Header list of 1f8z.pdb file
Complete list - 23 20 Bytes
HEADER LIPID BINDING PROTEIN 05-JUL-00 1F8Z
TITLE NMR STRUCTURE OF THE SIXTH LIGAND-BINDING MODULE OF THE LDL RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SIXTH LIGAND-BINDING MODULE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: PEPTIDE SYNTHESIS - BASED ON THE HUMAN SEQUENCE
KEYWDS LDL RECEPTOR, LIGAND-BINDING DOMAIN, CALCIUM-BINDING, FAMILIAL
KEYWDS 2 HYPERCHOLESTEROLEMIA, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.CLAYTON,I.M.BRERETON,P.A.KROON,R.SMITH
REVDAT 4 23-FEB-22 1F8Z 1 REMARK LINK
REVDAT 3 24-FEB-09 1F8Z 1 VERSN
REVDAT 2 01-APR-03 1F8Z 1 JRNL
REVDAT 1 18-OCT-00 1F8Z 0
JRNL AUTH D.CLAYTON,I.M.BRERETON,P.A.KROON,R.SMITH
JRNL TITL THREE-DIMENSIONAL NMR STRUCTURE OF THE SIXTH LIGAND-BINDING
JRNL TITL 2 MODULE OF THE HUMAN LDL RECEPTOR: COMPARISON OF TWO ADJACENT
JRNL TITL 3 MODULES WITH DIFFERENT LIGAND BINDING SPECIFICITIES.
JRNL REF FEBS LETT. V. 479 118 2000
JRNL REFN ISSN 0014-5793
JRNL PMID 10981718
JRNL DOI 10.1016/S0014-5793(00)01842-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), AXEL BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES ARE BASED ON 552 DISTANCE CONSTRAINTS, 18 BACKBONE
REMARK 3 ANGLE RESTRAINTS
REMARK 3 AND 14 SIDECHAIN ANGLE RESTRAINTS
REMARK 4
REMARK 4 1F8Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011390.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3 MM LB6, 10 MM CACL2, 1 MM
REMARK 210 3,3,3-TRIMETHYLSILYLPROPIONATE;
REMARK 210 3 MM LB6, 10 MM CACL2, 1 MM 3,3,
REMARK 210 3-TRIMETHYLSILYLPROPIONATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA, XEASY, DYANA 1.5, X
REMARK 210 -PLOR 3.1
REMARK 210 METHOD USED : STRUCTURE DETERMINATION BY
REMARK 210 TORSION ANGLE DYNAMICS,
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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 CYS A 15 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 1 CYS A 22 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 CYS A 22 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 CYS A 15 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 3 CYS A 22 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 CYS A 22 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 6 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 7 CYS A 22 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 8 CYS A 22 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 9 CYS A 22 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 11 CYS A 22 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 12 CYS A 22 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 13 CYS A 15 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 13 CYS A 22 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 14 CYS A 22 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 15 CYS A 15 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 15 CYS A 22 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 16 CYS A 22 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 17 CYS A 22 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 18 CYS A 22 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 19 CYS A 15 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 19 CYS A 22 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 20 CYS A 22 CA - CB - SG ANGL. DEV. = 7.7 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 ASP A 23 3.39 -150.33
REMARK 500 1 GLU A 25 38.03 -92.60
REMARK 500 1 TYR A 26 75.85 -2.20
