Header list of 1bvh.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 03-MAY-94 1BVH TITLE SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE TITLE 2 PHOSPHATASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACID PHOSPHATASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.1.3.2; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 ORGAN: HEART; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYDROLASE EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR T.M.LOGAN,M.-M.ZHOU,D.G.NETTESHEIM,R.P.MEADOWS,R.L.VAN ETTEN, AUTHOR 2 S.W.FESIK REVDAT 3 16-FEB-22 1BVH 1 REMARK REVDAT 2 24-FEB-09 1BVH 1 VERSN REVDAT 1 31-JUL-94 1BVH 0 JRNL AUTH T.M.LOGAN,M.M.ZHOU,D.G.NETTESHEIM,R.P.MEADOWS,R.L.VAN ETTEN, JRNL AUTH 2 S.W.FESIK JRNL TITL SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN JRNL TITL 2 TYROSINE PHOSPHATASE. JRNL REF BIOCHEMISTRY V. 33 11087 1994 JRNL REFN ISSN 0006-2960 JRNL PMID 7727361 JRNL DOI 10.1021/BI00203A005 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.-M.ZHOU,T.M.LOGAN,Y.THERIAULT,R.L.VAN ETTEN,S.W.FESIK REMARK 1 TITL BACKBONE 1H, 13C, AND 15N ASSIGNMENTS AND SECONDARY REMARK 1 TITL 2 STRUCTURE OF BOVINE LOW-MOLECULAR-WEIGHT PHOSPHOTYROSYL REMARK 1 TITL 3 PROTEIN PHOSPHATASE REMARK 1 REF BIOCHEMISTRY V. 33 5221 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1BVH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000172111. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 LYS A 6 162.94 -41.93 REMARK 500 1 CYS A 12 128.03 173.08 REMARK 500 1 LEU A 13 150.09 -44.91 REMARK 500 1 CYS A 17 128.09 66.80 REMARK 500 1 ARG A 18 78.63 43.11 REMARK 500 1 SER A 19 -61.48 163.63 REMARK 500 1 GLU A 23 -71.81 -73.27 REMARK 500 1 GLN A 33 31.03 171.28 REMARK 500 1 ASN A 38 36.13 -144.46 REMARK 500 1 VAL A 46 -5.18 80.25 REMARK 500 1 SER A 54 159.60 -45.42 REMARK 500 1 ARG A 64 33.37 -96.94 REMARK 500 1 ASN A 65 -43.07 -131.50 REMARK 500 1 ASN A 69 98.30 63.52 REMARK 500 1 ALA A 71 53.55 -119.77 REMARK 500 1 ARG A 75 158.96 61.06 REMARK 500 1 VAL A 77 151.48 -47.56 REMARK 500 1 PHE A 82 -79.07 -65.65 REMARK 500 1 THR A 84 -82.90 -45.85 REMARK 500 1 TYR A 87 72.48 -109.38 REMARK 500 1 MET A 91 46.59 -85.46 REMARK 500 1 ASP A 92 -93.76 56.93 REMARK 500 1 GLU A 93 -94.73 43.53 REMARK 500 1 ASN A 95 85.87 -31.94 REMARK 500 1 LEU A 96 56.98 29.48 REMARK 500 1 ASP A 98 -64.13 -92.77 REMARK 500 1 LYS A 107 88.97 -62.53 REMARK 500 1 ASN A 108 71.06 73.99 REMARK 500 1 ARG A 110 13.58 -143.82 REMARK 500 1 LEU A 116 152.54 -43.24 REMARK 500 1 TYR A 119 -81.96 -112.27 REMARK 500 1 PRO A 121 -161.68 -71.78 REMARK 500 1 GLN A 122 36.61 -144.35 REMARK 500 1 GLU A 128 46.75 -85.55 REMARK 500 1 ASN A 134 -48.17 -169.74 REMARK 500 1 ASP A 137 120.88 -177.42 REMARK 500 1 PHE A 138 -50.32 -170.85 REMARK 500 2 GLN A 3 170.80 67.18 REMARK 500 2 LYS A 6 166.32 -42.28 REMARK 500 2 CYS A 12 114.62 177.13 REMARK 500 2 LEU A 13 156.94 -46.74 REMARK 500 2 ILE A 16 -52.03 -152.55 REMARK 500 2 ARG A 18 60.07 -171.37 REMARK 500 2 SER A 19 -51.68 163.59 REMARK 500 2 GLU A 23 -72.81 -81.92 REMARK 500 2 GLN A 33 31.63 173.56 REMARK 500 2 VAL A 46 17.56 56.24 REMARK 500 2 VAL A 51 90.10 -65.17 REMARK 500 2 SER A 54 162.49 -43.99 REMARK 500 2 ARG A 64 41.84 -93.16 REMARK 500 REMARK 500 THIS ENTRY HAS 451 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 1 ARG A 