Header list of 1cx1.pdb file
Complete list - b 1 2 Bytes
HEADER HYDROLASE 27-AUG-99 1CX1 TITLE SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI TITLE 2 BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDOGLUCANASE C; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 176-328; COMPND 5 EC: 3.2.1.4; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CELLULOMONAS FIMI; SOURCE 3 ORGANISM_TAXID: 1708; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PTUG KEYWDS CELLULOSE-BINDING DOMAIN, CELLOOLIGOSACHARIDES, CELLULASE, PROTEIN- KEYWDS 2 CARBOHYDRATE INTERACTION, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 22 MDLTYP MINIMIZED AVERAGE AUTHOR E.BRUN,P.E.JOHNSON,L.A.CREAGH,C.A.HAYNES,P.TOMME,P.WEBSTER, AUTHOR 2 D.G.KILBURN,L.P.MCINTOSH REVDAT 3 01-FEB-17 1CX1 1 AUTHOR VERSN REVDAT 2 24-FEB-09 1CX1 1 VERSN REVDAT 1 02-APR-00 1CX1 0 JRNL AUTH E.BRUN,P.E.JOHNSON,A.L.CREAGH,P.TOMME,P.WEBSTER,C.A.HAYNES, JRNL AUTH 2 L.P.MCINTOSH JRNL TITL STRUCTURE AND BINDING SPECIFICITY OF THE SECOND N-TERMINAL JRNL TITL 2 CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI JRNL TITL 3 ENDOGLUCANASE C. JRNL REF BIOCHEMISTRY V. 39 2445 2000 JRNL REFN ISSN 0006-2960 JRNL PMID 10704194 JRNL DOI 10.1021/BI992079U REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.BRUN,P.E.JOHNSON,L.MACKENZIE,S.G.WITHERS,L.P.MCINTOSH REMARK 1 TITL THE CELLULOSE-BINDING DOMAINS FROM CELLULOMONAS FIMI BETA-1, REMARK 1 TITL 2 4-GLUCANASE CENC BIND NITROXIDE SPIN-LABELED REMARK 1 TITL 3 CELLOOLIGOSACCHARIDES IN MULTIPLE ORIENTATIONS REMARK 1 REF J.MOL.BIOL. V. 287 609 1999 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1999.2627 REMARK 1 REFERENCE 2 REMARK 1 AUTH P.E.JOHNSON,M.D.JOSHI,P.TOMME,D.G.KILBURN,L.P.MCINTOSH REMARK 1 TITL STRUCTURE OF THE N-TERMINAL CELLULOSE-BINDING DOMAIN OF REMARK 1 TITL 2 CELLULOMONAS FIMI CENC DETERMINED BY NUCELAR MAGNETIC REMARK 1 TITL 3 RESONANCE SPECTROSCOPY REMARK 1 REF BIOCHEMISTRY V. 35 14381 1997 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI961612S REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER, A. ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 1510 NOE DERIVED DISTANCE REMARK 3 RESTRAINTS THAT COMPRISE 700 INTRARESIDUE, 332 SEQUENTIAL, 83 REMARK 3 SHORT RANGE (1<|I-J|<=4), 394 LONG RANGE (|I-J|>4) WERE REMARK 3 INCLUDED.. 1 DISULPHIDE BOND DISTANCE RESTRAINT, 86 HYDROGEN BOND REMARK 3 RESTRAINTS, 53 PHI ANGLE RESTRAINTS, 70 PSI ANGLE RESTRAINTS, AND REMARK 3 48 CHI1 RESTRAINTS WERE ALSO INCLUDED. REMARK 4 REMARK 4 1CX1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-99. REMARK 100 THE RCSB ID CODE IS RCSB009598. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 35 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 50MMNACL REMARK 210 PRESSURE : 1ATM REMARK 210 SAMPLE CONTENTS : 1.5 TO 2 MM CBDN2 U-15N, 13C; UP REMARK 210 TO 22-FOLD MOLAR EXCESS OF REMARK 210 CELLOPENTAOSE; IN 50 MM NACL, 50 REMARK 210 MM PHOSPHATE BUFFER K AT PH* 6.5, REMARK 210 ; 1.5 TO 2 MM CBDN2 U-15N; UP TO REMARK 210 22-FOLD MOLAR EXCESS OF REMARK 210 CELLOPENTAOSE; IN 50 MM NACL, 50 REMARK 210 MM PHOSPHATE BUFFER K AT