Header list of 1cfc.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 02-AUG-95 1CFC
TITLE CALCIUM-FREE CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE,A.BAX
REVDAT 3 16-FEB-22 1CFC 1 REMARK
REVDAT 2 24-FEB-09 1CFC 1 VERSN
REVDAT 1 07-DEC-95 1CFC 0
JRNL AUTH H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE,A.BAX
JRNL TITL SOLUTION STRUCTURE OF CALCIUM-FREE CALMODULIN.
JRNL REF NAT.STRUCT.BIOL. V. 2 768 1995
JRNL REFN ISSN 1072-8368
JRNL PMID 7552748
JRNL DOI 10.1038/NSB0995-768
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 1CFC 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_1000172289.
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 : 25
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 ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 13 TYR A 138 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
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 ASP A 56 33.36 -79.83
REMARK 500 1 MET A 76 35.58 -92.27
REMARK 500 1 LYS A 77 -104.52 -94.09
REMARK 500 1 ASP A 78 -6.60 -52.29
REMARK 500 1 ASP A 80 167.56 -45.04
REMARK 500 1 LYS A 115 42.87 -79.52
REMARK 500 1 ASP A 129 81.17 -39.00
REMARK 500 1 ASP A 131 -155.33 -114.01
REMARK 500 1 ASP A 133 -83.40 -133.07
REMARK 500 1 GLU A 139 -39.07 -39.77
REMARK 500 1 ALA A 147 115.92 -179.66
REMARK 500 2 ASP A 2 16.47 -155.96
REMARK 500 2 ASP A 20 69.68 -100.06
REMARK 500 2 ASP A 56 37.70 -79.72
REMARK 500 2 ASN A 60 -91.95 -131.30
REMARK 500 2 LYS A 77 -23.37 -35.17
REMARK 500 2 THR A 79 37.17 -82.59
REMARK 500 2 ASP A 80 168.39 -46.40
REMARK 500 2 ALA A 102 -34.76 -39.93
REMARK 500 2 LYS A 115 38.18 -80.63
REMARK 500 2 ASP A 129 82.16 -39.12
REMARK 500 2 ASP A 131 -154.78 -113.55
REMARK 500 2 ASP A 133 -83.52 -132.08
REMARK 500 2 THR A 146 -76.34 -84.09
REMARK 500 2 ALA A 147 118.89 179.92
REMARK 500 3 ASP A 56 33.79 -79.65
REMARK 500 3 MET A 76 53.42 -97.84
REMARK 500 3 LYS A 77 -99.98 -123.32
REMARK 500 3 ASP A 78 -8.15 -46.15
REMARK 500 3 ASP A 80 168.24 -45.92
REMARK 500 3 ALA A 102 -32.13 -39.98
REMARK 500 3 LYS A 115 38.04 -79.98
REMARK 500 3 ASP A 129 81.31 -39.02
REMARK 500 3 ASP A 131 -158.51 -112.05
REMARK 500 3 ASP A 133 -82.42 -131.42
REMARK 500 3 ALA A 147 113.16 -174.64
REMARK 500 4 ASP A 56 36.07 -79.74
REMARK 500 4 ASN A 60 -91.95 -132.48
REMARK 500 4 MET A 76 99.64 -56.91
REMARK 500 4 LYS A 77 -92.74 -154.82
REMARK 500 4 ASP A 78 -9.13 -41.51
REMARK 500 4 ASP A 80 168.12 -49.63
REMARK 500 4 ALA A 102 -33.57 -39.90
REMARK 500 4 LYS A 115 38.71 -80.86
REMARK 500 4 ASP A 129 82.02 -39.20
REMARK 500 4 ASP A 131 -158.62 -112.16
REMARK 500 4 ASP A 133 -81.94 -128.30
REMARK 500 4 TYR A 138 -20.80 -39.85
REMARK 500 5 ASP A 2 17.88 -157.05
REMARK 500 5 ASP A 20 68.86 -100.03
REMARK 500
REMARK 500 THIS ENTRY HAS 296 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CFD RELATED DB: PDB
DBREF 1CFC 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 ASP 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 PHE A 19 1 14
HELIX 2 2 THR A 29 SER A 38 5 10
HELIX 3 3 GLU A 45 VAL A 55 1 11
HELIX 4 4 PHE A 65 LYS A 75 1 11
HELIX 5 5 GLU A 82 VAL A 91 1 10
HELIX 6 6 ALA A 102 ASN A 111 1 10
HELIX 7 7 ASP A 118 GLU A 127 1 10
HELIX 8 8 GLU A 139 THR A 146 1 8
SHEET 1 A 2 THR A 26 THR A 28 0
SHEET 2 A 2 THR A 62 ASP A 64 -1 N ILE A 63 O ILE A 27
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