18 0.30 SIDE CHAIN REMARK 500 1 ARG A 27 0.20 SIDE CHAIN REMARK 500 1 ARG A 53 0.29 SIDE CHAIN REMARK 500 1 ARG A 58 0.15 SIDE CHAIN REMARK 500 1 ARG A 64 0.28 SIDE CHAIN REMARK 500 1 ARG A 75 0.12 SIDE CHAIN REMARK 500 1 ARG A 97 0.19 SIDE CHAIN REMARK 500 1 ARG A 101 0.27 SIDE CHAIN REMARK 500 1 ARG A 110 0.32 SIDE CHAIN REMARK 500 1 ARG A 147 0.32 SIDE CHAIN REMARK 500 1 ARG A 150 0.32 SIDE CHAIN REMARK 500 1 ARG A 157 0.15 SIDE CHAIN REMARK 500 2 ARG A 18 0.29 SIDE CHAIN REMARK 500 2 ARG A 27 0.25 SIDE CHAIN REMARK 500 2 ARG A 53 0.32 SIDE CHAIN REMARK 500 2 ARG A 58 0.31 SIDE CHAIN REMARK 500 2 ARG A 64 0.29 SIDE CHAIN REMARK 500 2 ARG A 75 0.28 SIDE CHAIN REMARK 500 2 ARG A 97 0.24 SIDE CHAIN REMARK 500 2 ARG A 101 0.31 SIDE CHAIN REMARK 500 2 ARG A 147 0.16 SIDE CHAIN REMARK 500 2 ARG A 150 0.26 SIDE CHAIN REMARK 500 2 ARG A 157 0.29 SIDE CHAIN REMARK 500 3 ARG A 18 0.27 SIDE CHAIN REMARK 500 3 ARG A 27 0.29 SIDE CHAIN REMARK 500 3 ARG A 53 0.31 SIDE CHAIN REMARK 500 3 ARG A 58 0.30 SIDE CHAIN REMARK 500 3 ARG A 64 0.30 SIDE CHAIN REMARK 500 3 ARG A 75 0.25 SIDE CHAIN REMARK 500 3 ARG A 97 0.31 SIDE CHAIN REMARK 500 3 ARG A 110 0.14 SIDE CHAIN REMARK 500 3 ARG A 147 0.32 SIDE CHAIN REMARK 500 3 ARG A 150 0.14 SIDE CHAIN REMARK 500 3 ARG A 157 0.19 SIDE CHAIN REMARK 500 4 ARG A 18 0.19 SIDE CHAIN REMARK 500 4 ARG A 27 0.28 SIDE CHAIN REMARK 500 4 ARG A 53 0.28 SIDE CHAIN REMARK 500 4 ARG A 58 0.27 SIDE CHAIN REMARK 500 4 ARG A 75 0.29 SIDE CHAIN REMARK 500 4 ARG A 97 0.08 SIDE CHAIN REMARK 500 4 ARG A 101 0.19 SIDE CHAIN REMARK 500 4 ARG A 110 0.24 SIDE CHAIN REMARK 500 4 ARG A 147 0.22 SIDE CHAIN REMARK 500 4 ARG A 150 0.21 SIDE CHAIN REMARK 500 4 ARG A 157 0.24 SIDE CHAIN REMARK 500 5 ARG A 18 0.09 SIDE CHAIN REMARK 500 5 ARG A 27 0.13 SIDE CHAIN REMARK 500 5 ARG A 53 0.31 SIDE CHAIN REMARK 500 5 ARG A 58 0.23 SIDE CHAIN REMARK 500 5 ARG A 64 0.26 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 170 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BVH A 1 157 UNP P11064 PPAC_BOVIN 1 157 SEQRES 1 A 157 ALA GLU GLN VAL THR LYS SER VAL LEU PHE VAL CYS LEU SEQRES 2 A 157 GLY ASN ILE CYS ARG SER PRO ILE ALA GLU ALA VAL PHE SEQRES 3 A 157 ARG LYS LEU VAL THR ASP GLN ASN ILE SER ASP ASN TRP SEQRES 4 A 157 VAL ILE ASP SER GLY ALA VAL SER ASP TRP ASN VAL GLY SEQRES 5 A 157 ARG SER PRO ASP PRO ARG ALA VAL SER CYS LEU ARG ASN SEQRES 6 A 157 HIS GLY ILE ASN THR ALA HIS LYS ALA ARG GLN VAL THR SEQRES 7 A 157 LYS GLU ASP PHE VAL THR PHE ASP TYR ILE LEU CYS MET SEQRES 8 A 157 ASP GLU SER ASN LEU ARG ASP LEU ASN ARG LYS SER ASN SEQRES 9 A 157 GLN VAL LYS ASN CYS ARG ALA LYS ILE GLU LEU LEU GLY SEQRES 10 A 157 SER TYR ASP PRO GLN LYS GLN LEU ILE ILE GLU ASP PRO SEQRES 11 A 157 TYR TYR GLY ASN ASP ALA ASP PHE GLU THR VAL TYR GLN SEQRES 12 A 157 GLN CYS VAL ARG CYS CYS ARG ALA PHE LEU GLU LYS VAL SEQRES 13 A 157 ARG HELIX 1 H1 PRO A 20 VAL A 30 1 11 HELIX 2 H2 PRO A 57 HIS A 66 1 10 HELIX 3 H3 LYS A 79 THR A 84 5SEE REMARK 6 6 HELIX 4 H4 LEU A 96 LYS A 102 1 7 HELIX 5 H5 GLU A 139 VAL A 156 1CYS 149 PHI APPROX. -120 DEG. 18 SHEET 1 B1 4 TRP A 39 GLY A 44 0 SHEET 2 B1 4 LYS A 6 VAL A 11 1 N PHE A 10 N GLY A 44 SHEET 3 B1 4 TYR A 87 CYS A 90 1 O TYR A 87 N LEU A 9 SHEET 4 B1 4 LYS A 112 LEU A 115 1 O LYS A 112 N ILE A 88 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