Header list of 1bm5.pdb file
Complete list - b 16 2 Bytes
HEADER RETINOIC-ACID TRANSPORT 28-JUL-98 1BM5
TITLE THE SOLUTION STRUCTURE OF A SITE-DIRECTED MUTANT (R111M) OF HUMAN
TITLE 2 CELLULAR RETIONIC ACID BINDING PROTEIN-TYPE II, NMR, 31 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-17B
KEYWDS RETINOIC-ACID TRANSPORT, CRABPII
EXPDTA SOLUTION NMR
NUMMDL 31
AUTHOR H.WANG,H.YAN
REVDAT 4 16-FEB-22 1BM5 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BM5 1 VERSN
REVDAT 2 16-FEB-99 1BM5 1 SOURCE REMARK TITLE JRNL
REVDAT 2 2 1 KEYWDS
REVDAT 1 13-JAN-99 1BM5 0
JRNL AUTH L.WANG,H.YAN
JRNL TITL NMR STUDY SUGGESTS A MAJOR ROLE FOR ARG111 IN MAINTAINING
JRNL TITL 2 THE STRUCTURE AND DYNAMICAL PROPERTIES OF TYPE II HUMAN
JRNL TITL 3 CELLULAR RETINOIC ACID BINDING PROTEIN.
JRNL REF BIOCHEMISTRY V. 37 13021 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9737883
JRNL DOI 10.1021/BI981021X
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: THE STRUCTURES WERE CALCULATED
REMARK 3 FOLLOWING THE STANDARD DISTANCE GEOMETRY-SIMULATED ANNEALING
REMARK 3 PROTOCAL IN X-PLOR 3.1. SEVERAL ROUNDS OF REFINEMENT WERE
REMARK 3 PERFORMED.
REMARK 4
REMARK 4 1BM5 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_1000171903.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : PBS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HOMONUCLEAR; 3D 15N-EDITED
REMARK 210 NMR EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : VXR500; DMX750
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 : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 31
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 SER A 12 152.37 177.74
REMARK 500 1 VAL A 24 -34.44 -164.67
REMARK 500 1 ASN A 25 -159.09 -61.71
REMARK 500 1 LYS A 38 73.46 67.34
REMARK 500 1 THR A 56 -71.73 -102.80
REMARK 500 1 THR A 57 -41.52 -172.95
REMARK 500 1 THR A 60 102.96 -164.31
REMARK 500 1 GLU A 62 125.75 -171.87
REMARK 500 1 THR A 75 -144.99 -90.18
REMARK 500 1 GLU A 88 -42.20 -130.99
REMARK 500 1 SER A 89 -153.31 -136.71
REMARK 500 1 ASN A 91 26.84 -147.93
REMARK 500 1 GLU A 103 141.73 -178.94
REMARK 500 1 GLU A 118 172.50 -55.88
REMARK 500 1 ASP A 126 -76.49 78.72
REMARK 500 1 ASP A 127 22.67 -148.25
REMARK 500 2 SER A 12 147.09 177.95
REMARK 500 2 VAL A 24 -40.65 -140.21
REMARK 500 2 ASN A 25 -165.41 -59.74
REMARK 500 2 LYS A 38 72.49 66.37
REMARK 500 2 THR A 56 -80.02 -100.37
REMARK 500 2 THR A 57 -46.43 -158.06
REMARK 500 2 THR A 60 103.47 -163.83
REMARK 500 2 GLU A 62 119.58 -171.94
REMARK 500 2 THR A 75 -152.68 -63.86
REMARK 500 2 GLU A 88 -46.56 -135.11
REMARK 500 2 SER A 89 -152.67 -129.99
REMARK 500 2 ASN A 91 25.27 -143.78
REMARK 500 2 GLU A 103 141.41 -176.26
REMARK 500 2 GLU A 118 171.30 -57.94
REMARK 500 2 ASP A 126 -78.36 77.78
REMARK 500 2 ASP A 127 24.11 -146.57
REMARK 500 3 GLU A 13 24.57 -161.79
REMARK 500 3 ASN A 14 27.82 -161.14
REMARK 500 3 VAL A 24 -39.90 -150.70
REMARK 500 3 ASN A 25 -160.69 -60.80
REMARK 500 3 LYS A 38 74.19 -151.36
REMARK 500 3 THR A 56 -158.87 -99.26
REMARK 500 3 THR A 60 95.44 -163.71
REMARK 500 3 GLU A 62 111.35 -163.34
REMARK 500 3 THR A 75 -142.14 -97.31
REMARK 500 3 GLU A 88 -45.98 -136.69
REMARK 500 3 SER A 89 -153.63 -131.81
