Header list of 1blr.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSPORT 20-JUL-98 1BLR TITLE NMR SOLUTION STRUCTURE OF HUMAN CELLULAR RETINOIC ACID BINDING TITLE 2 PROTEIN-TYPE II, 22 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELL_LINE: BL21 (DE3)/PLYSS; SOURCE 6 GENE: CRABP-II; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3)/PLYSS; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET17B/PLYSS KEYWDS CRABPII, VITAMIN A, TRANSPORT EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR L.WANG,Y.LI,F.ABILDDARD,H.YAN,J.MARKELY REVDAT 3 16-FEB-22 1BLR 1 REMARK REVDAT 2 24-FEB-09 1BLR 1 VERSN REVDAT 1 13-JAN-99 1BLR 0 JRNL AUTH L.WANG,Y.LI,F.ABILDGAARD,J.L.MARKLEY,H.YAN JRNL TITL NMR SOLUTION STRUCTURE OF TYPE II HUMAN CELLULAR RETINOIC JRNL TITL 2 ACID BINDING PROTEIN: IMPLICATIONS FOR LIGAND BINDING. JRNL REF BIOCHEMISTRY V. 37 12727 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9737849 JRNL DOI 10.1021/BI9808924 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.J.KLEYWEGT,T.BERGFORS,H.SENN,P.LE MOTTE,B.GSELL,K.SHUDO, REMARK 1 AUTH 2 T.A.JONES REMARK 1 TITL CRYSTAL STRUCTURES OF CELLULAR RETINOIC ACID BINDING REMARK 1 TITL 2 PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID REMARK 1 TITL 3 AND A SYNTHETIC RETINOID REMARK 1 REF STRUCTURE V. 2 1241 1994 REMARK 1 REFN ISSN 0969-2126 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: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 1BLR 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_1000171896. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.3 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; TRIPLE RESONANCE REMARK 210 EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA500; DMX-500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : DGSA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 70 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: MODEL 1 - THE RESONANCES WERE DETERMINED BY MEANS OF REMARK 210 TRIPLE-RESONANCE NMR EXPERIMENTS ON 13C, 15N-LABELED CRABPII 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 ASN A 2 -143.36 76.54 REMARK 500 1 PHE A 3 -49.31 80.36 REMARK 500 1 ARG A 11 110.90 68.54 REMARK 500 1 GLU A 13 66.23 -159.11 REMARK 500 1 ASN A 25 65.61 -179.36 REMARK 500 1 VAL A 26 -15.85 90.22 REMARK 500 1 LEU A 28 73.16 44.84 REMARK 500 1 LYS A 30 26.49 42.72 REMARK 500 1 ILE A 31 49.71 28.64 REMARK 500 1 ALA A 32 -40.01 -175.18 REMARK 500 1 ALA A 34 -84.03 175.09 REMARK 500 1 ALA A 35 107.98 177.51 REMARK 500 1 SER A 37 -161.46 -124.45 REMARK 500 1 THR A 56 -42.19 -147.67 REMARK 500 1 THR A 57 -42.51 -162.65 REMARK 500 1 PHE A 65 -160.97 -113.08 REMARK 500 1 VAL A 67 140.50 -30.99 REMARK 500 1 GLU A 73 -177.50 -173.10 REMARK 500 1 CYS A 81 137.33 -172.08 REMARK 500 1 LEU A 84 119.88 -166.24 REMARK 500 1 GLU A 88 -55.38 -136.67 REMARK 500 1 SER A 89 -53.03 -121.13 REMARK 500 1 GLU A 90 -33.91 168.87 REMARK 500 1 CYS A 95 73.43 -163.98 REMARK 500 1 LEU A 100 14.17 59.72 REMARK 500 1 LYS A 101 -48.40 -170.01 REMARK 500 1 SER A 108 170.44 171.42 REMARK 500 1 ASN A 115 -90.50 59.18 REMARK 500 1 ASP A 116 34.47 -169.42 REMARK 500 1 MET A 123 93.55 -161.97 REMARK 500 1 ALA A 125 105.36 -175.79 REMARK 500 1 ASP A 127 -11.49 97.12 REMARK 500 2 ASN A 2 -142.64 73.73 REMARK 500 2 PHE A 3 -46.44 80.47 REMARK 500 2 ARG A 11 124.33 64.21 REMARK 500 2 GLU A 13 61.91 -177.99 REMARK 500 2 ASN A 25 69.50 -179.77 REMARK 500 2 VAL A 26 -13.19 87.79 REMARK 500 2 LEU A 28 71.46 47.27 REMARK 500 2 LYS A 30 26.18 43.17 REMARK 500 2 ILE A 31 37.47 32.60 REMARK 500 2 ALA A 32 -43.31 -162.46 REMARK 500 2 VAL A 33 89.37 -67.37 REMARK 500 2 ALA A 34 39.48 176.86 REMARK 