Header list of 1dmo.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 24-APR-96 1DMO
TITLE CALMODULIN, NMR, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: XENOPUS LAEVIS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAS;
SOURCE 9 EXPRESSION_SYSTEM_GENE: XENOPUS LAEVIS
KEYWDS CALCIUM-INDUCED CONFORMATIONAL CHANGE, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.ZHANG,T.TANAKA,M.IKURA
REVDAT 3 16-FEB-22 1DMO 1 REMARK
REVDAT 2 24-FEB-09 1DMO 1 VERSN
REVDAT 1 01-AUG-96 1DMO 0
JRNL AUTH M.ZHANG,T.TANAKA,M.IKURA
JRNL TITL CALCIUM-INDUCED CONFORMATIONAL TRANSITION REVEALED BY THE
JRNL TITL 2 SOLUTION STRUCTURE OF APO CALMODULIN.
JRNL REF NAT.STRUCT.BIOL. V. 2 758 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7552747
JRNL DOI 10.1038/NSB0995-758
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DMO 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_1000172843.
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 : 30
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: 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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 2 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 3 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 4 HIS A 107 CG HIS A 107 ND1 -0.119
REMARK 500 5 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 6 HIS A 107 CG HIS A 107 ND1 -0.119
REMARK 500 7 HIS A 107 CG HIS A 107 ND1 -0.122
REMARK 500 8 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 9 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 10 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 11 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 12 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 13 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 14 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 15 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 16 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 17 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 18 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 19 HIS A 107 CG HIS A 107 ND1 -0.119
REMARK 500 20 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 21 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 22 HIS A 107 CG HIS A 107 ND1 -0.122
REMARK 500 23 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 24 HIS A 107 CG HIS A 107 ND1 -0.119
REMARK 500 25 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 26 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 27 HIS A 107 CG HIS A 107 ND1 -0.122
REMARK 500 28 HIS A 107 CG HIS A 107 ND1 -0.121
REMARK 500 29 HIS A 107 CG HIS A 107 ND1 -0.120
REMARK 500 30 HIS A 107 CG HIS A 107 ND1 -0.122
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 GLN A 3 -141.21 56.89
REMARK 500 1 LEU A 4 -169.05 -58.42
REMARK 500 1 ASP A 22 -0.18 -53.14
REMARK 500 1 THR A 29 -28.20 -39.41
REMARK 500 1 GLU A 45 -18.25 -44.12
REMARK 500 1 ALA A 46 -70.67 -72.44
REMARK 500 1 VAL A 55 7.41 -58.96
REMARK 500 1 ASP A 56 30.35 -81.85
REMARK 500 1 ASP A 78 -170.24 49.04
REMARK 500 1 THR A 79 -147.11 -106.19
REMARK 500 1 SER A 81 -29.90 70.10
REMARK 500 1 GLU A 82 -19.90 -45.70
REMARK 500 1 VAL A 91 -4.62 -58.20
REMARK 500 1 ASP A 93 93.23 -43.50
REMARK 500 1 ASP A 95 -17.38 77.89
REMARK 500 1 GLU A 114 -99.08 -80.11
REMARK 500 1 LYS A 115 19.57 -146.01
REMARK 500 1 ALA A 128 36.63 -77.66
REMARK 500 1 ASN A 129 45.96 70.41
REMARK 500 1 ASP A 131 -39.06 -156.92
REMARK 500 1 ASN A 137 79.42 -69.82
REMARK 500 1 TYR A 138 -38.10 -39.86
REMARK 500 1 ALA A 147 -151.98 48.16
REMARK 500 2 ASP A 2 -33.34 -178.95
REMARK 500 2 LYS A 21 7.32 -65.98
REMARK 500 2 ASP A 22 -87.89 -81.20
