Header list of 1yx7.pdb file
Complete list - 2 20 Bytes
HEADER METAL BINDING PROTEIN 19-FEB-05 1YX7
TITLE NMR STRUCTURE OF CALSENSIN, ENERGY MINIMIZED AVERAGE STRUCTURE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALSENSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LAN3-6 ANTIGEN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPIS MARMORATA;
SOURCE 3 ORGANISM_TAXID: 38567;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS CALSENSIN, CALCIUM-BINDING PROTEIN EF-HAND, HELIX-LOOP-HELIX, NERVOUS
KEYWDS 2 SYSTEM, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR D.V.VENKITARAMANI,D.B.FULTON,A.H.ANDREOTTI,K.M.JOHANSEN,J.JOHANSEN
REVDAT 4 02-MAR-22 1YX7 1 REMARK
REVDAT 3 24-FEB-09 1YX7 1 VERSN
REVDAT 2 13-DEC-05 1YX7 1 JRNL
REVDAT 1 01-APR-05 1YX7 0
JRNL AUTH D.V.VENKITARAMANI,D.B.FULTON,A.H.ANDREOTTI,K.M.JOHANSEN,
JRNL AUTH 2 J.JOHANSEN
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF CALSENSIN, AN
JRNL TITL 2 INVERTEBRATE NEURONAL CALCIUM-BINDING PROTEIN.
JRNL REF PROTEIN SCI. V. 14 1894 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15937283
JRNL DOI 10.1110/PS.051412605
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032025.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 125 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.7 MM CALSENSIN, U15N, 13C; 125
REMARK 210 MM PHOSPHATE BUFFER, 2 MM DTT;
REMARK 210 1.7 MM CALSENSIN, U15N; 125 MM
REMARK 210 PHOSPHATE BUFFER, 2 MM DTT; 1.5
REMARK 210 MM CALSENSIN, 125 MM PHOSPHATE
REMARK 210 BUFFER, 2 MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.0, NMRVIEW 5.0.4
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 HB1 ALA A 12 H GLU A 69 1.25
REMARK 500 HD21 LEU A 42 HG SER A 43 1.32
REMARK 500 O LYS A 14 HB3 ALA A 18 1.34
REMARK 500 O GLN A 30 HG12 VAL A 34 1.37
REMARK 500 O GLU A 69 H ASN A 73 1.38
REMARK 500 O GLU A 69 HD21 ASN A 73 1.40
REMARK 500 O TYR A 39 HD11 LEU A 42 1.41
REMARK 500 O LEU A 72 HD21 ASN A 75 1.41
REMARK 500 O ALA A 74 H LEU A 78 1.44
REMARK 500 O LYS A 68 H LEU A 72 1.45
REMARK 500 O LEU A 29 H MET A 33 1.48
REMARK 500 O ALA A 76 H CYS A 80 1.50
REMARK 500 O ALA A 12 H LEU A 16 1.50
REMARK 500 O SER A 51 H ILE A 55 1.51
REMARK 500 O THR A 31 H THR A 35 1.51
REMARK 500 O ALA A 7 H GLU A 10 1.53
REMARK 500 HD13 LEU A 16 N ASP A 17 1.53
REMARK 500 O TYR A 39 H ALA A 41 1.54
REMARK 500 O LYS A 48 H ALA A 52 1.55
REMARK 500 OE2 GLU A 28 HD11 LEU A 54 1.57
REMARK 500 O LEU A 16 OG1 THR A 25 2.09
REMARK 500 O GLU A 69 ND2 ASN A 73 2.10
REMARK 500 O LEU A 27 NE2 GLN A 30 2.12
REMARK 500 O LYS A 65 OE2 GLU A 69 2.17
REMARK 500 OD1 ASP A 45 OE2 GLU A 49 2.17
REMARK 500 O ALA A 12 N LEU A 16 2.18
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 CYS A 3 -151.21 36.73
REMARK 500 LYS A 4 -152.46 -162.82
REMARK 500 LYS A 6 -34.31 158.52
REMARK 500 ALA A 7 1.77 -66.78
REMARK 500 ASP A 17 53.29 -140.62
REMARK 500 ASN A 19 -23.64 -147.26
REMARK 500 ASP A 21 -45.13 -148.29
REMARK 500 ALA A 26 -18.29 -48.62
REMARK 500 LEU A 36 62.17 -160.59
REMARK 500 TYR A 39 18.39 46.14
REMARK 500 LYS A 40 43.22 -67.21
REMARK 500 ALA A 41 16.89 -161.30
REMARK 500 LEU A 42 -120.56 -90.57
REMARK 500 SER A 43 -84.02 42.50
REMARK 500 ASP A 45 20.70 124.48
REMARK 500 ALA A 58 -29.41 -168.42
REMARK 500 ASN A 61 14.45 -151.05
REMARK 500 SER A 62 71.31 98.58
REMARK 500 ASP A 63 -35.93 -137.20
REMARK 500 SER A 67 -143.76 163.75
REMARK 500 LYS A 68 -36.20 -38.38
REMARK 500 GLN A 81 124.16 92.21
REMARK 500 LEU A 82 -169.14 148.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YX8 RELATED DB: PDB
DBREF 1YX7 A 1 83 UNP Q25088 CLSS_HAEMA 1 83
SEQRES 1 A 83 MET ALA CYS LYS VAL LYS ALA GLU LEU GLU ALA ALA PHE
SEQRES 2 A 83 LYS LYS LEU ASP ALA ASN GLY ASP GLY TYR VAL THR ALA
SEQRES 3 A 83 LEU GLU LEU GLN THR PHE MET VAL THR LEU ASP ALA TYR
SEQRES 4 A 83 LYS ALA LEU SER LYS ASP LYS VAL LYS GLU ALA SER ALA
SEQRES 5 A 83 LYS LEU ILE LYS MET ALA ASP LYS ASN SER ASP GLY LYS
SEQRES 6 A 83 ILE SER LYS GLU GLU PHE LEU ASN ALA ASN ALA GLU LEU
SEQRES 7 A 83 LEU CYS GLN LEU LYS
HELIX 1 1 ALA A 7 ASP A 17 1 11
HELIX 2 2 THR A 25 ASP A 37 1 13
HELIX 3 3 VAL A 47 LYS A 56 1 10
HELIX 4 4 SER A 67 CYS A 80 1 14
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
Complete list - 2 20 Bytes