Header list of 1jrf.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN, MEMBRANE PROTEIN 13-AUG-01 1JRF
TITLE NMR SOLUTION STRUCTURE OF THE VIRAL RECEPTOR DOMAIN OF TVA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUBGROUP A ROUS SARCOMA VIRUS RECEPTORS PG800 AND PG950;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LDL-A DOMAIN;
COMPND 5 SYNONYM: TVA LDL-A MODULE; LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX JAPONICA;
SOURCE 3 ORGANISM_COMMON: JAPANESE QUAIL;
SOURCE 4 ORGANISM_TAXID: 93934;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS DISULFIDE BOND, ALPHA HELIX, CALCIUM CAGE, SIGNALING PROTEIN,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.-Y.WANG,W.HUANG,K.DOLMER,P.G.W.GETTINS,L.RONG
REVDAT 4 23-FEB-22 1JRF 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1JRF 1 VERSN
REVDAT 2 01-APR-03 1JRF 1 JRNL
REVDAT 1 08-MAR-02 1JRF 0
JRNL AUTH Q.Y.WANG,W.HUANG,K.DOLMER,P.G.GETTINS,L.RONG
JRNL TITL SOLUTION STRUCTURE OF THE VIRAL RECEPTOR DOMAIN OF TVA AND
JRNL TITL 2 ITS IMPLICATIONS IN VIRAL ENTRY.
JRNL REF J.VIROL. V. 76 2848 2002
JRNL REFN ISSN 0022-538X
JRNL PMID 11861852
JRNL DOI 10.1128/JVI.76.6.2848-2856.2002
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA 1.4, DIANA 1.4
REMARK 3 AUTHORS : GUNTERT, P. (DIANA), GUNTERT, P. (DIANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JRF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014103.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 282
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM TVA LDL-A MODULE U-15N 13C;
REMARK 210 20MM CH3COOH, 10MM CACL2, AND 10%
REMARK 210 D2O, PH 5.3; 2MM TVA LDL-A
REMARK 210 MODULE U-15N; 20MM CD3COOD, 10MM
REMARK 210 CACL2, AND 99% D2O, PH 5.3; 2MM
REMARK 210 TVA LDL-A MODULE 14N; 20MM
REMARK 210 CH3COOH, 10MM CACL2, AND 99% D2O,
REMARK 210 PH 5.3; 2MM TVA LDL-A MODULE U-
REMARK 210 15N, 13C; 20MM CD3COOD, 10MM
REMARK 210 CACL2, AND 99% D2O, PH 5.3; 2MM
REMARK 210 TVA LDL-A MODULE U-15N; 20MM
REMARK 210 CH3COOH, 10MM CACL2, AND 10% D2O,
REMARK 210 PH 5.3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HNCACB; 15N-TOCSY; 1H-15N
REMARK 210 HSQC; 2D NOESY; HCCH-NOESY;
REMARK 210 NOESY-HSQC
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 : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 41 CA CA A 48 0.63
REMARK 500 H GLY A 31 OE1 GLU A 41 1.53
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 SER A 2 154.61 -41.21
REMARK 500 1 CYS A 5 73.16 179.49
REMARK 500 1 PHE A 10 -158.21 -65.11
REMARK 500 1 CYS A 12 56.62 74.85
REMARK 500 1 SER A 13 10.27 -146.35
REMARK 500 1 GLU A 14 109.55 174.10
REMARK 500 1 HIS A 19 85.33 179.07
REMARK 500 1 CYS A 22 -78.19 -129.57
REMARK 500 1 CYS A 29 80.59 39.38
REMARK 500 1 ASP A 30 -51.67 -137.88
REMARK 500 1 ASP A 34 38.24 -146.16
REMARK 500 1 TRP A 42 -77.08 -51.42
