Header list of 1o1v.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 10-FEB-03 1O1V
TITLE HUMAN ILEAL LIPID-BINDING PROTEIN (ILBP) IN COMPLEX WITH CHOLYLTAURINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GASTROTROPIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GT, ILEAL LIPID-BINDING PROTEIN, ILBP, INTESTINAL 15 KDA
COMPND 5 PROTEIN, I-15P, INTESTINAL BILE ACID-BINDING PROTEIN, I-BABP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FABP6 OR ILLBP OR ILBP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHUGA1
KEYWDS BETA CLAM STRUCTURE, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.KURZ,V.BRACHVOGEL,H.MATTER,S.STENGELIN,H.THUERING,W.KRAMER
REVDAT 3 23-FEB-22 1O1V 1 REMARK
REVDAT 2 24-FEB-09 1O1V 1 VERSN
REVDAT 1 18-FEB-03 1O1V 0
JRNL AUTH M.KURZ,V.BRACHVOGEL,H.MATTER,S.STENGELIN,H.THUERING,W.KRAMER
JRNL TITL INSIGHTS INTO THE BILE ACID TRANSPORTATION SYSTEM: THE HUMAN
JRNL TITL 2 ILEAL LIPID-BINDING PROTEIN-CHOLYLTAURINE COMPLEX AND ITS
JRNL TITL 3 COMPARISON WITH HOMOLOGOUS STRUCTURES.
JRNL REF PROTEINS V. 50 312 2003
JRNL REFN ISSN 0887-3585
JRNL PMID 12486725
JRNL DOI 10.1002/PROT.10289
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, SYBYL-TRIAD 6.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), TRIPOS (SYBYL-TRIAD)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DIANA, MD, EM, STRUCTURE BASED ON 1832
REMARK 3 NONTRIVIAL NOE DISTANCES FROM 2D-NOESY INCL. 40 INTERMOLECULAR
REMARK 3 DISTANCES.
REMARK 4
REMARK 4 1O1V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000001699.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM KH2PO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : UNLABELED; UNIFORM 15N LABELED;
REMARK 210 UNIFORM 15N/13C LABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D DQF-COSY; 2D-TOCSY;
REMARK 210 2D 1H-15N HSQC; 3D-NOESY-HMQC;
REMARK 210 3D-TOCSY-HMQC; 3D HNCA; 3D HNCO;
REMARK 210 3D-HCC(CO)NH-TOCSY; 3D HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.7.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY (DIANA),
REMARK 210 MOLECULAR DYNAMICS (SYBYL),
REMARK 210 ENERGY MINIMIZATION (SYBYL)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST INTERMOLECULAR RESTRAINT
REMARK 210 VIOLATION, DIANA TARGET FUNCTION
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: 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 TRP A 49 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES
REMARK 500 4 TRP A 49 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 5 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
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 GLU A 9 -49.16 -159.73
REMARK 500 1 ASP A 43 66.77 -150.35
REMARK 500 1 GLN A 45 -38.28 88.67
REMARK 500 1 SER A 54 70.25 47.89
REMARK 500 1 MET A 74 160.29 69.42
REMARK 500 1 GLU A 86 78.28 -100.84
REMARK 500 1 TYR A 97 140.65 -172.05
REMARK 500 1 TYR A 119 73.23 -163.38
REMARK 500 2 GLU A 9 -48.27 -160.70
REMARK 500 2 ASN A 13 40.76 36.05
REMARK 500 2 ASP A 43 68.89 -158.38
REMARK 500 2 MET A 74 155.71 68.69
REMARK 500 2 TYR A 97 139.12 -171.90
REMARK 500 2 TYR A 119 69.47 -157.75
REMARK 500 3 GLU A 9 -50.36 -162.02
REMARK 500 3 ASN A 13 44.67 33.11
REMARK 500 3 SER A 54 67.81 38.61
REMARK 500 3 MET A 74 162.51 64.90
REMARK 500 3 LYS A 80 76.03 -100.78