PH* 6.5, REMARK 210 ; 1.5 TO 2 MM CBDN2 UNLABELED; UP REMARK 210 TO 22-FOLD MOLAR EXCESS OF REMARK 210 CELLOPENTAOSE; IN 50 MM NACL, 50 REMARK 210 MM PHOSPHATE BUFFER K AT PH* 6.5, REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY; 2D NOESY; 4D_ REMARK 210 13C/15N-SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1A, FELIX 230, X-PLOR 3.8 REMARK 210 METHOD USED : ALL CALCULATIONS WERE PERFORMED REMARK 210 USING X-PLOR V3.8 WITH SCRIPTS REMARK 210 FROM THE X-PLOR 3.1 MANUAL A. A. REMARK 210 BRUNGER (1992), NEW HAVEN: YALE REMARK 210 UNIVERSITY PRESS ACCORDING TO THE REMARK 210 METHOD DESCRIBED BY M. NILGES, G. REMARK 210 M. CLORE & A. M. GRONENBORN REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS, REMARK 210 STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 22 REMARK 210 REMARK 210 REMARK: CBDN2 WAS STUDIED IN THE PRESENCE OF SATURATING REMARK 210 CONCENTRATIONS OF CELLOPENTAOSE. HOWEVER, DUE TO SPECTRAL REMARK 210 OVERLAP, THE OLIGOSACCHARIDE WAS NOT INCLUDED IN THE STRUCTURE REMARK 210 CALCULATIONS 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 HG1 THR A 149 H THR A 150 1.20 REMARK 500 HG1 THR A 27 H SER A 28 1.21 REMARK 500 OG1 THR A 27 H SER A 28 1.29 REMARK 500 O LYS A 135 H ALA A 138 1.30 REMARK 500 O PRO A 48 H ASP A 50 1.36 REMARK 500 O ALA A 90 H ARG A 92 1.37 REMARK 500 O THR A 103 H GLU A 105 1.40 REMARK 500 OG SER A 28 H ASP A 40 1.43 REMARK 500 HG1 THR A 71 O GLN A 145 1.52 REMARK 500 H SER A 23 O VAL A 54 1.53 REMARK 500 H MET A 37 O ILE A 143 1.59 REMARK 500 OG1 THR A 149 H THR A 150 1.60 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 SER A 2 -139.85 -72.63 REMARK 500 1 ASP A 4 115.64 -35.99 REMARK 500 1 SER A 5 101.42 59.09 REMARK 500 1 GLU A 6 168.11 -40.71 REMARK 500 1 VAL A 7 54.06 -106.87 REMARK 500 1 GLU A 8 119.37 -35.85 REMARK 500 1 PRO A 11 59.36 -67.33 REMARK 500 1 THR A 13 70.50 -170.37 REMARK 500 1 SER A 14 82.09 -161.33 REMARK 500 1 LEU A 24 123.06 -178.46 REMARK 500 1 THR A 27 -142.20 -109.90 REMARK 500 1 GLU A 29 101.75 -36.83 REMARK 500 1 PRO A 30 159.06 -48.16 REMARK 500 1 ALA A 33 -140.27 -56.26 REMARK 500 1 ASP A 34 -70.40 -35.65 REMARK 500 1 ASN A 47 96.34 -166.87 REMARK 500 1 TRP A 49 50.19 -62.95 REMARK 500 1 ASP A 50 -57.52 -133.16 REMARK 500 1 TYR A 55 148.91 -177.75 REMARK 500 1 VAL A 58 59.76 -163.21 REMARK 500 1 GLU A 62 117.40 -38.46 REMARK 500 1 PRO A 76 -141.72 -63.87 REMARK 500 1 MET A 78 163.50 166.25 REMARK 500 1 VAL A 80 -166.84 -128.50 REMARK 500 1 GLU A 86 -158.78 -90.07 REMARK 500 1 TYR A 91 -37.26 60.70 REMARK 500 1 PHE A 95 34.52 -90.97 REMARK 500 1 SER A 99 60.84 -112.33 REMARK 500 1 ALA A 107 -175.76 173.96 REMARK 500 1 ASP A 124 22.11 37.92 REMARK 500 1 ALA A 125 72.07 -151.77 REMARK 500 1 PRO A 126 -159.17 -74.22 REMARK 500 1 VAL A 129 112.98 -161.53 REMARK 500 1 LYS A 135 129.96 179.54 REMARK 500 1 ALA A 138 -145.86 -51.82 REMARK 500 1 TYR A 139 -112.11 171.89 REMARK 500 1 THR A 149 -157.92 -133.57 REMARK 500 1 THR A 150 -41.17 -139.64 REMARK 500 1 SER A 151 104.69 71.38 REMARK 500 2 SER A 2 -112.89 -91.72 REMARK 500 2 LEU A 3 -156.37 -168.10 REMARK 500 2 GLU