REMARK 500 2 ASP A 24 -34.12 -138.67
REMARK 500 2 THR A 29 -30.44 -39.78
REMARK 500 2 ALA A 46 -70.20 -76.37
REMARK 500 2 VAL A 55 -123.96 -89.20
REMARK 500 2 ASP A 56 28.08 35.88
REMARK 500 2 LYS A 77 108.10 71.94
REMARK 500 2 ASP A 78 139.99 -35.70
REMARK 500 2 THR A 79 167.19 -49.34
REMARK 500 2 ASP A 80 -70.54 -89.11
REMARK 500 2 SER A 81 23.71 174.60
REMARK 500 2 VAL A 91 -11.12 -48.68
REMARK 500 2 LYS A 94 -63.12 -149.78
REMARK 500 2 ASN A 97 81.45 38.33
REMARK 500 2 TYR A 99 103.03 -170.51
REMARK 500 2 LYS A 115 34.90 77.46
REMARK 500 2 ALA A 128 30.92 -73.23
REMARK 500 2 ASP A 131 -107.06 -99.19
REMARK 500 2 ASP A 133 -60.79 -148.35
REMARK 500 2 ASN A 137 79.97 -69.56
REMARK 500 2 THR A 146 -71.86 -97.95
REMARK 500 2 ALA A 147 -158.57 53.39
REMARK 500 3 GLN A 3 144.12 -175.61
REMARK 500 3 LEU A 4 99.81 56.43
REMARK 500 3 LYS A 21 65.79 -154.59
REMARK 500
REMARK 500 THIS ENTRY HAS 638 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 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 74 0.32 SIDE CHAIN
REMARK 500 1 ARG A 86 0.31 SIDE CHAIN
REMARK 500 1 ARG A 90 0.25 SIDE CHAIN
REMARK 500 1 ARG A 106 0.31 SIDE CHAIN
REMARK 500 1 ARG A 126 0.31 SIDE CHAIN
REMARK 500 2 ARG A 37 0.26 SIDE CHAIN
REMARK 500 2 ARG A 74 0.32 SIDE CHAIN
REMARK 500 2 ARG A 90 0.27 SIDE CHAIN
REMARK 500 2 ARG A 106 0.27 SIDE CHAIN
REMARK 500 2 ARG A 126 0.25 SIDE CHAIN
REMARK 500 3 ARG A 37 0.15 SIDE CHAIN
REMARK 500 3 ARG A 74 0.16 SIDE CHAIN
REMARK 500 3 ARG A 86 0.19 SIDE CHAIN
REMARK 500 3 ARG A 90 0.12 SIDE CHAIN
REMARK 500 3 ARG A 106 0.22 SIDE CHAIN
REMARK 500 3 ARG A 126 0.27 SIDE CHAIN
REMARK 500 4 ARG A 37 0.27 SIDE CHAIN
REMARK 500 4 ARG A 74 0.19 SIDE CHAIN
REMARK 500 4 ARG A 86 0.32 SIDE CHAIN
REMARK 500 4 ARG A 90 0.15 SIDE CHAIN
REMARK 500 4 ARG A 106 0.08 SIDE CHAIN
REMARK 500 4 ARG A 126 0.32 SIDE CHAIN
REMARK 500 5 ARG A 37 0.30 SIDE CHAIN
REMARK 500 5 ARG A 74 0.22 SIDE CHAIN
REMARK 500 5 ARG A 86 0.13 SIDE CHAIN
REMARK 500 5 ARG A 90 0.08 SIDE CHAIN
REMARK 500 5 ARG A 106 0.32 SIDE CHAIN
REMARK 500 5 ARG A 126 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.28 SIDE CHAIN
REMARK 500 6 ARG A 74 0.32 SIDE CHAIN
REMARK 500 6 ARG A 86 0.08 SIDE CHAIN
REMARK 500 6 ARG A 90 0.20 SIDE CHAIN
REMARK 500 6 ARG A 106 0.23 SIDE CHAIN
REMARK 500 6 ARG A 126 0.26 SIDE CHAIN
REMARK 500 7 ARG A 37 0.30 SIDE CHAIN
REMARK 500 7 ARG A 74 0.27 SIDE CHAIN
REMARK 500 7 ARG A 86 0.32 SIDE CHAIN
REMARK 500 7 ARG A 90 0.28 SIDE CHAIN
REMARK 500 7 ARG A 106 0.11 SIDE CHAIN
REMARK 500 7 ARG A 126 0.32 SIDE CHAIN
REMARK 500 8 ARG A 37 0.17 SIDE CHAIN
REMARK 500 8 ARG A 74 0.09 SIDE CHAIN
REMARK 500 8 ARG A 86 0.32 SIDE CHAIN
REMARK 500 8 ARG A 90 0.21 SIDE CHAIN
REMARK 500 8 ARG A 106 0.25 SIDE CHAIN
REMARK 500 8 ARG A 126 0.30 SIDE CHAIN
REMARK 500 9 ARG A 37 0.30 SIDE CHAIN
REMARK 500 9 ARG A 74 0.17 SIDE CHAIN
REMARK 500 9 ARG A 86 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 176 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DMO A 1 148 UNP P62155 CALM_XENLA 1 148
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASN ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
HELIX 1 1 GLU A 6 LEU A 18 1 13
HELIX 2 2 THR A 29 LEU A 39 1 11
HELIX 3 3 GLU A 45 VAL A 55 1 11
HELIX 4 4 PHE A 65 MET A 76 1 12
HELIX 5 5 GLU A 82 ARG A 90 1 9
HELIX 6 6 ALA A 102 LEU A 112 1 11
HELIX 7 7 ASP A 118 GLU A 127 1 10
HELIX 8 8 TYR A 138 GLN A 143 1 6
SHEET 1 A 2 ILE A 27 THR A 28 0
SHEET 2 A 2 THR A 62 ILE A 63 -1 N ILE A 63 O ILE A 27
SHEET 1 B 2 ILE A 100 SER A 101 0
SHEET 2 B 2 GLN A 135 VAL A 136 -1 O VAL A 136 N ILE A 100
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