ASP LYS ASP SER SEQRES 5 A 110 LEU LYS CYS PRO CYS ASP PRO GLU MET VAL SER ASN SER SEQRES 6 A 110 THR CYS ARG PHE PHE VAL CYS LYS CYS VAL GLU ARG ARG SEQRES 7 A 110 ALA GLU VAL THR SER ASN ASN GLU VAL VAL VAL LYS GLU SEQRES 8 A 110 GLU TYR LYS ASP GLU TYR ALA ASP ILE PRO GLU HIS LYS SEQRES 9 A 110 PRO THR TYR ASP LYS MET HELIX 1 1 PRO A 442 ASP A 448 1 7 SHEET 1 A 2 GLU A 495 VAL A 497 0 SHEET 2 A 2 PHE A 504 VAL A 506 -1 O PHE A 504 N VAL A 497 SSBOND 1 CYS A 443 CYS A 502 1555 1555 2.04 SSBOND 2 CYS A 490 CYS A 507 1555 1555 2.03 SSBOND 3 CYS A 492 CYS A 509 1555 1555 2.03 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