Header list of 1id8.pdb file
Complete list - b 23 2 Bytes
HEADER ISOMERASE 04-APR-01 1ID8 TITLE NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH TITLE 2 THE VITAMIN B12 NUCLEOTIDE CAVEAT 1ID8 CHIRALITY ERRORS AT CENTERS OF ILE 22, VAL 60 AND LEU 23. COMPND MOL_ID: 1; COMPND 2 MOLECULE: METHYLASPARTATE MUTASE S CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GLUTAMATE MUTASE; COMPND 5 EC: 5.4.99.1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM TETANOMORPHUM; SOURCE 3 ORGANISM_TAXID: 1553; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7-7 KEYWDS COENZYME B12, LIGAND BINDING, NUCLEOTIDE, PROTEIN NMR SPECTROSCOPY, KEYWDS 2 PROTEIN FOLDING, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR M.TOLLINGER,C.EICHMULLER,R.KONRAT,M.S.HUHTA,E.N.G.MARSH,B.KRAUTLER REVDAT 4 23-FEB-22 1ID8 1 REMARK LINK REVDAT 3 24-FEB-09 1ID8 1 VERSN REVDAT 2 01-APR-03 1ID8 1 JRNL REVDAT 1 27-JUN-01 1ID8 0 JRNL AUTH M.TOLLINGER,C.EICHMULLER,R.KONRAT,M.S.HUHTA,E.N.MARSH, JRNL AUTH 2 B.KRAUTLER JRNL TITL THE B(12)-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM JRNL TITL 2 CLOSTRIDIUM TETANOMORPHUM TRAPS THE NUCLEOTIDE MOIETY OF JRNL TITL 3 COENZYME B(12). JRNL REF J.MOL.BIOL. V. 309 777 2001 JRNL REFN ISSN 0022-2836 JRNL PMID 11397096 JRNL DOI 10.1006/JMBI.2001.4696 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.E.HOLLOWAY,E.N.MARSH REMARK 1 TITL ADENOSYLCOBALAMIN-DEPENDENT GLUTAMATE MUTASE FROM REMARK 1 TITL 2 CLOSTRIDIUM TETANOMORPHUM. OVEREXPRESSION IN ESCHERICHIA REMARK 1 TITL 3 COLI, PURIFICATION, AND CHARACTERIZATION OF THE RECOMBINANT REMARK 1 TITL 4 ENZYME REMARK 1 REF J.BIOL.CHEM. V. 269 20425 1994 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.TOLLINGER,R.KONRAT,B.H.HILBERT,E.N.MARSH,B.KRAUTLER REMARK 1 TITL HOW A PROTEIN PREPARES FOR B12 BINDING: STRUCTURE AND REMARK 1 TITL 2 DYNAMICS OF THE B12-BINDING SUBUNIT OF GLUTAMATE MUTASE FROM REMARK 1 TITL 3 CLOSTRIDIUM TETANOMORPHUM REMARK 1 REF STRUCTURE V. 6 1021 1998 REMARK 1 REFN ISSN 0969-2126 REMARK 1 DOI 10.1016/S0969-2126(98)00103-8 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ANSIG 3.3, X-PLOR 3.1 REMARK 3 AUTHORS : KRAULIS (ANSIG), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ID8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013178. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 299 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 10MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM MUTS U-15N; 18.0MM B12 REMARK 210 -NUCLEOTIDE; 10MM POTASSIUM REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 3D_15N-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING, REMARK 210 MOLECULAR DYNAMICS, ENERGY REMARK 210 MINIMAZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9 REMARK 210 REMARK 210 REMARK: NULL 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 HG SER A 122 HG1 THR A 125 1.22 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 1 HIS A 25 CG HIS A 25 CD2 0.057 REMARK 500 1 SER A 42 CB SER A 42 OG 0.084 REMARK 500 4 SER A 26 CB SER A 26 OG 0.087 REMARK 500 10 SER A 26 CB SER A 26 OG 0.087 REMARK 500 11 SER A 42 CB SER A 42 OG 0.086 REMARK 500 15 HIS A 25 CG HIS A 25 CD2 0.054 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 ILE A 6 CG1 - CB - CG2 ANGL. DEV. = 17.6 DEGREES REMARK 500 1 VAL A 7 CG1 - CB - CG2 ANGL. DEV. = 9.7 DEGREES REMARK 500 1 VAL A 7 CA - CB - CG2 ANGL. DEV. = 13.4 DEGREES REMARK 500 1 LEU A 8 CB - CG - CD2 ANGL. DEV. = 10.9 DEGREES REMARK 500 1 VAL A 10 CA - CB - CG2 ANGL. DEV. = 11.6 DEGREES REMARK 500 1 ILE A 11 CG1 - CB - CG2 ANGL. DEV. = 16.5 DEGREES REMARK 500 1 VAL A 18 CG1 - CB - CG2 ANGL. DEV. = 10.8 DEGREES REMARK 500 1 VAL A 18 CA - CB - CG2 ANGL. DEV. = 12.5 DEGREES REMARK 500 1 LYS A 21 C - N - CA ANGL. DEV. = 19.7 DEGREES REMARK 500 1 ILE A 22 CG1 - CB - CG2 ANGL. DEV. = 19.4 DEGREES REMARK 500 1 LEU A 23 CD1 - CG - CD2 ANGL. DEV. = 24.1 DEGREES REMARK 500 1 VAL A 34 CA - CB - CG2 ANGL. DEV. = 14.7 DEGREES REMARK 500 1 VAL A 35 CA - CB - CG2 ANGL. DEV. = 18.3 DEGREES REMARK 500 1 ILE A 37 CG1 - CB - CG2 ANGL. DEV. = 15.3 DEGREES REMARK 500 1 VAL A 39 CG1 - CB - CG2 ANGL. DEV. = 11.6 DEGREES REMARK 500 1 VAL A 39 CA - CB - CG2 ANGL. DEV. = 13.2 DEGREES REMARK 500 1 LEU A 40 CB - CG - CD2 ANGL. DEV. = 13.2 DEGREES REMARK 500 1 ILE A 47 CG1 - CB - CG2 ANGL. DEV. = 16.7 DEGREES REMARK 500 1 ILE A 51 CG1 - CB - CG2 ANGL. DEV. = 17.5 DEGREES REMARK 500 1 LEU A 57 CB - CG - CD2 ANGL. DEV. = 10.8 DEGREES REMARK 500 1 ILE A 58 CG1 - CB - CG2 ANGL. DEV. = 17.6 DEGREES REMARK 500 1 VAL A 60 CG1 - CB - CG2 ANGL. DEV. = 14.0 DEGREES REMARK 500 1 VAL A 60 CA - CB - CG1 ANGL. DEV. = 11.4 DEGREES REMARK 500 1 LEU A 63 CB - CG - CD2 ANGL. DEV. = 10.7 DEGREES REMARK 500 1 ILE A 69 CG1 - CB - CG2 ANGL. DEV. = 16.6 DEGREES REMARK 500 1 LEU A 74 CB - CG - CD2 ANGL. DEV. = 14.8 DEGREES REMARK 500 1 LEU A 83 CB - CG - CD2 ANGL. DEV. = 13.1 DEGREES REMARK 500 1 ILE A 86 CG1 - CB - CG2 ANGL. DEV. = 19.5 DEGREES REMARK 500 1 VAL A 90 CG1 - CB - CG2 ANGL. DEV. = 11.1 DEGREES REMARK 500 1 VAL A 90 CA - CB - CG2 ANGL. DEV. = 12.6 DEGREES REMARK 500 1 ILE A 94 CG1 - CB - CG2 ANGL. DEV. = 16.7 DEGREES REMARK 500 1 VAL A 95 CG1 - CB - CG2 ANGL. DEV. = 16.3 DEGREES REMARK 500 1 VAL A 95 CA - CB - CG2 ANGL. DEV. = 10.6 DEGREES REMARK 500 1 VAL A 96 CG1 - CB - CG2 ANGL. DEV. = 10.4 DEGREES REMARK 500 1 VAL A 96 CA - CB - CG2 ANGL. DEV. = 14.6 DEGREES REMARK 500 1 VAL A 104 CG1 - CB - CG2 ANGL. DEV. = 9.6 DEGREES REMARK 500 1 VAL A 104 CA - CB - CG2 ANGL. DEV. = 13.4 DEGREES REMARK 500 1 VAL A 116 CG1 - CB - CG2 ANGL. DEV. = 10.2 DEGREES REMARK 500 1 VAL A 116 CA - CB - CG2 ANGL. DEV. = 14.5 DEGREES REMARK 500 1 ILE A 127 CG1 - CB - CG2 ANGL. DEV. = 17.6 DEGREES REMARK 500 1 VAL A 133 CA - CB - CG2 ANGL. DEV. = 14.5 DEGREES REMARK 500 1 LEU A 134 CB - CG - CD2 ANGL. DEV. = 16.4 DEGREES REMARK 500 1 VAL A 136 CG1 - CB - CG2 ANGL. DEV. = 12.7 DEGREES REMARK 500 1 VAL A 136 CA - CB - CG2 ANGL. DEV. = 13.8 DEGREES REMARK 500 2 ILE A 6 CG1 - CB - CG2 ANGL. DEV. = 19.7 DEGREES REMARK 500 2 VAL A 7 CA - CB - CG2 ANGL. DEV. = 14.4 DEGREES REMARK 500 2 LEU A 8 CB - CG - CD2 ANGL. DEV. = 15.1 DEGREES REMARK 500 2 VAL A 10 CA - CB - CG2 ANGL. DEV. = 13.5 DEGREES REMARK 500 2 ILE A 11 CG1 - CB - CG2 ANGL. DEV. = 21.0 DEGREES REMARK 500 2 VAL A 18 CG1 - CB - CG2 ANGL. DEV. = 11.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 637 ANGLE DEVIATIONS. 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 THR A 5 120.20 -174.36 REMARK 500 1 VAL A 10 -123.79 88.28 REMARK 500 1 ILE A 11 148.18 67.03 REMARK 500 1 ASP A 14 72.97 -172.52 REMARK 500 1 CYS A 15 -84.25 71.26 REMARK 500 1 HIS A 16 -65.70 -154.64 REMARK 500 1 ALA A 17 92.02 -165.34 REMARK 500 1 LYS A 21 55.38 -12.51 REMARK 500 1 VAL A 35 54.87 -140.36 REMARK 500 1 GLN A 43 -85.90 -88.16 REMARK 500 1 LYS A 54 61.09 81.15 REMARK 500 1 SER A 61 63.61 -114.39 REMARK 500 1 LEU A 63 70.59 -115.13 REMARK 500 1 TYR A 64 87.30 72.22 REMARK 500 1 GLN A 66 -14.65 -144.78 REMARK 500 1 CYS A 71 -72.13 -62.91 REMARK 500 1 LYS A 72 33.09 -90.17 REMARK 500 1 ASN A 93 94.30 25.44 REMARK 500 1 ILE A 94 123.66 69.91 REMARK 500 1 LYS A 98 105.12 -169.47 REMARK 500 1 GLN A 99 -58.94 87.14 REMARK 500 1 PRO A 102 -158.64 -68.23 REMARK 500 1 VAL A 104 -70.96 -57.81 REMARK 500 2 THR A 5 109.28 172.36 REMARK 500 2 VAL A 10 -130.16 99.63 REMARK 500 2 ILE A 11 102.34 56.09 REMARK 500 2 SER A 13 -86.68 -108.59 REMARK 500 2 CYS A 15 -133.05 63.35 REMARK 500 2 ALA A 17 -168.21 72.55 REMARK 500 2 VAL A 18 15.93 82.23 REMARK 500 2 LYS A 21 72.69 -32.57 REMARK 500 2 ILE A 22 15.66 56.40 REMARK 500 2 ILE A 37 -79.47 -89.95 REMARK 500 2 GLN A 43 -94.63 -80.81 REMARK 500 2 LYS A 54 47.36 129.69 REMARK 500 2 ALA A 55 108.36 -59.73 REMARK 500 2 ASP A 56 -82.64 -86.67 REMARK 500 2 TYR A 64 96.02 81.29 REMARK 500 2 ILE A 94 72.36 60.33 REMARK 500 2 VAL A 95 -161.89 -78.16 REMARK 500 2 VAL A 96 118.85 61.46 REMARK 500 2 GLN A 99 -53.01 98.29 REMARK 500 2 PRO A 102 -154.95 -69.34 REMARK 500 3 GLU A 2 81.92 -152.45 REMARK 500 3 LYS A 3 -159.26 -87.65 REMARK 500 3 LYS A 4 63.16 -153.59 REMARK 500 3 VAL A 10 -113.97 110.68 REMARK 500 3 ILE A 11 154.30 56.06 REMARK 500 3 SER A 13 -111.50 -151.25 REMARK 500 3 ASP A 14 -142.67 -173.24 REMARK 500 REMARK 500 THIS ENTRY HAS 330 RAMACHANDRAN OUTLIERS. 