Header list of 1hej.pdb file
Complete list - 25 20 Bytes
HEADER HYDROLASE(XYLAN DEGRADATION) 22-NOV-00 1HEJ TITLE C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI TITLE 2 XYLANASE 11A COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE D; COMPND 3 CHAIN: C; COMPND 4 FRAGMENT: XYLAN BINDING DOMAIN 2; COMPND 5 SYNONYM: XYLANASE D, CBM2B-2, XBD2; COMPND 6 EC: 3.2.1.8; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CELLULOMONAS FIMI; SOURCE 3 ORGANISM_TAXID: 1708; SOURCE 4 STRAIN: JM83; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS HYDROLASE(XYLAN DEGRADATION), HYDROLASE, XYLAN BINDING KEYWDS 2 DOMAIN, XYLANASE, BETA-SHEET EXPDTA SOLUTION NMR NUMMDL 5 AUTHOR P.J.SIMPSON,X.HEFANG,D.N.BOLAM,P.WHITE,S.M.HANCOCK, AUTHOR 2 H.J.GILBERT,M.P.WILLIAMSON REVDAT 2 24-FEB-09 1HEJ 1 VERSN REVDAT 1 10-MAY-01 1HEJ 0 JRNL AUTH D.N.BOLAM,H.XIE,P.WHITE,P.J.SIMPSON,S.M.HANCOCK, JRNL AUTH 2 M.P.WILLIAMSON,H.J.GILBERT JRNL TITL EVIDENCE FOR SYNERGY BETWEEN FAMILY 2B JRNL TITL 2 CARBOHYDRATE BINDING MODULES IN CELLULOMONAS FIMI JRNL TITL 3 XYLANASE 11A JRNL REF BIOCHEMISTRY V. 40 2468 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11327868 JRNL DOI 10.1021/BI002564L REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: YASAP PROTOCOL. DETAILS IN THE JRNL REMARK 3 CITATION. REMARK 4 REMARK 4 1HEJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-00. REMARK 100 THE PDBE ID CODE IS EBI-5576. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.0 REMARK 210 SAMPLE CONTENTS : SODIUM PHOSPHATE 50 MM, REMARK 210 SODIUM AZIDE 10 MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY, DQF-COSY, NOESY, REMARK 210 E.COSY, HSQC, NOESY-HMQC, REMARK 210 TOCSY-HMQC, HNHA, HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 600 REMARK 210 SPECTROMETER MODEL : DRX500; DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : MSI FELIX 97.0 REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/ REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5 REMARK 210 CONFORMERS, SELECTION CRITERIA : RANDOM SELECTION OF 5 REMARK 210 FROM THE 23 LOWEST ENERGY STRUCTURES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR REMARK 210 NMR SPECTROSCOPY ON A UNIFORMLY 15N-LABELLED SAMPLE OF REMARK 210 XBD2 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 400 REMARK 400 COMPOUND REMARK 400 ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC LINKAGES IN XYLANS. REMARK 400 BELONGS TO CELLULASE FAMILY G (FAMILY 11 OF GLYCOSYL REMARK 400 HYDROLASES). 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 TRP C 570 -92.89 -132.89 REMARK 500 1 ALA C 571 -75.86 -138.83 REMARK 500 1 SER C 583 -66.82 81.33 REMARK 500 1 SER C 585 66.08 -110.98 REMARK 500 1 VAL C 587 31.92 -160.14 REMARK 500 1 LEU C 592 -167.84 -65.60 REMARK 500 1 ALA C 604 158.33 164.20 REMARK 500 1 SER C 609 29.39 -163.16 REMARK 500 1 LYS C 630 -67.14 -94.29 REMARK 500 1 CYS C 641 68.68 -160.05 REMARK 500 2 GLU C 568 152.64 -42.52 REMARK 500 2 GLU C 569 97.02 -160.08 REMARK 500 2 ASN C 575 67.60 -157.56 REMARK 500 2 SER C 584 -75.04 -44.31 REMARK 500 2 VAL C 587 29.97 -158.84 REMARK 500 2 ASN C 603 30.21 76.52 REMARK 500 2 ALA C 604 146.26 163.90 REMARK 500 2 SER C 609 35.56 -177.78 REMARK 500 2 LYS C 630 -40.99 -139.76 REMARK 500 2 CYS C 641 70.19 -160.57 REMARK 500 3 SER C 561 31.96 -99.01 REMARK 500 3 GLU C 568 160.40 -39.98 REMARK 500 3 TRP C 570 -96.76 -141.50 REMARK 500 3 ALA C 571 -72.89 -139.40 REMARK 500 3 SER C 584 -81.23 74.57 