A 6 94.91 35.89 REMARK 500 2 VAL A 7 162.77 -45.73 REMARK 500 2 PRO A 11 36.56 -53.02 REMARK 500 2 HIS A 12 138.99 -170.34 REMARK 500 2 THR A 13 70.30 -170.35 REMARK 500 2 SER A 14 77.10 -169.84 REMARK 500 2 TRP A 22 -167.62 -53.05 REMARK 500 2 THR A 27 -142.70 -109.90 REMARK 500 2 PRO A 30 154.76 -44.21 REMARK 500 REMARK 500 THIS ENTRY HAS 861 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1ULO RELATED DB: PDB REMARK 900 N-TERMINAL CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE C FROM REMARK 900 CELLULOMONAS FIMI NMR, MINIMIZED AVERAGE STRUCTURE REMARK 900 RELATED ID: 1ULP RELATED DB: PDB REMARK 900 N-TERMINAL CELLULOSE-BINDING DOMAIN OF ENDOGLUCANASE C FROM REMARK 900 CELLULOMONAS FIMI NMR ENSEMBLE 25 STRUCTURES DBREF 1CX1 A 1 153 UNP P14090 GUNC_CELFI 176 328 SEQADV 1CX1 ALA A 1 UNP P14090 VAL 176 CLONING ARTIFACT SEQADV 1CX1 SER A 2 UNP P14090 ALA 177 CLONING ARTIFACT SEQRES 1 A 153 ALA SER LEU ASP SER GLU VAL GLU LEU LEU PRO HIS THR SEQRES 2 A 153 SER PHE ALA GLU SER LEU GLY PRO TRP SER LEU TYR GLY SEQRES 3 A 153 THR SER GLU PRO VAL PHE ALA ASP GLY ARG MET CYS VAL SEQRES 4 A 153 ASP LEU PRO GLY GLY GLN GLY ASN PRO TRP ASP ALA GLY SEQRES 5 A 153 LEU VAL TYR ASN GLY VAL PRO VAL GLY GLU GLY GLU SER SEQRES 6 A 153 TYR VAL LEU SER PHE THR ALA SER ALA THR PRO ASP MET SEQRES 7 A 153 PRO VAL ARG VAL LEU VAL GLY GLU GLY GLY GLY ALA TYR SEQRES 8 A 153 ARG THR ALA PHE GLU GLN GLY SER ALA PRO LEU THR GLY SEQRES 9 A 153 GLU PRO ALA THR ARG GLU TYR ALA PHE THR SER ASN LEU SEQRES 10 A 153 THR PHE PRO PRO ASP GLY ASP ALA PRO GLY GLN VAL ALA SEQRES 11 A 153 PHE HIS LEU GLY LYS ALA GLY ALA TYR GLU PHE CYS ILE SEQRES 12 A 153 SER GLN VAL SER LEU THR THR SER ALA THR SHEET 1 A 5 SER A 23 TYR A 25 0 SHEET 2 A 5 GLY A 52 TYR A 55 -1 N GLY A 52 O TYR A 25 SHEET 3 A 5 GLN A 128 HIS A 132 -1 O VAL A 129 N TYR A 55 SHEET 4 A 5 MET A 78 GLY A 85 -1 N ARG A 81 O HIS A 132 SHEET 5 A 5 GLN A 97 LEU A 102 -1 N GLN A 97 O VAL A 82 SHEET 1 B 5 VAL A 31 PHE A 32 0 SHEET 2 B 5 MET A 37 ASP A 40 -1 N CYS A 38 O VAL A 31 SHEET 3 B 5 GLU A 140 THR A 149 -1 N PHE A 141 O VAL A 39 SHEET 4 B 5 SER A 65 ALA A 74 -1 O VAL A 67 N THR A 149 SHEET 5 B 5 ALA A 107 THR A 114 -1 O ALA A 107 N ALA A 72 SSBOND 1 CYS A 38 CYS A 142 1555 1555 2.02 CISPEP 1 THR A 75 PRO A 76 1 -0.78 CISPEP 2 THR A 75 PRO A 76 2 -0.27 CISPEP 3 THR A 75 PRO A 76 3 -0.86 CISPEP 4 THR A 75 PRO A 76 4 -0.72 CISPEP 5 THR A 75 PRO A 76 5 -0.16 CISPEP 6 THR A 75 PRO A 76 6 -0.12 CISPEP 7 THR A 75 PRO A 76 7 -0.61 CISPEP 8 THR A 75 PRO A 76 8 0.07 CISPEP 9 THR A 75 PRO A 76 9 -0.04 CISPEP 10 THR A 75 PRO A 76 10 -0.60 CISPEP 11 THR A 75 PRO A 76 11 -0.41 CISPEP 12 THR A 75 PRO A 76 12 -0.23 CISPEP 13 THR A 75 PRO A 76 13 0.48 CISPEP 14 THR A 75 PRO A 76 14 -0.34 CISPEP 15 THR A 75 PRO A 76 15 -0.24 CISPEP 16 THR A 75 PRO A 76 16 -0.32 CISPEP 17 THR A 75 PRO A 76 17 -0.19 CISPEP 18 THR A 75 PRO A 76 18 -0.95 CISPEP 19 THR A 75 PRO A 76 19 -0.98 CISPEP 20 THR A 75 PRO A 76 20 -0.26 CISPEP 21 THR A 75 PRO A 76 21 0.04 CISPEP 22 THR A 75 PRO A 76 22 -0.26 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 1 2 Bytes