Header list of 1cmg.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 19-JUL-95 1CMG
TITLE NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN (VERTEBRATE);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALMODULIN CALCIUM TR2C-DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRCB1
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.EVENAS,B.E.FINN,T.DRAKENBERG,J.P.WALTHO,E.THULIN,S.FORSEN
REVDAT 3 16-FEB-22 1CMG 1 REMARK
REVDAT 2 24-FEB-09 1CMG 1 VERSN
REVDAT 1 07-DEC-95 1CMG 0
JRNL AUTH B.E.FINN,J.EVENAS,T.DRAKENBERG,J.P.WALTHO,E.THULIN,S.FORSEN
JRNL TITL CALCIUM-INDUCED STRUCTURAL CHANGES AND DOMAIN AUTONOMY IN
JRNL TITL 2 CALMODULIN.
JRNL REF NAT.STRUCT.BIOL. V. 2 777 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7552749
JRNL DOI 10.1038/NSB0995-777
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.E.FINN,T.DRAKENBERG,S.FORSEN
REMARK 1 TITL THE STRUCTURE OF APO-CALMODULIN: A 1H NMR EXAMINATION OF
REMARK 1 TITL 2 CARBOXY-TERMINAL DOMAIN
REMARK 1 REF FEBS LETT. V. 336 368 1993
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CMG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172393.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 LYS A 77 132.18 173.01
REMARK 500 1 ASP A 78 84.83 40.66
REMARK 500 1 SER A 81 104.22 59.45
REMARK 500 1 ASP A 131 57.83 -177.47
REMARK 500 1 THR A 146 -85.78 -61.20
REMARK 500 2 THR A 79 -173.16 52.73
REMARK 500 2 ASP A 80 -64.97 -144.18
REMARK 500 2 SER A 81 22.99 47.59
REMARK 500 2 LEU A 112 13.46 -145.83
REMARK 500 2 GLU A 114 153.67 62.05
REMARK 500 2 ASP A 131 -36.29 -156.67
REMARK 500 3 THR A 79 97.95 58.51
REMARK 500 3 LEU A 112 35.70 174.92
REMARK 500 3 GLU A 114 -160.72 72.31
REMARK 500 3 THR A 117 -155.92 -112.10
REMARK 500 3 ILE A 130 -71.07 -86.78
REMARK 500 3 ASP A 131 58.10 179.62
REMARK 500 3 ALA A 147 97.27 -59.29
REMARK 500 4 LYS A 77 93.58 67.43
REMARK 500 4 ASP A 80 -88.96 39.48
REMARK 500 4 SER A 81 111.32 177.51
REMARK 500 4 LEU A 112 18.14 -152.62
REMARK 500 4 GLU A 114 -169.12 62.09
REMARK 500 4 THR A 146 -46.54 -130.87
REMARK 500 4 ALA A 147 48.80 -93.92
REMARK 500 5 ASP A 78 -47.58 82.74
REMARK 500 5 THR A 79 -166.95 60.13
REMARK 500 5 ASP A 80 14.25 56.85
REMARK 500 5 VAL A 108 41.02 -103.16
REMARK 500 5 LEU A 112 22.69 -159.50
REMARK 500 5 GLU A 114 -141.18 56.84
REMARK 500 5 LEU A 116 -160.67 -59.31
REMARK 500 6 LYS A 77 156.12 65.88
REMARK 500 6 ASP A 80 -75.89 -117.44
REMARK 500 6 SER A 81 117.27 165.67
REMARK 500 6 GLU A 114 141.45 63.49
REMARK 500 6 LYS A 115 100.59 -50.39
REMARK 500 6 THR A 146 -62.46 -91.91
REMARK 500 7 ASP A 80 -59.88 -127.68
REMARK 500 7 GLU A 82 -89.13 -79.98
REMARK 500 7 GLU A 114 -134.53 45.45
REMARK 500 7 THR A 117 -159.73 -77.55
REMARK 500 7 ALA A 128 -65.18 -92.59
REMARK 500 7 ASP A 131 65.01 173.46
REMARK 500 7 GLN A 143 -34.65 -39.38
REMARK 500 7 THR A 146 -89.27 -125.24
REMARK 500 8 LYS A 77 78.84 -169.66
REMARK 500 8 LEU A 112 23.48 -163.80
REMARK 500 8 GLU A 114 146.39 67.80
REMARK 500 9 ASP A 78 176.63 -59.33
REMARK 500
REMARK 500 THIS ENTRY HAS 130 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 86 0.15 SIDE CHAIN