REMARK 500 3 VAL C 587 31.51 -160.88 REMARK 500 3 ALA C 604 173.36 165.28 REMARK 500 3 SER C 633 39.50 -148.20 REMARK 500 4 GLU C 568 165.00 -41.43 REMARK 500 4 TRP C 570 -100.11 -151.94 REMARK 500 4 ALA C 571 -68.89 -142.03 REMARK 500 4 SER C 583 -105.49 50.57 REMARK 500 4 SER C 584 -94.53 40.24 REMARK 500 4 LEU C 592 -168.01 -61.86 REMARK 500 4 ALA C 604 156.71 163.98 REMARK 500 4 ARG C 616 83.34 -159.96 REMARK 500 4 LYS C 630 -63.86 -97.57 REMARK 500 4 SER C 633 -150.47 -80.06 REMARK 500 4 SER C 634 -149.05 -135.30 REMARK 500 4 THR C 636 174.98 -47.15 REMARK 500 4 CYS C 641 69.96 -160.98 REMARK 500 5 GLU C 568 170.02 -44.48 REMARK 500 5 TRP C 570 -100.55 -140.70 REMARK 500 5 ALA C 571 -71.01 -143.54 REMARK 500 5 SER C 584 -2.62 76.92 REMARK 500 5 SER C 585 96.65 -160.26 REMARK 500 5 VAL C 587 31.55 -159.87 REMARK 500 5 LEU C 592 -173.37 -65.62 REMARK 500 5 ALA C 604 169.67 163.98 REMARK 500 5 SER C 609 20.95 -154.63 REMARK 500 5 LYS C 630 -29.74 174.94 REMARK 500 5 SER C 633 43.47 -156.64 REMARK 500 5 SER C 634 -153.19 170.82 REMARK 500 5 THR C 636 176.98 -53.10 REMARK 500 5 CYS C 641 85.81 -160.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG C 566 0.32 SIDE CHAIN REMARK 500 1 ARG C 573 0.30 SIDE CHAIN REMARK 500 1 ARG C 616 0.16 SIDE CHAIN REMARK 500 2 ARG C 566 0.28 SIDE CHAIN REMARK 500 2 ARG C 616 0.29 SIDE CHAIN REMARK 500 3 ARG C 566 0.31 SIDE CHAIN REMARK 500 3 ARG C 573 0.29 SIDE CHAIN REMARK 500 3 ARG C 616 0.24 SIDE CHAIN REMARK 500 4 ARG C 566 0.32 SIDE CHAIN REMARK 500 4 ARG C 573 0.31 SIDE CHAIN REMARK 500 4 ARG C 616 0.20 SIDE CHAIN REMARK 500 5 ARG C 566 0.29 SIDE CHAIN REMARK 500 5 ARG C 573 0.27 SIDE CHAIN REMARK 500 5 ARG C 616 0.15 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HEH RELATED DB: PDB REMARK 900 C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI REMARK 900 XYLANASE 11A (MINIMIZED AVERAGE STRUCTURE) REMARK 900 RELATED ID: 1E5B RELATED DB: PDB REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G REMARK 900 MUTANT REMARK 900 RELATED ID: 1E5C RELATED DB: PDB REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G REMARK 900 MUTANT REMARK 900 RELATED ID: 1XBD RELATED DB: PDB REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI REMARK 900 XYLANASE D, NMR, 5 STRUCTURES REMARK 900 RELATED ID: 2XBD RELATED DB: PDB REMARK 900 INTERNAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI REMARK 900 XYLANASE D, NMR, MINIMIZED AVERAGE STRUCTURE DBREF 1HEJ C 557 644 UNP P54865 XYND_CELFI 557 644 SEQRES 1 C 88 THR GLY SER CYS SER VAL SER ALA VAL ARG GLY GLU GLU SEQRES 2 C 88 TRP ALA ASP ARG PHE ASN VAL THR TYR SER VAL SER GLY SEQRES 3 C 88 SER SER SER TRP VAL VAL THR LEU GLY LEU ASN GLY GLY SEQRES 4 C 88 GLN SER VAL GLN SER SER TRP ASN ALA ALA LEU THR GLY SEQRES 5 C 88 SER SER GLY THR VAL THR ALA ARG PRO ASN GLY SER GLY SEQRES 6 C 88 ASN SER PHE GLY VAL THR PHE TYR LYS ASN GLY SER SER SEQRES 7 C 88 ALA THR PRO GLY ALA THR CYS ALA THR GLY SHEET 1 A 4 VAL C 562 GLU C 568 0 SHEET 2 A 4 ARG C 573 SER C 581 -1 N SER C 579 O SER C 563 SHEET 3 A 4 SER C 623 TYR C 629 -1 O PHE C 624 N TYR C 578 SHEET 4 A 4 VAL C 598 TRP C 602 -1 O TRP C 602 N GLY C 625 SHEET 1 B 4 GLY C 638 ALA C 642 0 SHEET 2 B 4 VAL C 587 LEU C 592 -1 N THR C 589 O THR C 640 SHEET 3 B 4 VAL C 613 ARG C 616 -1 O VAL C 613 N LEU C 590 SHEET 4 B 4 ALA C 605 GLY C 608 -1 O ALA C 605 N ARG C 616 SSBOND 1 CYS C 560 CYS C 641 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 - 25 20 Bytes