500 2 SER A 55 -166.65 -117.32 REMARK 500 2 THR A 56 -44.04 -148.96 REMARK 500 2 THR A 57 -45.17 -150.64 REMARK 500 2 GLU A 62 138.33 -171.95 REMARK 500 2 PHE A 65 -161.96 -123.57 REMARK 500 2 ASP A 77 115.75 178.43 REMARK 500 REMARK 500 THIS ENTRY HAS 670 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 11 0.21 SIDE CHAIN REMARK 500 1 ARG A 29 0.31 SIDE CHAIN REMARK 500 1 ARG A 59 0.32 SIDE CHAIN REMARK 500 1 ARG A 79 0.27 SIDE CHAIN REMARK 500 1 ARG A 111 0.20 SIDE CHAIN REMARK 500 1 ARG A 132 0.32 SIDE CHAIN REMARK 500 1 ARG A 136 0.24 SIDE CHAIN REMARK 500 2 ARG A 11 0.29 SIDE CHAIN REMARK 500 2 ARG A 29 0.28 SIDE CHAIN REMARK 500 2 ARG A 59 0.31 SIDE CHAIN REMARK 500 2 ARG A 79 0.21 SIDE CHAIN REMARK 500 2 ARG A 111 0.26 SIDE CHAIN REMARK 500 2 ARG A 132 0.25 SIDE CHAIN REMARK 500 2 ARG A 136 0.30 SIDE CHAIN REMARK 500 3 ARG A 11 0.26 SIDE CHAIN REMARK 500 3 ARG A 29 0.31 SIDE CHAIN REMARK 500 3 ARG A 59 0.30 SIDE CHAIN REMARK 500 3 ARG A 79 0.23 SIDE CHAIN REMARK 500 3 ARG A 111 0.22 SIDE CHAIN REMARK 500 3 ARG A 132 0.27 SIDE CHAIN REMARK 500 3 ARG A 136 0.31 SIDE CHAIN REMARK 500 4 ARG A 11 0.31 SIDE CHAIN REMARK 500 4 ARG A 29 0.31 SIDE CHAIN REMARK 500 4 ARG A 59 0.23 SIDE CHAIN REMARK 500 4 ARG A 79 0.25 SIDE CHAIN REMARK 500 4 ARG A 111 0.23 SIDE CHAIN REMARK 500 4 ARG A 132 0.28 SIDE CHAIN REMARK 500 4 ARG A 136 0.25 SIDE CHAIN REMARK 500 5 ARG A 11 0.32 SIDE CHAIN REMARK 500 5 ARG A 29 0.25 SIDE CHAIN REMARK 500 5 ARG A 59 0.30 SIDE CHAIN REMARK 500 5 ARG A 79 0.23 SIDE CHAIN REMARK 500 5 ARG A 111 0.21 SIDE CHAIN REMARK 500 5 ARG A 132 0.23 SIDE CHAIN REMARK 500 5 ARG A 136 0.32 SIDE CHAIN REMARK 500 6 ARG A 11 0.25 SIDE CHAIN REMARK 500 6 ARG A 29 0.24 SIDE CHAIN REMARK 500 6 ARG A 59 0.30 SIDE CHAIN REMARK 500 6 ARG A 79 0.23 SIDE CHAIN REMARK 500 6 ARG A 111 0.16 SIDE CHAIN REMARK 500 6 ARG A 132 0.32 SIDE CHAIN REMARK 500 6 ARG A 136 0.31 SIDE CHAIN REMARK 500 7 ARG A 11 0.30 SIDE CHAIN REMARK 500 7 ARG A 29 0.26 SIDE CHAIN REMARK 500 7 ARG A 59 0.32 SIDE CHAIN REMARK 500 7 ARG A 79 0.32 SIDE CHAIN REMARK 500 7 ARG A 111 0.21 SIDE CHAIN REMARK 500 7 ARG A 132 0.23 SIDE CHAIN REMARK 500 7 ARG A 136 0.22 SIDE CHAIN REMARK 500 8 ARG A 11 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 154 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BLR A 1 137 UNP P29373 RABP2_HUMAN 1 137 SEQRES 1 A 137 PRO ASN PHE SER GLY ASN TRP LYS ILE ILE ARG SER GLU SEQRES 2 A 137 ASN PHE GLU GLU LEU LEU LYS VAL LEU GLY VAL ASN VAL SEQRES 3 A 137 MET LEU ARG LYS ILE ALA VAL ALA ALA ALA SER LYS PRO SEQRES 4 A 137 ALA VAL GLU ILE LYS GLN GLU GLY ASP THR PHE TYR ILE SEQRES 5 A 137 LYS THR SER THR THR VAL ARG THR THR GLU ILE ASN PHE SEQRES 6 A 137 LYS VAL GLY GLU GLU PHE GLU GLU GLN THR VAL ASP GLY SEQRES 7 A 137 ARG PRO CYS LYS SER LEU VAL LYS TRP GLU SER GLU ASN SEQRES 8 A 137 LYS MET VAL CYS GLU GLN LYS LEU LEU LYS GLY GLU GLY SEQRES 9 A 137 PRO LYS THR SER TRP THR ARG GLU LEU THR ASN ASP GLY SEQRES 10 A 137 GLU LEU ILE LEU THR MET THR ALA ASP ASP VAL VAL CYS SEQRES 11 A 137 THR ARG VAL TYR VAL ARG GLU HELIX 1 1 PHE A 15 VAL A 21 1 7 HELIX 2 2 ARG A 29 ILE A 31 5 3 SHEET 1 A 4 THR A 49 LYS A 53 0 SHEET 2 A 4 VAL A 41 GLU A 46 -1 N GLU A 46 O THR A 49 SHEET 3 A 4 GLY A 5 SER A 12 -1 N TRP A 7 O VAL A 41 SHEET 4 A 4 ARG A 132 ARG A 136 -1 N VAL A 135 O LYS A 8 SHEET 1 B 2 GLU A 70 GLN A 74 0 SHEET 2 B 2 PRO A 80 LEU A 84 -1 N SER A 83 O PHE A 71 SHEET 1 C 2 VAL A 85 TRP A 87 0 SHEET 2 C 2 MET A 93 CYS A 95 -1 N VAL A 94 O LYS A 86 SHEET 1 D 2 THR A 107 GLU A 112 0 SHEET 2 D 2 ILE A 120 ALA A 125 -1 N THR A 124 O SER A 108 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