REMARK 500 1 ARG A 90 0.13 SIDE CHAIN
REMARK 500 1 ARG A 106 0.27 SIDE CHAIN
REMARK 500 1 ARG A 126 0.32 SIDE CHAIN
REMARK 500 2 ARG A 86 0.32 SIDE CHAIN
REMARK 500 2 ARG A 90 0.27 SIDE CHAIN
REMARK 500 2 ARG A 106 0.28 SIDE CHAIN
REMARK 500 2 ARG A 126 0.13 SIDE CHAIN
REMARK 500 3 ARG A 86 0.31 SIDE CHAIN
REMARK 500 3 ARG A 90 0.20 SIDE CHAIN
REMARK 500 3 ARG A 106 0.24 SIDE CHAIN
REMARK 500 3 ARG A 126 0.28 SIDE CHAIN
REMARK 500 4 ARG A 86 0.23 SIDE CHAIN
REMARK 500 4 ARG A 90 0.31 SIDE CHAIN
REMARK 500 4 ARG A 106 0.28 SIDE CHAIN
REMARK 500 4 ARG A 126 0.12 SIDE CHAIN
REMARK 500 5 ARG A 86 0.20 SIDE CHAIN
REMARK 500 5 ARG A 90 0.12 SIDE CHAIN
REMARK 500 5 ARG A 106 0.11 SIDE CHAIN
REMARK 500 5 ARG A 126 0.18 SIDE CHAIN
REMARK 500 6 ARG A 86 0.08 SIDE CHAIN
REMARK 500 6 ARG A 90 0.26 SIDE CHAIN
REMARK 500 6 ARG A 106 0.29 SIDE CHAIN
REMARK 500 6 ARG A 126 0.12 SIDE CHAIN
REMARK 500 7 ARG A 86 0.16 SIDE CHAIN
REMARK 500 7 ARG A 90 0.21 SIDE CHAIN
REMARK 500 7 ARG A 106 0.16 SIDE CHAIN
REMARK 500 7 ARG A 126 0.14 SIDE CHAIN
REMARK 500 8 ARG A 86 0.16 SIDE CHAIN
REMARK 500 8 ARG A 90 0.31 SIDE CHAIN
REMARK 500 8 ARG A 106 0.29 SIDE CHAIN
REMARK 500 8 ARG A 126 0.29 SIDE CHAIN
REMARK 500 9 ARG A 86 0.18 SIDE CHAIN
REMARK 500 9 ARG A 90 0.25 SIDE CHAIN
REMARK 500 9 ARG A 106 0.26 SIDE CHAIN
REMARK 500 9 ARG A 126 0.24 SIDE CHAIN
REMARK 500 10 ARG A 86 0.29 SIDE CHAIN
REMARK 500 10 ARG A 90 0.26 SIDE CHAIN
REMARK 500 10 ARG A 106 0.32 SIDE CHAIN
REMARK 500 10 ARG A 126 0.21 SIDE CHAIN
REMARK 500 11 ARG A 86 0.32 SIDE CHAIN
REMARK 500 11 ARG A 90 0.10 SIDE CHAIN
REMARK 500 11 ARG A 106 0.27 SIDE CHAIN
REMARK 500 11 ARG A 126 0.30 SIDE CHAIN
REMARK 500 12 ARG A 86 0.25 SIDE CHAIN
REMARK 500 12 ARG A 90 0.32 SIDE CHAIN
REMARK 500 12 ARG A 106 0.31 SIDE CHAIN
REMARK 500 12 ARG A 126 0.29 SIDE CHAIN
REMARK 500 13 ARG A 86 0.20 SIDE CHAIN
REMARK 500 13 ARG A 90 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: EF3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1CMG A 76 148 UNP P62157 CALM_BOVIN 76 148
SEQRES 1 A 73 MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA
SEQRES 2 A 73 PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER
SEQRES 3 A 73 ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU
SEQRES 4 A 73 LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU
SEQRES 5 A 73 ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU
SEQRES 6 A 73 PHE VAL GLN MET MET THR ALA LYS
HELIX 1 1 GLU A 82 PHE A 92 5 11
HELIX 2 2 ALA A 102 VAL A 108 1 7
HELIX 3 3 ASP A 118 ALA A 128 1 11
HELIX 4 4 TYR A 138 MET A 145 1 8
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 N VAL A 136 O ILE A 100
SITE 1 EF3 12 ASP A 93 LYS A 94 ASP A 95 GLY A 96
SITE 2 EF3 12 ASN A 97 GLY A 98 TYR A 99 ILE A 100
SITE 3 EF3 12 SER A 101 ALA A 102 ALA A 103 GLU A 104
SITE 1 EF4 12 ASP A 129 ILE A 130 ASP A 131 GLY A 132
SITE 2 EF4 12 ASP A 133 GLY A 134 GLN A 135 VAL A 136
SITE 3 EF4 12 ASN A 137 TYR A 138 GLU A 139 GLU A 140
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 16 2 Bytes