Header list of 1cej.pdb file
Complete list - b 16 2 Bytes
HEADER SURFACE PROTEIN 08-MAR-99 1CEJ TITLE SOLUTION STRUCTURE OF AN EGF MODULE PAIR FROM THE PLASMODIUM TITLE 2 FALCIPARUM MEROZOITE SURFACE PROTEIN 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (MEROZOITE SURFACE PROTEIN 1); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT; COMPND 5 SYNONYM: MEROZOITE SURFACE ANTIGEN 1, MAJOR BLOOD-STAGE SURFACE COMPND 6 ANTIGEN; COMPND 7 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 STRAIN: SMD1168; SOURCE 6 CELL: MEROZOITE STAGE; SOURCE 7 CELLULAR_LOCATION: SECRETED; SOURCE 8 GENE: MSP-1; SOURCE 9 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: SMD1168; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PPIC9K; SOURCE 14 OTHER_DETAILS: GPI-ANCHOR KEYWDS EGF-LIKE DOMAIN, EXTRACELLULAR, MODULAR PROTEIN, SURFACE ANTIGEN, KEYWDS 2 MALARIA VACCINE COMPONENT, SURFACE PROTEIN EXPDTA SOLUTION NMR NUMMDL 32 AUTHOR W.D.MORGAN,B.BIRDSALL,T.A.FRENKIEL,M.G.GRADWELL,P.A.BURGHAUS, AUTHOR 2 S.E.H.SYED,C.UTHAIPIBULL,A.A.HOLDER,J.FEENEY REVDAT 4 16-FEB-22 1CEJ 1 REMARK REVDAT 3 24-FEB-09 1CEJ 1 VERSN REVDAT 2 01-APR-03 1CEJ 1 JRNL REVDAT 1 28-MAY-99 1CEJ 0 JRNL AUTH W.D.MORGAN,B.BIRDSALL,T.A.FRENKIEL,M.G.GRADWELL, JRNL AUTH 2 P.A.BURGHAUS,S.E.SYED,C.UTHAIPIBULL,A.A.HOLDER,J.FEENEY JRNL TITL SOLUTION STRUCTURE OF AN EGF MODULE PAIR FROM THE PLASMODIUM JRNL TITL 2 FALCIPARUM MEROZOITE SURFACE PROTEIN 1. JRNL REF J.MOL.BIOL. V. 289 113 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10339410 JRNL DOI 10.1006/JMBI.1999.2753 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-99. REMARK 100 THE DEPOSITION ID IS D_1000000605. 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 : 50 MM NAPO4, 100 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.843 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO RESTRAINT VIOLATIONS, ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 18 REMARK 210 REMARK 210 REMARK: MULTIDIMENSIONAL HETERONUCLEAR EXPERIMENTS WITH 13C,15N REMARK 210 UNIFORMLY-LABELED SAMPLE; SEE JRNL CITATION OF THIS ENTRY FOR REMARK 210 EXPERIMENTAL DETAILS 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 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 CYS A 7 144.25 66.03 REMARK 500 1 VAL A 8 101.97 -179.79 REMARK 500 1 LYS A 9 -41.05 175.08 REMARK 500 1 LYS A 10 -155.59 -98.04 REMARK 500 1 LEU A 31 -165.38 -59.96 REMARK 500 1 ASN A 33 15.47 58.07 REMARK 500 1 GLU A 37 86.97 -166.81 REMARK 500 1 PRO A 45 -33.34 -35.52 REMARK 500 1 GLU A 51 51.24 -99.78 REMARK 500 1 ASN A 52 73.08 41.96 REMARK 500 1 ASN A 53 85.14 59.68 REMARK 