Header list of 2bgp.pdb file
Complete list - 25 20 Bytes
HEADER CARBOHYDRATE BINDING PROTEIN 04-JAN-05 2BGP TITLE MANNAN BINDING MODULE FROM MAN5C IN BOUND CONFORMATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDO-B1,4-MANNANASE 5C; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 197-328; COMPND 5 SYNONYM: CBM35 FROM BETA-1,4-MANNANASE MAN5C; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: MANNAN SPECIFIC CARBOHYDRATE BINDING MODULE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CELLVIBRIO JAPONICUS; SOURCE 3 ORGANISM_TAXID: 155077; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM83 (DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET22B; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGP1 KEYWDS CARBOHYDRATE BINDING PROTEIN, MANNAN, CARBOHYDRATE BINDING KEYWDS 2 MODULE EXPDTA SOLUTION NMR NUMMDL 5 AUTHOR R.B.TUNNICLIFFE,D.N.BOLAM,G.PELL,H.J.GILBERT,M.P.WILLIAMSON REVDAT 2 24-FEB-09 2BGP 1 VERSN REVDAT 1 09-MAR-05 2BGP 0 JRNL AUTH R.B.TUNNICLIFFE,D.N.BOLAM,G.PELL,H.J.GILBERT, JRNL AUTH 2 M.P.WILLIAMSON JRNL TITL STRUCTURE OF A MANNAN-SPECIFIC FAMILY 35 JRNL TITL 2 CARBOHYDRATE-BINDING MODULE: EVIDENCE FOR JRNL TITL 3 SIGNIFICANT CONFORMATIONAL CHANGES UPON LIGAND JRNL TITL 4 BINDING JRNL REF J.MOL.BIOL. V. 347 287 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 15740741 JRNL DOI 10.1016/J.JMB.2005.01.038 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, REMARK 3 RICE,SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2BGP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JAN-05. REMARK 100 THE PDBE ID CODE IS EBI-22275. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 50MM SODIUM PHOSPHATE, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE REMARK 210 EXPERIMENTS, HNHA, REMARK 210 15N,13C-EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, CNS REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5 REMARK 210 CONFORMERS, SELECTION CRITERIA : RANDOM 5 STRUCTURES FROM REMARK 210 20 LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NONE 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 VAL A 3 REMARK 465 PRO A 4 REMARK 465 GLU A 5 REMARK 465 GLY A 6 REMARK 465 ASN A 7 REMARK 465 GLY A 124 REMARK 465 LEU A 125 REMARK 465 THR A 126 REMARK 465 ILE A 127 REMARK 465 ARG A 128 REMARK 465 SER A 129 REMARK 465 PRO A 130 REMARK 465 ALA A 131 REMARK 465 ASN A 132 REMARK 465 LEU A 133 REMARK 465 GLU A 134 REMARK 465 HIS A 135 REMARK 465 HIS A 136 REMARK 465 HIS A 137 REMARK 465 HIS A 138 REMARK 465 HIS A 139 REMARK 465 HIS A 140 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 SER A 58 - O ALA A 81 1.57 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 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 ALA A 16 -166.12 -79.86 REMARK 500 1 PRO A 21 6.44 -65.90 REMARK 500 1 GLU A 30 78.43 -158.13 REMARK 500 1 SER A 57 77.87 -160.21 REMARK 500 1 PRO A 59 47.88 -65.93 REMARK 500 1 TYR A 60 -85.01 -143.07 REMARK 500 1 SER A 61 160.70 176.40 REMARK 500 1 SER A 62 -141.07 -137.48 REMARK 500 1 ALA A 79 -162.62 -104.16 REMARK 500 1 PRO A 84 78.85 -59.61 REMARK 500 1 SER A 116 147.22 -178.29 REMARK 500 2 ALA A 20 151.45 -46.96 REMARK 500 2 PRO A 21 3.33 -67.02 REMARK 500 2 ALA A 37 133.38 -170.04 REMARK 500 2 SER A 57 109.32 -161.24 REMARK 500 2 SER A 58 84.68 -154.00 REMARK 500 2 PRO A 59 85.83 -56.13 REMARK 500 2 TYR A 60 -92.89 -117.38 REMARK 500 2 SER A 61 -106.52 -139.41 REMARK 500 2 SER A 62 144.23 -175.80 REMARK 500 2 LYS A 63 169.50 179.69 REMARK 500 2 PHE A 78 -93.72 -169.94 REMARK 500 2 