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 2 TYR A 117 0.07 SIDE CHAIN REMARK 500 7 TYR A 117 0.07 SIDE CHAIN REMARK 500 14 TYR A 117 0.09 SIDE CHAIN REMARK 500 15 TYR A 117 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOP A 138 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DBI A 139 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FMF RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE B12-BINDING SUBUNIT OF GLUTAMATE MUTASE REMARK 900 (MUTS) REMARK 900 RELATED ID: 1CB7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GLUTAMATE MUTASE (GLM) COMPLEXED WITH REMARK 900 METHYLCOBALAMIN DBREF 1ID8 A 1 137 UNP Q05488 GLMS_CLOTT 1 137 SEQRES 1 A 137 MET GLU LYS LYS THR ILE VAL LEU GLY VAL ILE GLY SER SEQRES 2 A 137 ASP CYS HIS ALA VAL GLY ASN LYS ILE LEU ASP HIS SER SEQRES 3 A 137 PHE THR ASN ALA GLY PHE ASN VAL VAL ASN ILE GLY VAL SEQRES 4 A 137 LEU SER SER GLN GLU ASP PHE ILE ASN ALA ALA ILE GLU SEQRES 5 A 137 THR LYS ALA ASP LEU ILE CYS VAL SER SER LEU TYR GLY SEQRES 6 A 137 GLN GLY GLU ILE ASP CYS LYS GLY LEU ARG GLU LYS CYS SEQRES 7 A 137 ASP GLU ALA GLY LEU LYS GLY ILE LYS LEU PHE VAL GLY SEQRES 8 A 137 GLY ASN ILE VAL VAL GLY LYS GLN ASN TRP PRO ASP VAL SEQRES 9 A 137 GLU GLN ARG PHE LYS ALA MET GLY PHE ASP ARG VAL TYR SEQRES 10 A 137 PRO PRO GLY THR SER PRO GLU THR THR ILE ALA ASP MET SEQRES 11 A 137 LYS GLU VAL LEU GLY VAL GLU HET FOP A 138 14 HET DBI A 139 39 HETNAM FOP 2-HYDROXY-PROPYL-AMMONIUM HETNAM DBI PHOSPHORIC ACID MONO-[5-(5,6-DIMETHYL-BENZOIMIDAZOL-1- HETNAM 2 DBI YL)-4-HYDROXY-2-HYDROXYMETHYL-TETRAHYDRO-FURAN-3-YL] HETNAM 3 DBI ESTER HETSYN FOP F-LOOP OF VITAMIN B12 HETSYN DBI DIMETHYLBENZIMIDAZOLE-NUCLEOTIDE FORMUL 2 FOP C3 H10 N O 1+ FORMUL 3 DBI C14 H19 N2 O7 P HELIX 1 1 ASP A 24 ASN A 29 1 6 HELIX 2 2 ASN A 48 THR A 53 1 6 HELIX 3 3 GLN A 66 ARG A 75 1 10 HELIX 4 4 ASP A 103 GLY A 112 1 10 HELIX 5 5 ALA A 128 VAL A 136 1 9 SHEET 1 A 5 VAL A 34 ASN A 36 0 SHEET 2 A 5 ILE A 6 GLY A 9 1 O ILE A 6 N VAL A 35 SHEET 3 A 5 LEU A 57 SER A 62 1 O LEU A 57 N VAL A 7 SHEET 4 A 5 LYS A 87 GLY A 92 1 O LYS A 87 N ILE A 58 SHEET 5 A 5 ASP A 114 TYR A 117 1 O ARG A 115 N VAL A 90 LINK O7 FOP A 138 P DBI A 139 1555 1555 1.59 SITE 1 AC1 2 LEU A 63 DBI A 139 SITE 1 AC2 10 ASP A 14 LEU A 23 VAL A 60 SER A 61 SITE 2 AC2 10 LEU A 63 GLY A 91 TYR A 117 PRO A 119 SITE 3 AC2 10 THR A 121 FOP A 138 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