Header list of 1k7b.pdb file
Complete list - 5 20 Bytes
HEADER MEMBRANE PROTEIN 18-OCT-01 1K7B
TITLE NMR SOLUTION STRUCTURE OF STVA47, THE VIRAL-BINDING DOMAIN OF TVA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBGROUP A ROUS SARCOMA VIRUS RECEPTOR PG800 AND PG950;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE EXTRACELLULAR VIRAL-BINDING DOMAIN;
COMPND 5 SYNONYM: LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX COTURNIX;
SOURCE 3 ORGANISM_COMMON: COMMON QUAIL;
SOURCE 4 ORGANISM_TAXID: 9091;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: MBP-FUSION PMAL
KEYWDS BETA HAIRPIN, 3-10 HELIX, CALCIUM BINDING, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.TONELLI,R.J.PETERS,T.L.JAMES,D.A.AGARD
REVDAT 4 05-FEB-20 1K7B 1 REMARK SEQADV ATOM
REVDAT 3 24-FEB-09 1K7B 1 VERSN
REVDAT 2 01-APR-03 1K7B 1 JRNL
REVDAT 1 19-DEC-01 1K7B 0
JRNL AUTH M.TONELLI,R.J.PETERS,T.L.JAMES,D.A.AGARD
JRNL TITL THE SOLUTION STRUCTURE OF THE VIRAL BINDING DOMAIN OF TVA,
JRNL TITL 2 THE CELLULAR RECEPTOR FOR SUBGROUP A AVIAN LEUKOSIS AND
JRNL TITL 3 SARCOMA VIRUS.
JRNL REF FEBS LETT. V. 509 161 2001
JRNL REFN ISSN 0014-5793
JRNL PMID 11768384
JRNL DOI 10.1016/S0014-5793(01)03086-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, DYANA 1.5, AMBER 6.0
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT (DYANA), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 1016 NOE-DERIVED RESTRAINTS: 120 INTRA, 346 SEQUENTIAL, 268 MEDIUM
REMARK 3 AND 282 LONG-RANGE RESTRAINTS.
REMARK 3 THE FIRST 5 RESIDUES (S5-G9) SHOW ONLY INTRA-RESIDUE AND
REMARK 3 SEQUENTIAL NOE CONNECTIVITES AND WERE NOT INCLUDED IN OUR
REMARK 3 STRUCTURAL CALCULATIONS.
REMARK 4
REMARK 4 1K7B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014650.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0.065
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~2MM STVA47 15N,13C; 50MM D3
REMARK 210 -NAACETATE; 5MM CALCIUM CLORIDE;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; DMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6X, SPARKY 3
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS (DYANA) FOLLOWED
REMARK 210 BY MOLECULAR DYNAMICS (AMBER)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ILE A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 PHE A 8
REMARK 465 GLY A 9
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 50 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 CYS A 50 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 CYS A 50 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 4 CYS A 50 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 CYS A 50 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 6 CYS A 50 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 7 CYS A 50 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 8 CYS A 50 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 9 CYS A 50 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 10 CYS A 50 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 11 CYS A 50 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 12 CYS A 50 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 13 CYS A 50 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 14 CYS A 50 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 15 CYS A 50 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 16 CYS A 50 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 17 CYS A 50 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 18 CYS A 50 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 18 GLY A 51 CA - C - O ANGL. DEV. = 41.0 DEGREES
