Header list of 1n7l.pdb file
Complete list - t 27 2 Bytes
HEADER SIGNALING PROTEIN 15-NOV-02 1N7L
TITLE SOLUTION NMR STRUCTURE OF PHOSPHOLAMBAN IN DETERGENT MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARDIAC PHOSPHOLAMBAN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PLB;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 GENE: PLN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3PHI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMAL
KEYWDS HELIX-TURN-HELIX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.ZAMOON,A.MASCIONI,D.D.THOMAS,G.VEGLIA
REVDAT 3 27-OCT-21 1N7L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1N7L 1 VERSN
REVDAT 1 28-OCT-03 1N7L 0
JRNL AUTH J.ZAMOON,A.MASCIONI,D.D.THOMAS,G.VEGLIA
JRNL TITL NMR SOLUTION STRUCTURE AND TOPOLOGICAL ORIENTATION OF
JRNL TITL 2 MONOMERIC PHOSPHOLAMBAN IN DODECYLPHOSPHOCHOLINE MICELLES.
JRNL REF BIOPHYS.J. V. 85 2589 2003
JRNL REFN ISSN 0006-3495
JRNL PMID 14507721
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, XPLOR-NIH 2.0.4
REMARK 3 AUTHORS : VARIAN (VNMR), CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N7L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017618.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 4.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM PHOSPHOLAMBAN U-15N,13C; 20
REMARK 210 MM PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O; PH=4.2; 600 MM DPC;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; HNCA; HN(CO)CA;
REMARK 210 HNCACB; HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0, XPLOR-NIH
REMARK 210 2.0.4
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
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 HH11 ARG A 14 OE1 GLN A 23 1.44
REMARK 500 OG SER A 11 HH21 ARG A 14 1.46
REMARK 500 O ALA A 12 HH11 ARG A 15 1.48
REMARK 500 O GLN A 24 H ASN A 28 1.49
REMARK 500 HH21 ARG A 15 OE1 GLN A 24 1.49
REMARK 500 O ASN A 31 H ASN A 35 1.51
REMARK 500 OE2 GLU A 3 HH12 ARG A 10 1.57
REMARK 500 OE2 GLU A 20 HH22 ARG A 26 1.59
REMARK 500 HD21 ASN A 31 OD1 ASN A 35 1.59
REMARK 500 HE21 GLN A 27 OD1 ASN A 31 1.59
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 THR A 18 17.65 -145.38
REMARK 500 1 GLU A 20 -132.48 -76.78
REMARK 500 1 MET A 21 -163.49 -67.92
REMARK 500 1 PRO A 22 79.52 -64.57
REMARK 500 2 GLU A 3 -72.09 -89.31
REMARK 500 2 GLU A 20 -126.33 -76.96
REMARK 500 2 PRO A 22 81.48 -63.25
REMARK 500 3 GLU A 20 -127.09 -69.17
REMARK 500 3 MET A 21 -165.57 -65.94
REMARK 500 3 PRO A 22 80.07 -65.45
REMARK 500 4 ARG A 15 -39.41 -39.90
REMARK 500 4 THR A 18 20.29 -148.63
REMARK 500 4 ILE A 19 113.79 -39.41
REMARK 500 4 GLU A 20 -128.98 -84.59
REMARK 500 4 MET A 21 170.50 -57.98
REMARK 500 4 PRO A 22 81.26 -63.88
REMARK 500 4 GLN A 23 -51.37 -124.87
REMARK 500 5 GLU A 3 -72.82 -89.19
REMARK 500 5 THR A 18 -3.46 -146.98
REMARK 500 5 GLU A 20 -137.47 -98.85
REMARK 500 5 MET A 21 -163.63 -68.33
REMARK 500 5 PRO A 22 84.70 -62.89
REMARK 500 5 GLN A 23 55.04 -61.21
REMARK 500 6 MET A 2 47.02 -74.97
REMARK 500 6 THR A 18 -29.61 -149.29
REMARK 500 6 GLU A 20 -128.80 -81.24
REMARK 500 6 MET A 21 -172.78 -67.74
REMARK 500 6 PRO A 22 78.28 -68.97
REMARK 500 7 MET A 2 42.68 -77.05
REMARK 500 7 ARG A 15 -37.19 -37.50
REMARK 500 7 THR A 18 21.65 -147.52
REMARK 500 7 GLU A 20 -127.42 -64.03
REMARK 500 7 MET A 21 -177.47 -64.71