ALA A 79 -153.92 -169.15 REMARK 500 2 ALA A 81 -168.56 47.46 REMARK 500 2 THR A 82 -41.66 -160.40 REMARK 500 2 PRO A 84 63.00 -67.22 REMARK 500 2 ASP A 108 67.97 -153.82 REMARK 500 2 SER A 116 137.27 -177.00 REMARK 500 3 ALA A 16 -165.25 -123.68 REMARK 500 3 PRO A 21 4.86 -67.99 REMARK 500 3 ALA A 37 107.13 -170.15 REMARK 500 3 SER A 57 81.19 -161.82 REMARK 500 3 PRO A 59 61.58 -61.59 REMARK 500 3 TYR A 60 -88.62 -166.81 REMARK 500 3 SER A 61 174.06 -45.19 REMARK 500 3 SER A 62 105.05 -173.94 REMARK 500 3 GLU A 80 88.42 -51.45 REMARK 500 3 PRO A 84 82.98 -51.27 REMARK 500 3 ASP A 108 88.36 -158.10 REMARK 500 3 SER A 116 144.62 -179.41 REMARK 500 4 ALA A 16 -165.34 -124.60 REMARK 500 4 PRO A 21 1.94 -66.82 REMARK 500 4 ALA A 37 144.24 -170.21 REMARK 500 4 SER A 57 72.26 -160.40 REMARK 500 4 PRO A 59 81.58 -53.73 REMARK 500 4 TYR A 60 -115.11 -176.12 REMARK 500 4 SER A 61 146.10 179.11 REMARK 500 4 SER A 62 -135.14 -140.73 REMARK 500 4 VAL A 64 140.14 -38.12 REMARK 500 4 PRO A 84 81.74 -54.00 REMARK 500 4 TYR A 111 132.28 -37.94 REMARK 500 5 ALA A 16 -166.12 -79.86 REMARK 500 5 PRO A 21 6.44 -65.90 REMARK 500 5 GLU A 30 78.43 -158.13 REMARK 500 5 SER A 57 77.87 -160.21 REMARK 500 5 PRO A 59 47.88 -65.93 REMARK 500 5 TYR A 60 -85.01 -143.07 REMARK 500 5 SER A 61 160.70 176.40 REMARK 500 5 SER A 62 -141.07 -137.48 REMARK 500 5 ALA A 79 -162.62 -104.16 REMARK 500 5 PRO A 84 78.85 -59.61 REMARK 500 5 SER A 116 147.22 -178.29 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2BGP RELATED DB: PDB REMARK 900 MANNAN BINDING MODULE FROM MAN5C IN BOUND REMARK 900 CONFORMATION REMARK 999 REMARK 999 SEQUENCE REMARK 999 PROTEIN SEQUENCE STARTS AT RESIDUE 204 OF FULL LENGTH REMARK 999 PROTEIN. ACTUAL PROTEIN SAMPLE CONTAINED RESIDUES 197-328 REMARK 999 PLUS HIS-TAG SEQUENCE LEHHHHHH AT C-TERMINUS. DBREF 2BGP A 1 132 UNP Q840C0 Q840C0 197 328 DBREF 2BGP A 133 140 PDB 2BGP 2BGP 133 140 SEQRES 1 A 140 MET ALA VAL PRO GLU GLY ASN SER TRP THR TYR THR ALA SEQRES 2 A 140 ALA SER ALA SER ILE THR ALA PRO ALA GLN LEU VAL GLY SEQRES 3 A 140 ASN VAL GLY GLU LEU GLN GLY ALA GLY SER ALA VAL ILE SEQRES 4 A 140 TRP ASN VAL ASP VAL PRO VAL THR GLY GLU TYR ARG ILE SEQRES 5 A 140 ASN LEU THR TRP SER SER PRO TYR SER SER LYS VAL ASN SEQRES 6 A 140 THR LEU VAL MET ASP GLY THR ALA LEU SER TYR ALA PHE SEQRES 7 A 140 ALA GLU ALA THR VAL PRO VAL THR TYR VAL GLN THR LYS SEQRES 8 A 140 THR LEU SER ALA GLY ASN HIS SER PHE GLY VAL ARG VAL SEQRES 9 A 140 GLY SER SER ASP TRP GLY TYR MET ASN VAL HIS SER LEU SEQRES 10 A 140 LYS LEU GLU LEU LEU GLY GLY LEU THR ILE ARG SER PRO SEQRES 11 A 140 ALA ASN LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 ALA A 13 SER A 15 5 SHEET 1 AA 4 SER A 8 THR A 12 0 SHEET 2 AA 4 SER A 116 GLY A 123 -1 O LEU A 117 N TYR A 11 SHEET 3 AA 4 THR A 47 TRP A 56 -1 O ARG A 51 N GLU A 120 SHEET 4 AA 4 VAL A 85 ALA A 95 -1 O VAL A 85 N TRP A 56 SHEET 1 AB 5 ALA A 16 THR A 19 0 SHEET 2 AB 5 ALA A 37 VAL A 44 -1 O ALA A 37 N THR A 19 SHEET 3 AB 5 GLY A 96 VAL A 104 -1 O GLY A 96 N VAL A 44 SHEET 4 AB 5 SER A 62 ASP A 70 -1 O THR A 66 N ARG A 103 SHEET 5 AB 5 THR A 72 GLU A 80 -1 O THR A 72 N MET A 69 SHEET 1 AC 3 GLN A 23 GLY A 26 0 SHEET 2 AC 3 VAL A 28 GLN A 32 -1 O GLU A 30 N GLN A 23 SHEET 3 AC 3 TYR A 111 HIS A 115 -1 O MET A 112 N LEU A 31 CISPEP 1 ALA A 20 PRO A 21 1 0.71 CISPEP 2 ALA A 20 PRO A 21 2 0.40 CISPEP 3 ALA A 20 PRO A 21 3 0.49 CISPEP 4 ALA A 20 PRO A 21 4 0.48 CISPEP 5 ALA A 20 PRO A 21 5 0.71 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 - 25 20 Bytes