REMARK 500 19 CYS A 50 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 20 CYS A 50 CA - CB - SG ANGL. DEV. = 7.5 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 CYS A 11 -143.38 -140.22
REMARK 500 1 CYS A 18 -87.81 -84.56
REMARK 500 1 TRP A 33 42.81 -91.61
REMARK 500 1 ASP A 40 4.44 -150.66
REMARK 500 1 ASP A 42 -1.24 50.96
REMARK 500 1 CYS A 50 27.26 44.91
REMARK 500 2 CYS A 11 -157.73 -147.13
REMARK 500 2 CYS A 18 -88.32 -85.65
REMARK 500 2 CYS A 28 179.20 -59.19
REMARK 500 2 TRP A 33 41.91 -92.76
REMARK 500 2 ASP A 40 -1.78 -144.16
REMARK 500 2 ASP A 42 -1.29 50.54
REMARK 500 2 CYS A 50 28.08 45.50
REMARK 500 3 CYS A 11 -155.84 -147.26
REMARK 500 3 CYS A 18 -90.18 -89.17
REMARK 500 3 CYS A 28 -178.32 -66.61
REMARK 500 3 TRP A 33 42.82 -92.97
REMARK 500 3 ASP A 40 4.36 -150.29
REMARK 500 3 ASP A 42 -2.77 50.49
REMARK 500 3 CYS A 50 25.31 46.47
REMARK 500 4 CYS A 11 -157.07 -149.68
REMARK 500 4 CYS A 18 -90.92 -91.46
REMARK 500 4 CYS A 28 -178.33 -69.31
REMARK 500 4 TRP A 33 43.06 -92.60
REMARK 500 4 ASP A 40 5.61 -150.28
REMARK 500 4 ASP A 42 -2.95 50.31
REMARK 500 5 CYS A 18 -92.56 -90.20
REMARK 500 5 ALA A 24 71.26 -113.87
REMARK 500 5 CYS A 28 -179.28 -69.79
REMARK 500 5 TRP A 33 43.82 -93.42
REMARK 500 5 ASP A 40 4.73 -150.52
REMARK 500 5 ASP A 42 -3.24 49.78
REMARK 500 5 CYS A 50 29.37 44.34
REMARK 500 6 CYS A 18 -89.46 -91.70
REMARK 500 6 TRP A 33 43.20 -92.65
REMARK 500 6 ASP A 42 -2.03 50.53
REMARK 500 6 CYS A 50 28.56 45.17
REMARK 500 7 CYS A 18 -90.38 -89.72
REMARK 500 7 TRP A 33 43.06 -93.04
REMARK 500 7 ASP A 42 -3.03 50.49
REMARK 500 7 CYS A 50 29.92 45.09
REMARK 500 8 CYS A 18 -89.63 -91.93
REMARK 500 8 CYS A 28 -180.00 -66.00
REMARK 500 8 TRP A 33 43.24 -92.54
REMARK 500 8 ASP A 40 3.92 -150.23
REMARK 500 8 ASP A 42 -1.63 50.18
REMARK 500 9 CYS A 18 -90.09 -87.20
REMARK 500 9 TRP A 33 43.40 -92.14
REMARK 500 9 ASP A 40 4.59 -150.28
REMARK 500 9 ASP A 42 -2.88 50.74
REMARK 500
REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5210 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT FILE
DBREF 1K7B A 11 51 UNP P98162 RSVR_COTJA 30 70
SEQADV 1K7B ILE A 5 UNP P98162 CLONING ARTIFACT
SEQADV 1K7B SER A 6 UNP P98162 CLONING ARTIFACT
SEQADV 1K7B GLU A 7 UNP P98162 CLONING ARTIFACT
SEQADV 1K7B PHE A 8 UNP P98162 CLONING ARTIFACT
SEQADV 1K7B GLY A 9 UNP P98162 CLONING ARTIFACT
SEQADV 1K7B SER A 10 UNP P98162 CLONING ARTIFACT
SEQRES 1 A 47 ILE SER GLU PHE GLY SER CYS PRO PRO GLY GLN PHE ARG
SEQRES 2 A 47 CYS SER GLU PRO PRO GLY ALA HIS GLY GLU CYS TYR PRO
SEQRES 3 A 47 GLN ASP TRP LEU CYS ASP GLY HIS PRO ASP CYS ASP ASP
SEQRES 4 A 47 GLY ARG ASP GLU TRP GLY CYS GLY
HELIX 1 1 ASP A 32 LEU A 34 5 3
HELIX 2 2 GLU A 47 GLY A 51 5 5
SHEET 1 A 2 GLN A 15 PHE A 16 0
SHEET 2 A 2 TYR A 29 PRO A 30 -1 O TYR A 29 N PHE A 16
SSBOND 1 CYS A 11 CYS A 28 1555 1555 2.04
SSBOND 2 CYS A 18 CYS A 41 1555 1555 2.04
SSBOND 3 CYS A 35 CYS A 50 1555 1555 2.02
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 - 5 20 Bytes