REMARK 500 1 CYS A 44 -47.99 -147.48
REMARK 500 2 SER A 3 90.87 44.36
REMARK 500 2 CYS A 5 74.86 178.84
REMARK 500 2 PHE A 10 -158.86 -71.56
REMARK 500 2 CYS A 12 56.83 75.82
REMARK 500 2 GLU A 14 108.41 175.06
REMARK 500 2 HIS A 19 84.42 179.26
REMARK 500 2 CYS A 22 -74.43 -136.75
REMARK 500 2 CYS A 29 78.51 49.22
REMARK 500 2 ASP A 30 -62.00 -139.64
REMARK 500 2 ASP A 34 35.24 -142.49
REMARK 500 2 ASP A 37 -55.04 -122.16
REMARK 500 2 GLU A 41 31.39 -147.79
REMARK 500 2 TRP A 42 -86.34 -51.17
REMARK 500 3 SER A 2 126.42 -178.08
REMARK 500 3 SER A 3 74.81 59.24
REMARK 500 3 CYS A 5 73.83 179.18
REMARK 500 3 PHE A 10 -156.16 -61.00
REMARK 500 3 CYS A 12 49.88 76.25
REMARK 500 3 GLU A 14 113.81 176.43
REMARK 500 3 HIS A 19 84.69 178.85
REMARK 500 3 CYS A 22 -73.28 -142.74
REMARK 500 3 CYS A 29 78.60 47.04
REMARK 500 3 ASP A 30 -62.52 -139.91
REMARK 500 3 CYS A 35 -161.49 -122.29
REMARK 500 3 ASP A 37 -56.20 -132.33
REMARK 500 3 TRP A 42 -89.15 -52.30
REMARK 500 4 SER A 2 -46.30 -147.95
REMARK 500 4 SER A 3 -67.85 -131.87
REMARK 500 4 CYS A 5 75.26 178.93
REMARK 500 4 PHE A 10 -156.47 -63.53
REMARK 500 4 CYS A 12 51.28 75.38
REMARK 500 4 GLU A 14 113.43 176.24
REMARK 500 4 HIS A 19 86.38 178.68
REMARK 500 4 CYS A 22 -74.34 -144.01
REMARK 500 4 CYS A 29 75.76 49.50
REMARK 500 4 ASP A 30 -62.42 -137.49
REMARK 500 4 CYS A 35 -168.25 -116.48
REMARK 500
REMARK 500 THIS ENTRY HAS 279 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 48 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 27 O
REMARK 620 2 ASP A 30 OD2 76.4
REMARK 620 3 HIS A 32 O 162.2 85.9
REMARK 620 4 ASP A 34 OD2 96.0 106.8 87.2
REMARK 620 5 ASP A 40 OD2 94.3 170.0 103.4 77.6
REMARK 620 6 GLU A 41 OE1 100.8 74.9 76.1 163.0 103.6
REMARK 620 N 1 2 3 4 5
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 48
DBREF 1JRF A 1 47 UNP P98162 RSVR_COTJA 26 72
SEQADV 1JRF GLY A 1 UNP P98162 SER 26 CLONING ARTIFACT
SEQADV 1JRF SER A 2 UNP P98162 LEU 27 CLONING ARTIFACT
SEQRES 1 A 47 GLY SER SER ARG CYS PRO PRO GLY GLN PHE ARG CYS SER
SEQRES 2 A 47 GLU PRO PRO GLY ALA HIS GLY GLU CYS TYR PRO GLN ASP
SEQRES 3 A 47 TRP LEU CYS ASP GLY HIS PRO ASP CYS ASP ASP GLY ARG
SEQRES 4 A 47 ASP GLU TRP GLY CYS GLY THR SER
HET CA A 48 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 TYR A 23 LEU A 28 5 6
HELIX 2 2 GLU A 41 THR A 46 1 6
SSBOND 1 CYS A 5 CYS A 22 1555 1555 2.07
SSBOND 2 CYS A 12 CYS A 35 1555 1555 1.98
SSBOND 3 CYS A 29 CYS A 44 1555 1555 1.99
LINK O TRP A 27 CA CA A 48 1555 1555 2.50
LINK OD2 ASP A 30 CA CA A 48 1555 1555 2.31
LINK O HIS A 32 CA CA A 48 1555 1555 2.18
LINK OD2 ASP A 34 CA CA A 48 1555 1555 2.64
LINK OD2 ASP A 40 CA CA A 48 1555 1555 3.02
LINK OE1 GLU A 41 CA CA A 48 1555 1555 2.60
SITE 1 AC1 6 TRP A 27 ASP A 30 HIS A 32 ASP A 34
SITE 2 AC1 6 ASP A 40 GLU A 41
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