REMARK 500 1 MET A 31 17.15 56.81
REMARK 500 2 CYS A 22 63.86 68.06
REMARK 500 2 ASP A 23 9.97 -150.42
REMARK 500 2 ARG A 24 28.23 43.10
REMARK 500 2 GLU A 25 41.38 -101.65
REMARK 500 2 TYR A 26 80.39 1.07
REMARK 500 2 MET A 31 17.41 55.80
REMARK 500 3 ASP A 23 3.64 -150.61
REMARK 500 3 GLU A 25 39.82 -93.95
REMARK 500 3 TYR A 26 79.06 -3.96
REMARK 500 3 MET A 31 11.17 51.23
REMARK 500 4 ASP A 23 -5.07 -141.70
REMARK 500 4 GLU A 25 44.71 -98.48
REMARK 500 4 TYR A 26 82.95 -2.60
REMARK 500 4 MET A 31 16.46 46.11
REMARK 500 5 CYS A 22 65.00 67.67
REMARK 500 5 ASP A 23 1.11 -150.48
REMARK 500 5 GLU A 25 40.48 -89.99
REMARK 500 5 TYR A 26 76.31 1.40
REMARK 500 5 MET A 31 12.54 57.51
REMARK 500 5 VAL A 38 46.80 -102.93
REMARK 500 6 ASP A 23 2.49 -150.18
REMARK 500 6 GLU A 25 43.65 -98.37
REMARK 500 6 TYR A 26 83.97 -3.66
REMARK 500 6 MET A 31 14.48 53.72
REMARK 500 6 CYS A 37 -75.50 -52.57
REMARK 500 7 ASP A 23 6.44 -150.45
REMARK 500 7 ARG A 24 29.96 48.95
REMARK 500 7 GLU A 25 41.92 -92.29
REMARK 500 7 TYR A 26 79.79 -5.74
REMARK 500 7 MET A 31 15.90 59.42
REMARK 500 8 ASP A 23 6.64 -150.60
REMARK 500 8 GLU A 25 41.76 -92.12
REMARK 500 8 TYR A 26 76.96 -6.52
REMARK 500 8 MET A 31 13.40 54.65
REMARK 500 8 VAL A 38 43.16 -95.19
REMARK 500 9 ASP A 23 9.32 -150.43
REMARK 500 9 GLU A 25 45.38 -97.83
REMARK 500 9 TYR A 26 85.73 -11.39
REMARK 500 9 MET A 31 15.65 52.17
REMARK 500 10 ASP A 23 12.17 -150.56
REMARK 500 10 ARG A 24 33.62 39.90
REMARK 500 10 GLU A 25 40.15 -96.73
REMARK 500 10 TYR A 26 76.82 1.36
REMARK 500 10 CYS A 37 -73.42 -68.87
REMARK 500 11 CYS A 22 61.59 63.48
REMARK 500 11 ASP A 23 -0.20 -143.53
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 40 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 20 O
REMARK 620 2 ASP A 23 OD1 61.5
REMARK 620 3 GLU A 25 O 138.9 117.7
REMARK 620 4 GLU A 25 N 129.9 68.5 69.3
REMARK 620 5 TYR A 26 N 179.5 118.0 41.0 49.7
REMARK 620 6 ASP A 27 OD2 62.9 113.1 84.2 148.8 117.3
REMARK 620 7 ASP A 33 OD2 87.2 140.9 101.2 134.6 93.3 65.0
REMARK 620 8 GLU A 34 OE2 70.2 66.2 150.4 87.3 109.8 122.7 82.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 40
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LDL RELATED DB: PDB
REMARK 900 1LDL CONTAINS THE FIRST LIGAND-BINDING MODULE OF THE LDL RECEPTOR
REMARK 900 RELATED ID: 1LDR RELATED DB: PDB
REMARK 900 1LDR CONTAINS THE SECOND LIGAND-BINDING MODULE OF THE LDL RECEPTOR
DBREF 1F8Z A 1 39 UNP P01130 LDLR_HUMAN 234 272
SEQRES 1 A 39 ALA THR CYS ARG PRO ASP GLU PHE GLN CYS SER ASP GLY
SEQRES 2 A 39 ASN CYS ILE HIS GLY SER ARG GLN CYS ASP ARG GLU TYR
SEQRES 3 A 39 ASP CYS LYS ASP MET SER ASP GLU VAL GLY CYS VAL ASN
HET CA A 40 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 MET A 31 VAL A 35 5 5
SHEET 1 A 2 GLU A 7 GLN A 9 0
SHEET 2 A 2 CYS A 15 HIS A 17 -1 O ILE A 16 N PHE A 8
SSBOND 1 CYS A 3 CYS A 15 1555 1555 2.02
SSBOND 2 CYS A 10 CYS A 28 1555 1555 2.02
SSBOND 3 CYS A 22 CYS A 37 1555 1555 2.02
LINK O ARG A 20 CA CA A 40 1555 1555 2.79
LINK OD1 ASP A 23 CA CA A 40 1555 1555 2.65
LINK O GLU A 25 CA CA A 40 1555 1555 3.19
LINK N GLU A 25 CA CA A 40 1555 1555 3.02
LINK N TYR A 26 CA CA A 40 1555 1555 3.25
LINK OD2 ASP A 27 CA CA A 40 1555 1555 2.64
LINK OD2 ASP A 33 CA CA A 40 1555 1555 2.63
LINK OE2 GLU A 34 CA CA A 40 1555 1555 2.62
SITE 1 AC1 7 ARG A 20 ASP A 23 GLU A 25 TYR A 26
SITE 2 AC1 7 ASP A 27 ASP A 33 GLU A 34
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 - 23 20 Bytes