REMARK 500 3 ASN A 91 28.53 -143.46
REMARK 500 3 GLU A 103 140.53 -175.96
REMARK 500 3 GLU A 118 173.91 -55.90
REMARK 500 3 ASP A 126 -79.31 77.15
REMARK 500 3 ASP A 127 23.91 -146.19
REMARK 500 4 SER A 12 165.43 176.29
REMARK 500 4 GLU A 13 25.77 -159.32
REMARK 500
REMARK 500 THIS ENTRY HAS 515 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 0.28 SIDE CHAIN
REMARK 500 1 ARG A 29 0.22 SIDE CHAIN
REMARK 500 1 ARG A 59 0.23 SIDE CHAIN
REMARK 500 1 ARG A 79 0.26 SIDE CHAIN
REMARK 500 1 ARG A 132 0.26 SIDE CHAIN
REMARK 500 1 ARG A 136 0.28 SIDE CHAIN
REMARK 500 2 ARG A 11 0.31 SIDE CHAIN
REMARK 500 2 ARG A 29 0.22 SIDE CHAIN
REMARK 500 2 ARG A 59 0.31 SIDE CHAIN
REMARK 500 2 ARG A 79 0.31 SIDE CHAIN
REMARK 500 2 ARG A 132 0.27 SIDE CHAIN
REMARK 500 2 ARG A 136 0.29 SIDE CHAIN
REMARK 500 3 ARG A 11 0.29 SIDE CHAIN
REMARK 500 3 ARG A 29 0.18 SIDE CHAIN
REMARK 500 3 ARG A 59 0.24 SIDE CHAIN
REMARK 500 3 ARG A 79 0.23 SIDE CHAIN
REMARK 500 3 ARG A 132 0.22 SIDE CHAIN
REMARK 500 3 ARG A 136 0.22 SIDE CHAIN
REMARK 500 4 ARG A 11 0.29 SIDE CHAIN
REMARK 500 4 ARG A 29 0.32 SIDE CHAIN
REMARK 500 4 ARG A 59 0.24 SIDE CHAIN
REMARK 500 4 ARG A 79 0.28 SIDE CHAIN
REMARK 500 4 ARG A 132 0.32 SIDE CHAIN
REMARK 500 4 ARG A 136 0.28 SIDE CHAIN
REMARK 500 5 ARG A 11 0.32 SIDE CHAIN
REMARK 500 5 ARG A 29 0.23 SIDE CHAIN
REMARK 500 5 ARG A 59 0.22 SIDE CHAIN
REMARK 500 5 ARG A 79 0.22 SIDE CHAIN
REMARK 500 5 ARG A 132 0.32 SIDE CHAIN
REMARK 500 5 ARG A 136 0.27 SIDE CHAIN
REMARK 500 6 ARG A 11 0.28 SIDE CHAIN
REMARK 500 6 ARG A 29 0.22 SIDE CHAIN
REMARK 500 6 ARG A 59 0.30 SIDE CHAIN
REMARK 500 6 ARG A 79 0.30 SIDE CHAIN
REMARK 500 6 ARG A 132 0.28 SIDE CHAIN
REMARK 500 6 ARG A 136 0.29 SIDE CHAIN
REMARK 500 7 ARG A 11 0.24 SIDE CHAIN
REMARK 500 7 ARG A 29 0.29 SIDE CHAIN
REMARK 500 7 ARG A 59 0.23 SIDE CHAIN
REMARK 500 7 ARG A 79 0.30 SIDE CHAIN
REMARK 500 7 ARG A 132 0.26 SIDE CHAIN
REMARK 500 7 ARG A 136 0.26 SIDE CHAIN
REMARK 500 8 ARG A 11 0.25 SIDE CHAIN
REMARK 500 8 ARG A 29 0.22 SIDE CHAIN
REMARK 500 8 ARG A 59 0.27 SIDE CHAIN
REMARK 500 8 ARG A 79 0.23 SIDE CHAIN
REMARK 500 8 ARG A 132 0.27 SIDE CHAIN
REMARK 500 8 ARG A 136 0.28 SIDE CHAIN
REMARK 500 9 ARG A 11 0.28 SIDE CHAIN
REMARK 500 9 ARG A 29 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 186 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BM5 A 1 137 UNP P29373 RABP2_HUMAN 1 137
SEQADV 1BM5 MET A 111 UNP P29373 ARG 111 CONFLICT
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 MET 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 LEU A 22 1 8
HELIX 2 2 MET A 27 ALA A 36 1 10
SHEET 1 A10 THR A 60 LYS A 66 0
SHEET 2 A10 THR A 49 SER A 55 -1 N THR A 54 O THR A 61
SHEET 3 A10 ALA A 40 GLN A 45 -1 N LYS A 44 O TYR A 51
SHEET 4 A10 GLY A 5 GLU A 13 -1 N TRP A 7 O VAL A 41
SHEET 5 A10 THR A 131 VAL A 135 -1 N VAL A 135 O LYS A 8
SHEET 6 A10 LEU A 119 ALA A 125 -1 N LEU A 121 O ARG A 132
SHEET 7 A10 THR A 107 LEU A 113 -1 N GLU A 112 O ILE A 120
SHEET 8 A10 LYS A 92 LEU A 99 -1 N GLN A 97 O THR A 107
SHEET 9 A10 PRO A 80 TRP A 87 -1 N LYS A 86 O VAL A 94
SHEET 10 A10 PHE A 71 GLN A 74 -1 N GLU A 73 O CYS A 81
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