REMARK 500 3 TYR A 97 143.26 -173.87
REMARK 500 4 GLU A 9 -50.04 -161.11
REMARK 500 4 ASN A 13 40.79 37.38
REMARK 500 4 ASP A 43 73.98 -156.20
REMARK 500 4 GLN A 45 -8.48 74.07
REMARK 500 4 SER A 54 73.29 47.03
REMARK 500 4 MET A 74 163.50 67.33
REMARK 500 5 GLU A 9 -60.77 -141.16
REMARK 500 5 ASP A 43 69.80 -153.48
REMARK 500 5 GLN A 45 -27.58 83.22
REMARK 500 5 MET A 74 171.51 61.18
REMARK 500 5 TYR A 97 142.99 -172.99
REMARK 500 5 ASP A 106 -17.49 73.55
REMARK 500 6 GLU A 9 -58.15 -145.95
REMARK 500 6 ASN A 13 45.63 30.89
REMARK 500 6 MET A 74 174.34 59.32
REMARK 500 6 TYR A 97 138.28 -172.93
REMARK 500 7 GLU A 9 -60.24 -143.47
REMARK 500 7 SER A 54 77.35 47.86
REMARK 500 7 MET A 74 176.68 60.31
REMARK 500 8 GLU A 9 -52.10 -158.73
REMARK 500 8 GLN A 45 -41.95 81.77
REMARK 500 8 SER A 54 79.48 46.99
REMARK 500 8 MET A 74 -78.92 64.41
REMARK 500 8 LEU A 90 76.31 -112.71
REMARK 500 8 ASN A 96 -47.11 162.21
REMARK 500 9 ASP A 43 64.59 -157.05
REMARK 500 9 SER A 54 75.42 50.17
REMARK 500 9 THR A 73 68.37 -111.50
REMARK 500 9 GLU A 86 64.24 -102.94
REMARK 500 9 ASN A 96 -47.09 164.39
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 TYR A 97 0.09 SIDE CHAIN
REMARK 500 2 TYR A 97 0.09 SIDE CHAIN
REMARK 500 3 TYR A 97 0.07 SIDE CHAIN
REMARK 500 3 TYR A 119 0.09 SIDE CHAIN
REMARK 500 5 TYR A 14 0.07 SIDE CHAIN
REMARK 500 5 TYR A 97 0.08 SIDE CHAIN
REMARK 500 8 TYR A 53 0.07 SIDE CHAIN
REMARK 500 8 TYR A 119 0.12 SIDE CHAIN
REMARK 500 9 TYR A 53 0.07 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 TCH A 128
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O1U RELATED DB: PDB
DBREF 1O1V A 1 127 UNP P51161 ILBP_HUMAN 1 127
SEQRES 1 A 127 ALA PHE THR GLY LYS PHE GLU MET GLU SER GLU LYS ASN
SEQRES 2 A 127 TYR ASP GLU PHE MET LYS LEU LEU GLY ILE SER SER ASP
SEQRES 3 A 127 VAL ILE GLU LYS ALA ARG ASN PHE LYS ILE VAL THR GLU
SEQRES 4 A 127 VAL GLN GLN ASP GLY GLN ASP PHE THR TRP SER GLN HIS
SEQRES 5 A 127 TYR SER GLY GLY HIS THR MET THR ASN LYS PHE THR VAL
SEQRES 6 A 127 GLY LYS GLU SER ASN ILE GLN THR MET GLY GLY LYS THR
SEQRES 7 A 127 PHE LYS ALA THR VAL GLN MET GLU GLY GLY LYS LEU VAL
SEQRES 8 A 127 VAL ASN PHE PRO ASN TYR HIS GLN THR SER GLU ILE VAL
SEQRES 9 A 127 GLY ASP LYS LEU VAL GLU VAL SER THR ILE GLY GLY VAL
SEQRES 10 A 127 THR TYR GLU ARG VAL SER LYS ARG LEU ALA
HET TCH A 128 79
HETNAM TCH TAUROCHOLIC ACID
FORMUL 2 TCH C26 H45 N O7 S
HELIX 1 1 ASN A 13 GLY A 22 1 10
HELIX 2 2 SER A 24 PHE A 34 1 11
SHEET 1 A10 HIS A 57 THR A 60 0
SHEET 2 A10 SER A 50 TYR A 53 -1 N TYR A 53 O HIS A 57
SHEET 3 A10 VAL A 37 GLN A 41 -1 N GLU A 39 O SER A 50
SHEET 4 A10 THR A 3 GLU A 11 -1 N PHE A 6 O THR A 38
SHEET 5 A10 VAL A 117 LEU A 126 -1 O LYS A 124 N GLU A 7
SHEET 6 A10 LYS A 107 ILE A 114 -1 N LEU A 108 O SER A 123
SHEET 7 A10 TYR A 97 VAL A 104 -1 N THR A 100 O VAL A 111
SHEET 8 A10 LEU A 90 PHE A 94 -1 N LEU A 90 O SER A 101
SHEET 9 A10 LYS A 77 VAL A 83 -1 N THR A 82 O ASN A 93
SHEET 10 A10 GLU A 68 THR A 73 -1 N SER A 69 O ALA A 81
SHEET 1 B 2 ASP A 46 PHE A 47 0
SHEET 2 B 2 PHE A 63 THR A 64 -1 O PHE A 63 N PHE A 47
SITE 1 AC1 10 TYR A 14 MET A 18 ILE A 23 VAL A 27
SITE 2 AC1 10 TRP A 49 TYR A 53 ASN A 61 MET A 74
SITE 3 AC1 10 LEU A 90 ARG A 121
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