500 1 ASP A 57 136.77 -28.03 REMARK 500 1 ASP A 66 14.15 -159.50 REMARK 500 1 SER A 69 -167.89 -168.48 REMARK 500 1 SER A 83 108.85 -55.18 REMARK 500 1 PRO A 85 119.27 -31.17 REMARK 500 1 PHE A 87 -106.65 -132.08 REMARK 500 1 SER A 94 111.33 176.13 REMARK 500 2 ILE A 2 141.63 -176.94 REMARK 500 2 GLN A 6 137.72 66.41 REMARK 500 2 VAL A 8 -124.29 57.29 REMARK 500 2 LYS A 9 44.54 -100.24 REMARK 500 2 GLN A 14 171.52 -54.40 REMARK 500 2 ASN A 15 18.74 56.67 REMARK 500 2 ARG A 20 -115.92 -83.11 REMARK 500 2 HIS A 21 -157.14 59.59 REMARK 500 2 ASP A 23 -42.83 76.40 REMARK 500 2 GLU A 24 8.98 -161.45 REMARK 500 2 LEU A 31 -167.61 -69.52 REMARK 500 2 ASN A 33 17.09 57.89 REMARK 500 2 PRO A 45 -32.75 -35.32 REMARK 500 2 THR A 48 -159.20 -140.00 REMARK 500 2 CYS A 49 -38.81 -145.35 REMARK 500 2 ASN A 50 3.18 -69.33 REMARK 500 2 GLU A 51 60.68 -105.45 REMARK 500 2 ASN A 52 72.15 40.07 REMARK 500 2 ASN A 53 80.98 58.69 REMARK 500 2 ASP A 57 131.21 -26.25 REMARK 500 2 SER A 67 -94.74 58.71 REMARK 500 2 SER A 69 -94.65 -143.67 REMARK 500 2 ASN A 70 -48.88 -136.89 REMARK 500 2 THR A 79 36.17 -93.14 REMARK 500 2 SER A 83 102.89 -53.31 REMARK 500 2 PRO A 85 113.36 -31.40 REMARK 500 2 PHE A 87 -109.18 -153.39 REMARK 500 2 SER A 93 -92.81 -114.69 REMARK 500 2 SER A 95 -97.70 -106.95 REMARK 500 3 ILE A 2 -148.11 -92.83 REMARK 500 3 SER A 3 16.84 175.31 REMARK 500 3 HIS A 5 93.58 55.96 REMARK 500 REMARK 500 THIS ENTRY HAS 757 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1CEJ A 1 96 UNP P04933 MSP1_PLAFW 1526 1621 SEQRES 1 A 96 ASN ILE SER GLN HIS GLN CYS VAL LYS LYS GLN CYS PRO SEQRES 2 A 96 GLN ASN SER GLY CYS PHE ARG HIS LEU ASP GLU ARG GLU SEQRES 3 A 96 GLU CYS LYS CYS LEU LEU ASN TYR LYS GLN GLU GLY ASP SEQRES 4 A 96 LYS CYS VAL GLU ASN PRO ASN PRO THR CYS ASN GLU ASN SEQRES 5 A 96 ASN GLY GLY CYS ASP ALA ASP ALA LYS CYS THR GLU GLU SEQRES 6 A 96 ASP SER GLY SER ASN GLY LYS LYS ILE THR CYS GLU CYS SEQRES 7 A 96 THR LYS PRO ASP SER TYR PRO LEU PHE ASP GLY ILE PHE SEQRES 8 A 96 CYS SER SER SER ASN SHEET 1 S1 2 GLY A 17 PHE A 19 0 SHEET 2 S1 2 GLU A 27 LYS A 29 -1 N GLU A 27 O PHE A 19 SHEET 1 S2 2 LYS A 35 GLU A 37 0 SHEET 2 S2 2 LYS A 40 VAL A 42 -1 N VAL A 42 O GLN A 36 SHEET 1 S3 2 LYS A 61 THR A 63 0 SHEET 2 S3 2 THR A 75 GLU A 77 -1 N THR A 75 O THR A 63 SSBOND 1 CYS A 7 CYS A 18 1555 1555 2.02 SSBOND 2 CYS A 12 CYS A 28 1555 1555 2.02 SSBOND 3 CYS A 30 CYS A 41 1555 1555 2.02 SSBOND 4 CYS A 49 CYS A 62 1555 1555 2.02 SSBOND 5 CYS A 56 CYS A 76 1555 1555 2.02 SSBOND 6 CYS A 78 CYS A 92 1555 1555 2.02 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 16 2 Bytes