REMARK 500 7 PRO A 22 79.92 -65.28
REMARK 500 8 ARG A 14 -39.83 -39.15
REMARK 500 8 THR A 18 22.76 -148.52
REMARK 500 8 GLU A 20 -128.71 -76.09
REMARK 500 8 PRO A 22 79.89 -64.16
REMARK 500 9 GLU A 3 -112.10 -96.07
REMARK 500 9 THR A 18 -1.80 -146.84
REMARK 500 9 GLU A 20 -127.52 -87.08
REMARK 500 9 MET A 21 -173.06 -66.51
REMARK 500 9 PRO A 22 79.92 -66.64
REMARK 500 10 GLU A 3 -72.53 -91.25
REMARK 500 10 THR A 18 -2.49 -141.72
REMARK 500 10 GLU A 20 -128.16 -70.78
REMARK 500 10 PRO A 22 80.39 -65.18
REMARK 500 11 GLU A 3 -81.65 -103.48
REMARK 500 11 THR A 18 25.23 -147.24
REMARK 500 11 GLU A 20 -128.27 -67.63
REMARK 500
REMARK 500 THIS ENTRY HAS 99 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 10 0.32 SIDE CHAIN
REMARK 500 1 ARG A 14 0.30 SIDE CHAIN
REMARK 500 1 ARG A 15 0.20 SIDE CHAIN
REMARK 500 1 ARG A 26 0.32 SIDE CHAIN
REMARK 500 2 ARG A 10 0.32 SIDE CHAIN
REMARK 500 2 ARG A 14 0.17 SIDE CHAIN
REMARK 500 2 ARG A 15 0.26 SIDE CHAIN
REMARK 500 2 ARG A 26 0.30 SIDE CHAIN
REMARK 500 3 ARG A 10 0.31 SIDE CHAIN
REMARK 500 3 ARG A 14 0.20 SIDE CHAIN
REMARK 500 3 ARG A 15 0.27 SIDE CHAIN
REMARK 500 3 ARG A 26 0.26 SIDE CHAIN
REMARK 500 4 ARG A 10 0.26 SIDE CHAIN
REMARK 500 4 ARG A 14 0.23 SIDE CHAIN
REMARK 500 4 ARG A 15 0.18 SIDE CHAIN
REMARK 500 4 ARG A 26 0.32 SIDE CHAIN
REMARK 500 5 ARG A 10 0.32 SIDE CHAIN
REMARK 500 5 ARG A 14 0.20 SIDE CHAIN
REMARK 500 5 ARG A 15 0.23 SIDE CHAIN
REMARK 500 5 ARG A 26 0.10 SIDE CHAIN
REMARK 500 6 ARG A 10 0.31 SIDE CHAIN
REMARK 500 6 ARG A 14 0.18 SIDE CHAIN
REMARK 500 6 ARG A 15 0.21 SIDE CHAIN
REMARK 500 6 ARG A 26 0.31 SIDE CHAIN
REMARK 500 7 ARG A 10 0.32 SIDE CHAIN
REMARK 500 7 ARG A 14 0.32 SIDE CHAIN
REMARK 500 7 ARG A 15 0.31 SIDE CHAIN
REMARK 500 7 ARG A 26 0.28 SIDE CHAIN
REMARK 500 8 ARG A 10 0.31 SIDE CHAIN
REMARK 500 8 ARG A 14 0.27 SIDE CHAIN
REMARK 500 8 ARG A 15 0.27 SIDE CHAIN
REMARK 500 8 ARG A 26 0.32 SIDE CHAIN
REMARK 500 9 ARG A 10 0.32 SIDE CHAIN
REMARK 500 9 ARG A 14 0.31 SIDE CHAIN
REMARK 500 9 ARG A 15 0.32 SIDE CHAIN
REMARK 500 9 ARG A 26 0.29 SIDE CHAIN
REMARK 500 10 ARG A 10 0.31 SIDE CHAIN
REMARK 500 10 ARG A 14 0.31 SIDE CHAIN
REMARK 500 10 ARG A 15 0.27 SIDE CHAIN
REMARK 500 10 ARG A 26 0.30 SIDE CHAIN
REMARK 500 11 ARG A 10 0.32 SIDE CHAIN
REMARK 500 11 ARG A 14 0.27 SIDE CHAIN
REMARK 500 11 ARG A 15 0.31 SIDE CHAIN
REMARK 500 11 ARG A 26 0.28 SIDE CHAIN
REMARK 500 12 ARG A 10 0.29 SIDE CHAIN
REMARK 500 12 ARG A 14 0.32 SIDE CHAIN
REMARK 500 12 ARG A 15 0.31 SIDE CHAIN
REMARK 500 12 ARG A 26 0.28 SIDE CHAIN
REMARK 500 13 ARG A 10 0.31 SIDE CHAIN
REMARK 500 13 ARG A 14 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N7L A 2 53 UNP P61015 PPLA_RABIT 1 52
SEQADV 1N7L ALA A 1 UNP P61015 CLONING ARTIFACT
SEQADV 1N7L ALA A 37 UNP P61015 CYS 36 ENGINEERED MUTATION
SEQADV 1N7L PHE A 42 UNP P61015 CYS 41 ENGINEERED MUTATION
SEQADV 1N7L ALA A 47 UNP P61015 CYS 46 ENGINEERED MUTATION
SEQRES 1 A 53 ALA MET GLU LYS VAL GLN TYR LEU THR ARG SER ALA ILE
SEQRES 2 A 53 ARG ARG ALA SER THR ILE GLU MET PRO GLN GLN ALA ARG
SEQRES 3 A 53 GLN ASN LEU GLN ASN LEU PHE ILE ASN PHE ALA LEU ILE
SEQRES 4 A 53 LEU ILE PHE LEU LEU LEU ILE ALA ILE ILE VAL MET LEU
SEQRES 5 A 53 LEU
HELIX 1 1 MET A 2 THR A 18 1 17
HELIX 2 2 PRO A 22 LEU A 52 1 31
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 - t 27 2 Bytes